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Volumn 20, Issue 2, 2015, Pages 343-354

The discovery of Hsp70 domain with cell-penetrating activity

Author keywords

Cell penetrating peptides; Hsp70; Intracellular transport; Membrane; Vesicles

Indexed keywords

AMILORIDE; AMINO ACID; AVIDIN; BIOTIN; CELL PENETRATING PEPTIDE; CHAPERONE; CHLORPROMAZINE; DYNASORE; HEAT SHOCK PROTEIN 70; KRN PEPTIDE; KST PEPTIDE; TAT PEPTIDE; UNCLASSIFIED DRUG; YFN PEPTIDE; ANTIBODY; RECOMBINANT PROTEIN;

EID: 84925543243     PISSN: 13558145     EISSN: 14661268     Source Type: Journal    
DOI: 10.1007/s12192-014-0554-z     Document Type: Article
Times cited : (16)

References (58)
  • 1
    • 36248937161 scopus 로고    scopus 로고
    • Drug-induced Myc-mediated apoptosis of cancer cells is inhibