메뉴 건너뛰기




Volumn 21, Issue 3, 2016, Pages 379-404

The human HSP70 family of chaperones: where do we stand?

Author keywords

Disease relevance; Function; Hsp70; Inhibitors; Regulation; Structure; Therapeutic implications

Indexed keywords

CHAPERONE; CHEMICAL COMPOUND; HEAT SHOCK PROTEIN 70; PROTEIN DNAK; MULTIPROTEIN COMPLEX; PROTEIN AGGREGATE;

EID: 84957654556     PISSN: 13558145     EISSN: 14661268     Source Type: Journal    
DOI: 10.1007/s12192-016-0676-6     Document Type: Review
Times cited : (407)

References (316)
  • 1
    • 3442878404 scopus 로고    scopus 로고
    • Plasma levels of heat shock protein 70 in patients with prostate cancer: a potential biomarker for prostate cancer
    • COI: 1:CAS:528:DC%2BD2cXntFOhtLo%3D, PID: 15279691
    • Abe M, Manola JB, Oh WK et al (2004) Plasma levels of heat shock protein 70 in patients with prostate cancer: a potential biomarker for prostate cancer. Clin Prostate Cancer 3:49–53
    • (2004) Clin Prostate Cancer , vol.3 , pp. 49-53
    • Abe, M.1    Manola, J.B.2    Oh, W.K.3
  • 2
    • 84882250523 scopus 로고    scopus 로고
    • Allosteric heat shock protein 70 inhibitors rapidly rescue synaptic plasticity deficits by reducing aberrant tau
    • COI: 1:CAS:528:DC%2BC3sXmsFChsbw%3D, PID: 23607970
    • Abisambra J, Jinwal UK, Miyata Y et al (2013) Allosteric heat shock protein 70 inhibitors rapidly rescue synaptic plasticity deficits by reducing aberrant tau. Biol Psychiatry 74:367–374
    • (2013) Biol Psychiatry , vol.74 , pp. 367-374
    • Abisambra, J.1    Jinwal, U.K.2    Miyata, Y.3
  • 3
    • 68849108869 scopus 로고    scopus 로고
    • Inflammation and cancer: how friendly is the relationship for cancer patients?
    • COI: 1:CAS:528:DC%2BD1MXhtVenurnI, PID: 19665429
    • Aggarwal BB, Gehlot P (2009) Inflammation and cancer: how friendly is the relationship for cancer patients? Curr Opin Pharmacol 9:351–369
    • (2009) Curr Opin Pharmacol , vol.9 , pp. 351-369
    • Aggarwal, B.B.1    Gehlot, P.2
  • 4
    • 82755187767 scopus 로고    scopus 로고
    • Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface
    • COI: 1:CAS:528:DC%2BC3MXhs1Wkt73M, PID: 22065753
    • Ahmad A, Bhattacharya A, McDonald RA et al (2011) Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface. Proc Natl Acad Sci U S A 108:18966–18971
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 18966-18971
    • Ahmad, A.1    Bhattacharya, A.2    McDonald, R.A.3
  • 5
    • 77954955686 scopus 로고    scopus 로고
    • Heat shock factors: integrators of cell stress, development and lifespan
    • COI: 1:CAS:528:DC%2BC3cXosl2rtLw%3D, PID: 20628411
    • Akerfelt M, Morimoto RI, Sistonen L (2010) Heat shock factors: integrators of cell stress, development and lifespan. Nat Rev Mol Cell Biol 11:545–555
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 545-555
    • Akerfelt, M.1    Morimoto, R.I.2    Sistonen, L.3
  • 6
    • 0026619974 scopus 로고
    • Regulation of expression of the interleukin 6 gene: structure and function of the transcription factor NF-IL6
    • COI: 1:CAS:528:DyaK3sXitlWks7k%3D, PID: 1385054
    • Akira S, Isshiki H, Nakajima T et al (1992) Regulation of expression of the interleukin 6 gene: structure and function of the transcription factor NF-IL6. Ciba Found Symp 167:47–62
    • (1992) Ciba Found Symp , vol.167 , pp. 47-62
    • Akira, S.1    Isshiki, H.2    Nakajima, T.3
  • 7
    • 84887037839 scopus 로고    scopus 로고
    • Expression of heat shock proteins in medulloblastoma
    • PID: 23992239
    • Alexiou GA, Vartholomatos G, Stefanaki K et al (2013) Expression of heat shock proteins in medulloblastoma. J Neurosurg Pediatr 12:452–457
    • (2013) J Neurosurg Pediatr , vol.12 , pp. 452-457
    • Alexiou, G.A.1    Vartholomatos, G.2    Stefanaki, K.3
  • 8
    • 84908278601 scopus 로고    scopus 로고
    • Expression of heat shock proteins in brain tumors
    • PID: 25269047
    • Alexiou GA, Karamoutsios A, Lallas G et al (2014) Expression of heat shock proteins in brain tumors. Turk Neurosurg 24:745–749
    • (2014) Turk Neurosurg , vol.24 , pp. 745-749
    • Alexiou, G.A.1    Karamoutsios, A.2    Lallas, G.3
  • 9
    • 81055124264 scopus 로고    scopus 로고
    • Combining curcumin (diferuloylmethane) and heat shock protein inhibition for neurofibromatosis 2 treatment: analysis of response and resistance pathways
    • COI: 1:CAS:528:DC%2BC3MXhsVeltLfN, PID: 21903608
    • Angelo LS, Wu JY, Meng F et al (2011) Combining curcumin (diferuloylmethane) and heat shock protein inhibition for neurofibromatosis 2 treatment: analysis of response and resistance pathways. Mol Cancer Ther 10:2094–2103
    • (2011) Mol Cancer Ther , vol.10 , pp. 2094-2103
    • Angelo, L.S.1    Wu, J.Y.2    Meng, F.3
  • 10
    • 84873306516 scopus 로고    scopus 로고
    • Binding partners for curcumin in human schwannoma cells: biologic implications
    • COI: 1:CAS:528:DC%2BC3sXkt1Whsw%3D%3D, PID: 23294827
    • Angelo LS, Maxwell DS, Wu JY et al (2013) Binding partners for curcumin in human schwannoma cells: biologic implications. Bioorg Med Chem 21:932–939
    • (2013) Bioorg Med Chem , vol.21 , pp. 932-939
    • Angelo, L.S.1    Maxwell, D.S.2    Wu, J.Y.3
  • 11
    • 79960691369 scopus 로고    scopus 로고
    • Biochemical and structural studies on the high affinity of Hsp70 for ADP
    • COI: 1:CAS:528:DC%2BC3MXptFahu7g%3D, PID: 21608060
    • Arakawa A, Handa N, Shirouzu M, Yokoyama S (2011) Biochemical and structural studies on the high affinity of Hsp70 for ADP. Protein Sci 20:1367–1379
    • (2011) Protein Sci , vol.20 , pp. 1367-1379
    • Arakawa, A.1    Handa, N.2    Shirouzu, M.3    Yokoyama, S.4
  • 12
    • 0034613163 scopus 로고    scopus 로고
    • ATP and ADP modulate a cation channel formed by Hsc70 in acidic phospholipid membranes
    • COI: 1:CAS:528:DC%2BD3cXntlCjtbc%3D, PID: 10899168
    • Arispe N, De Maio A (2000) ATP and ADP modulate a cation channel formed by Hsc70 in acidic phospholipid membranes. J Biol Chem 275:30839–30843
    • (2000) J Biol Chem , vol.275 , pp. 30839-30843
    • Arispe, N.1    De Maio, A.2
  • 13
    • 0033120990 scopus 로고    scopus 로고
    • Cutting edge: receptor-mediated endocytosis of heat shock proteins by professional antigen-presenting cells
    • COI: 1:CAS:528:DyaK1MXitFGqsL0%3D, PID: 10201889
    • Arnold-Schild D, Hanau D, Spehner D et al (1999) Cutting edge: receptor-mediated endocytosis of heat shock proteins by professional antigen-presenting cells. J Immunol 162:3757–3760
    • (1999) J Immunol , vol.162 , pp. 3757-3760
    • Arnold-Schild, D.1    Hanau, D.2    Spehner, D.3
  • 14
    • 0034113617 scopus 로고    scopus 로고
    • HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine
    • COI: 1:CAS:528:DC%2BD3cXisVOru7g%3D, PID: 10742151
    • Asea A, Kraeft SK, Kurt-Jones EA et al (2000) HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine. Nat Med 6:435–442
    • (2000) Nat Med , vol.6 , pp. 435-442
    • Asea, A.1    Kraeft, S.K.2    Kurt-Jones, E.A.3
  • 15
    • 0037177825 scopus 로고    scopus 로고
    • Novel signal transduction pathway utilized by extracellular HSP70: role of toll-like receptor (TLR) 2 and TLR4
    • COI: 1:CAS:528:DC%2BD38XjslSgt7s%3D, PID: 11836257
    • Asea A, Rehli M, Kabingu E et al (2002) Novel signal transduction pathway utilized by extracellular HSP70: role of toll-like receptor (TLR) 2 and TLR4. J Biol Chem 277:15028–15034
    • (2002) J Biol Chem , vol.277 , pp. 15028-15034
    • Asea, A.1    Rehli, M.2    Kabingu, E.3
  • 16
    • 0031820882 scopus 로고    scopus 로고
    • Expression of p53, bcl-2 and heat shock protein (hsp72) in malignant and benign ovarian tumours
    • COI: 1:STN:280:DyaK1czmt1amtQ%3D%3D, PID: 9696931
    • Athanassiadou P, Petrakakou E, Sakelariou V et al (1998) Expression of p53, bcl-2 and heat shock protein (hsp72) in malignant and benign ovarian tumours. Eur J Cancer Prev 7:225–231
    • (1998) Eur J Cancer Prev , vol.7 , pp. 225-231
    • Athanassiadou, P.1    Petrakakou, E.2    Sakelariou, V.3
  • 17
    • 84875414858 scopus 로고    scopus 로고
    • A modified HSP70 inhibitor shows broad activity as an anticancer agent
    • COI: 1:CAS:528:DC%2BC3sXktlersrw%3D, PID: 23303345
    • Balaburski GM, Leu JI, Beeharry N et al (2013) A modified HSP70 inhibitor shows broad activity as an anticancer agent. Mol Cancer Res 11:219–229
    • (2013) Mol Cancer Res , vol.11 , pp. 219-229
    • Balaburski, G.M.1    Leu, J.I.2    Beeharry, N.3
  • 18
    • 84907998986 scopus 로고    scopus 로고
    • Hsp70 is an independent stress marker among frequent users of mobile phones
    • PID: 25404380
    • Balakrishnan K, Murali V, Rathika C et al (2014) Hsp70 is an independent stress marker among frequent users of mobile phones. J Environ Pathol Toxicol Oncol 33:339–347
    • (2014) J Environ Pathol Toxicol Oncol , vol.33 , pp. 339-347
    • Balakrishnan, K.1    Murali, V.2    Rathika, C.3
  • 19
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • COI: 1:CAS:528:DyaK1MXjt1yisL8%3D, PID: 10330192
    • Ballinger CA, Connell P, Wu Y et al (1999) Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol Cell Biol 19:4535–4545
    • (1999) Mol Cell Biol , vol.19 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3
  • 20
    • 0033747044 scopus 로고    scopus 로고
    • Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-kappa B pathway
    • COI: 1:CAS:528:DC%2BD3cXosVWjtbY%3D, PID: 11058573
    • Basu S, Binder RJ, Suto R, Anderson KM, Srivastava PK (2000) Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-kappa B pathway. Int Immunol 12:1539–1546
    • (2000) Int Immunol , vol.12 , pp. 1539-1546
    • Basu, S.1    Binder, R.J.2    Suto, R.3    Anderson, K.M.4    Srivastava, P.K.5
  • 21
    • 11444263900 scopus 로고    scopus 로고
    • Surface expression of Hsp25 and Hsp72 differentially regulates tumor growth and metastasis
    • COI: 1:CAS:528:DC%2BD2MXlslOl, PID: 15627887
    • Bausero MA, Page DT, Osinaga E, Asea A (2004) Surface expression of Hsp25 and Hsp72 differentially regulates tumor growth and metastasis. Tumour Biol 25:243–251
    • (2004) Tumour Biol , vol.25 , pp. 243-251
    • Bausero, M.A.1    Page, D.T.2    Osinaga, E.3    Asea, A.4
  • 22
    • 23844544016 scopus 로고    scopus 로고
    • Alternative mechanism by which IFN-gamma enhances tumor recognition: active release of heat shock protein 72
    • COI: 1:CAS:528:DC%2BD2MXos1Gitro%3D, PID: 16116176
    • Bausero MA, Gastpar R, Multhoff G, Asea A (2005) Alternative mechanism by which IFN-gamma enhances tumor recognition: active release of heat shock protein 72. J Immunol 175:2900–2912
    • (2005) J Immunol , vol.175 , pp. 2900-2912
    • Bausero, M.A.1    Gastpar, R.2    Multhoff, G.3    Asea, A.4
  • 23
    • 84893862822 scopus 로고    scopus 로고
    • Validation of heat shock protein 70 as a tumor-specific biomarker for monitoring the outcome of radiation therapy in tumor mouse models
    • COI: 1:CAS:528:DC%2BC2cXisFejtL8%3D, PID: 24521683
    • Bayer C, Liebhardt ME, Schmid TE et al (2014) Validation of heat shock protein 70 as a tumor-specific biomarker for monitoring the outcome of radiation therapy in tumor mouse models. Int J Radiat Oncol Biol Phys 88:694–700
    • (2014) Int J Radiat Oncol Biol Phys , vol.88 , pp. 694-700
    • Bayer, C.1    Liebhardt, M.E.2    Schmid, T.E.3
  • 24
    • 0034253533 scopus 로고    scopus 로고
    • Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome
    • COI: 1:CAS:528:DC%2BD3cXlslymt74%3D, PID: 10934466
    • Beere HM, Wolf BB, Cain K et al (2000) Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome. Nat Cell Biol 2:469–475
    • (2000) Nat Cell Biol , vol.2 , pp. 469-475
    • Beere, H.M.1    Wolf, B.B.2    Cain, K.3
  • 25
    • 64649094781 scopus 로고    scopus 로고
    • Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate
    • COI: 1:CAS:528:DC%2BD1MXnt1Sru7o%3D, PID: 19439666
    • Bertelsen EB, Chang L, Gestwicki JE, Zuiderweg ER (2009) Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate. Proc Natl Acad Sci U S A 106:8471–8476
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 8471-8476
    • Bertelsen, E.B.1    Chang, L.2    Gestwicki, J.E.3    Zuiderweg, E.R.4
  • 26
    • 4744371115 scopus 로고    scopus 로고
    • The heat-shock protein receptors: some answers and more questions
    • COI: 1:CAS:528:DC%2BD2cXpsVGgtLg%3D, PID: 15361121
    • Binder RJ, Vatner R, Srivastava P (2004) The heat-shock protein receptors: some answers and more questions. Tissue Antigens 64:442–451
    • (2004) Tissue Antigens , vol.64 , pp. 442-451
    • Binder, R.J.1    Vatner, R.2    Srivastava, P.3
  • 27
    • 84896725293 scopus 로고    scopus 로고
    • Are Hsp70 protein expression and genetic polymorphism implicated in multiple sclerosis inflammation?
    • COI: 1:CAS:528:DC%2BC2cXhsFCqtbo%3D, PID: 24485944
    • Boiocchi C, Osera C, Monti MC et al (2014) Are Hsp70 protein expression and genetic polymorphism implicated in multiple sclerosis inflammation? J Neuroimmunol 268:84–88
    • (2014) J Neuroimmunol , vol.268 , pp. 84-88
    • Boiocchi, C.1    Osera, C.2    Monti, M.C.3
  • 29
    • 0028834648 scopus 로고
    • Members of the 70 kDa heat shock protein family specifically recognize sulfoglycolipids: role in gamete recognition and mycoplasma-related infertility
    • COI: 1:CAS:528:DyaK2MXosVGntbo%3D, PID: 7559808
    • Boulanger J, Faulds D, Eddy EM, Lingwood CA (1995) Members of the 70 kDa heat shock protein family specifically recognize sulfoglycolipids: role in gamete recognition and mycoplasma-related infertility. J Cell Physiol 165:7–17
    • (1995) J Cell Physiol , vol.165 , pp. 7-17
    • Boulanger, J.1    Faulds, D.2    Eddy, E.M.3    Lingwood, C.A.4
  • 30
    • 81555207195 scopus 로고    scopus 로고
    • Antimyeloma effects of the heat shock protein 70 molecular chaperone inhibitor MAL3-101
    • PID: 21977030
    • Braunstein MJ, Scott SS, Scott CM et al (2011) Antimyeloma effects of the heat shock protein 70 molecular chaperone inhibitor MAL3-101. J Oncol 2011:232037
    • (2011) J Oncol , vol.2011 , pp. 232037
    • Braunstein, M.J.1    Scott, S.S.2    Scott, C.M.3
  • 31
    • 84943355161 scopus 로고    scopus 로고
    • Quantitative analysis of liposomal heat shock protein 70 (Hsp70) in the blood of tumor patients using a novel lipHsp70 ELISA
    • Breuninger S, Erl J, Knape C et al (2014) Quantitative analysis of liposomal heat shock protein 70 (Hsp70) in the blood of tumor patients using a novel lipHsp70 ELISA. J Clin Cell Immunol 5:5
    • (2014) J Clin Cell Immunol , vol.5 , pp. 5
    • Breuninger, S.1    Erl, J.2    Knape, C.3
  • 32
    • 40749101072 scopus 로고    scopus 로고
    • hsp70 genes in the human genome: conservation and differentiation patterns predict a wide array of overlapping and specialized functions
    • PID: 18215318
    • Brocchieri L, de Conway ME, Macario AJ (2008) hsp70 genes in the human genome: conservation and differentiation patterns predict a wide array of overlapping and specialized functions. BMC Evol Biol 8:19
    • (2008) BMC Evol Biol , vol.8 , pp. 19
    • Brocchieri, L.1    de Conway, M.E.2    Macario, A.J.3
  • 33
    • 0033561687 scopus 로고    scopus 로고
    • Selectivity of the molecular chaperone-specific immunosuppressive agent 15-deoxyspergualin: modulation of Hsc70 ATPase activity without compromising DnaJ chaperone interactions
    • COI: 1:CAS:528:DyaK1MXhvFSktr8%3D, PID: 10086320
    • Brodsky JL (1999) Selectivity of the molecular chaperone-specific immunosuppressive agent 15-deoxyspergualin: modulation of Hsc70 ATPase activity without compromising DnaJ chaperone interactions. Biochem Pharmacol 57:877–880
    • (1999) Biochem Pharmacol , vol.57 , pp. 877-880
    • Brodsky, J.L.1
  • 34
    • 0037484291 scopus 로고    scopus 로고
    • Expression of the molecular chaperone Hsp70 in detergent-resistant microdomains correlates with its membrane delivery and release
    • COI: 1:CAS:528:DC%2BD3sXksVems7k%3D, PID: 12682040
    • Broquet AH, Thomas G, Masliah J, Trugnan G, Bachelet M (2003) Expression of the molecular chaperone Hsp70 in detergent-resistant microdomains correlates with its membrane delivery and release. J Biol Chem 278:21601–21606
    • (2003) J Biol Chem , vol.278 , pp. 21601-21606
    • Broquet, A.H.1    Thomas, G.2    Masliah, J.3    Trugnan, G.4    Bachelet, M.5
  • 35
    • 84857509287 scopus 로고    scopus 로고
    • Molecular chaperones in mammary cancer growth and breast tumor therapy
    • COI: 1:CAS:528:DC%2BC38Xislais7o%3D, PID: 22105880
    • Calderwood SK, Gong J (2012) Molecular chaperones in mammary cancer growth and breast tumor therapy. J Cell Biochem 113:1096–1103
    • (2012) J Cell Biochem , vol.113 , pp. 1096-1103
    • Calderwood, S.K.1    Gong, J.2
  • 36
    • 76649097628 scopus 로고    scopus 로고
    • Membrane-associated Hsp72 from tumor-derived exosomes mediates STAT3-dependent immunosuppressive function of mouse and human myeloid-derived suppressor cells
    • COI: 1:CAS:528:DC%2BC3cXhsVOktL4%3D, PID: 20093776
    • Chalmin F, Ladoire S, Mignot G et al (2010) Membrane-associated Hsp72 from tumor-derived exosomes mediates STAT3-dependent immunosuppressive function of mouse and human myeloid-derived suppressor cells. J Clin Invest 120:457–471
    • (2010) J Clin Invest , vol.120 , pp. 457-471
    • Chalmin, F.1    Ladoire, S.2    Mignot, G.3
  • 37
    • 79951837256 scopus 로고    scopus 로고
    • Chemical screens against a reconstituted multiprotein complex: myricetin blocks DnaJ regulation of DnaK through an allosteric mechanism
    • COI: 1:CAS:528:DC%2BC3MXit1Kjtrc%3D, PID: 21338918
    • Chang L, Miyata Y, Ung PM et al (2011) Chemical screens against a reconstituted multiprotein complex: myricetin blocks DnaJ regulation of DnaK through an allosteric mechanism. Chem Biol 18:210–221
    • (2011) Chem Biol , vol.18 , pp. 210-221
    • Chang, L.1    Miyata, Y.2    Ung, P.M.3
  • 38
    • 84876983496 scopus 로고    scopus 로고
    • Crohn’s disease and polymorphism of heat shock protein gene HSP70-2 in the Chinese population
    • COI: 1:CAS:528:DC%2BC3sXmslSmtL4%3D, PID: 23425104
    • Chen J, Ren J, Gu G et al (2013) Crohn’s disease and polymorphism of heat shock protein gene HSP70-2 in the Chinese population. J Gastroenterol Hepatol 28:814–818
    • (2013) J Gastroenterol Hepatol , vol.28 , pp. 814-818
    • Chen, J.1    Ren, J.2    Gu, G.3
  • 39
    • 84924588111 scopus 로고    scopus 로고
    • Broad and direct interaction between TLR and Siglec families of pattern recognition receptors and its regulation by Neu1
    • PID: 25187624
    • Chen GY, Brown NK, Wu W et al (2014) Broad and direct interaction between TLR and Siglec families of pattern recognition receptors and its regulation by Neu1. Elife 3:e04066
    • (2014) Elife , vol.3 , pp. e04066
    • Chen, G.Y.1    Brown, N.K.2    Wu, W.3
  • 40
    • 1542426626 scopus 로고    scopus 로고
    • Curcumin confers radiosensitizing effect in prostate cancer cell line PC-3
    • COI: 1:CAS:528:DC%2BD2cXhsFOht7g%3D, PID: 14985701
    • Chendil D, Ranga RS, Meigooni D, Sathishkumar S, Ahmed MM (2004) Curcumin confers radiosensitizing effect in prostate cancer cell line PC-3. Oncogene 23:1599–1607
    • (2004) Oncogene , vol.23 , pp. 1599-1607
    • Chendil, D.1    Ranga, R.S.2    Meigooni, D.3    Sathishkumar, S.4    Ahmed, M.M.5
  • 41
    • 84904902310 scopus 로고    scopus 로고
    • Downregulation of miRNA-134 protects neural cells against ischemic injury in N2A cells and mouse brain with ischemic stroke by targeting HSPA12B
    • COI: 1:CAS:528:DC%2BC2cXht1Oru7jP, PID: 25003713
    • Chi W, Meng F, Li Y et al (2014) Downregulation of miRNA-134 protects neural cells against ischemic injury in N2A cells and mouse brain with ischemic stroke by targeting HSPA12B. Neuroscience 277:111–122
    • (2014) Neuroscience , vol.277 , pp. 111-122
    • Chi, W.1    Meng, F.2    Li, Y.3
  • 42
    • 0031842063 scopus 로고    scopus 로고
    • MKT-077, localized lipophilic cation: antitumor activity against human tumor xenografts serially transplanted into nude mice
    • COI: 1:CAS:528:DyaK1cXjvFKgtbs%3D, PID: 9615763
    • Chiba Y, Kubota T, Watanabe M et al (1998) MKT-077, localized lipophilic cation: antitumor activity against human tumor xenografts serially transplanted into nude mice. Anticancer Res 18:1047–1052
    • (1998) Anticancer Res , vol.18 , pp. 1047-1052
    • Chiba, Y.1    Kubota, T.2    Watanabe, M.3
  • 43
    • 83755171532 scopus 로고    scopus 로고
    • A small molecule that binds to an ATPase domain of Hsc70 promotes membrane trafficking of mutant cystic fibrosis transmembrane conductance regulator
    • COI: 1:CAS:528:DC%2BC3MXhsVGgsb3P, PID: 22074182
    • Cho HJ, Gee HY, Baek KH et al (2011) A small molecule that binds to an ATPase domain of Hsc70 promotes membrane trafficking of mutant cystic fibrosis transmembrane conductance regulator. J Am Chem Soc 133:20267–20276
    • (2011) J Am Chem Soc , vol.133 , pp. 20267-20276
    • Cho, H.J.1    Gee, H.Y.2    Baek, K.H.3
  • 44
    • 84871750894 scopus 로고    scopus 로고
    • mTOR is essential for the proteotoxic stress response, HSF1 activation and heat shock protein synthesis
    • COI: 1:CAS:528:DC%2BC38XpvVCnsbg%3D, PID: 22768106
    • Chou SD, Prince T, Gong J, Calderwood SK (2012) mTOR is essential for the proteotoxic stress response, HSF1 activation and heat shock protein synthesis. PLoS ONE 7:e39679
    • (2012) PLoS ONE , vol.7 , pp. e39679
    • Chou, S.D.1    Prince, T.2    Gong, J.3    Calderwood, S.K.4
  • 45
    • 0037223571 scopus 로고    scopus 로고
    • Expression profiling in multistage hepatocarcinogenesis: identification of HSP70 as a molecular marker of early hepatocellular carcinoma
    • COI: 1:CAS:528:DC%2BD3sXovVWhuw%3D%3D, PID: 12500205
    • Chuma M, Sakamoto M, Yamazaki K et al (2003) Expression profiling in multistage hepatocarcinogenesis: identification of HSP70 as a molecular marker of early hepatocellular carcinoma. Hepatology 37:198–207
    • (2003) Hepatology , vol.37 , pp. 198-207
    • Chuma, M.1    Sakamoto, M.2    Yamazaki, K.3
  • 46
    • 21744445069 scopus 로고    scopus 로고
    • Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications
    • COI: 1:CAS:528:DC%2BD2MXmsFymur4%3D, PID: 16038406
    • Ciocca DR, Calderwood SK (2005) Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications. Cell Stress Chaperones 10:86–103
    • (2005) Cell Stress Chaperones , vol.10 , pp. 86-103
    • Ciocca, D.R.1    Calderwood, S.K.2
  • 47
    • 34250859071 scopus 로고    scopus 로고
    • A pilot study with a therapeutic vaccine based on hydroxyapatite ceramic particles and self-antigens in cancer patients
    • COI: 1:CAS:528:DC%2BD2sXkslyntbw%3D, PID: 17441505
    • Ciocca DR, Frayssinet P, Cuello-Carrion FD (2007) A pilot study with a therapeutic vaccine based on hydroxyapatite ceramic particles and self-antigens in cancer patients. Cell Stress Chaperones 12:33–43
    • (2007) Cell Stress Chaperones , vol.12 , pp. 33-43
    • Ciocca, D.R.1    Frayssinet, P.2    Cuello-Carrion, F.D.3
  • 49
    • 84872358363 scopus 로고    scopus 로고
    • Heat shock proteins and heat shock factor 1 in carcinogenesis and tumor development: an update
    • COI: 1:CAS:528:DC%2BC38XhtFOgsb3M, PID: 22885793
    • Ciocca DR, Arrigo AP, Calderwood SK (2013) Heat shock proteins and heat shock factor 1 in carcinogenesis and tumor development: an update. Arch Toxicol 87:19–48
    • (2013) Arch Toxicol , vol.87 , pp. 19-48
    • Ciocca, D.R.1    Arrigo, A.P.2    Calderwood, S.K.3
  • 50
    • 36549030784 scopus 로고    scopus 로고
    • The inhibitory cytokine IL-35 contributes to regulatory T-cell function
    • COI: 1:CAS:528:DC%2BD2sXhtlCrtbzI, PID: 18033300
    • Collison LW, Workman CJ, Kuo TT et al (2007) The inhibitory cytokine IL-35 contributes to regulatory T-cell function. Nature 450:566–569
    • (2007) Nature , vol.450 , pp. 566-569
    • Collison, L.W.1    Workman, C.J.2    Kuo, T.T.3
  • 51
    • 84907055560 scopus 로고    scopus 로고
    • Hsp70-Bag3 interactions regulate cancer-related signaling networks
    • COI: 1:CAS:528:DC%2BC2cXhsVOisbzN, PID: 24994713
    • Colvin TA, Gabai VL, Gong J et al (2014) Hsp70-Bag3 interactions regulate cancer-related signaling networks. Cancer Res 74:4731–4740
    • (2014) Cancer Res , vol.74 , pp. 4731-4740
    • Colvin, T.A.1    Gabai, V.L.2    Gong, J.3
  • 52
    • 84862281225 scopus 로고    scopus 로고
    • Methylthioninium chloride (methylene blue) induces autophagy and attenuates tauopathy in vitro and in vivo
    • COI: 1:CAS:528:DC%2BC38Xht1art73N, PID: 22361619
    • Congdon EE, Wu JW, Myeku N et al (2012) Methylthioninium chloride (methylene blue) induces autophagy and attenuates tauopathy in vitro and in vivo. Autophagy 8:609–622
    • (2012) Autophagy , vol.8 , pp. 609-622
    • Congdon, E.E.1    Wu, J.W.2    Myeku, N.3
  • 53
    • 0035146685 scopus 로고    scopus 로고
    • The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
    • COI: 1:CAS:528:DC%2BD3MXkslGqsQ%3D%3D, PID: 11146632
    • Connell P, Ballinger CA, Jiang J et al (2001) The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. Nat Cell Biol 3:93–96
    • (2001) Nat Cell Biol , vol.3 , pp. 93-96
    • Connell, P.1    Ballinger, C.A.2    Jiang, J.3
  • 54
    • 84874873682 scopus 로고
    • The stress response: changes in eukaryotic gene expression in response to environmental stress
    • COI: 1:STN:280:DC%2BC3cvjtlKrtA%3D%3D, PID: 17791792
    • Craig EA (1985) The stress response: changes in eukaryotic gene expression in response to environmental stress. Science 230:800–801
    • (1985) Science , vol.230 , pp. 800-801
    • Craig, E.A.1
  • 55
    • 33646847503 scopus 로고    scopus 로고
    • The diverse roles of J-proteins, the obligate Hsp70 co-chaperone
    • COI: 1:CAS:528:DC%2BD28XksFSnsL8%3D, PID: 16634144
    • Craig EA, Huang P, Aron R, Andrew A (2006) The diverse roles of J-proteins, the obligate Hsp70 co-chaperone. Rev Physiol Biochem Pharmacol 156:1–21
    • (2006) Rev Physiol Biochem Pharmacol , vol.156 , pp. 1-21
    • Craig, E.A.1    Huang, P.2    Aron, R.3    Andrew, A.4
  • 56
    • 25444461158 scopus 로고    scopus 로고
    • Hsp70-2 is required for tumor cell growth and survival
    • COI: 1:CAS:528:DC%2BD28XhslCrtbY%3D, PID: 15970673
    • Daugaard M, Jäättelä M, Rohde M (2005) Hsp70-2 is required for tumor cell growth and survival. Cell Cycle 4:877–880
    • (2005) Cell Cycle , vol.4 , pp. 877-880
    • Daugaard, M.1    Jäättelä, M.2    Rohde, M.3
  • 57
    • 34047274469 scopus 로고    scopus 로고
    • Lens epithelium-derived growth factor is an Hsp70-2 regulated guardian of lysosomal stability in human cancer
    • COI: 1:CAS:528:DC%2BD2sXivV2nsrw%3D, PID: 17363574
    • Daugaard M, Kirkegaard-Sorensen T, Ostenfeld MS et al (2007a) Lens epithelium-derived growth factor is an Hsp70-2 regulated guardian of lysosomal stability in human cancer. Cancer Res 67:2559–2567
    • (2007) Cancer Res , vol.67 , pp. 2559-2567
    • Daugaard, M.1    Kirkegaard-Sorensen, T.2    Ostenfeld, M.S.3
  • 58
    • 34447528828 scopus 로고    scopus 로고
    • The heat shock protein 70 family: highly homologous proteins with overlapping and distinct functions
    • COI: 1:CAS:528:DC%2BD2sXotlaisLk%3D, PID: 17544402
    • Daugaard M, Rohde M, Jäättelä M (2007b) The heat shock protein 70 family: highly homologous proteins with overlapping and distinct functions. FEBS Lett 581:3702–3710
    • (2007) FEBS Lett , vol.581 , pp. 3702-3710
    • Daugaard, M.1    Rohde, M.2    Jäättelä, M.3
  • 59
    • 0027942501 scopus 로고
    • Phase II study of deoxyspergualin in metastatic breast cancer
    • COI: 1:STN:280:DyaK2M3gsVWmsw%3D%3D, PID: 7896543
    • Dhingra K, Valero V, Gutierrez L et al (1994) Phase II study of deoxyspergualin in metastatic breast cancer. Invest New Drugs 12:235–241
    • (1994) Invest New Drugs , vol.12 , pp. 235-241
    • Dhingra, K.1    Valero, V.2    Gutierrez, L.3
  • 60
    • 84885567675 scopus 로고    scopus 로고
    • Increased expression of heat shock protein 70 in chronic obstructive pulmonary disease
    • COI: 1:CAS:528:DC%2BC3sXhslWhurzI, PID: 24095952
    • Dong J, Guo L, Liao Z et al (2013) Increased expression of heat shock protein 70 in chronic obstructive pulmonary disease. Int Immunopharmacol 17:885–893
    • (2013) Int Immunopharmacol , vol.17 , pp. 885-893
    • Dong, J.1    Guo, L.2    Liao, Z.3
  • 61
    • 78149468416 scopus 로고    scopus 로고
    • Extracellular heat shock protein 70 (HSPA1A) and classical vascular risk factors in a general population
    • COI: 1:CAS:528:DC%2BC3cXht12qtbbI, PID: 20490736
    • Dulin E, Garcia-Barreno P, Guisasola MC (2010) Extracellular heat shock protein 70 (HSPA1A) and classical vascular risk factors in a general population. Cell Stress Chaperones 15:929–937
    • (2010) Cell Stress Chaperones , vol.15 , pp. 929-937
    • Dulin, E.1    Garcia-Barreno, P.2    Guisasola, M.C.3
  • 62
    • 84859967986 scopus 로고    scopus 로고
    • Serum HSP70: a novel biomarker for early detection of pancreatic cancer
    • COI: 1:CAS:528:DC%2BC38Xls12htL0%3D, PID: 22158074
    • Dutta SK, Girotra M, Singla M et al (2012) Serum HSP70: a novel biomarker for early detection of pancreatic cancer. Pancreas 41:530–534
    • (2012) Pancreas , vol.41 , pp. 530-534
    • Dutta, S.K.1    Girotra, M.2    Singla, M.3
  • 63
    • 33744477339 scopus 로고    scopus 로고
    • Expression and prognostic significance of heat-shock proteins in myelodysplastic syndromes
    • COI: 1:CAS:528:DC%2BD28Xls1Srtb4%3D, PID: 16670079
    • Duval A, Olaru D, Campos L et al (2006) Expression and prognostic significance of heat-shock proteins in myelodysplastic syndromes. Haematologica 91:713–714
    • (2006) Haematologica , vol.91 , pp. 713-714
    • Duval, A.1    Olaru, D.2    Campos, L.3
  • 64
    • 0023649886 scopus 로고
    • Structure and expression of a human gene coding for a 71 kd heat shock ‘cognate’ protein
    • COI: 1:CAS:528:DyaL2sXmtlSgt7Y%3D, PID: 3037489
    • Dworniczak B, Mirault ME (1987) Structure and expression of a human gene coding for a 71 kd heat shock ‘cognate’ protein. Nucleic Acids Res 15:5181–5197
    • (1987) Nucleic Acids Res , vol.15 , pp. 5181-5197
    • Dworniczak, B.1    Mirault, M.E.2
  • 65
    • 33750359212 scopus 로고    scopus 로고
    • Enhanced immunogenicity of heat shock protein 70 peptide complexes from dendritic cell-tumor fusion cells
    • COI: 1:CAS:528:DC%2BD28XhtFSns7%2FE, PID: 17056519
    • Enomoto Y, Bharti A, Khaleque AA et al (2006) Enhanced immunogenicity of heat shock protein 70 peptide complexes from dendritic cell-tumor fusion cells. J Immunol 177:5946–5955
    • (2006) J Immunol , vol.177 , pp. 5946-5955
    • Enomoto, Y.1    Bharti, A.2    Khaleque, A.A.3
  • 66
    • 33646902375 scopus 로고    scopus 로고
    • The effect of aging on the chaperone concentrations in the hepatic, endoplasmic reticulum of male rats: the possible role of protein misfolding due to the loss of chaperones in the decline in physiological function seen with age
    • PID: 16720739
    • Erickson RR, Dunning LM, Holtzman JL (2006) The effect of aging on the chaperone concentrations in the hepatic, endoplasmic reticulum of male rats: the possible role of protein misfolding due to the loss of chaperones in the decline in physiological function seen with age. J Gerontol A Biol Sci Med Sci 61:435–443
    • (2006) J Gerontol A Biol Sci Med Sci , vol.61 , pp. 435-443
    • Erickson, R.R.1    Dunning, L.M.2    Holtzman, J.L.3
  • 67
    • 33749460895 scopus 로고    scopus 로고
    • (−)-Epigallocatechin gallate overcomes resistance to etoposide-induced cell death by targeting the molecular chaperone glucose-regulated protein 78
    • COI: 1:CAS:528:DC%2BD28Xps1ahsr0%3D, PID: 16982771
    • Ermakova SP, Kang BS, Choi BY et al (2006) (−)-Epigallocatechin gallate overcomes resistance to etoposide-induced cell death by targeting the molecular chaperone glucose-regulated protein 78. Cancer Res 66:9260–9269
    • (2006) Cancer Res , vol.66 , pp. 9260-9269
    • Ermakova, S.P.1    Kang, B.S.2    Choi, B.Y.3
  • 68
    • 77953734857 scopus 로고    scopus 로고
    • Heat shock protein 70 (hsp70) as an emerging drug target
    • COI: 1:CAS:528:DC%2BC3cXjvVejsLc%3D, PID: 20334364
    • Evans CG, Chang L, Gestwicki JE (2010) Heat shock protein 70 (hsp70) as an emerging drug target. J Med Chem 53:4585–4602
    • (2010) J Med Chem , vol.53 , pp. 4585-4602
    • Evans, C.G.1    Chang, L.2    Gestwicki, J.E.3
  • 69
    • 84948808419 scopus 로고    scopus 로고
    • Investigating apoptozole as a chemical probe for HSP70 inhibition
    • PID: 26458144
    • Evans LE, Cheeseman MD, Yahya N, Jones K (2015) Investigating apoptozole as a chemical probe for HSP70 inhibition. PLoS ONE 10:e0140006
    • (2015) PLoS ONE , vol.10 , pp. e0140006
    • Evans, L.E.1    Cheeseman, M.D.2    Yahya, N.3    Jones, K.4
  • 70
    • 2942551229 scopus 로고    scopus 로고
    • Phospholipase c inhibitor, u73122, stimulates release of hsp-70 stress protein from A431 human carcinoma cells
    • PID: 14989758
    • Evdonin AL, Guzhova IV, Margulis BA, Medvedeva ND (2004) Phospholipase c inhibitor, u73122, stimulates release of hsp-70 stress protein from A431 human carcinoma cells. Cancer Cell Int 4:2
    • (2004) Cancer Cell Int , vol.4 , pp. 2
    • Evdonin, A.L.1    Guzhova, I.V.2    Margulis, B.A.3    Medvedeva, N.D.4
  • 71
    • 33646549927 scopus 로고    scopus 로고
    • The release of Hsp70 from A431 carcinoma cells is mediated by secretory-like granules
    • COI: 1:CAS:528:DC%2BD28XmsVOju7o%3D, PID: 16584808
    • Evdonin AL, Martynova MG, Bystrova OA et al (2006) The release of Hsp70 from A431 carcinoma cells is mediated by secretory-like granules. Eur J Cell Biol 85:443–455
    • (2006) Eur J Cell Biol , vol.85 , pp. 443-455
    • Evdonin, A.L.1    Martynova, M.G.2    Bystrova, O.A.3
  • 72
    • 84943415897 scopus 로고    scopus 로고
    • Identification of miR-215 mediated targets/pathways via translational immunoprecipitation expression analysis (TrIP-chip)
    • PID: 26287603
    • Fesler A, Xu X, Zheng X et al (2015) Identification of miR-215 mediated targets/pathways via translational immunoprecipitation expression analysis (TrIP-chip). Oncotarget 6:24463–24473
    • (2015) Oncotarget , vol.6 , pp. 24463-24473
    • Fesler, A.1    Xu, X.2    Zheng, X.3
  • 73
    • 0035847010 scopus 로고    scopus 로고
    • Identification of an inhibitor of hsc70-mediated protein translocation and ATP hydrolysis
    • COI: 1:CAS:528:DC%2BD3MXmtVyntQ%3D%3D, PID: 11036084
    • Fewell SW, Day BW, Brodsky JL (2001) Identification of an inhibitor of hsc70-mediated protein translocation and ATP hydrolysis. J Biol Chem 276:910–914
    • (2001) J Biol Chem , vol.276 , pp. 910-914
    • Fewell, S.W.1    Day, B.W.2    Brodsky, J.L.3
  • 74
    • 84966515280 scopus 로고    scopus 로고
    • Multi-layered molecular mechanisms of polypeptide holding, unfolding and disaggregation by HSP70/HSP110 chaperones
    • PID: 26097841
    • Finka A, Sharma SK, Goloubinoff P (2015a) Multi-layered molecular mechanisms of polypeptide holding, unfolding and disaggregation by HSP70/HSP110 chaperones. Front Mol Biosci 2:29
    • (2015) Front Mol Biosci , vol.2 , pp. 29
    • Finka, A.1    Sharma, S.K.2    Goloubinoff, P.3
  • 75
    • 84930864339 scopus 로고    scopus 로고
    • Quantitative proteomics of heat-treated human cells show an across-the-board mild depletion of housekeeping proteins to massively accumulate few HSPs
    • COI: 1:CAS:528:DC%2BC2MXhtVOiu7nN, PID: 25847399
    • Finka A, Sood V, Quadroni M, Rios PL, Goloubinoff P (2015b) Quantitative proteomics of heat-treated human cells show an across-the-board mild depletion of housekeeping proteins to massively accumulate few HSPs. Cell Stress Chaperones 20:605–620
    • (2015) Cell Stress Chaperones , vol.20 , pp. 605-620
    • Finka, A.1    Sood, V.2    Quadroni, M.3    Rios, P.L.4    Goloubinoff, P.5
  • 76
    • 0025100372 scopus 로고
    • Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
    • COI: 1:CAS:528:DyaK3cXlsVOqtbc%3D, PID: 2143562
    • Flaherty KM, Luca-Flaherty C, McKay DB (1990) Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature 346:623–628
    • (1990) Nature , vol.346 , pp. 623-628
    • Flaherty, K.M.1    Luca-Flaherty, C.2    McKay, D.B.3
  • 77
    • 84949521619 scopus 로고    scopus 로고
    • Immunomodulatory activity of extracellular Hsp70 mediated via paired receptors Siglec-5 and Siglec-14
    • COI: 1:CAS:528:DC%2BC2MXhs1egsL%2FK, PID: 26459514
    • Fong JJ, Sreedhara K, Deng L et al (2015) Immunomodulatory activity of extracellular Hsp70 mediated via paired receptors Siglec-5 and Siglec-14. EMBO J 34:2775–2788
    • (2015) EMBO J , vol.34 , pp. 2775-2788
    • Fong, J.J.1    Sreedhara, K.2    Deng, L.3
  • 78
    • 84873701617 scopus 로고    scopus 로고
    • Hsp70/Hsp90 chaperone machinery is involved in the assembly of the purinosome
    • COI: 1:CAS:528:DC%2BC3sXjsVehsb4%3D, PID: 23359685
    • French JB, Zhao H, An S et al (2013) Hsp70/Hsp90 chaperone machinery is involved in the assembly of the purinosome. Proc Natl Acad Sci U S A 110:2528–2533
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 2528-2533
    • French, J.B.1    Zhao, H.2    An, S.3
  • 79
    • 84856920241 scopus 로고    scopus 로고
    • Defective nuclear localization of Hsp70 is associated with dyserythropoiesis and GATA-1 cleavage in myelodysplastic syndromes
    • COI: 1:CAS:528:DC%2BC38XjtVSrsL8%3D, PID: 22160620
    • Frisan E, Vandekerckhove J, De TA et al (2012) Defective nuclear localization of Hsp70 is associated with dyserythropoiesis and GATA-1 cleavage in myelodysplastic syndromes. Blood 119:1532–1542
    • (2012) Blood , vol.119 , pp. 1532-1542
    • Frisan, E.1    Vandekerckhove, J.2    De, T.A.3
  • 80
    • 0030746053 scopus 로고    scopus 로고
    • Hsp70 prevents activation of stress kinases. A novel pathway of cellular thermotolerance
    • COI: 1:CAS:528:DyaK2sXkslKms7c%3D, PID: 9218432
    • Gabai VL, Meriin AB, Mosser DD et al (1997) Hsp70 prevents activation of stress kinases. A novel pathway of cellular thermotolerance. J Biol Chem 272:18033–18037
    • (1997) J Biol Chem , vol.272 , pp. 18033-18037
    • Gabai, V.L.1    Meriin, A.B.2    Mosser, D.D.3
  • 81
    • 18844378888 scopus 로고    scopus 로고
    • Increased expression of the major heat shock protein Hsp72 in human prostate carcinoma cells is dispensable for their viability but confers resistance to a variety of anticancer agents
    • COI: 1:CAS:528:DC%2BD2MXjvVOlsLc%3D, PID: 15735699
    • Gabai VL, Budagova KR, Sherman MY (2005) Increased expression of the major heat shock protein Hsp72 in human prostate carcinoma cells is dispensable for their viability but confers resistance to a variety of anticancer agents. Oncogene 24:3328–3338
    • (2005) Oncogene , vol.24 , pp. 3328-3338
    • Gabai, V.L.1    Budagova, K.R.2    Sherman, M.Y.3
  • 82
    • 84925302405 scopus 로고    scopus 로고
    • HINT1 peptide/Hsp70 complex induces NK-cell-dependent immunoregulation in a model of autoimmune demyelination
    • COI: 1:CAS:528:DC%2BC2cXhsVygs7%2FP, PID: 25092109
    • Galazka G, Jurewicz A, Domowicz M et al (2014) HINT1 peptide/Hsp70 complex induces NK-cell-dependent immunoregulation in a model of autoimmune demyelination. Eur J Immunol 44:3026–3044
    • (2014) Eur J Immunol , vol.44 , pp. 3026-3044
    • Galazka, G.1    Jurewicz, A.2    Domowicz, M.3
  • 83
    • 77954583336 scopus 로고    scopus 로고
    • Heat shock protein 70 together with its co-chaperone CHIP inhibits TNF-alpha induced apoptosis by promoting proteasomal degradation of apoptosis signal-regulating kinase1
    • COI: 1:CAS:528:DC%2BC3cXotVOltbk%3D, PID: 20349136
    • Gao Y, Han C, Huang H et al (2010) Heat shock protein 70 together with its co-chaperone CHIP inhibits TNF-alpha induced apoptosis by promoting proteasomal degradation of apoptosis signal-regulating kinase1. Apoptosis 15:822–833
    • (2010) Apoptosis , vol.15 , pp. 822-833
    • Gao, Y.1    Han, C.2    Huang, H.3
  • 84
    • 84930872330 scopus 로고    scopus 로고
    • Increased circulating heat shock protein 70 (HSPA1A) levels in gestational diabetes mellitus: a pilot study
    • COI: 1:CAS:528:DC%2BC2MXjvVCmtbs%3D, PID: 25720752
    • Garamvolgyi Z, Prohaszka Z, Rigo J Jr, Kecskemeti A, Molvarec A (2015) Increased circulating heat shock protein 70 (HSPA1A) levels in gestational diabetes mellitus: a pilot study. Cell Stress Chaperones 20:575–581
    • (2015) Cell Stress Chaperones , vol.20 , pp. 575-581
    • Garamvolgyi, Z.1    Prohaszka, Z.2    Rigo, J.3    Kecskemeti, A.4    Molvarec, A.5
  • 85
    • 28844492580 scopus 로고    scopus 로고
    • Chemosensitization and radiosensitization of tumors by plant polyphenols
    • COI: 1:CAS:528:DC%2BD2MXhtlWht73M, PID: 16356126
    • Garg AK, Buchholz TA, Aggarwal BB (2005) Chemosensitization and radiosensitization of tumors by plant polyphenols. Antioxid Redox Signal 7:1630–1647
    • (2005) Antioxid Redox Signal , vol.7 , pp. 1630-1647
    • Garg, A.K.1    Buchholz, T.A.2    Aggarwal, B.B.3
  • 86
    • 20444431560 scopus 로고    scopus 로고
    • Heat shock protein 70 surface-positive tumor exosomes stimulate migratory and cytolytic activity of natural killer cells
    • COI: 1:CAS:528:DC%2BD2MXltFemu7w%3D, PID: 15958569
    • Gastpar R, Gehrmann M, Bausero MA et al (2005) Heat shock protein 70 surface-positive tumor exosomes stimulate migratory and cytolytic activity of natural killer cells. Cancer Res 65:5238–5247
    • (2005) Cancer Res , vol.65 , pp. 5238-5247
    • Gastpar, R.1    Gehrmann, M.2    Bausero, M.A.3
  • 87
    • 12244269328 scopus 로고    scopus 로고
    • Effects of antineoplastic agents on cytoplasmic and membrane-bound heat shock protein 70 (Hsp70) levels
    • COI: 1:CAS:528:DC%2BD3sXhtlSis7s%3D, PID: 12530536
    • Gehrmann M, Pfister K, Hutzler P et al (2002) Effects of antineoplastic agents on cytoplasmic and membrane-bound heat shock protein 70 (Hsp70) levels. Biol Chem 383:1715–1725
    • (2002) Biol Chem , vol.383 , pp. 1715-1725
    • Gehrmann, M.1    Pfister, K.2    Hutzler, P.3
  • 88
    • 11844259397 scopus 로고    scopus 로고
    • Dual function of membrane-bound heat shock protein 70 (Hsp70), Bag-4, and Hsp40: protection against radiation-induced effects and target structure for natural killer cells
    • COI: 1:CAS:528:DC%2BD2cXhtVGmtb3N, PID: 15592361
    • Gehrmann M, Marienhagen J, Eichholtz-Wirth H et al (2005) Dual function of membrane-bound heat shock protein 70 (Hsp70), Bag-4, and Hsp40: protection against radiation-induced effects and target structure for natural killer cells. Cell Death Differ 12:38–51
    • (2005) Cell Death Differ , vol.12 , pp. 38-51
    • Gehrmann, M.1    Marienhagen, J.2    Eichholtz-Wirth, H.3
  • 89
    • 44849133308 scopus 로고    scopus 로고
    • Tumor-specific Hsp70 plasma membrane localization is enabled by the glycosphingolipid Gb3
    • PID: 18382692
    • Gehrmann M, Liebisch G, Schmitz G et al (2008a) Tumor-specific Hsp70 plasma membrane localization is enabled by the glycosphingolipid Gb3. PLoS ONE 3:e1925
    • (2008) PLoS ONE , vol.3 , pp. e1925
    • Gehrmann, M.1    Liebisch, G.2    Schmitz, G.3
  • 90
    • 65949111072 scopus 로고    scopus 로고
    • The therapeutic implications of clinically applied modifiers of heat shock protein 70 (Hsp70) expression by tumor cells
    • COI: 1:CAS:528:DC%2BD1cXptVSrtL0%3D, PID: 18347936
    • Gehrmann M, Radons J, Molls M, Multhoff G (2008b) The therapeutic implications of clinically applied modifiers of heat shock protein 70 (Hsp70) expression by tumor cells. Cell Stress Chaperones 13:1–10
    • (2008) Cell Stress Chaperones , vol.13 , pp. 1-10
    • Gehrmann, M.1    Radons, J.2    Molls, M.3    Multhoff, G.4
  • 91
    • 84864075586 scopus 로고    scopus 로고
    • Immunotherapeutic targeting of membrane Hsp70-expressing tumors using recombinant human granzyme B
    • COI: 1:CAS:528:DC%2BC38XhtV2mtrnM, PID: 22829941
    • Gehrmann M, Stangl S, Kirschner A et al (2012) Immunotherapeutic targeting of membrane Hsp70-expressing tumors using recombinant human granzyme B. PLoS ONE 7:e41341
    • (2012) PLoS ONE , vol.7 , pp. e41341
    • Gehrmann, M.1    Stangl, S.2    Kirschner, A.3
  • 92
    • 84905645522 scopus 로고    scopus 로고
    • Heat shock protein 70 serum levels differ significantly in patients with chronic hepatitis, liver cirrhosis, and hepatocellular carcinoma
    • PID: 25071768
    • Gehrmann M, Cervello M, Montalto G et al (2014a) Heat shock protein 70 serum levels differ significantly in patients with chronic hepatitis, liver cirrhosis, and hepatocellular carcinoma. Front Immunol 5:307
    • (2014) Front Immunol , vol.5 , pp. 307
    • Gehrmann, M.1    Cervello, M.2    Montalto, G.3
  • 93
    • 84903551848 scopus 로고    scopus 로고
    • Hsp70—a biomarker for tumor detection and monitoring of outcome of radiation therapy in patients with squamous cell carcinoma of the head and neck
    • PID: 24912482
    • Gehrmann M, Specht HM, Bayer C et al (2014b) Hsp70—a biomarker for tumor detection and monitoring of outcome of radiation therapy in patients with squamous cell carcinoma of the head and neck. Radiat Oncol 9:131
    • (2014) Radiat Oncol , vol.9 , pp. 131
    • Gehrmann, M.1    Specht, H.M.2    Bayer, C.3
  • 94
    • 84941254975 scopus 로고    scopus 로고
    • Imaging of Hsp70-positive tumors with cmHsp70.1 antibody-conjugated gold nanoparticles
    • COI: 1:CAS:528:DC%2BC28XkvFSlsbg%3D, PID: 26392771
    • Gehrmann MK, Kimm MA, Stangl S et al (2015) Imaging of Hsp70-positive tumors with cmHsp70.1 antibody-conjugated gold nanoparticles. Int J Nanomedicine 10:5687–5700
    • (2015) Int J Nanomedicine , vol.10 , pp. 5687-5700
    • Gehrmann, M.K.1    Kimm, M.A.2    Stangl, S.3
  • 95
    • 24644474832 scopus 로고    scopus 로고
    • Proteomic identification of proteins conjugated to ISG15 in mouse and human cells
    • COI: 1:CAS:528:DC%2BD2MXhtVWns7bE, PID: 16139798
    • Giannakopoulos NV, Luo JK, Papov V et al (2005) Proteomic identification of proteins conjugated to ISG15 in mouse and human cells. Biochem Biophys Res Commun 336:496–506
    • (2005) Biochem Biophys Res Commun , vol.336 , pp. 496-506
    • Giannakopoulos, N.V.1    Luo, J.K.2    Papov, V.3
  • 96
    • 84865618692 scopus 로고    scopus 로고
    • Inhibition of HSP70: a challenging anti-cancer strategy
    • COI: 1:CAS:528:DC%2BC38XhtVOlsr7J, PID: 22750096
    • Goloudina AR, Demidov ON, Garrido C (2012) Inhibition of HSP70: a challenging anti-cancer strategy. Cancer Lett 325:117–124
    • (2012) Cancer Lett , vol.325 , pp. 117-124
    • Goloudina, A.R.1    Demidov, O.N.2    Garrido, C.3
  • 97
    • 73949095492 scopus 로고    scopus 로고
    • A heat shock protein 70-based vaccine with enhanced immunogenicity for clinical use
    • COI: 1:CAS:528:DC%2BD1MXhsFOnsLfO, PID: 19949080
    • Gong J, Zhang Y, Durfee J et al (2010) A heat shock protein 70-based vaccine with enhanced immunogenicity for clinical use. J Immunol 184:488–496
    • (2010) J Immunol , vol.184 , pp. 488-496
    • Gong, J.1    Zhang, Y.2    Durfee, J.3
  • 98
    • 84941096182 scopus 로고    scopus 로고
    • Geranylgeranylacetone selectively binds to the HSP70 of Helicobacter pylori and alters its coccoid morphology
    • PID: 26345206
    • Grave E, Yokota S, Yamamoto S et al (2015) Geranylgeranylacetone selectively binds to the HSP70 of Helicobacter pylori and alters its coccoid morphology. Sci Rep 5:13738
    • (2015) Sci Rep , vol.5 , pp. 13738
    • Grave, E.1    Yokota, S.2    Yamamoto, S.3
  • 99
    • 0032568541 scopus 로고    scopus 로고
    • Role of the J-domain in the cooperation of Hsp40 with Hsp70
    • COI: 1:CAS:528:DyaK1cXjtlKgsLc%3D, PID: 9600925
    • Greene MK, Maskos K, Landry SJ (1998) Role of the J-domain in the cooperation of Hsp40 with Hsp70. Proc Natl Acad Sci U S A 95:6108–6113
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 6108-6113
    • Greene, M.K.1    Maskos, K.2    Landry, S.J.3
  • 100
    • 0142103373 scopus 로고    scopus 로고
    • Cell surface-bound heat shock protein 70 (Hsp70) mediates perforin-independent apoptosis by specific binding and uptake of granzyme B
    • COI: 1:CAS:528:DC%2BD3sXotFWgtbo%3D, PID: 12874291
    • Gross C, Koelch W, DeMaio A, Arispe N, Multhoff G (2003) Cell surface-bound heat shock protein 70 (Hsp70) mediates perforin-independent apoptosis by specific binding and uptake of granzyme B. J Biol Chem 278:41173–41181
    • (2003) J Biol Chem , vol.278 , pp. 41173-41181
    • Gross, C.1    Koelch, W.2    DeMaio, A.3    Arispe, N.4    Multhoff, G.5
  • 101
    • 84949554848 scopus 로고    scopus 로고
    • Correlation of Hsp70 serum levels with gross tumor volume and composition of lymphocyte subpopulations in patients with squamous cell and adeno non-small cell lung cancer
    • PID: 26579130
    • Gunther S, Ostheimer C, Stangl S et al (2015) Correlation of Hsp70 serum levels with gross tumor volume and composition of lymphocyte subpopulations in patients with squamous cell and adeno non-small cell lung cancer. Front Immunol 6:556
    • (2015) Front Immunol , vol.6 , pp. 556
    • Gunther, S.1    Ostheimer, C.2    Stangl, S.3
  • 102
    • 28544433004 scopus 로고    scopus 로고
    • Abrogation of heat shock protein 70 induction as a strategy to increase antileukemia activity of heat shock protein 90 inhibitor 17-allylamino-demethoxy geldanamycin
    • COI: 1:CAS:528:DC%2BD2MXht1Wgu7zO, PID: 16288046
    • Guo F, Rocha K, Bali P et al (2005a) Abrogation of heat shock protein 70 induction as a strategy to increase antileukemia activity of heat shock protein 90 inhibitor 17-allylamino-demethoxy geldanamycin. Cancer Res 65:10536–10544
    • (2005) Cancer Res , vol.65 , pp. 10536-10544
    • Guo, F.1    Rocha, K.2    Bali, P.3
  • 103
    • 19944433616 scopus 로고    scopus 로고
    • Mechanistic role of heat shock protein 70 in Bcr-Abl-mediated resistance to apoptosis in human acute leukemia cells
    • COI: 1:CAS:528:DC%2BD2MXhtFCgtL0%3D, PID: 15388581
    • Guo F, Sigua C, Bali P et al (2005b) Mechanistic role of heat shock protein 70 in Bcr-Abl-mediated resistance to apoptosis in human acute leukemia cells. Blood 105:1246–1255
    • (2005) Blood , vol.105 , pp. 1246-1255
    • Guo, F.1    Sigua, C.2    Bali, P.3
  • 104
    • 84898462646 scopus 로고    scopus 로고
    • Targeting GRP75 improves HSP90 inhibitor efficacy by enhancing p53-mediated apoptosis in hepatocellular carcinoma
    • PID: 24465691
    • Guo W, Yan L, Yang L et al (2014) Targeting GRP75 improves HSP90 inhibitor efficacy by enhancing p53-mediated apoptosis in hepatocellular carcinoma. PLoS ONE 9:e85766
    • (2014) PLoS ONE , vol.9 , pp. e85766
    • Guo, W.1    Yan, L.2    Yang, L.3
  • 105
    • 0242606282 scopus 로고    scopus 로고
    • Heat shock protein 70 binding inhibits the nuclear import of apoptosis-inducing factor
    • COI: 1:CAS:528:DC%2BD3sXotVWnsbk%3D, PID: 14555980
    • Gurbuxani S, Schmitt E, Cande C et al (2003) Heat shock protein 70 binding inhibits the nuclear import of apoptosis-inducing factor. Oncogene 22:6669–6678
    • (2003) Oncogene , vol.22 , pp. 6669-6678
    • Gurbuxani, S.1    Schmitt, E.2    Cande, C.3
  • 106
    • 0030747256 scopus 로고    scopus 로고
    • Major stress protein Hsp70 interacts with NF-kB regulatory complex in human T-lymphoma cells
    • COI: 1:CAS:528:DyaK2sXks1Kksb0%3D, PID: 9250404
    • Guzhova IV, Darieva ZA, Melo AR, Margulis BA (1997) Major stress protein Hsp70 interacts with NF-kB regulatory complex in human T-lymphoma cells. Cell Stress Chaperones 2:132–139
    • (1997) Cell Stress Chaperones , vol.2 , pp. 132-139
    • Guzhova, I.V.1    Darieva, Z.A.2    Melo, A.R.3    Margulis, B.A.4
  • 107
    • 0037418010 scopus 로고    scopus 로고
    • Two Hsp70 family members expressed in atherosclerotic lesions
    • COI: 1:CAS:528:DC%2BD3sXhtF2gtbk%3D, PID: 12552099
    • Han Z, Truong QA, Park S, Breslow JL (2003) Two Hsp70 family members expressed in atherosclerotic lesions. Proc Natl Acad Sci U S A 100:1256–1261
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 1256-1261
    • Han, Z.1    Truong, Q.A.2    Park, S.3    Breslow, J.L.4
  • 108
    • 0034522797 scopus 로고    scopus 로고
    • Hsp70 plasma membrane expression on primary tumor biopsy material and bone marrow of leukemic patients
    • COI: 1:CAS:528:DC%2BD3MXkslyguw%3D%3D, PID: 11189449
    • Hantschel M, Pfister K, Jordan A et al (2000) Hsp70 plasma membrane expression on primary tumor biopsy material and bone marrow of leukemic patients. Cell Stress Chaperones 5:438–442
    • (2000) Cell Stress Chaperones , vol.5 , pp. 438-442
    • Hantschel, M.1    Pfister, K.2    Jordan, A.3
  • 109
    • 84860835752 scopus 로고    scopus 로고
    • (−)-Epigallocatechin-3-gallate, a green tea-derived catechin, synergizes with celecoxib to inhibit IL-1-induced tumorigenic mediators by human pancreatic adenocarcinoma cells Colo357
    • PID: 22497997
    • Härdtner C, Multhoff G, Falk W, Radons J (2012) (−)-Epigallocatechin-3-gallate, a green tea-derived catechin, synergizes with celecoxib to inhibit IL-1-induced tumorigenic mediators by human pancreatic adenocarcinoma cells Colo357. Eur J Pharmacol 684:36–43
    • (2012) Eur J Pharmacol , vol.684 , pp. 36-43
    • Härdtner, C.1    Multhoff, G.2    Falk, W.3    Radons, J.4
  • 110
    • 0023179598 scopus 로고
    • Chromosomal location of human genes encoding major heat-shock protein HSP70
    • COI: 1:CAS:528:DyaL2sXhvFShsLY%3D, PID: 3470951
    • Harrison GS, Drabkin HA, Kao FT et al (1987) Chromosomal location of human genes encoding major heat-shock protein HSP70. Somat Cell Mol Genet 13:119–130
    • (1987) Somat Cell Mol Genet , vol.13 , pp. 119-130
    • Harrison, G.S.1    Drabkin, H.A.2    Kao, F.T.3
  • 111
    • 0030936995 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
    • COI: 1:CAS:528:DyaK2sXis1Kns78%3D, PID: 9103205
    • Harrison CJ, Hayer-Hartl M, Di LM, Hartl F, Kuriyan J (1997) Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 276:431–435
    • (1997) Science , vol.276 , pp. 431-435
    • Harrison, C.J.1    Hayer-Hartl, M.2    Di, L.M.3    Hartl, F.4    Kuriyan, J.5
  • 112
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • COI: 1:CAS:528:DyaK28XjsFyltb8%3D, PID: 8637592
    • Hartl FU (1996) Molecular chaperones in cellular protein folding. Nature 381:571–579
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 113
    • 77958449033 scopus 로고    scopus 로고
    • Heat shock factor 1 ameliorates proteotoxicity in cooperation with the transcription factor NFAT
    • COI: 1:CAS:528:DC%2BC3cXhtFegsbvK, PID: 20834230
    • Hayashida N, Fujimoto M, Tan K et al (2010) Heat shock factor 1 ameliorates proteotoxicity in cooperation with the transcription factor NFAT. EMBO J 29:3459–3469
    • (2010) EMBO J , vol.29 , pp. 3459-3469
    • Hayashida, N.1    Fujimoto, M.2    Tan, K.3
  • 114
    • 84925436120 scopus 로고    scopus 로고
    • Heat shock protein 70 gene polymorphisms and cancer risk: a meta-analysis
    • PID: 25143984
    • He L, Deng T, Luo HS (2014) Heat shock protein 70 gene polymorphisms and cancer risk: a meta-analysis. ScientificWorldJournal 2014:540309
    • (2014) ScientificWorldJournal , vol.2014 , pp. 540309
    • He, L.1    Deng, T.2    Luo, H.S.3
  • 115
    • 70449732252 scopus 로고    scopus 로고
    • Dendritic cell subsets in primary and secondary T cell responses at body surfaces
    • COI: 1:CAS:528:DC%2BD1MXhsVWlsLfJ, PID: 19915624
    • Heath WR, Carbone FR (2009) Dendritic cell subsets in primary and secondary T cell responses at body surfaces. Nat Immunol 10:1237–1244
    • (2009) Nat Immunol , vol.10 , pp. 1237-1244
    • Heath, W.R.1    Carbone, F.R.2
  • 116
    • 79953708224 scopus 로고    scopus 로고
    • HSP70 expression: does it a novel fatigue signalling factor from immune system to the brain?
    • COI: 1:CAS:528:DC%2BC3MXktl2jt7s%3D, PID: 21374645
    • Heck TG, Scholer CM, de Bittencourt PI (2011) HSP70 expression: does it a novel fatigue signalling factor from immune system to the brain? Cell Biochem Funct 29:215–226
    • (2011) Cell Biochem Funct , vol.29 , pp. 215-226
    • Heck, T.G.1    Scholer, C.M.2    de Bittencourt, P.I.3
  • 117
    • 77957153127 scopus 로고    scopus 로고
    • Molecular chaperones and protein-folding catalysts as intercellular signaling regulators in immunity and inflammation
    • COI: 1:CAS:528:DC%2BC3cXhtFertrnL, PID: 20445014
    • Henderson B, Pockley AG (2010) Molecular chaperones and protein-folding catalysts as intercellular signaling regulators in immunity and inflammation. J Leukoc Biol 88:445–462
    • (2010) J Leukoc Biol , vol.88 , pp. 445-462
    • Henderson, B.1    Pockley, A.G.2
  • 118
    • 77950349873 scopus 로고    scopus 로고
    • Caught with their PAMPs down? The extracellular signalling actions of molecular chaperones are not due to microbial contaminants
    • COI: 1:CAS:528:DC%2BC3cXhsVyhurs%3D, PID: 19731087
    • Henderson B, Calderwood SK, Coates AR et al (2010) Caught with their PAMPs down? The extracellular signalling actions of molecular chaperones are not due to microbial contaminants. Cell Stress Chaperones 15:123–141
    • (2010) Cell Stress Chaperones , vol.15 , pp. 123-141
    • Henderson, B.1    Calderwood, S.K.2    Coates, A.R.3
  • 119
    • 0037064023 scopus 로고    scopus 로고
    • The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex
    • COI: 1:CAS:528:DC%2BD38Xns1Cns7w%3D, PID: 12161444
    • Hernandez MP, Sullivan WP, Toft DO (2002) The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex. J Biol Chem 277:38294–38304
    • (2002) J Biol Chem , vol.277 , pp. 38294-38304
    • Hernandez, M.P.1    Sullivan, W.P.2    Toft, D.O.3
  • 120
    • 0024541931 scopus 로고
    • Selective release from cultured mammalian cells of heat-shock (stress) proteins that resemble glia-axon transfer proteins
    • COI: 1:CAS:528:DyaL1MXhtlaltbg%3D, PID: 2918030
    • Hightower LE, Guidon PT Jr (1989) Selective release from cultured mammalian cells of heat-shock (stress) proteins that resemble glia-axon transfer proteins. J Cell Physiol 138:257–266
    • (1989) J Cell Physiol , vol.138 , pp. 257-266
    • Hightower, L.E.1    Guidon, P.T.2
  • 121
    • 0030038266 scopus 로고    scopus 로고
    • Geranylgeranylacetone induces heat shock proteins in cultured guinea pig gastric mucosal cells and rat gastric mucosa
    • COI: 1:CAS:528:DyaK28XkvFOnsLg%3D, PID: 8690199
    • Hirakawa T, Rokutan K, Nikawa T, Kishi K (1996) Geranylgeranylacetone induces heat shock proteins in cultured guinea pig gastric mucosal cells and rat gastric mucosa. Gastroenterology 111:345–357
    • (1996) Gastroenterology , vol.111 , pp. 345-357
    • Hirakawa, T.1    Rokutan, K.2    Nikawa, T.3    Kishi, K.4
  • 122
    • 80053942696 scopus 로고    scopus 로고
    • EGCG downregulates IL-1RI expression and suppresses IL-1-induced tumorigenic factors in human pancreatic adenocarcinoma cells
    • COI: 1:CAS:528:DC%2BC3MXht12qsL7K, PID: 21787753
    • Hoffmann J, Junker H, Schmieder A et al (2011) EGCG downregulates IL-1RI expression and suppresses IL-1-induced tumorigenic factors in human pancreatic adenocarcinoma cells. Biochem Pharmacol 82:1153–1162
    • (2011) Biochem Pharmacol , vol.82 , pp. 1153-1162
    • Hoffmann, J.1    Junker, H.2    Schmieder, A.3
  • 123
    • 0028842615 scopus 로고
    • Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
    • PID: 7585962
    • Höhfeld J, Minami Y, Hartl FU (1995) Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell 83:589–598
    • (1995) Cell , vol.83 , pp. 589-598
    • Höhfeld, J.1    Minami, Y.2    Hartl, F.U.3
  • 124
    • 0038143287 scopus 로고    scopus 로고
    • Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons
    • COI: 1:CAS:528:DC%2BD3sXjvVSktrk%3D, PID: 12598533
    • Holtz WA, O’Malley KL (2003) Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons. J Biol Chem 278:19367–19377
    • (2003) J Biol Chem , vol.278 , pp. 19367-19377
    • Holtz, W.A.1    O’Malley, K.L.2
  • 125
    • 84858984020 scopus 로고    scopus 로고
    • Eleven days of moderate exercise and heat exposure induces acclimation without significant HSP70 and apoptosis responses of lymphocytes in college-aged males
    • COI: 1:CAS:528:DC%2BC3MXhsFOgt7jI, PID: 21796498
    • Hom LL, Lee EC, Apicella JM et al (2012) Eleven days of moderate exercise and heat exposure induces acclimation without significant HSP70 and apoptosis responses of lymphocytes in college-aged males. Cell Stress Chaperones 17:29–39
    • (2012) Cell Stress Chaperones , vol.17 , pp. 29-39
    • Hom, L.L.1    Lee, E.C.2    Apicella, J.M.3
  • 126
    • 84863582759 scopus 로고    scopus 로고
    • Combined administration of EGCG and IL-1 receptor antagonist efficiently downregulates IL-1-induced tumorigenic factors in U-2 OS human osteosarcoma cells
    • PID: 22641358
    • Hönicke AS, Ender SA, Radons J (2012) Combined administration of EGCG and IL-1 receptor antagonist efficiently downregulates IL-1-induced tumorigenic factors in U-2 OS human osteosarcoma cells. Int J Oncol 41:753–758
    • (2012) Int J Oncol , vol.41 , pp. 753-758
    • Hönicke, A.S.1    Ender, S.A.2    Radons, J.3
  • 127
    • 84860219621 scopus 로고    scopus 로고
    • Activation of the unfolded protein response is an early event in Alzheimer’s and Parkinson’s disease
    • COI: 1:CAS:528:DC%2BC38XlvVOmur4%3D, PID: 22302012
    • Hoozemans JJ, van Haastert ES, Nijholt DA, Rozemuller AJ, Scheper W (2012) Activation of the unfolded protein response is an early event in Alzheimer’s and Parkinson’s disease. Neurodegener Dis 10:212–215
    • (2012) Neurodegener Dis , vol.10 , pp. 212-215
    • Hoozemans, J.J.1    van Haastert, E.S.2    Nijholt, D.A.3    Rozemuller, A.J.4    Scheper, W.5
  • 128
    • 38949189367 scopus 로고    scopus 로고
    • Exercise-recruited NK cells display exercise-associated eHSP-70
    • PID: 18198664
    • Horn P, Kalz A, Lim CL et al (2007) Exercise-recruited NK cells display exercise-associated eHSP-70. Exerc Immunol Rev 13:100–111
    • (2007) Exerc Immunol Rev , vol.13 , pp. 100-111
    • Horn, P.1    Kalz, A.2    Lim, C.L.3
  • 129
    • 46149125267 scopus 로고    scopus 로고
    • Membrane-associated stress proteins: more than simply chaperones
    • COI: 1:CAS:528:DC%2BD1cXnsFCrsbY%3D, PID: 18371297
    • Horvath I, Multhoff G, Sonnleitner A, Vigh L (2008) Membrane-associated stress proteins: more than simply chaperones. Biochim Biophys Acta 1778:1653–1664
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 1653-1664
    • Horvath, I.1    Multhoff, G.2    Sonnleitner, A.3    Vigh, L.4
  • 130
    • 33750448249 scopus 로고    scopus 로고
    • A novel endothelial-specific heat shock protein HspA12B is required in both zebrafish development and endothelial functions in vitro
    • COI: 1:CAS:528:DC%2BD2sXit1Cmsw%3D%3D, PID: 16968741
    • Hu G, Tang J, Zhang B et al (2006) A novel endothelial-specific heat shock protein HspA12B is required in both zebrafish development and endothelial functions in vitro. J Cell Sci 119:4117–4126
    • (2006) J Cell Sci , vol.119 , pp. 4117-4126
    • Hu, G.1    Tang, J.2    Zhang, B.3
  • 131
    • 0038389383 scopus 로고    scopus 로고
    • Differential, stage-dependent expression of Hsp70, Hsp110 and Bcl-2 in colorectal cancer
    • PID: 12753152
    • Hwang TS, Han HS, Choi HK et al (2003) Differential, stage-dependent expression of Hsp70, Hsp110 and Bcl-2 in colorectal cancer. J Gastroenterol Hepatol 18:690–700
    • (2003) J Gastroenterol Hepatol , vol.18 , pp. 690-700
    • Hwang, T.S.1    Han, H.S.2    Choi, H.K.3
  • 132
    • 84884772594 scopus 로고    scopus 로고
    • Identification and characterization of a novel human methyltransferase modulating Hsp70 protein function through lysine methylation
    • COI: 1:CAS:528:DC%2BC3sXhsFenur7M, PID: 23921388
    • Jakobsson ME, Moen A, Bousset L et al (2013) Identification and characterization of a novel human methyltransferase modulating Hsp70 protein function through lysine methylation. J Biol Chem 288:27752–27763
    • (2013) J Biol Chem , vol.288 , pp. 27752-27763
    • Jakobsson, M.E.1    Moen, A.2    Bousset, L.3
  • 133
    • 84930084889 scopus 로고    scopus 로고
    • Curcumin inhibits cancer stem cell phenotypes in ex vivo models of colorectal liver metastases, and is clinically safe and tolerable in combination with FOLFOX chemotherapy
    • COI: 1:CAS:528:DC%2BC2MXos1emtr0%3D, PID: 25979230
    • James MI, Iwuji C, Irving G et al (2015) Curcumin inhibits cancer stem cell phenotypes in ex vivo models of colorectal liver metastases, and is clinically safe and tolerable in combination with FOLFOX chemotherapy. Cancer Lett 364:135–141
    • (2015) Cancer Lett , vol.364 , pp. 135-141
    • James, M.I.1    Iwuji, C.2    Irving, G.3
  • 134
    • 79953029117 scopus 로고    scopus 로고
    • The C-terminus of Hsp70-interacting protein promotes Met receptor degradation
    • PID: 21325980
    • Jang KW, Lee JE, Kim SY et al (2011) The C-terminus of Hsp70-interacting protein promotes Met receptor degradation. J Thorac Oncol 6:679–687
    • (2011) J Thorac Oncol , vol.6 , pp. 679-687
    • Jang, K.W.1    Lee, J.E.2    Kim, S.Y.3
  • 135
    • 84885475457 scopus 로고    scopus 로고
    • Elevated extracellular HSP70 (HSPA1A) level as an independent prognostic marker of mortality in patients with heart failure
    • COI: 1:CAS:528:DC%2BC3sXhsF2gsLvJ, PID: 23564583
    • Jenei ZM, Gombos T, Forhecz Z et al (2013) Elevated extracellular HSP70 (HSPA1A) level as an independent prognostic marker of mortality in patients with heart failure. Cell Stress Chaperones 18:809–813
    • (2013) Cell Stress Chaperones , vol.18 , pp. 809-813
    • Jenei, Z.M.1    Gombos, T.2    Forhecz, Z.3
  • 136
    • 84899002037 scopus 로고    scopus 로고
    • Expressions of miR-15a and its target gene HSPA1B in the spermatozoa of patients with varicocele
    • COI: 1:CAS:528:DC%2BC2cXovFGnuro%3D, PID: 24481955
    • Ji Z, Lu R, Mou L et al (2014) Expressions of miR-15a and its target gene HSPA1B in the spermatozoa of patients with varicocele. Reproduction 147:693–701
    • (2014) Reproduction , vol.147 , pp. 693-701
    • Ji, Z.1    Lu, R.2    Mou, L.3
  • 137
    • 59349105146 scopus 로고    scopus 로고
    • The role of polyomaviruses in human disease
    • COI: 1:CAS:528:DC%2BD1MXhs1ejt7c%3D, PID: 18995875
    • Jiang M, Abend JR, Johnson SF, Imperiale MJ (2009) The role of polyomaviruses in human disease. Virology 384:266–273
    • (2009) Virology , vol.384 , pp. 266-273
    • Jiang, M.1    Abend, J.R.2    Johnson, S.F.3    Imperiale, M.J.4
  • 138
    • 70349617699 scopus 로고    scopus 로고
    • Chemical manipulation of hsp70 ATPase activity regulates tau stability
    • COI: 1:CAS:528:DC%2BD1MXht12qu7zN, PID: 19793966
    • Jinwal UK, Miyata Y, Koren J III et al (2009) Chemical manipulation of hsp70 ATPase activity regulates tau stability. J Neurosci 29:12079–12088
    • (2009) J Neurosci , vol.29 , pp. 12079-12088
    • Jinwal, U.K.1    Miyata, Y.2    Koren, J.3
  • 139
    • 84864029423 scopus 로고    scopus 로고
    • Antileukemic activity of the HSP70 inhibitor pifithrin-mu in acute leukemia
    • COI: 1:STN:280:DC%2BC38fislKksA%3D%3D, PID: 22829184
    • Kaiser M, Kuhnl A, Reins J et al (2011) Antileukemic activity of the HSP70 inhibitor pifithrin-mu in acute leukemia. Blood Cancer J 1, e28
    • (2011) Blood Cancer J , vol.1
    • Kaiser, M.1    Kuhnl, A.2    Reins, J.3
  • 140
    • 77954947810 scopus 로고    scopus 로고
    • The HSP70 chaperone machinery: J proteins as drivers of functional specificity
    • COI: 1:CAS:528:DC%2BC3cXpt1arsLo%3D, PID: 20651708
    • Kampinga HH, Craig EA (2010) The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat Rev Mol Cell Biol 11:579–592
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 141
    • 0031763046 scopus 로고    scopus 로고
    • Expression of 70-kDa heat shock protein in oral lesions: marker of biological stress or pathogenicity
    • COI: 1:CAS:528:DyaK1MXitVSktA%3D%3D, PID: 9930361
    • Kaur J, Srivastava A, Ralhan R (1998) Expression of 70-kDa heat shock protein in oral lesions: marker of biological stress or pathogenicity. Oral Oncol 34:496–501
    • (1998) Oral Oncol , vol.34 , pp. 496-501
    • Kaur, J.1    Srivastava, A.2    Ralhan, R.3
  • 142
    • 0033560745 scopus 로고    scopus 로고
    • Prognostic significance of heat shock proteins 27 and 70 in patients with squamous cell carcinoma of the esophagus
    • COI: 1:STN:280:DyaK1M3jvVSltQ%3D%3D, PID: 10223556
    • Kawanishi K, Shiozaki H, Doki Y et al (1999) Prognostic significance of heat shock proteins 27 and 70 in patients with squamous cell carcinoma of the esophagus. Cancer 85:1649–1657
    • (1999) Cancer , vol.85 , pp. 1649-1657
    • Kawanishi, K.1    Shiozaki, H.2    Doki, Y.3
  • 143
    • 26944442444 scopus 로고    scopus 로고
    • Induction of heat shock proteins by heregulin beta1 leads to protection from apoptosis and anchorage-independent growth
    • COI: 1:CAS:528:DC%2BD2MXhtVCnt7jP, PID: 16007186
    • Khaleque MA, Bharti A, Sawyer D et al (2005) Induction of heat shock proteins by heregulin beta1 leads to protection from apoptosis and anchorage-independent growth. Oncogene 24:6564–6573
    • (2005) Oncogene , vol.24 , pp. 6564-6573
    • Khaleque, M.A.1    Bharti, A.2    Sawyer, D.3
  • 144
    • 0026580335 scopus 로고
    • A member of the C/EBP family, NF-IL6 beta, forms a heterodimer and transcriptionally synergizes with NF-IL6
    • COI: 1:CAS:528:DyaK3sXhs1Ojt78%3D, PID: 1741402
    • Kinoshita S, Akira S, Kishimoto T (1992) A member of the C/EBP family, NF-IL6 beta, forms a heterodimer and transcriptionally synergizes with NF-IL6. Proc Natl Acad Sci U S A 89:1473–1476
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 1473-1476
    • Kinoshita, S.1    Akira, S.2    Kishimoto, T.3
  • 145
    • 84871689599 scopus 로고    scopus 로고
    • Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones
    • COI: 1:CAS:528:DC%2BC38Xhs1ajtbvO, PID: 23123194
    • Kityk R, Kopp J, Sinning I, Mayer MP (2012) Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones. Mol Cell 48:863–874
    • (2012) Mol Cell , vol.48 , pp. 863-874
    • Kityk, R.1    Kopp, J.2    Sinning, I.3    Mayer, M.P.4
  • 146
    • 0141615683 scopus 로고    scopus 로고
    • Heat shock protein 70 (Hsp70) membrane expression on head-and-neck cancer biopsy-a target for natural killer (NK) cells
    • COI: 1:CAS:528:DC%2BD3sXns12rt7g%3D, PID: 14529789
    • Kleinjung T, Arndt O, Feldmann HJ et al (2003) Heat shock protein 70 (Hsp70) membrane expression on head-and-neck cancer biopsy-a target for natural killer (NK) cells. Int J Radiat Oncol Biol Phys 57:820–826
    • (2003) Int J Radiat Oncol Biol Phys , vol.57 , pp. 820-826
    • Kleinjung, T.1    Arndt, O.2    Feldmann, H.J.3
  • 147
    • 77449089380 scopus 로고    scopus 로고
    • Facilitating Akt clearance via manipulation of Hsp70 activity and levels
    • COI: 1:CAS:528:DC%2BC3cXlvFClsg%3D%3D, PID: 19889640
    • Koren J, Jinwal UK, Jin Y et al (2010) Facilitating Akt clearance via manipulation of Hsp70 activity and levels. J Biol Chem 285:2498–2505
    • (2010) J Biol Chem , vol.285 , pp. 2498-2505
    • Koren, J.1    Jinwal, U.K.2    Jin, Y.3
  • 148
    • 84860369416 scopus 로고    scopus 로고
    • Rhodacyanine derivative selectively targets cancer cells and overcomes tamoxifen resistance
    • COI: 1:CAS:528:DC%2BC38Xnt1Crt7o%3D, PID: 22563386
    • Koren J, Miyata Y, Kiray J et al (2012) Rhodacyanine derivative selectively targets cancer cells and overcomes tamoxifen resistance. PLoS ONE 7:e35566
    • (2012) PLoS ONE , vol.7 , pp. e35566
    • Koren, J.1    Miyata, Y.2    Kiray, J.3
  • 149
    • 70350001064 scopus 로고    scopus 로고
    • Hsp70 translocates to the nuclei and nucleoli, binds to XRCC1 and PARP-1, and protects HeLa cells from single-strand DNA breaks
    • COI: 1:CAS:528:DC%2BD1MXns1eqsrg%3D, PID: 19089598
    • Kotoglou P, Kalaitzakis A, Vezyraki P et al (2009) Hsp70 translocates to the nuclei and nucleoli, binds to XRCC1 and PARP-1, and protects HeLa cells from single-strand DNA breaks. Cell Stress Chaperones 14:391–406
    • (2009) Cell Stress Chaperones , vol.14 , pp. 391-406
    • Kotoglou, P.1    Kalaitzakis, A.2    Vezyraki, P.3
  • 150
    • 0030064081 scopus 로고    scopus 로고
    • MKT-077, a novel rhodacyanine dye in clinical trials, exhibits anticarcinoma activity in preclinical studies based on selective mitochondrial accumulation
    • COI: 1:CAS:528:DyaK28XnslOisw%3D%3D, PID: 8564968
    • Koya K, Li Y, Wang H et al (1996) MKT-077, a novel rhodacyanine dye in clinical trials, exhibits anticarcinoma activity in preclinical studies based on selective mitochondrial accumulation. Cancer Res 56:538–543
    • (1996) Cancer Res , vol.56 , pp. 538-543
    • Koya, K.1    Li, Y.2    Wang, H.3
  • 151
    • 18544379571 scopus 로고    scopus 로고
    • Identification of crucial residues for the antibacterial activity of the proline-rich peptide, pyrrhocoricin
    • COI: 1:CAS:528:DC%2BD38Xnt1eiurw%3D, PID: 12199701
    • Kragol G, Hoffmann R, Chattergoon MA et al (2002) Identification of crucial residues for the antibacterial activity of the proline-rich peptide, pyrrhocoricin. Eur J Biochem 269:4226–4237
    • (2002) Eur J Biochem , vol.269 , pp. 4226-4237
    • Kragol, G.1    Hoffmann, R.2    Chattergoon, M.A.3
  • 152
    • 2542558307 scopus 로고    scopus 로고
    • Treatment of colon and lung cancer patients with ex vivo heat shock protein 70-peptide-activated, autologous natural killer cells: a clinical phase i trial
    • COI: 1:CAS:528:DC%2BD2cXksVKnsbc%3D, PID: 15173076
    • Krause SW, Gastpar R, Andreesen R et al (2004) Treatment of colon and lung cancer patients with ex vivo heat shock protein 70-peptide-activated, autologous natural killer cells: a clinical phase i trial. Clin Cancer Res 10:3699–3707
    • (2004) Clin Cancer Res , vol.10 , pp. 3699-3707
    • Krause, S.W.1    Gastpar, R.2    Andreesen, R.3
  • 153
    • 84872186457 scopus 로고    scopus 로고
    • Induction of endoplasmic reticulum stress genes, BiP and chop, in genetic and environmental models of retinal degeneration
    • COI: 1:CAS:528:DC%2BC3sXhs1Kgs7o%3D, PID: 23074209
    • Kroeger H, Messah C, Ahern K et al (2012) Induction of endoplasmic reticulum stress genes, BiP and chop, in genetic and environmental models of retinal degeneration. Invest Ophthalmol Vis Sci 53:7590–7599
    • (2012) Invest Ophthalmol Vis Sci , vol.53 , pp. 7590-7599
    • Kroeger, H.1    Messah, C.2    Ahern, K.3
  • 154
    • 17144374753 scopus 로고    scopus 로고
    • Toward an understanding of NKT cell biology: progress and paradoxes
    • COI: 1:CAS:528:DC%2BD2MXktFOju7k%3D, PID: 15771592
    • Kronenberg M (2005) Toward an understanding of NKT cell biology: progress and paradoxes. Annu Rev Immunol 23:877–900
    • (2005) Annu Rev Immunol , vol.23 , pp. 877-900
    • Kronenberg, M.1
  • 155
    • 20744436655 scopus 로고    scopus 로고
    • Exosome-dependent trafficking of HSP70: a novel secretory pathway for cellular stress proteins
    • COI: 1:CAS:528:DC%2BD2MXltVygsrc%3D, PID: 15826944
    • Lancaster GI, Febbraio MA (2005) Exosome-dependent trafficking of HSP70: a novel secretory pathway for cellular stress proteins. J Biol Chem 280:23349–23355
    • (2005) J Biol Chem , vol.280 , pp. 23349-23355
    • Lancaster, G.I.1    Febbraio, M.A.2
  • 156
    • 44149104599 scopus 로고    scopus 로고
    • Heat shock proteins: essential proteins for apoptosis regulation
    • COI: 1:CAS:528:DC%2BD1cXotlCrt70%3D, PID: 18266962
    • Lanneau D, Brunet M, Frisan E et al (2008) Heat shock proteins: essential proteins for apoptosis regulation. J Cell Mol Med 12:743–761
    • (2008) J Cell Mol Med , vol.12 , pp. 743-761
    • Lanneau, D.1    Brunet, M.2    Frisan, E.3
  • 157
    • 84859778293 scopus 로고    scopus 로고
    • mTOR signaling in growth control and disease
    • COI: 1:CAS:528:DC%2BC38Xls1eguro%3D, PID: 22500797
    • Laplante M, Sabatini DM (2012) mTOR signaling in growth control and disease. Cell 149:274–293
    • (2012) Cell , vol.149 , pp. 274-293
    • Laplante, M.1    Sabatini, D.M.2
  • 158
    • 0029114617 scopus 로고
    • Immunohistochemical expression of C-myc oncogene, heat shock protein 70 and HLA-DR molecules in malignant cutaneous melanoma
    • COI: 1:CAS:528:DyaK2MXosVaqurw%3D, PID: 7633656
    • Lazaris AC, Theodoropoulos GE, Aroni K, Saetta A, Davaris PS (1995) Immunohistochemical expression of C-myc oncogene, heat shock protein 70 and HLA-DR molecules in malignant cutaneous melanoma. Virchows Arch 426:461–467
    • (1995) Virchows Arch , vol.426 , pp. 461-467
    • Lazaris, A.C.1    Theodoropoulos, G.E.2    Aroni, K.3    Saetta, A.4    Davaris, P.S.5
  • 159
    • 0032931738 scopus 로고    scopus 로고
    • Structure-immunosuppressive activity relationships of new analogues of 15-deoxyspergualin. 1. Structural modifications of the hydroxyglycine moiety
    • COI: 1:CAS:528:DyaK1MXhslOhtg%3D%3D, PID: 9925733
    • Lebreton L, Annat J, Derrepas P, Dutartre P, Renaut P (1999) Structure-immunosuppressive activity relationships of new analogues of 15-deoxyspergualin. 1. Structural modifications of the hydroxyglycine moiety. J Med Chem 42:277–290
    • (1999) J Med Chem , vol.42 , pp. 277-290
    • Lebreton, L.1    Annat, J.2    Derrepas, P.3    Dutartre, P.4    Renaut, P.5
  • 160
    • 14844307612 scopus 로고    scopus 로고
    • HSP70 deficiency results in activation of c-Jun N-terminal kinase, extracellular signal-regulated kinase, and caspase-3 in hyperosmolarity-induced apoptosis
    • COI: 1:CAS:528:DC%2BD2MXhsV2qsbo%3D, PID: 15590690
    • Lee JS, Lee JJ, Seo JS (2005) HSP70 deficiency results in activation of c-Jun N-terminal kinase, extracellular signal-regulated kinase, and caspase-3 in hyperosmolarity-induced apoptosis. J Biol Chem 280:6634–6641
    • (2005) J Biol Chem , vol.280 , pp. 6634-6641
    • Lee, J.S.1    Lee, J.J.2    Seo, J.S.3
  • 161
    • 33748462461 scopus 로고    scopus 로고
    • Release of heat shock protein 70 (Hsp70) and the effects of extracellular Hsp70 on matrix metalloproteinase-9 expression in human monocytic U937 cells
    • COI: 1:CAS:528:DC%2BD28XpsFKnurg%3D, PID: 16953115
    • Lee KJ, Kim YM, Kim DY et al (2006) Release of heat shock protein 70 (Hsp70) and the effects of extracellular Hsp70 on matrix metalloproteinase-9 expression in human monocytic U937 cells. Exp Mol Med 38:364–374
    • (2006) Exp Mol Med , vol.38 , pp. 364-374
    • Lee, K.J.1    Kim, Y.M.2    Kim, D.Y.3
  • 162
    • 77953485026 scopus 로고    scopus 로고
    • Induction of the unfolded protein response and cell death pathway in Alzheimer’s disease, but not in aged Tg2576 mice
    • COI: 1:CAS:528:DC%2BC3cXnt1Gnsr8%3D, PID: 20368688
    • Lee JH, Won SM, Suh J et al (2010) Induction of the unfolded protein response and cell death pathway in Alzheimer’s disease, but not in aged Tg2576 mice. Exp Mol Med 42:386–394
    • (2010) Exp Mol Med , vol.42 , pp. 386-394
    • Lee, J.H.1    Won, S.M.2    Suh, J.3
  • 163
    • 33846603312 scopus 로고    scopus 로고
    • IFN-stimulated gene 15 functions as a critical antiviral molecule against influenza, herpes, and Sindbis viruses
    • COI: 1:CAS:528:DC%2BD2sXht12gtbc%3D, PID: 17227866
    • Lenschow DJ, Lai C, Frias-Staheli N et al (2007) IFN-stimulated gene 15 functions as a critical antiviral molecule against influenza, herpes, and Sindbis viruses. Proc Natl Acad Sci U S A 104:1371–1376
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 1371-1376
    • Lenschow, D.J.1    Lai, C.2    Frias-Staheli, N.3
  • 164
    • 70349768075 scopus 로고    scopus 로고
    • A small molecule inhibitor of inducible heat shock protein 70
    • COI: 1:CAS:528:DC%2BD1MXhsVChtLnF, PID: 19818706
    • Leu JI, Pimkina J, Frank A, Murphy ME, George DL (2009) A small molecule inhibitor of inducible heat shock protein 70. Mol Cell 36:15–27
    • (2009) Mol Cell , vol.36 , pp. 15-27
    • Leu, J.I.1    Pimkina, J.2    Frank, A.3    Murphy, M.E.4    George, D.L.5
  • 165
    • 0025363926 scopus 로고
    • The human heat-shock protein family. Expression of a novel heat-inducible HSP70 (HSP70B’) and isolation of its cDNA and genomic DNA
    • COI: 1:CAS:528:DyaK3cXlsVKgsr4%3D, PID: 2327978
    • Leung TK, Rajendran MY, Monfries C, Hall C, Lim L (1990) The human heat-shock protein family. Expression of a novel heat-inducible HSP70 (HSP70B’) and isolation of its cDNA and genomic DNA. Biochem J 267:125–132
    • (1990) Biochem J , vol.267 , pp. 125-132
    • Leung, T.K.1    Rajendran, M.Y.2    Monfries, C.3    Hall, C.4    Lim, L.5
  • 166
    • 79953708490 scopus 로고    scopus 로고
    • HSP70 decreases receptor-dependent phosphorylation of Smad2 and blocks TGF-beta-induced epithelial-mesenchymal transition
    • PID: 21477782
    • Li Y, Kang X, Wang Q (2011) HSP70 decreases receptor-dependent phosphorylation of Smad2 and blocks TGF-beta-induced epithelial-mesenchymal transition. J Genet Genomics 38:111–116
    • (2011) J Genet Genomics , vol.38 , pp. 111-116
    • Li, Y.1    Kang, X.2    Wang, Q.3
  • 167
    • 84887886374 scopus 로고    scopus 로고
    • Analogs of the allosteric heat shock protein 70 (Hsp70) inhibitor, MKT-077, as anti-cancer agents
    • Li X, Srinivasan SR, Connarn J et al. (2013a) Analogs of the allosteric heat shock protein 70 (Hsp70) inhibitor, MKT-077, as anti-cancer agents. ACS Med Chem Lett 4
    • (2013) ACS Med Chem Lett , pp. 4
    • Li, X.1    Srinivasan, S.R.2    Connarn, J.3
  • 168
    • 84879992522 scopus 로고    scopus 로고
    • Heat shock protein 70 acts as a potential biomarker for early diagnosis of heart failure
    • COI: 1:CAS:528:DC%2BC3sXhtFOmtb%2FE, PID: 23874478
    • Li Z, Song Y, Xing R et al (2013b) Heat shock protein 70 acts as a potential biomarker for early diagnosis of heart failure. PLoS ONE 8:e67964
    • (2013) PLoS ONE , vol.8 , pp. e67964
    • Li, Z.1    Song, Y.2    Xing, R.3
  • 169
    • 84929597660 scopus 로고    scopus 로고
    • Validation of the Hsp70-Bag3 protein-protein interaction as a potential therapeutic target in cancer
    • COI: 1:CAS:528:DC%2BC2MXlsVyrsLk%3D, PID: 25564440
    • Li X, Colvin T, Rauch JN et al (2015) Validation of the Hsp70-Bag3 protein-protein interaction as a potential therapeutic target in cancer. Mol Cancer Ther 14:642–648
    • (2015) Mol Cancer Ther , vol.14 , pp. 642-648
    • Li, X.1    Colvin, T.2    Rauch, J.N.3
  • 170
    • 33947533484 scopus 로고    scopus 로고
    • Fatty acyl benzamido antibacterials based on inhibition of DnaK-catalyzed protein folding
    • COI: 1:CAS:528:DC%2BD2sXhsFKhu7Y%3D, PID: 17170117
    • Liebscher M, Jahreis G, Lucke C et al (2007) Fatty acyl benzamido antibacterials based on inhibition of DnaK-catalyzed protein folding. J Biol Chem 282:4437–4446
    • (2007) J Biol Chem , vol.282 , pp. 4437-4446
    • Liebscher, M.1    Jahreis, G.2    Lucke, C.3
  • 171
    • 0024151897 scopus 로고
    • The heat-shock proteins
    • COI: 1:CAS:528:DyaL1MXhtlSmtbg%3D, PID: 2853609
    • Lindquist S, Craig EA (1988) The heat-shock proteins. Annu Rev Genet 22:631–677
    • (1988) Annu Rev Genet , vol.22 , pp. 631-677
    • Lindquist, S.1    Craig, E.A.2
  • 172
    • 84880047576 scopus 로고    scopus 로고
    • Triptolide induces the expression of miR-142-3p: a negative regulator of heat shock protein 70 and pancreatic cancer cell proliferation
    • COI: 1:CAS:528:DC%2BC3sXhtVGltLfE, PID: 23635652
    • MacKenzie TN, Mujumdar N, Banerjee S et al (2013) Triptolide induces the expression of miR-142-3p: a negative regulator of heat shock protein 70 and pancreatic cancer cell proliferation. Mol Cancer Ther 12:1266–1275
    • (2013) Mol Cancer Ther , vol.12 , pp. 1266-1275
    • MacKenzie, T.N.1    Mujumdar, N.2    Banerjee, S.3
  • 173
    • 47849116709 scopus 로고    scopus 로고
    • Elevated serum 70 kDa heat shock protein level reflects tissue damage and disease severity in the syndrome of hemolysis, elevated liver enzymes, and low platelet count
    • COI: 1:CAS:528:DC%2BD1cXpsValu7w%3D, PID: 18249485
    • Madach K, Molvarec A, Rigo J Jr et al (2008) Elevated serum 70 kDa heat shock protein level reflects tissue damage and disease severity in the syndrome of hemolysis, elevated liver enzymes, and low platelet count. Eur J Obstet Gynecol Reprod Biol 139:133–138
    • (2008) Eur J Obstet Gynecol Reprod Biol , vol.139 , pp. 133-138
    • Madach, K.1    Molvarec, A.2    Rigo, J.3
  • 174
    • 0035013496 scopus 로고    scopus 로고
    • Expression of heat shock proteins HSP70 and HSP27 in primary non-small cell lung carcinomas. An immunohistochemical study
    • COI: 1:CAS:528:DC%2BD3MXksVOjtr0%3D, PID: 11396134
    • Malusecka E, Zborek A, Krzyzowska-Gruca S, Krawczyk Z (2001) Expression of heat shock proteins HSP70 and HSP27 in primary non-small cell lung carcinomas. An immunohistochemical study. Anticancer Res 21:1015–1021
    • (2001) Anticancer Res , vol.21 , pp. 1015-1021
    • Malusecka, E.1    Zborek, A.2    Krzyzowska-Gruca, S.3    Krawczyk, Z.4
  • 175
    • 33750570923 scopus 로고    scopus 로고
    • Heat shock protein 70 is secreted from tumor cells by a nonclassical pathway involving lysosomal endosomes
    • COI: 1:CAS:528:DC%2BD28Xht1WrsL3J, PID: 17114456
    • Mambula SS, Calderwood SK (2006) Heat shock protein 70 is secreted from tumor cells by a nonclassical pathway involving lysosomal endosomes. J Immunol 177:7849–7857
    • (2006) J Immunol , vol.177 , pp. 7849-7857
    • Mambula, S.S.1    Calderwood, S.K.2
  • 176
    • 0035808322 scopus 로고    scopus 로고
    • The ATPase domain of hsp70 possesses a unique binding specificity for 3′-sulfogalactolipids
    • COI: 1:CAS:528:DC%2BD3MXmtFSrtg%3D%3D, PID: 11024054
    • Mamelak D, Lingwood C (2001) The ATPase domain of hsp70 possesses a unique binding specificity for 3′-sulfogalactolipids. J Biol Chem 276:449–456
    • (2001) J Biol Chem , vol.276 , pp. 449-456
    • Mamelak, D.1    Lingwood, C.2
  • 177
    • 0038381506 scopus 로고    scopus 로고
    • hsp72 inhibits focal adhesion kinase degradation in ATP-depleted renal epithelial cells
    • COI: 1:CAS:528:DC%2BD3sXjs1Khs78%3D, PID: 12611892
    • Mao H, Li F, Ruchalski K et al (2003) hsp72 inhibits focal adhesion kinase degradation in ATP-depleted renal epithelial cells. J Biol Chem 278:18214–18220
    • (2003) J Biol Chem , vol.278 , pp. 18214-18220
    • Mao, H.1    Li, F.2    Ruchalski, K.3
  • 178
    • 36549077002 scopus 로고    scopus 로고
    • Nutraceutical strategy in aging: targeting heat shock protein and inflammatory profile through understanding interleukin-6 polymorphism
    • COI: 1:CAS:528:DC%2BD1cXpvVGhsQ%3D%3D, PID: 18056967
    • Marotta F, Koike K, Lorenzetti A et al (2007) Nutraceutical strategy in aging: targeting heat shock protein and inflammatory profile through understanding interleukin-6 polymorphism. Ann N Y Acad Sci 1119:196–202
    • (2007) Ann N Y Acad Sci , vol.1119 , pp. 196-202
    • Marotta, F.1    Koike, K.2    Lorenzetti, A.3
  • 179
    • 15644384251 scopus 로고    scopus 로고
    • Cooperative and competitive protein interactions at the hsp70 promoter
    • COI: 1:CAS:528:DyaK1cXps1Kn, PID: 9407112
    • Mason PB Jr, Lis JT (1997) Cooperative and competitive protein interactions at the hsp70 promoter. J Biol Chem 272:33227–33233
    • (1997) J Biol Chem , vol.272 , pp. 33227-33233
    • Mason, P.B.1    Lis, J.T.2
  • 180
    • 77954662908 scopus 로고    scopus 로고
    • A novel, small molecule inhibitor of Hsc70/Hsp70 potentiates Hsp90 inhibitor induced apoptosis in HCT116 colon carcinoma cells
    • COI: 1:CAS:528:DC%2BC3cXns1SisbY%3D, PID: 20012863
    • Massey AJ, Williamson DS, Browne H et al (2010) A novel, small molecule inhibitor of Hsc70/Hsp70 potentiates Hsp90 inhibitor induced apoptosis in HCT116 colon carcinoma cells. Cancer Chemother Pharmacol 66:535–545
    • (2010) Cancer Chemother Pharmacol , vol.66 , pp. 535-545
    • Massey, A.J.1    Williamson, D.S.2    Browne, H.3
  • 181
    • 84885050263 scopus 로고    scopus 로고
    • Hsp70 silencing with siRNA in nanocarriers enhances cancer cell death induced by the inhibitor of Hsp90
    • COI: 1:CAS:528:DC%2BC3sXmvF2itL8%3D, PID: 23583203
    • Matokanovic M, Barisic K, Filipovic-Grcic J, Maysinger D (2013) Hsp70 silencing with siRNA in nanocarriers enhances cancer cell death induced by the inhibitor of Hsp90. Eur J Pharm Sci 50:149–158
    • (2013) Eur J Pharm Sci , vol.50 , pp. 149-158
    • Matokanovic, M.1    Barisic, K.2    Filipovic-Grcic, J.3    Maysinger, D.4
  • 182
    • 84906096557 scopus 로고    scopus 로고
    • Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins
    • COI: 1:CAS:528:DC%2BC2cXmvVShtb8%3D, PID: 24760129
    • Mattoo RU, Goloubinoff P (2014) Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins. Cell Mol Life Sci 71:3311–3325
    • (2014) Cell Mol Life Sci , vol.71 , pp. 3311-3325
    • Mattoo, R.U.1    Goloubinoff, P.2
  • 183
    • 84880515581 scopus 로고    scopus 로고
    • Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates
    • COI: 1:CAS:528:DC%2BC3sXhtFeksbvK, PID: 23737532
    • Mattoo RU, Sharma SK, Priya S, Finka A, Goloubinoff P (2013) Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates. J Biol Chem 288:21399–21411
    • (2013) J Biol Chem , vol.288 , pp. 21399-21411
    • Mattoo, R.U.1    Sharma, S.K.2    Priya, S.3    Finka, A.4    Goloubinoff, P.5
  • 184
    • 84869988993 scopus 로고    scopus 로고
    • Cysteine reactivity distinguishes redox sensing by the heat-inducible and constitutive forms of heat shock protein 70
    • COI: 1:CAS:528:DC%2BC38XhsleisLvE, PID: 23177194
    • Miyata Y, Rauch JN, Jinwal UK et al (2012) Cysteine reactivity distinguishes redox sensing by the heat-inducible and constitutive forms of heat shock protein 70. Chem Biol 19:1391–1399
    • (2012) Chem Biol , vol.19 , pp. 1391-1399
    • Miyata, Y.1    Rauch, J.N.2    Jinwal, U.K.3
  • 185
    • 84879767467 scopus 로고    scopus 로고
    • Synthesis and initial evaluation of YM-08, a blood–brain barrier permeable derivative of the heat shock protein 70 (Hsp70) inhibitor MKT-077, which reduces tau levels
    • COI: 1:CAS:528:DC%2BC3sXjslSnsbo%3D, PID: 23472668
    • Miyata Y, Li X, Lee HF et al (2013) Synthesis and initial evaluation of YM-08, a blood–brain barrier permeable derivative of the heat shock protein 70 (Hsp70) inhibitor MKT-077, which reduces tau levels. ACS Chem Neurosci 4:930–939
    • (2013) ACS Chem Neurosci , vol.4 , pp. 930-939
    • Miyata, Y.1    Li, X.2    Lee, H.F.3
  • 186
    • 0024380865 scopus 로고
    • Identification, characterization, and purification of two mammalian stress proteins present in mitochondria, grp 75, a member of the hsp 70 family and hsp 58, a homolog of the bacterial groEL protein
    • COI: 1:CAS:528:DyaK3cXltV2j, PID: 2573603
    • Mizzen LA, Chang C, Garrels JI, Welch WJ (1989) Identification, characterization, and purification of two mammalian stress proteins present in mitochondria, grp 75, a member of the hsp 70 family and hsp 58, a homolog of the bacterial groEL protein. J Biol Chem 264:20664–20675
    • (1989) J Biol Chem , vol.264 , pp. 20664-20675
    • Mizzen, L.A.1    Chang, C.2    Garrels, J.I.3    Welch, W.J.4
  • 187
    • 33748949102 scopus 로고    scopus 로고
    • Association of elevated serum heat-shock protein 70 concentration with transient hypertension of pregnancy, preeclampsia and superimposed preeclampsia: a case–control study
    • COI: 1:CAS:528:DC%2BD28Xpsl2ru7g%3D, PID: 16761027
    • Molvarec A, Prohaszka Z, Nagy B et al (2006) Association of elevated serum heat-shock protein 70 concentration with transient hypertension of pregnancy, preeclampsia and superimposed preeclampsia: a case–control study. J Hum Hypertens 20:780–786
    • (2006) J Hum Hypertens , vol.20 , pp. 780-786
    • Molvarec, A.1    Prohaszka, Z.2    Nagy, B.3
  • 188
    • 33947175477 scopus 로고    scopus 로고
    • Association of increased serum heat shock protein 70 and C-reactive protein concentrations and decreased serum alpha(2)-HS glycoprotein concentration with the syndrome of hemolysis, elevated liver enzymes, and low platelet count
    • COI: 1:CAS:528:DC%2BD2sXjtFGgt74%3D, PID: 17023052
    • Molvarec A, Prohaszka Z, Nagy B et al (2007a) Association of increased serum heat shock protein 70 and C-reactive protein concentrations and decreased serum alpha(2)-HS glycoprotein concentration with the syndrome of hemolysis, elevated liver enzymes, and low platelet count. J Reprod Immunol 73:172–179
    • (2007) J Reprod Immunol , vol.73 , pp. 172-179
    • Molvarec, A.1    Prohaszka, Z.2    Nagy, B.3
  • 189
    • 34247638382 scopus 로고    scopus 로고
    • Serum heat shock protein 70 levels are decreased in normal human pregnancy
    • COI: 1:CAS:528:DC%2BD2sXkvFGgsbo%3D, PID: 17296233
    • Molvarec A, Rigo J Jr, Nagy B et al (2007b) Serum heat shock protein 70 levels are decreased in normal human pregnancy. J Reprod Immunol 74:163–169
    • (2007) J Reprod Immunol , vol.74 , pp. 163-169
    • Molvarec, A.1    Rigo, J.2    Nagy, B.3
  • 190
    • 77951252849 scopus 로고    scopus 로고
    • Circulating heat shock protein 70 (HSPA1A) in normal and pathological pregnancies
    • COI: 1:CAS:528:DC%2BC3cXktlSit7Y%3D, PID: 19821156
    • Molvarec A, Tamasi L, Losonczy G et al (2010) Circulating heat shock protein 70 (HSPA1A) in normal and pathological pregnancies. Cell Stress Chaperones 15:237–247
    • (2010) Cell Stress Chaperones , vol.15 , pp. 237-247
    • Molvarec, A.1    Tamasi, L.2    Losonczy, G.3
  • 191
    • 24344505476 scopus 로고    scopus 로고
    • Human natural killer cells: molecular mechanisms controlling NK cell activation and tumor cell lysis
    • COI: 1:CAS:528:DC%2BD2MXpvFaktLY%3D, PID: 16109445
    • Moretta L, Bottino C, Pende D et al (2005) Human natural killer cells: molecular mechanisms controlling NK cell activation and tumor cell lysis. Immunol Lett 100:7–13
    • (2005) Immunol Lett , vol.100 , pp. 7-13
    • Moretta, L.1    Bottino, C.2    Pende, D.3
  • 192
    • 34848859541 scopus 로고    scopus 로고
    • Heat shock protein 70 (Hsp70): membrane location, export and immunological relevance
    • COI: 1:CAS:528:DC%2BD2sXhtFers7%2FO, PID: 17920520
    • Multhoff G (2007) Heat shock protein 70 (Hsp70): membrane location, export and immunological relevance. Methods 43:229–237
    • (2007) Methods , vol.43 , pp. 229-237
    • Multhoff, G.1
  • 193
    • 0030224714 scopus 로고    scopus 로고
    • Cell surface expression of heat shock proteins and the immune response
    • COI: 1:CAS:528:DyaK28XmsFChu7c%3D, PID: 9222602
    • Multhoff G, Hightower LE (1996) Cell surface expression of heat shock proteins and the immune response. Cell Stress Chaperones 1:167–176
    • (1996) Cell Stress Chaperones , vol.1 , pp. 167-176
    • Multhoff, G.1    Hightower, L.E.2
  • 194
    • 84875221247 scopus 로고    scopus 로고
    • Radiation, inflammation, and immune responses in cancer
    • PID: 22675673
    • Multhoff G, Radons J (2012) Radiation, inflammation, and immune responses in cancer. Front Oncol 2:58. doi:10.3389/fonc.2012.00058
    • (2012) Front Oncol , vol.2 , pp. 58
    • Multhoff, G.1    Radons, J.2
  • 195
    • 0028953056 scopus 로고
    • A stress-inducible 72-kDa heat-shock protein (HSP72) is expressed on the surface of human tumor cells, but not on normal cells
    • COI: 1:CAS:528:DyaK2MXlsVCmtLY%3D, PID: 7705958
    • Multhoff G, Botzler C, Wiesnet M et al (1995) A stress-inducible 72-kDa heat-shock protein (HSP72) is expressed on the surface of human tumor cells, but not on normal cells. Int J Cancer 61:272–279
    • (1995) Int J Cancer , vol.61 , pp. 272-279
    • Multhoff, G.1    Botzler, C.2    Wiesnet, M.3
  • 196
    • 0031132876 scopus 로고    scopus 로고
    • Heat shock protein 72 on tumor cells: a recognition structure for natural killer cells
    • COI: 1:CAS:528:DyaK2sXivVCksb0%3D, PID: 9126997
    • Multhoff G, Botzler C, Jennen L et al (1997) Heat shock protein 72 on tumor cells: a recognition structure for natural killer cells. J Immunol 158:4341–4350
    • (1997) J Immunol , vol.158 , pp. 4341-4350
    • Multhoff, G.1    Botzler, C.2    Jennen, L.3
  • 197
    • 0032727033 scopus 로고    scopus 로고
    • Heat shock protein 70 (Hsp70) stimulates proliferation and cytolytic activity of natural killer cells
    • COI: 1:CAS:528:DyaK1MXnvVehs7s%3D, PID: 10560910
    • Multhoff G, Mizzen L, Winchester CC et al (1999) Heat shock protein 70 (Hsp70) stimulates proliferation and cytolytic activity of natural killer cells. Exp Hematol 27:1627–1636
    • (1999) Exp Hematol , vol.27 , pp. 1627-1636
    • Multhoff, G.1    Mizzen, L.2    Winchester, C.C.3
  • 198
    • 0035205080 scopus 로고    scopus 로고
    • A 14-mer Hsp70 peptide stimulates natural killer (NK) cell activity
    • COI: 1:CAS:528:DC%2BD38XivVOiuw%3D%3D, PID: 11795470
    • Multhoff G, Pfister K, Gehrmann M et al (2001) A 14-mer Hsp70 peptide stimulates natural killer (NK) cell activity. Cell Stress Chaperones 6:337–344
    • (2001) Cell Stress Chaperones , vol.6 , pp. 337-344
    • Multhoff, G.1    Pfister, K.2    Gehrmann, M.3
  • 199
    • 84867829868 scopus 로고    scopus 로고
    • Dual role of heat shock proteins (HSPs) in anti-tumor immunity
    • COI: 1:CAS:528:DC%2BC38Xhsl2it7nF, PID: 22804240
    • Multhoff G, Pockley AG, Streffer C, Gaipl US (2012) Dual role of heat shock proteins (HSPs) in anti-tumor immunity. Curr Mol Med 12:1174–1182
    • (2012) Curr Mol Med , vol.12 , pp. 1174-1182
    • Multhoff, G.1    Pockley, A.G.2    Streffer, C.3    Gaipl, U.S.4
  • 200
    • 84941880491 scopus 로고    scopus 로고
    • The role of heat shock protein 70 (Hsp70) in radiation-induced immunomodulation
    • COI: 1:CAS:528:DC%2BC2MXivFWrtr0%3D, PID: 25681671
    • Multhoff G, Pockley AG, Schmid TE, Schilling D (2015) The role of heat shock protein 70 (Hsp70) in radiation-induced immunomodulation. Cancer Lett 368:179–184
    • (2015) Cancer Lett , vol.368 , pp. 179-184
    • Multhoff, G.1    Pockley, A.G.2    Schmid, T.E.3    Schilling, D.4
  • 201
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • COI: 1:CAS:528:DyaL1cXht1Kqsb8%3D, PID: 3545499
    • Munro S, Pelham HR (1987) A C-terminal signal prevents secretion of luminal ER proteins. Cell 48:899–907
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.2
  • 202
    • 84937691999 scopus 로고    scopus 로고
    • Role of membrane Hsp70 in radiation sensitivity of tumor cells
    • PID: 26197988
    • Murakami N, Kuhnel A, Schmid TE et al (2015) Role of membrane Hsp70 in radiation sensitivity of tumor cells. Radiat Oncol 10:149
    • (2015) Radiat Oncol , vol.10 , pp. 149
    • Murakami, N.1    Kuhnel, A.2    Schmid, T.E.3
  • 203
    • 80455158315 scopus 로고    scopus 로고
    • Heat shock proteins and cancer vaccines: developments in the past decade and chaperoning in the decade to come
    • COI: 1:CAS:528:DC%2BC3MXhtlyqtLfO, PID: 22043955
    • Murshid A, Gong J, Stevenson MA, Calderwood SK (2011) Heat shock proteins and cancer vaccines: developments in the past decade and chaperoning in the decade to come. Expert Rev Vaccines 10:1553–1568
    • (2011) Expert Rev Vaccines , vol.10 , pp. 1553-1568
    • Murshid, A.1    Gong, J.2    Stevenson, M.A.3    Calderwood, S.K.4
  • 204
    • 0032501429 scopus 로고    scopus 로고
    • Identification of a binding site on Hsc70 for the immunosuppressant 15-deoxyspergualin
    • COI: 1:CAS:528:DyaK1cXotFShsL8%3D, PID: 9875240
    • Nadler SG, Dischino DD, Malacko AR et al (1998) Identification of a binding site on Hsc70 for the immunosuppressant 15-deoxyspergualin. Biochem Biophys Res Commun 253:176–180
    • (1998) Biochem Biophys Res Commun , vol.253 , pp. 176-180
    • Nadler, S.G.1    Dischino, D.D.2    Malacko, A.R.3
  • 205
    • 0034494832 scopus 로고    scopus 로고
    • Preventive effects of drinking green tea on cancer and cardiovascular disease: epidemiological evidence for multiple targeting prevention
    • COI: 1:CAS:528:DC%2BD3MXksVOlsrk%3D, PID: 11237198
    • Nakachi K, Matsuyama S, Miyake S, Suganuma M, Imai K (2000) Preventive effects of drinking green tea on cancer and cardiovascular disease: epidemiological evidence for multiple targeting prevention. Biofactors 13:49–54
    • (2000) Biofactors , vol.13 , pp. 49-54
    • Nakachi, K.1    Matsuyama, S.2    Miyake, S.3    Suganuma, M.4    Imai, K.5
  • 206
    • 78149434868 scopus 로고    scopus 로고
    • Increased serum HSP70 levels are associated with the duration of diabetes
    • COI: 1:CAS:528:DC%2BC3cXht12qtbbJ, PID: 20496051
    • Nakhjavani M, Morteza A, Khajeali L et al (2010) Increased serum HSP70 levels are associated with the duration of diabetes. Cell Stress Chaperones 15:959–964
    • (2010) Cell Stress Chaperones , vol.15 , pp. 959-964
    • Nakhjavani, M.1    Morteza, A.2    Khajeali, L.3
  • 207
    • 80053587355 scopus 로고    scopus 로고
    • Effects of phytochemicals on ionization radiation-mediated carcinogenesis and cancer therapy
    • COI: 1:CAS:528:DC%2BC3MXht12rsbbF, PID: 22030216
    • Nambiar D, Rajamani P, Singh RP (2011) Effects of phytochemicals on ionization radiation-mediated carcinogenesis and cancer therapy. Mutat Res 728:139–157
    • (2011) Mutat Res , vol.728 , pp. 139-157
    • Nambiar, D.1    Rajamani, P.2    Singh, R.P.3
  • 208
    • 79953113775 scopus 로고    scopus 로고
    • Circulating heat shock protein 70 in health, aging and disease
    • COI: 1:CAS:528:DC%2BC3MXkslygt7k%3D, PID: 21443787
    • Njemini R, Bautmans I, Onyema OO et al (2011) Circulating heat shock protein 70 in health, aging and disease. BMC Immunol 12:24
    • (2011) BMC Immunol , vol.12 , pp. 24
    • Njemini, R.1    Bautmans, I.2    Onyema, O.O.3
  • 209
    • 36249030048 scopus 로고    scopus 로고
    • Decreased enzyme activities of chaperones PDI and BiP in aged mouse livers
    • COI: 1:CAS:528:DC%2BD2sXhtlCrsLjM, PID: 17996725
    • Nuss JE, Choksi KB, DeFord JH, Papaconstantinou J (2008) Decreased enzyme activities of chaperones PDI and BiP in aged mouse livers. Biochem Biophys Res Commun 365:355–361
    • (2008) Biochem Biophys Res Commun , vol.365 , pp. 355-361
    • Nuss, J.E.1    Choksi, K.B.2    DeFord, J.H.3    Papaconstantinou, J.4
  • 210
    • 0034608892 scopus 로고    scopus 로고
    • Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases and bypasses Bcl-2
    • COI: 1:CAS:528:DC%2BD3cXkvFCntbY%3D, PID: 10884417
    • Nylandsted J, Rohde M, Brand K et al (2000) Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases and bypasses Bcl-2. Proc Natl Acad Sci U S A 97:7871–7876
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 7871-7876
    • Nylandsted, J.1    Rohde, M.2    Brand, K.3
  • 211
    • 4344651318 scopus 로고    scopus 로고
    • Heat shock protein 70 promotes cell survival by inhibiting lysosomal membrane permeabilization
    • COI: 1:CAS:528:DC%2BD2cXmvFehtrw%3D, PID: 15314073
    • Nylandsted J, Gyrd-Hansen M, Danielewicz A et al (2004) Heat shock protein 70 promotes cell survival by inhibiting lysosomal membrane permeabilization. J Exp Med 200:425–435
    • (2004) J Exp Med , vol.200 , pp. 425-435
    • Nylandsted, J.1    Gyrd-Hansen, M.2    Danielewicz, A.3
  • 212
    • 77958566761 scopus 로고    scopus 로고
    • Phenothiazine-mediated rescue of cognition in tau transgenic mice requires neuroprotection and reduced soluble tau burden
    • PID: 21040568
    • O’Leary JC III, Li Q, Marinec P et al (2010) Phenothiazine-mediated rescue of cognition in tau transgenic mice requires neuroprotection and reduced soluble tau burden. Mol Neurodegener 5:45
    • (2010) Mol Neurodegener , vol.5 , pp. 45
    • O’Leary, J.C.1    Li, Q.2    Marinec, P.3
  • 213
    • 84889100021 scopus 로고    scopus 로고
    • Rapid systemic and local treatments with the antibacterial peptide dimer A3-APO and its monomeric metabolite eliminate bacteria and reduce inflammation in intradermal lesions infected with Propionibacterium acnes and meticillin-resistant Staphylococcus aureus
    • COI: 1:CAS:528:DC%2BC3sXhsFemtLzK, PID: 24074727
    • Ostorhazi E, Voros E, Nemes-Nikodem E et al (2013) Rapid systemic and local treatments with the antibacterial peptide dimer A3-APO and its monomeric metabolite eliminate bacteria and reduce inflammation in intradermal lesions infected with Propionibacterium acnes and meticillin-resistant Staphylococcus aureus. Int J Antimicrob Agents 42:537–543
    • (2013) Int J Antimicrob Agents , vol.42 , pp. 537-543
    • Ostorhazi, E.1    Voros, E.2    Nemes-Nikodem, E.3
  • 214
    • 33845755480 scopus 로고    scopus 로고
    • The induction mechanism of the molecular chaperone HSP70 in the gastric mucosa by Geranylgeranylacetone (HSP-inducer)
    • COI: 1:CAS:528:DC%2BD2sXhvVSqtw%3D%3D, PID: 17182004
    • Otaka M, Yamamoto S, Ogasawara K et al (2007) The induction mechanism of the molecular chaperone HSP70 in the gastric mucosa by Geranylgeranylacetone (HSP-inducer). Biochem Biophys Res Commun 353:399–404
    • (2007) Biochem Biophys Res Commun , vol.353 , pp. 399-404
    • Otaka, M.1    Yamamoto, S.2    Ogasawara, K.3
  • 215
    • 0028281442 scopus 로고
    • Stch encodes the ‘ATPase core’ of a microsomal stress 70 protein
    • COI: 1:CAS:528:DyaK2cXjtFOqt7c%3D, PID: 8131751
    • Otterson GA, Flynn GC, Kratzke RA et al (1994) Stch encodes the ‘ATPase core’ of a microsomal stress 70 protein. EMBO J 13:1216–1225
    • (1994) EMBO J , vol.13 , pp. 1216-1225
    • Otterson, G.A.1    Flynn, G.C.2    Kratzke, R.A.3
  • 216
    • 0034700271 scopus 로고    scopus 로고
    • Interaction between heat shock proteins and antimicrobial peptides
    • COI: 1:CAS:528:DC%2BD3cXnsVGgtbc%3D, PID: 11087363
    • Otvos L Jr, O I, Rogers ME et al (2000) Interaction between heat shock proteins and antimicrobial peptides. Biochemistry 39:14150–14159
    • (2000) Biochemistry , vol.39 , pp. 14150-14159
    • Otvos, L.1    Rogers, M.E.2
  • 217
    • 23644459481 scopus 로고    scopus 로고
    • Designer antibacterial peptides kill fluoroquinolone-resistant clinical isolates
    • COI: 1:CAS:528:DC%2BD2MXmt1Wku74%3D, PID: 16078852
    • Otvos L Jr, Wade JD, Lin F et al (2005) Designer antibacterial peptides kill fluoroquinolone-resistant clinical isolates. J Med Chem 48:5349–5359
    • (2005) J Med Chem , vol.48 , pp. 5349-5359
    • Otvos, L.1    Wade, J.D.2    Lin, F.3
  • 218
    • 84896360072 scopus 로고    scopus 로고
    • The designer proline-rich antibacterial peptide A3-APO prevents Bacillus anthracis mortality by deactivating bacterial toxins
    • COI: 1:CAS:528:DC%2BC2cXjtl2gsr4%3D, PID: 24164262
    • Otvos L, Flick-Smith H, Fox M et al (2014) The designer proline-rich antibacterial peptide A3-APO prevents Bacillus anthracis mortality by deactivating bacterial toxins. Protein Pept Lett 21:374–381
    • (2014) Protein Pept Lett , vol.21 , pp. 374-381
    • Otvos, L.1    Flick-Smith, H.2    Fox, M.3
  • 219
    • 84888293891 scopus 로고    scopus 로고
    • MicroRNAs regulate the chaperone network in cerebral ischemia
    • COI: 1:CAS:528:DC%2BC3sXhtlWgurnP, PID: 24323423
    • Ouyang YB, Giffard RG (2013) MicroRNAs regulate the chaperone network in cerebral ischemia. Transl Stroke Res 4:693–703
    • (2013) Transl Stroke Res , vol.4 , pp. 693-703
    • Ouyang, Y.B.1    Giffard, R.G.2
  • 220
    • 77949905797 scopus 로고    scopus 로고
    • Expression of HSP27, HSP72 and MRP proteins in in vitro co-culture of colon tumour cell spheroids with normal cells after incubation with rhTGF-beta1 and/or CPT-11
    • COI: 1:CAS:528:DC%2BC3cXhslWht7c%3D, PID: 20093746
    • Paduch R, Jakubowicz-Gil J, Kandefer-Szerszen M (2009) Expression of HSP27, HSP72 and MRP proteins in in vitro co-culture of colon tumour cell spheroids with normal cells after incubation with rhTGF-beta1 and/or CPT-11. J Biosci 34:927–940
    • (2009) J Biosci , vol.34 , pp. 927-940
    • Paduch, R.1    Jakubowicz-Gil, J.2    Kandefer-Szerszen, M.3
  • 221
    • 0042071558 scopus 로고    scopus 로고
    • Identification and purification from the plasma of type 1 diabetic subjects of a proteolytically active Grp94. Evidence that Grp94 is entirely responsible for plasma proteolytic activity
    • COI: 1:CAS:528:DC%2BD3sXls1yns70%3D, PID: 12827241
    • Pagetta A, Folda A, Brunati AM, Finotti P (2003) Identification and purification from the plasma of type 1 diabetic subjects of a proteolytically active Grp94. Evidence that Grp94 is entirely responsible for plasma proteolytic activity. Diabetologia 46:996–1006
    • (2003) Diabetologia , vol.46 , pp. 996-1006
    • Pagetta, A.1    Folda, A.2    Brunati, A.M.3    Finotti, P.4
  • 222
    • 64749115962 scopus 로고    scopus 로고
    • A soluble sulfogalactosyl ceramide mimic promotes Delta F508 CFTR escape from endoplasmic reticulum associated degradation
    • COI: 1:CAS:528:DC%2BD1MXltVCms7k%3D, PID: 19389632
    • Park HJ, Mylvaganum M, McPherson A et al (2009) A soluble sulfogalactosyl ceramide mimic promotes Delta F508 CFTR escape from endoplasmic reticulum associated degradation. Chem Biol 16:461–470
    • (2009) Chem Biol , vol.16 , pp. 461-470
    • Park, H.J.1    Mylvaganum, M.2    McPherson, A.3
  • 223
    • 84876225032 scopus 로고    scopus 로고
    • HSPA9 overexpression inhibits apoptin-induced apoptosis in the HepG2 cell line
    • COI: 1:CAS:528:DC%2BC3sXpsFCktb8%3D, PID: 23589050
    • Peng C, Yang P, Cui Y et al (2013) HSPA9 overexpression inhibits apoptin-induced apoptosis in the HepG2 cell line. Oncol Rep 29:2431–2437
    • (2013) Oncol Rep , vol.29 , pp. 2431-2437
    • Peng, C.1    Yang, P.2    Cui, Y.3
  • 224
    • 34547919601 scopus 로고    scopus 로고
    • Patient survival by Hsp70 membrane phenotype: association with different routes of metastasis
    • PID: 17580361
    • Pfister K, Radons J, Busch R et al (2007) Patient survival by Hsp70 membrane phenotype: association with different routes of metastasis. Cancer 110:926–935
    • (2007) Cancer , vol.110 , pp. 926-935
    • Pfister, K.1    Radons, J.2    Busch, R.3
  • 225
    • 17744372861 scopus 로고    scopus 로고
    • Roles of the heat shock transcription factors in regulation of the heat shock response and beyond
    • COI: 1:CAS:528:DC%2BD3MXlvVOms78%3D, PID: 11344080
    • Pirkkala L, Nykanen P, Sistonen L (2001) Roles of the heat shock transcription factors in regulation of the heat shock response and beyond. FASEB J 15:1118–1131
    • (2001) FASEB J , vol.15 , pp. 1118-1131
    • Pirkkala, L.1    Nykanen, P.2    Sistonen, L.3
  • 226
    • 0023156658 scopus 로고
    • Preclinical antitumor activity and pharmacological properties of deoxyspergualin
    • COI: 1:CAS:528:DyaL2sXhs1ylsrk%3D, PID: 3802074
    • Plowman J, Harrison SD Jr, Trader MW et al (1987) Preclinical antitumor activity and pharmacological properties of deoxyspergualin. Cancer Res 47:685–689
    • (1987) Cancer Res , vol.47 , pp. 685-689
    • Plowman, J.1    Harrison, S.D.2    Trader, M.W.3
  • 227
    • 33845525384 scopus 로고    scopus 로고
    • Overexpression of the heat-shock protein 70 is associated to imatinib resistance in chronic myeloid leukemia
    • COI: 1:CAS:528:DC%2BD28XhtlSqurrK, PID: 17109025
    • Pocaly M, Lagarde V, Etienne G et al (2007) Overexpression of the heat-shock protein 70 is associated to imatinib resistance in chronic myeloid leukemia. Leukemia 21:93–101
    • (2007) Leukemia , vol.21 , pp. 93-101
    • Pocaly, M.1    Lagarde, V.2    Etienne, G.3
  • 228
    • 0031770945 scopus 로고    scopus 로고
    • Detection of heat shock protein 70 (Hsp70) and anti-Hsp70 antibodies in the serum of normal individuals
    • COI: 1:CAS:528:DyaK1cXnvFSisro%3D, PID: 9845422
    • Pockley AG, Shepherd J, Corton JM (1998) Detection of heat shock protein 70 (Hsp70) and anti-Hsp70 antibodies in the serum of normal individuals. Immunol Invest 27:367–377
    • (1998) Immunol Invest , vol.27 , pp. 367-377
    • Pockley, A.G.1    Shepherd, J.2    Corton, J.M.3
  • 229
    • 0032896726 scopus 로고    scopus 로고
    • Identification of human heat shock protein 60 (Hsp60) and anti-Hsp60 antibodies in the peripheral circulation of normal individuals
    • COI: 1:CAS:528:DyaK1MXjtF2lt7g%3D, PID: 10467106
    • Pockley AG, Bulmer J, Hanks BM, Wright BH (1999) Identification of human heat shock protein 60 (Hsp60) and anti-Hsp60 antibodies in the peripheral circulation of normal individuals. Cell Stress Chaperones 4:29–35
    • (1999) Cell Stress Chaperones , vol.4 , pp. 29-35
    • Pockley, A.G.1    Bulmer, J.2    Hanks, B.M.3    Wright, B.H.4
  • 230
    • 38949134137 scopus 로고    scopus 로고
    • The dual immunoregulatory roles of stress proteins
    • COI: 1:CAS:528:DC%2BD1cXhvVWhtr4%3D, PID: 18182297
    • Pockley AG, Muthana M, Calderwood SK (2008) The dual immunoregulatory roles of stress proteins. Trends Biochem Sci 33:71–79
    • (2008) Trends Biochem Sci , vol.33 , pp. 71-79
    • Pockley, A.G.1    Muthana, M.2    Calderwood, S.K.3
  • 231
    • 84911874159 scopus 로고    scopus 로고
    • Extracellular cell stress proteins as biomarkers of human disease
    • COI: 1:CAS:528:DC%2BC2cXhvFalsbrO, PID: 25399600
    • Pockley AG, Henderson B, Multhoff G (2014) Extracellular cell stress proteins as biomarkers of human disease. Biochem Soc Trans 42:1744–1751
    • (2014) Biochem Soc Trans , vol.42 , pp. 1744-1751
    • Pockley, A.G.1    Henderson, B.2    Multhoff, G.3
  • 232
    • 0032834594 scopus 로고    scopus 로고
    • Phase I trial of the selective mitochondrial toxin MKT077 in chemo-resistant solid tumours
    • COI: 1:STN:280:DyaK1MvjvVGluw%3D%3D, PID: 10509153
    • Propper DJ, Braybrooke JP, Taylor DJ et al (1999) Phase I trial of the selective mitochondrial toxin MKT077 in chemo-resistant solid tumours. Ann Oncol 10:923–927
    • (1999) Ann Oncol , vol.10 , pp. 923-927
    • Propper, D.J.1    Braybrooke, J.P.2    Taylor, D.J.3
  • 233
    • 84943355219 scopus 로고    scopus 로고
    • The detection and role of heat shock protein 70 in various nondisease conditions and disease conditions: a literature review
    • COI: 1:CAS:528:DC%2BC2MXhtFCgur3I, PID: 26139132
    • Qu B, Jia Y, Liu Y et al (2015) The detection and role of heat shock protein 70 in various nondisease conditions and disease conditions: a literature review. Cell Stress Chaperones 20:885–892
    • (2015) Cell Stress Chaperones , vol.20 , pp. 885-892
    • Qu, B.1    Jia, Y.2    Liu, Y.3
  • 234
    • 84872538586 scopus 로고    scopus 로고
    • HSP-molecular chaperones in cancer biogenesis and tumor therapy: an overview
    • COI: 1:CAS:528:DC%2BC3sXjt1ynsg%3D%3D, PID: 23225410
    • Rappa F, Farina F, Zummo G et al (2012) HSP-molecular chaperones in cancer biogenesis and tumor therapy: an overview. Anticancer Res 32:5139–5150
    • (2012) Anticancer Res , vol.32 , pp. 5139-5150
    • Rappa, F.1    Farina, F.2    Zummo, G.3
  • 235
    • 17944366977 scopus 로고    scopus 로고
    • Heat-shock protein 70 antagonizes apoptosis-inducing factor
    • COI: 1:CAS:528:DC%2BD3MXmvF2ls7s%3D, PID: 11533664
    • Ravagnan L, Gurbuxani S, Susin SA et al (2001) Heat-shock protein 70 antagonizes apoptosis-inducing factor. Nat Cell Biol 3:839–843
    • (2001) Nat Cell Biol , vol.3 , pp. 839-843
    • Ravagnan, L.1    Gurbuxani, S.2    Susin, S.A.3
  • 236
    • 0035114098 scopus 로고    scopus 로고
    • Serum heat shock protein and anti-heat shock protein antibody levels in aging
    • COI: 1:CAS:528:DC%2BD3MXhsVOhtrw%3D, PID: 11226747
    • Rea IM, McNerlan S, Pockley AG (2001) Serum heat shock protein and anti-heat shock protein antibody levels in aging. Exp Gerontol 36:341–352
    • (2001) Exp Gerontol , vol.36 , pp. 341-352
    • Rea, I.M.1    McNerlan, S.2    Pockley, A.G.3
  • 237
    • 78751478982 scopus 로고    scopus 로고
    • Peptides and aptamers targeting HSP70: a novel approach for anticancer chemotherapy
    • COI: 1:CAS:528:DC%2BC3MXlsFKlsw%3D%3D, PID: 21224349
    • Rerole AL, Gobbo J, De TA et al (2011) Peptides and aptamers targeting HSP70: a novel approach for anticancer chemotherapy. Cancer Res 71:484–495
    • (2011) Cancer Res , vol.71 , pp. 484-495
    • Rerole, A.L.1    Gobbo, J.2    De, T.A.3
  • 238
    • 34250561475 scopus 로고
    • A new puffing pattern induced by temperature shock and DNP in Drosophila
    • COI: 1:CAS:528:DyaF3sXivVOgtw%3D%3D
    • Ritossa F (1962) A new puffing pattern induced by temperature shock and DNP in Drosophila. Experientia 18:571–573
    • (1962) Experientia , vol.18 , pp. 571-573
    • Ritossa, F.1
  • 239
    • 14644435819 scopus 로고    scopus 로고
    • Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms
    • COI: 1:CAS:528:DC%2BD2MXitFOks7o%3D, PID: 15741319
    • Rohde M, Daugaard M, Jensen MH et al (2005) Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms. Genes Dev 19:570–582
    • (2005) Genes Dev , vol.19 , pp. 570-582
    • Rohde, M.1    Daugaard, M.2    Jensen, M.H.3
  • 240
    • 84927927167 scopus 로고    scopus 로고
    • The elimination of miR-23a in heat-stressed cells promotes NOXA-induced cell death and is prevented by HSP70
    • COI: 1:STN:280:DC%2BC2Mzhtlyjsg%3D%3D, PID: 25429623
    • Roufayel R, Johnston DS, Mosser DD (2014) The elimination of miR-23a in heat-stressed cells promotes NOXA-induced cell death and is prevented by HSP70. Cell Death Dis 5:e1546
    • (2014) Cell Death Dis , vol.5 , pp. e1546
    • Roufayel, R.1    Johnston, D.S.2    Mosser, D.D.3
  • 241
    • 79960927001 scopus 로고    scopus 로고
    • Allosteric drugs: the interaction of antitumor compound MKT-077 with human Hsp70 chaperones
    • COI: 1:CAS:528:DC%2BC3MXpsFeisrw%3D, PID: 21708173
    • Rousaki A, Miyata Y, Jinwal UK et al (2011) Allosteric drugs: the interaction of antitumor compound MKT-077 with human Hsp70 chaperones. J Mol Biol 411:614–632
    • (2011) J Mol Biol , vol.411 , pp. 614-632
    • Rousaki, A.1    Miyata, Y.2    Jinwal, U.K.3
  • 242
    • 70450176418 scopus 로고    scopus 로고
    • The antibacterial effect of a proline-rich antibacterial peptide A3-APO
    • COI: 1:CAS:528:DC%2BD1MXhsVSmt73F, PID: 19747127
    • Rozgonyi F, Szabo D, Kocsis B et al (2009) The antibacterial effect of a proline-rich antibacterial peptide A3-APO. Curr Med Chem 16:3996–4002
    • (2009) Curr Med Chem , vol.16 , pp. 3996-4002
    • Rozgonyi, F.1    Szabo, D.2    Kocsis, B.3
  • 243
    • 0347285295 scopus 로고    scopus 로고
    • A trip to the ER: coping with stress
    • COI: 1:CAS:528:DC%2BD2cXjtFegsw%3D%3D, PID: 14729177
    • Rutkowski DT, Kaufman RJ (2004) A trip to the ER: coping with stress. Trends Cell Biol 14:20–28
    • (2004) Trends Cell Biol , vol.14 , pp. 20-28
    • Rutkowski, D.T.1    Kaufman, R.J.2
  • 244
    • 43949105866 scopus 로고    scopus 로고
    • Regulatory T cells and immune tolerance
    • COI: 1:CAS:528:DC%2BD1cXntFaltrg%3D, PID: 18510923
    • Sakaguchi S, Yamaguchi T, Nomura T, Ono M (2008) Regulatory T cells and immune tolerance. Cell 133:775–787
    • (2008) Cell , vol.133 , pp. 775-787
    • Sakaguchi, S.1    Yamaguchi, T.2    Nomura, T.3    Ono, M.4
  • 246
    • 0030750217 scopus 로고    scopus 로고
    • Expression of heat shock protein 72 in renal cell carcinoma: possible role and prognostic implications in cancer patients
    • COI: 1:CAS:528:DyaK2sXks1Srt7c%3D, PID: 9291808
    • Santarosa M, Favaro D, Quaia M, Galligioni E (1997) Expression of heat shock protein 72 in renal cell carcinoma: possible role and prognostic implications in cancer patients. Eur J Cancer 33:873–877
    • (1997) Eur J Cancer , vol.33 , pp. 873-877
    • Santarosa, M.1    Favaro, D.2    Quaia, M.3    Galligioni, E.4
  • 247
    • 68849112162 scopus 로고    scopus 로고
    • Binding of heat shock protein 70 to extracellular phosphatidylserine promotes killing of normoxic and hypoxic tumor cells
    • COI: 1:CAS:528:DC%2BD1MXpvFOltrg%3D, PID: 19289606
    • Schilling D, Gehrmann M, Steinem C et al (2009) Binding of heat shock protein 70 to extracellular phosphatidylserine promotes killing of normoxic and hypoxic tumor cells. FASEB J 23:2467–2477
    • (2009) FASEB J , vol.23 , pp. 2467-2477
    • Schilling, D.1    Gehrmann, M.2    Steinem, C.3
  • 248
    • 84893203556 scopus 로고    scopus 로고
    • Functional analysis of Hsp70 inhibitors
    • COI: 1:CAS:528:DC%2BC3sXhslylsLzJ, PID: 24265689
    • Schlecht R, Scholz SR, Dahmen H et al (2013) Functional analysis of Hsp70 inhibitors. PLoS ONE 8:e78443
    • (2013) PLoS ONE , vol.8 , pp. e78443
    • Schlecht, R.1    Scholz, S.R.2    Dahmen, H.3
  • 249
    • 10744227948 scopus 로고    scopus 로고
    • Chemosensitization by a non-apoptogenic heat shock protein 70-binding apoptosis-inducing factor mutant
    • COI: 1:CAS:528:DC%2BD3sXpvVagt78%3D, PID: 14678980
    • Schmitt E, Parcellier A, Gurbuxani S et al (2003) Chemosensitization by a non-apoptogenic heat shock protein 70-binding apoptosis-inducing factor mutant. Cancer Res 63:8233–8240
    • (2003) Cancer Res , vol.63 , pp. 8233-8240
    • Schmitt, E.1    Parcellier, A.2    Gurbuxani, S.3
  • 250
    • 33646241764 scopus 로고    scopus 로고
    • Heat shock protein 70 neutralization exerts potent antitumor effects in animal models of colon cancer and melanoma
    • COI: 1:CAS:528:DC%2BD28XjsFSlt7k%3D, PID: 16618741
    • Schmitt E, Maingret L, Puig PE et al (2006) Heat shock protein 70 neutralization exerts potent antitumor effects in animal models of colon cancer and melanoma. Cancer Res 66:4191–4197
    • (2006) Cancer Res , vol.66 , pp. 4191-4197
    • Schmitt, E.1    Maingret, L.2    Puig, P.E.3
  • 251
    • 45849091944 scopus 로고    scopus 로고
    • Structure of the Hsp110:Hsc70 nucleotide exchange machine
    • COI: 1:CAS:528:DC%2BD1cXpsFOgtLs%3D, PID: 18550409
    • Schuermann JP, Jiang J, Cuellar J et al (2008) Structure of the Hsp110:Hsc70 nucleotide exchange machine. Mol Cell 31:232–243
    • (2008) Mol Cell , vol.31 , pp. 232-243
    • Schuermann, J.P.1    Jiang, J.2    Cuellar, J.3
  • 252
    • 43249125196 scopus 로고    scopus 로고
    • New insights into the mechanism of heat shock response activation
    • COI: 1:CAS:528:DC%2BD1cXks1aiu7s%3D, PID: 18239856
    • Shamovsky I, Nudler E (2008) New insights into the mechanism of heat shock response activation. Cell Mol Life Sci 65:855–861
    • (2008) Cell Mol Life Sci , vol.65 , pp. 855-861
    • Shamovsky, I.1    Nudler, E.2
  • 253
    • 78649309029 scopus 로고    scopus 로고
    • The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase
    • COI: 1:CAS:528:DC%2BC3cXhtlSgur%2FP, PID: 20953191
    • Sharma SK, De Los RP, Christen P, Lustig A, Goloubinoff P (2010) The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase. Nat Chem Biol 6:914–920
    • (2010) Nat Chem Biol , vol.6 , pp. 914-920
    • Sharma, S.K.1    De Los, R.P.2    Christen, P.3    Lustig, A.4    Goloubinoff, P.5
  • 254
    • 84946559449 scopus 로고    scopus 로고
    • Shevtsov MA, Nikolaev BP, Yakovleva LY et al. (2015) 70-kDa heat shock protein coated magnetic nanocarriers as a nanovaccine for induction of anti-tumor immune response in experimental glioma. J Control Release
    • Shevtsov MA, Nikolaev BP, Yakovleva LY et al. (2015) 70-kDa heat shock protein coated magnetic nanocarriers as a nanovaccine for induction of anti-tumor immune response in experimental glioma. J Control Release
  • 255
    • 55849121192 scopus 로고    scopus 로고
    • Green tea extracts for the prevention of metachronous colorectal adenomas: a pilot study
    • COI: 1:CAS:528:DC%2BD1cXhtlCkur7E, PID: 18990744
    • Shimizu M, Fukutomi Y, Ninomiya M et al (2008) Green tea extracts for the prevention of metachronous colorectal adenomas: a pilot study. Cancer Epidemiol Biomarkers Prev 17:3020–3025
    • (2008) Cancer Epidemiol Biomarkers Prev , vol.17 , pp. 3020-3025
    • Shimizu, M.1    Fukutomi, Y.2    Ninomiya, M.3
  • 256
    • 0034058193 scopus 로고    scopus 로고
    • Clinical application of malignancy potential grading as a prognostic factor of human esophageal cancers
    • COI: 1:STN:280:DC%2BD3c3nvFSgtA%3D%3D, PID: 10819064
    • Shiozaki H, Doki Y, Kawanishi K et al (2000) Clinical application of malignancy potential grading as a prognostic factor of human esophageal cancers. Surgery 127:552–561
    • (2000) Surgery , vol.127 , pp. 552-561
    • Shiozaki, H.1    Doki, Y.2    Kawanishi, K.3
  • 257
    • 13244278043 scopus 로고    scopus 로고
    • Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange
    • COI: 1:CAS:528:DC%2BD2MXhs1Oitrc%3D, PID: 15694338
    • Shomura Y, Dragovic Z, Chang HC et al (2005) Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange. Mol Cell 17:367–379
    • (2005) Mol Cell , vol.17 , pp. 367-379
    • Shomura, Y.1    Dragovic, Z.2    Chang, H.C.3
  • 258
    • 46349093110 scopus 로고    scopus 로고
    • Induction of the human heat shock promoter HSP70B by nutritional stress: implications for cancer gene therapy
    • COI: 1:CAS:528:DC%2BD1cXnsl2rt7w%3D, PID: 18584345
    • Siddiqui F, Avery PR, Li CY et al (2008) Induction of the human heat shock promoter HSP70B by nutritional stress: implications for cancer gene therapy. Cancer Invest 26:553–561
    • (2008) Cancer Invest , vol.26 , pp. 553-561
    • Siddiqui, F.1    Avery, P.R.2    Li, C.Y.3
  • 259
    • 0034608387 scopus 로고    scopus 로고
    • Cross-presentation of glycoprotein 96-associated antigens on major histocompatibility complex class I molecules requires receptor-mediated endocytosis
    • COI: 1:CAS:528:DC%2BD3cXjvFyntb0%3D, PID: 10839811
    • Singh-Jasuja H, Toes RE, Spee P et al (2000) Cross-presentation of glycoprotein 96-associated antigens on major histocompatibility complex class I molecules requires receptor-mediated endocytosis. J Exp Med 191:1965–1974
    • (2000) J Exp Med , vol.191 , pp. 1965-1974
    • Singh-Jasuja, H.1    Toes, R.E.2    Spee, P.3
  • 260
    • 0035911242 scopus 로고    scopus 로고
    • Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) contributes to interferon gamma-dependent natural killer cell protection from tumor metastasis
    • COI: 1:CAS:528:DC%2BD3MXitFKhs7Y%3D, PID: 11257133
    • Smyth MJ, Cretney E, Takeda K et al (2001) Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) contributes to interferon gamma-dependent natural killer cell protection from tumor metastasis. J Exp Med 193:661–670
    • (2001) J Exp Med , vol.193 , pp. 661-670
    • Smyth, M.J.1    Cretney, E.2    Takeda, K.3
  • 261
    • 84926683486 scopus 로고    scopus 로고
    • Heat shock protein 70 (Hsp70) peptide activated natural killer (NK) cells for the treatment of patients with non-small cell lung cancer (NSCLC) after radiochemotherapy (RCTx)—from preclinical studies to a clinical phase II trial
    • PID: 25926832
    • Specht HM, Ahrens N, Blankenstein C et al (2015) Heat shock protein 70 (Hsp70) peptide activated natural killer (NK) cells for the treatment of patients with non-small cell lung cancer (NSCLC) after radiochemotherapy (RCTx)—from preclinical studies to a clinical phase II trial. Front Immunol 6:162
    • (2015) Front Immunol , vol.6 , pp. 162
    • Specht, H.M.1    Ahrens, N.2    Blankenstein, C.3
  • 262
    • 16844371156 scopus 로고    scopus 로고
    • Immunotherapy for human cancer using heat shock protein-peptide complexes
    • COI: 1:CAS:528:DC%2BD28XktVamtg%3D%3D, PID: 15717943
    • Srivastava PK (2005) Immunotherapy for human cancer using heat shock protein-peptide complexes. Curr Oncol Rep 7:104–108
    • (2005) Curr Oncol Rep , vol.7 , pp. 104-108
    • Srivastava, P.K.1
  • 263
    • 79551657031 scopus 로고    scopus 로고
    • Targeting membrane heat-shock protein 70 (Hsp70) on tumors by cmHsp70.1 antibody
    • COI: 1:CAS:528:DC%2BC3MXosF2qsw%3D%3D, PID: 21187371
    • Stangl S, Gehrmann M, Riegger J et al (2011) Targeting membrane heat-shock protein 70 (Hsp70) on tumors by cmHsp70.1 antibody. Proc Natl Acad Sci U S A 108:733–738
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 733-738
    • Stangl, S.1    Gehrmann, M.2    Riegger, J.3
  • 264
    • 33244474580 scopus 로고    scopus 로고
    • Hsp70 inhibits heat-induced apoptosis upstream of mitochondria by preventing Bax translocation
    • COI: 1:CAS:528:DC%2BD2MXht1SktLjE, PID: 16172114
    • Stankiewicz AR, Lachapelle G, Foo CP, Radicioni SM, Mosser DD (2005) Hsp70 inhibits heat-induced apoptosis upstream of mitochondria by preventing Bax translocation. J Biol Chem 280:38729–38739
    • (2005) J Biol Chem , vol.280 , pp. 38729-38739
    • Stankiewicz, A.R.1    Lachapelle, G.2    Foo, C.P.3    Radicioni, S.M.4    Mosser, D.D.5
  • 265
    • 69849089290 scopus 로고    scopus 로고
    • 2-Phenylacetylenesulfonamide (PAS) induces p53-independent apoptotic killing of B-chronic lymphocytic leukemia (CLL) cells
    • COI: 1:CAS:528:DC%2BD1MXhtVSgsbfK, PID: 19515722
    • Steele AJ, Prentice AG, Hoffbrand AV et al (2009) 2-Phenylacetylenesulfonamide (PAS) induces p53-independent apoptotic killing of B-chronic lymphocytic leukemia (CLL) cells. Blood 114:1217–1225
    • (2009) Blood , vol.114 , pp. 1217-1225
    • Steele, A.J.1    Prentice, A.G.2    Hoffbrand, A.V.3
  • 266
    • 32144463144 scopus 로고    scopus 로고
    • Opposing actions of STAT-1 and STAT-3
    • COI: 1:CAS:528:DC%2BD2MXhtFCjtrnO, PID: 16243709
    • Stephanou A, Latchman DS (2005) Opposing actions of STAT-1 and STAT-3. Growth Factors 23:177–182
    • (2005) Growth Factors , vol.23 , pp. 177-182
    • Stephanou, A.1    Latchman, D.S.2
  • 267
    • 0033555548 scopus 로고    scopus 로고
    • Signal transducer and activator of transcription-1 and heat shock factor-1 interact and activate the transcription of the Hsp-70 and Hsp-90beta gene promoters
    • COI: 1:CAS:528:DyaK1MXpsFOntw%3D%3D, PID: 9880553
    • Stephanou A, Isenberg DA, Nakajima K, Latchman DS (1999) Signal transducer and activator of transcription-1 and heat shock factor-1 interact and activate the transcription of the Hsp-70 and Hsp-90beta gene promoters. J Biol Chem 274:1723–1728
    • (1999) J Biol Chem , vol.274 , pp. 1723-1728
    • Stephanou, A.1    Isenberg, D.A.2    Nakajima, K.3    Latchman, D.S.4
  • 268
    • 84859489665 scopus 로고    scopus 로고
    • Inducible heat shock protein 70 reduces T cell responses and stimulatory capacity of monocyte-derived dendritic cells
    • COI: 1:CAS:528:DC%2BC38XltVyku7Y%3D, PID: 22334699
    • Stocki P, Wang XN, Dickinson AM (2012) Inducible heat shock protein 70 reduces T cell responses and stimulatory capacity of monocyte-derived dendritic cells. J Biol Chem 287:12387–12394
    • (2012) J Biol Chem , vol.287 , pp. 12387-12394
    • Stocki, P.1    Wang, X.N.2    Dickinson, A.M.3
  • 269
    • 0031472407 scopus 로고    scopus 로고
    • Heat shock protein 72/73 in relation to cytoplasmic p53 expression and prognosis in colorectal adenocarcinomas
    • COI: 1:CAS:528:DyaK1cXis1yjsA%3D%3D, PID: 9421355
    • Sun XF, Zhang H, Carstensen J, Jansson A, Nordenskjold B (1997) Heat shock protein 72/73 in relation to cytoplasmic p53 expression and prognosis in colorectal adenocarcinomas. Int J Cancer 74:600–604
    • (1997) Int J Cancer , vol.74 , pp. 600-604
    • Sun, X.F.1    Zhang, H.2    Carstensen, J.3    Jansson, A.4    Nordenskjold, B.5
  • 270
    • 77957272491 scopus 로고    scopus 로고
    • Peptide-binding sites as revealed by the crystal structures of the human Hsp40 Hdj1 C-terminal domain in complex with the octapeptide from human Hsp70
    • COI: 1:CAS:528:DC%2BC3cXhtFehurfF, PID: 20809635
    • Suzuki H, Noguchi S, Arakawa H et al (2010) Peptide-binding sites as revealed by the crystal structures of the human Hsp40 Hdj1 C-terminal domain in complex with the octapeptide from human Hsp70. Biochemistry 49:8577–8584
    • (2010) Biochemistry , vol.49 , pp. 8577-8584
    • Suzuki, H.1    Noguchi, S.2    Arakawa, H.3
  • 271
    • 79951857812 scopus 로고    scopus 로고
    • BAG3 (BCL2-associated athanogene 3) interacts with MMP-2 to positively regulate invasion by ovarian carcinoma cells
    • COI: 1:CAS:528:DC%2BC3MXisFGms78%3D, PID: 21316839
    • Suzuki M, Iwasaki M, Sugio A et al (2011) BAG3 (BCL2-associated athanogene 3) interacts with MMP-2 to positively regulate invasion by ovarian carcinoma cells. Cancer Lett 303:65–71
    • (2011) Cancer Lett , vol.303 , pp. 65-71
    • Suzuki, M.1    Iwasaki, M.2    Sugio, A.3
  • 272
    • 84935906364 scopus 로고    scopus 로고
    • A3.30 Plasma level of HSP70 protein is increased in Czech patients with idiopathic inflammatory myopathy
    • Svitalkova T, Remakova M, Plestilova L et al (2014) A3.30 Plasma level of HSP70 protein is increased in Czech patients with idiopathic inflammatory myopathy. Ann Rheum Dis 73(Suppl 1):A54
    • (2014) Ann Rheum Dis , vol.73 , pp. A54
    • Svitalkova, T.1    Remakova, M.2    Plestilova, L.3
  • 273
    • 0037334496 scopus 로고    scopus 로고
    • Clinical significance of heat shock protein-70 expression in bladder cancer
    • PID: 12639682
    • Syrigos KN, Harrington KJ, Karayiannakis AJ et al (2003) Clinical significance of heat shock protein-70 expression in bladder cancer. Urology 61:677–680
    • (2003) Urology , vol.61 , pp. 677-680
    • Syrigos, K.N.1    Harrington, K.J.2    Karayiannakis, A.J.3
  • 274
    • 0033534588 scopus 로고    scopus 로고
    • An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators
    • COI: 1:CAS:528:DyaK1MXmtFGmtg%3D%3D, PID: 9873016
    • Takayama S, Xie Z, Reed JC (1999) An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators. J Biol Chem 274:781–786
    • (1999) J Biol Chem , vol.274 , pp. 781-786
    • Takayama, S.1    Xie, Z.2    Reed, J.C.3
  • 275
    • 84858967994 scopus 로고    scopus 로고
    • HSP90 and HSP70 proteins are essential for stabilization and activation of WASF3 metastasis-promoting protein
    • COI: 1:CAS:528:DC%2BC38XktlKkurc%3D, PID: 22315230
    • Teng Y, Ngoka L, Mei Y, Lesoon L, Cowell JK (2012) HSP90 and HSP70 proteins are essential for stabilization and activation of WASF3 metastasis-promoting protein. J Biol Chem 287:10051–10059
    • (2012) J Biol Chem , vol.287 , pp. 10051-10059
    • Teng, Y.1    Ngoka, L.2    Mei, Y.3    Lesoon, L.4    Cowell, J.K.5
  • 276
    • 3242664245 scopus 로고    scopus 로고
    • Cardiovascular disease delay in centenarian offspring: role of heat shock proteins
    • COI: 1:CAS:528:DC%2BD2cXms12nsLc%3D, PID: 15247074
    • Terry DF, McCormick M, Andersen S et al (2004) Cardiovascular disease delay in centenarian offspring: role of heat shock proteins. Ann N Y Acad Sci 1019:502–505
    • (2004) Ann N Y Acad Sci , vol.1019 , pp. 502-505
    • Terry, D.F.1    McCormick, M.2    Andersen, S.3
  • 277
    • 33845446813 scopus 로고    scopus 로고
    • Role of scavenger receptors in the binding and internalization of heat shock protein 70
    • COI: 1:CAS:528:DC%2BD28Xht1Kitr%2FJ, PID: 17142759
    • Theriault JR, Adachi H, Calderwood SK (2006) Role of scavenger receptors in the binding and internalization of heat shock protein 70. J Immunol 177:8604–8611
    • (2006) J Immunol , vol.177 , pp. 8604-8611
    • Theriault, J.R.1    Adachi, H.2    Calderwood, S.K.3
  • 278
    • 22144458740 scopus 로고    scopus 로고
    • Expression of heat-shock proteins is associated with major adverse prognostic factors in acute myeloid leukemia
    • COI: 1:CAS:528:DC%2BD2MXmsVCrs70%3D, PID: 16038731
    • Thomas X, Campos L, Mounier C et al (2005) Expression of heat-shock proteins is associated with major adverse prognostic factors in acute myeloid leukemia. Leuk Res 29:1049–1058
    • (2005) Leuk Res , vol.29 , pp. 1049-1058
    • Thomas, X.1    Campos, L.2    Mounier, C.3
  • 279
    • 0016373748 scopus 로고
    • Protein synthesis in salivary glands of Drosophila melanogaster: relation to chromosome puffs
    • COI: 1:CAS:528:DyaE2cXks1Wgsr4%3D, PID: 4219221
    • Tissieres A, Mitchell HK, Tracy UM (1974) Protein synthesis in salivary glands of Drosophila melanogaster: relation to chromosome puffs. J Mol Biol 84:389–398
    • (1974) J Mol Biol , vol.84 , pp. 389-398
    • Tissieres, A.1    Mitchell, H.K.2    Tracy, U.M.3
  • 280
    • 0031692853 scopus 로고    scopus 로고
    • Heat shock protein 72 expression in osteosarcomas correlates with good response to neoadjuvant chemotherapy
    • COI: 1:CAS:528:DyaK1cXntFGgsbo%3D, PID: 9781640
    • Trieb K, Lechleitner T, Lang S et al (1998) Heat shock protein 72 expression in osteosarcomas correlates with good response to neoadjuvant chemotherapy. Hum Pathol 29:1050–1055
    • (1998) Hum Pathol , vol.29 , pp. 1050-1055
    • Trieb, K.1    Lechleitner, T.2    Lang, S.3
  • 281
    • 33644845097 scopus 로고    scopus 로고
    • Heat shock protein and innate immunity
    • COI: 1:CAS:528:DC%2BD2cXovFyjs7o%3D, PID: 16225770
    • Tsan MF, Gao B (2004) Heat shock protein and innate immunity. Cell Mol Immunol 1:274–279
    • (2004) Cell Mol Immunol , vol.1 , pp. 274-279
    • Tsan, M.F.1    Gao, B.2
  • 282
    • 84940890580 scopus 로고    scopus 로고
    • MicroRNAs mediated targeting on the Yin-yang dynamics of DNA methylation in disease and development
    • COI: 1:CAS:528:DC%2BC2MXos1entb8%3D, PID: 25979370
    • Tu J, Liao J, Luk AC et al (2015) MicroRNAs mediated targeting on the Yin-yang dynamics of DNA methylation in disease and development. Int J Biochem Cell Biol 67:115–120
    • (2015) Int J Biochem Cell Biol , vol.67 , pp. 115-120
    • Tu, J.1    Liao, J.2    Luk, A.C.3
  • 283
    • 55249125453 scopus 로고    scopus 로고
    • Functional divergence between co-chaperones of Hsc70
    • COI: 1:CAS:528:DC%2BD1cXhtFKgsr%2FL, PID: 18684711
    • Tzankov S, Wong MJ, Shi K, Nassif C, Young JC (2008) Functional divergence between co-chaperones of Hsc70. J Biol Chem 283:27100–27109
    • (2008) J Biol Chem , vol.283 , pp. 27100-27109
    • Tzankov, S.1    Wong, M.J.2    Shi, K.3    Nassif, C.4    Young, J.C.5
  • 284
    • 33745600210 scopus 로고    scopus 로고
    • Toll-like receptor-dependent activation of antigen presenting cells by Hsp60, gp96 and Hsp70
    • New York: Cambridge University Press
    • Vabulas, R.M., and Wagner, H. (2005). Toll-like receptor-dependent activation of antigen presenting cells by Hsp60, gp96 and Hsp70. In: Molecular chaperones and cell signalling, eds. B. Henderson and A. G. Pockley (New York, Cambridge University Press), 113–132
    • (2005) B. Henderson and A. G. Pockley , pp. 113-132
    • Vabulas, R.M.1    Wagner, H.2
  • 285
    • 44849084963 scopus 로고    scopus 로고
    • Hsp70 translocates into the plasma membrane after stress and is released into the extracellular environment in a membrane-associated form that activates macrophages
    • COI: 1:CAS:528:DC%2BD1cXisl2jtLc%3D, PID: 18322243
    • Vega VL, Rodriguez-Silva M, Frey T et al (2008) Hsp70 translocates into the plasma membrane after stress and is released into the extracellular environment in a membrane-associated form that activates macrophages. J Immunol 180:4299–4307
    • (2008) J Immunol , vol.180 , pp. 4299-4307
    • Vega, V.L.1    Rodriguez-Silva, M.2    Frey, T.3
  • 286
    • 84871548554 scopus 로고    scopus 로고
    • HSP70 enhances immunosuppressive function of CD4(+)CD25(+)FoxP3(+) T regulatory cells and cytotoxicity in CD4(+)CD25(−) T cells
    • COI: 1:CAS:528:DC%2BC3sXmtVSrtg%3D%3D, PID: 23300563
    • Wachstein J, Tischer S, Figueiredo C et al (2012) HSP70 enhances immunosuppressive function of CD4(+)CD25(+)FoxP3(+) T regulatory cells and cytotoxicity in CD4(+)CD25(−) T cells. PLoS ONE 7:e51747
    • (2012) PLoS ONE , vol.7 , pp. e51747
    • Wachstein, J.1    Tischer, S.2    Figueiredo, C.3
  • 287
    • 0034671731 scopus 로고    scopus 로고
    • Selective toxicity of MKT-077 to cancer cells is mediated by its binding to the hsp70 family protein mot-2 and reactivation of p53 function
    • COI: 1:CAS:528:DC%2BD3MXjsVKrsA%3D%3D, PID: 11156371
    • Wadhwa R, Sugihara T, Yoshida A et al (2000) Selective toxicity of MKT-077 to cancer cells is mediated by its binding to the hsp70 family protein mot-2 and reactivation of p53 function. Cancer Res 60:6818–6821
    • (2000) Cancer Res , vol.60 , pp. 6818-6821
    • Wadhwa, R.1    Sugihara, T.2    Yoshida, A.3
  • 288
    • 0036499004 scopus 로고    scopus 로고
    • Heat-shock proteins as activators of the innate immune system
    • COI: 1:CAS:528:DC%2BD38XhsFahtrc%3D, PID: 11864840
    • Wallin RP, Lundqvist A, More SH et al (2002) Heat-shock proteins as activators of the innate immune system. Trends Immunol 23:130–135
    • (2002) Trends Immunol , vol.23 , pp. 130-135
    • Wallin, R.P.1    Lundqvist, A.2    More, S.H.3
  • 289
    • 79955478704 scopus 로고    scopus 로고
    • RNAi knockdown of Hop (Hsp70/Hsp90 organising protein) decreases invasion via MMP-2 down regulation
    • COI: 1:CAS:528:DC%2BC3MXlsV2nt7Y%3D, PID: 21470770
    • Walsh N, Larkin A, Swan N et al (2011) RNAi knockdown of Hop (Hsp70/Hsp90 organising protein) decreases invasion via MMP-2 down regulation. Cancer Lett 306:180–189
    • (2011) Cancer Lett , vol.306 , pp. 180-189
    • Walsh, N.1    Larkin, A.2    Swan, N.3
  • 290
    • 10744220813 scopus 로고    scopus 로고
    • Novel heat shock protein Hsp70L1 activates dendritic cells and acts as a Th1 polarizing adjuvant
    • COI: 1:CAS:528:DC%2BD2cXhvVOhsb4%3D, PID: 14592822
    • Wan T, Zhou X, Chen G et al (2004) Novel heat shock protein Hsp70L1 activates dendritic cells and acts as a Th1 polarizing adjuvant. Blood 103:1747–1754
    • (2004) Blood , vol.103 , pp. 1747-1754
    • Wan, T.1    Zhou, X.2    Chen, G.3
  • 291
    • 77952332824 scopus 로고    scopus 로고
    • Inhibition of hsp70 by methylene blue affects signaling protein function and ubiquitination and modulates polyglutamine protein degradation
    • COI: 1:CAS:528:DC%2BC3cXmtVyks7s%3D, PID: 20348093
    • Wang AM, Morishima Y, Clapp KM et al (2010) Inhibition of hsp70 by methylene blue affects signaling protein function and ubiquitination and modulates polyglutamine protein degradation. J Biol Chem 285:15714–15723
    • (2010) J Biol Chem , vol.285 , pp. 15714-15723
    • Wang, A.M.1    Morishima, Y.2    Clapp, K.M.3
  • 292
    • 79960385035 scopus 로고    scopus 로고
    • Induction of cytotoxic T lymphocytes against ovarian cancer-initiating cells
    • COI: 1:CAS:528:DC%2BC3MXhtVKlsrvM, PID: 21154809
    • Weng D, Song B, Durfee J et al (2011) Induction of cytotoxic T lymphocytes against ovarian cancer-initiating cells. Int J Cancer 129:1990–2001
    • (2011) Int J Cancer , vol.129 , pp. 1990-2001
    • Weng, D.1    Song, B.2    Durfee, J.3
  • 293
    • 84880111912 scopus 로고    scopus 로고
    • Immunotherapy of radioresistant mammary tumors with early metastasis using molecular chaperone vaccines combined with ionizing radiation
    • COI: 1:CAS:528:DC%2BC3sXhtVKgtb%2FJ, PID: 23772032
    • Weng D, Song B, Koido S, Calderwood SK, Gong J (2013) Immunotherapy of radioresistant mammary tumors with early metastasis using molecular chaperone vaccines combined with ionizing radiation. J Immunol 191:755–763
    • (2013) J Immunol , vol.191 , pp. 755-763
    • Weng, D.1    Song, B.2    Koido, S.3    Calderwood, S.K.4    Gong, J.5
  • 294
    • 60749101582 scopus 로고    scopus 로고
    • Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1
    • COI: 1:CAS:528:DC%2BD1MXitVyntr0%3D, PID: 19229036
    • Westerheide SD, Anckar J, Stevens SM Jr, Sistonen L, Morimoto RI (2009) Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1. Science 323:1063–1066
    • (2009) Science , vol.323 , pp. 1063-1066
    • Westerheide, S.D.1    Anckar, J.2    Stevens, S.M.3    Sistonen, L.4    Morimoto, R.I.5
  • 295
    • 0025955517 scopus 로고
    • Stress-induced oligomerization and chromosomal relocalization of heat-shock factor
    • COI: 1:CAS:528:DyaK3MXmsleruro%3D, PID: 1944557
    • Westwood JT, Clos J, Wu C (1991) Stress-induced oligomerization and chromosomal relocalization of heat-shock factor. Nature 353:822–827
    • (1991) Nature , vol.353 , pp. 822-827
    • Westwood, J.T.1    Clos, J.2    Wu, C.3
  • 296
    • 0037452541 scopus 로고    scopus 로고
    • 3′Sulfogalactolipid binding specifically inhibits Hsp70 ATPase activity in vitro
    • COI: 1:CAS:528:DC%2BD3sXjvFeisA%3D%3D, PID: 12578374
    • Whetstone H, Lingwood C (2003) 3′Sulfogalactolipid binding specifically inhibits Hsp70 ATPase activity in vitro. Biochemistry 42:1611–1617
    • (2003) Biochemistry , vol.42 , pp. 1611-1617
    • Whetstone, H.1    Lingwood, C.2
  • 297
    • 33947530122 scopus 로고    scopus 로고
    • De-repression of heat shock transcription factor-1 in interleukin-6-treated hepatocytes is mediated by downregulation of glycogen synthase kinase 3beta and MAPK/ERK-1
    • COI: 1:CAS:528:DC%2BD2sXivVOnsLg%3D, PID: 17273789
    • Wigmore SJ, Sangster K, McNally SJ et al (2007) De-repression of heat shock transcription factor-1 in interleukin-6-treated hepatocytes is mediated by downregulation of glycogen synthase kinase 3beta and MAPK/ERK-1. Int J Mol Med 19:413–420
    • (2007) Int J Mol Med , vol.19 , pp. 413-420
    • Wigmore, S.J.1    Sangster, K.2    McNally, S.J.3
  • 298
    • 54749143530 scopus 로고    scopus 로고
    • An apoptosis-inducing small molecule that binds to heat shock protein 70
    • COI: 1:CAS:528:DC%2BD1cXht1SjtbbL, PID: 18729127
    • Williams DR, Ko SK, Park S, Lee MR, Shin I (2008) An apoptosis-inducing small molecule that binds to heat shock protein 70. Angew Chem Int Ed Engl 47:7466–7469
    • (2008) Angew Chem Int Ed Engl , vol.47 , pp. 7466-7469
    • Williams, D.R.1    Ko, S.K.2    Park, S.3    Lee, M.R.4    Shin, I.5
  • 299
    • 64349121987 scopus 로고    scopus 로고
    • Novel adenosine-derived inhibitors of 70 kDa heat shock protein, discovered through structure-based design
    • COI: 1:CAS:528:DC%2BD1MXis1arsbg%3D, PID: 19256508
    • Williamson DS, Borgognoni J, Clay A et al (2009) Novel adenosine-derived inhibitors of 70 kDa heat shock protein, discovered through structure-based design. J Med Chem 52:1510–1513
    • (2009) J Med Chem , vol.52 , pp. 1510-1513
    • Williamson, D.S.1    Borgognoni, J.2    Clay, A.3
  • 300
    • 67349200953 scopus 로고    scopus 로고
    • Tau aggregation inhibitor (TAI) therapy with Rember™ arrests disease progression in mild and moderate Alzheimer’s disease over 50 weeks
    • Wischik CM, Betham P, Wischik DJ, Seng KM (2008) Tau aggregation inhibitor (TAI) therapy with Rember™ arrests disease progression in mild and moderate Alzheimer’s disease over 50 weeks. Alzheimers Dement 4:T167
    • (2008) Alzheimers Dement , vol.4 , pp. T167
    • Wischik, C.M.1    Betham, P.2    Wischik, D.J.3    Seng, K.M.4
  • 301
    • 61449200234 scopus 로고    scopus 로고
    • Inhibition of simian virus 40 replication by targeting the molecular chaperone function and ATPase activity of T antigen
    • COI: 1:CAS:528:DC%2BD1MXivVCrtLo%3D, PID: 19200446
    • Wright CM, Seguin SP, Fewell SW et al (2009) Inhibition of simian virus 40 replication by targeting the molecular chaperone function and ATPase activity of T antigen. Virus Res 141:71–80
    • (2009) Virus Res , vol.141 , pp. 71-80
    • Wright, C.M.1    Seguin, S.P.2    Fewell, S.W.3
  • 302
    • 13444250890 scopus 로고    scopus 로고
    • DeltaNp63alpha up-regulates the Hsp70 gene in human cancer
    • COI: 1:CAS:528:DC%2BD2MXhtVWntrk%3D, PID: 15705872
    • Wu G, Osada M, Guo Z et al (2005) DeltaNp63alpha up-regulates the Hsp70 gene in human cancer. Cancer Res 65:758–766
    • (2005) Cancer Res , vol.65 , pp. 758-766
    • Wu, G.1    Osada, M.2    Guo, Z.3
  • 303
    • 78650864456 scopus 로고    scopus 로고
    • Induction of HSPA4 and HSPA14 by NBS1 overexpression contributes to NBS1-induced in vitro metastatic and transformation activity
    • PID: 21208456
    • Wu CY, Lin CT, Wu MZ, Wu KJ (2011) Induction of HSPA4 and HSPA14 by NBS1 overexpression contributes to NBS1-induced in vitro metastatic and transformation activity. J Biomed Sci 18:1
    • (2011) J Biomed Sci , vol.18 , pp. 1
    • Wu, C.Y.1    Lin, C.T.2    Wu, M.Z.3    Wu, K.J.4
  • 304
    • 84955211536 scopus 로고    scopus 로고
    • MiR-133b-5p regulates the expression of the heat shock protein 70 during rat neuronal cell apoptosis induced by the gp120 V3 loop peptide
    • Xia C, Cai Y, Lin Y et al. (2015) MiR-133b-5p regulates the expression of the heat shock protein 70 during rat neuronal cell apoptosis induced by the gp120 V3 loop peptide. J Med Virol
    • (2015) J Med Virol
    • Xia, C.1    Cai, Y.2    Lin, Y.3
  • 305
    • 84865150278 scopus 로고    scopus 로고
    • Development of stable HSPA1A promoter-driven luciferase reporter HepG2 cells for assessing the toxicity of organic pollutants present in air
    • COI: 1:CAS:528:DC%2BC38XhtFWhsr3P, PID: 22367790
    • Xin L, Li X, Deng H et al (2012) Development of stable HSPA1A promoter-driven luciferase reporter HepG2 cells for assessing the toxicity of organic pollutants present in air. Cell Stress Chaperones 17:567–576
    • (2012) Cell Stress Chaperones , vol.17 , pp. 567-576
    • Xin, L.1    Li, X.2    Deng, H.3
  • 306
    • 33947267567 scopus 로고    scopus 로고
    • High levels of heat shock protein Hsp72 in cancer cells suppress default senescence pathways
    • COI: 1:CAS:528:DC%2BD2sXitlSjsbo%3D, PID: 17332370
    • Yaglom JA, Gabai VL, Sherman MY (2007) High levels of heat shock protein Hsp72 in cancer cells suppress default senescence pathways. Cancer Res 67:2373–2381
    • (2007) Cancer Res , vol.67 , pp. 2373-2381
    • Yaglom, J.A.1    Gabai, V.L.2    Sherman, M.Y.3
  • 307
    • 0037469068 scopus 로고    scopus 로고
    • Monotherapy with LF 15-0195, an analogue of 15-deoxyspergualin, significantly prolongs renal allograft survival in monkeys
    • COI: 1:CAS:528:DC%2BD3sXjt1alsb0%3D, PID: 12717197
    • Yang H, Chen G, Kanai N et al (2003) Monotherapy with LF 15-0195, an analogue of 15-deoxyspergualin, significantly prolongs renal allograft survival in monkeys. Transplantation 75:1166–1171
    • (2003) Transplantation , vol.75 , pp. 1166-1171
    • Yang, H.1    Chen, G.2    Kanai, N.3
  • 308
    • 35348923465 scopus 로고    scopus 로고
    • Tea and cancer prevention: molecular mechanisms and human relevance
    • COI: 1:CAS:528:DC%2BD2sXhtF2mtL7J, PID: 17234229
    • Yang CS, Lambert JD, Ju J, Lu G, Sang S (2007) Tea and cancer prevention: molecular mechanisms and human relevance. Toxicol Appl Pharmacol 224:265–273
    • (2007) Toxicol Appl Pharmacol , vol.224 , pp. 265-273
    • Yang, C.S.1    Lambert, J.D.2    Ju, J.3    Lu, G.4    Sang, S.5
  • 309
    • 84862810272 scopus 로고    scopus 로고
    • Hsp70 promotes chemoresistance by blocking Bax mitochondrial translocation in ovarian cancer cells
    • COI: 1:CAS:528:DC%2BC38XktlGltrc%3D, PID: 22281241
    • Yang X, Wang J, Zhou Y et al (2012) Hsp70 promotes chemoresistance by blocking Bax mitochondrial translocation in ovarian cancer cells. Cancer Lett 321:137–143
    • (2012) Cancer Lett , vol.321 , pp. 137-143
    • Yang, X.1    Wang, J.2    Zhou, Y.3
  • 310
    • 84923002608 scopus 로고    scopus 로고
    • Upregulation of heat shock proteins (HSPA12A, HSP90B1, HSPA4, HSPA5 and HSPA6) in tumour tissues is associated with poor outcomes from HBV-related early-stage hepatocellular carcinoma
    • PID: 25798051
    • Yang Z, Zhuang L, Szatmary P et al (2015) Upregulation of heat shock proteins (HSPA12A, HSP90B1, HSPA4, HSPA5 and HSPA6) in tumour tissues is associated with poor outcomes from HBV-related early-stage hepatocellular carcinoma. Int J Med Sci 12:256–263
    • (2015) Int J Med Sci , vol.12 , pp. 256-263
    • Yang, Z.1    Zhuang, L.2    Szatmary, P.3
  • 311
    • 63649126549 scopus 로고    scopus 로고
    • A novel role of microRNA in late preconditioning: upregulation of endothelial nitric oxide synthase and heat shock protein 70
    • COI: 1:CAS:528:DC%2BD1MXisFelu7w%3D, PID: 19213952
    • Yin C, Salloum FN, Kukreja RC (2009) A novel role of microRNA in late preconditioning: upregulation of endothelial nitric oxide synthase and heat shock protein 70. Circ Res 104:572–575
    • (2009) Circ Res , vol.104 , pp. 572-575
    • Yin, C.1    Salloum, F.N.2    Kukreja, R.C.3
  • 312
    • 77958596589 scopus 로고    scopus 로고
    • Down-regulation of heat-shock protein 70 (HSP-70) correlated with responsiveness to neoadjuvant aromatase inhibitor therapy in breast cancer patients
    • COI: 1:CAS:528:DC%2BC3cXhtlGksbjE, PID: 20944124
    • Yiu CC, Chanplakorn N, Chan MS et al (2010) Down-regulation of heat-shock protein 70 (HSP-70) correlated with responsiveness to neoadjuvant aromatase inhibitor therapy in breast cancer patients. Anticancer Res 30:3465–3472
    • (2010) Anticancer Res , vol.30 , pp. 3465-3472
    • Yiu, C.C.1    Chanplakorn, N.2    Chan, M.S.3
  • 313
    • 84904130683 scopus 로고    scopus 로고
    • miR-16-1 promotes the aberrant alpha-synuclein accumulation in parkinson disease via targeting heat shock protein 70
    • Zhang Z, Cheng Y (2014) miR-16-1 promotes the aberrant alpha-synuclein accumulation in parkinson disease via targeting heat shock protein 70. Scientific World J 2014:938348
    • (2014) Scientific World J , vol.2014 , pp. 938348
    • Zhang, Z.1    Cheng, Y.2
  • 314
    • 0029937037 scopus 로고    scopus 로고
    • Structural analysis of substrate binding by the molecular chaperone DnaK
    • COI: 1:CAS:528:DyaK28Xjs1ejtb0%3D, PID: 8658133
    • Zhu X, Zhao X, Burkholder WF et al (1996) Structural analysis of substrate binding by the molecular chaperone DnaK. Science 272:1606–1614
    • (1996) Science , vol.272 , pp. 1606-1614
    • Zhu, X.1    Zhao, X.2    Burkholder, W.F.3
  • 315
    • 0030864750 scopus 로고    scopus 로고
    • HSP70-2 is required for CDC2 kinase activity in meiosis I of mouse spermatocytes
    • COI: 1:CAS:528:DyaK2sXltlSmtro%3D, PID: 9247342
    • Zhu D, Dix DJ, Eddy EM (1997) HSP70-2 is required for CDC2 kinase activity in meiosis I of mouse spermatocytes. Development 124:3007–3014
    • (1997) Development , vol.124 , pp. 3007-3014
    • Zhu, D.1    Dix, D.J.2    Eddy, E.M.3
  • 316
    • 84870916379 scopus 로고    scopus 로고
    • An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones
    • COI: 1:CAS:528:DC%2BC38XhvVaju7fE, PID: 23217711
    • Zhuravleva A, Clerico EM, Gierasch LM (2012) An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones. Cell 151:1296–1307
    • (2012) Cell , vol.151 , pp. 1296-1307
    • Zhuravleva, A.1    Clerico, E.M.2    Gierasch, L.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.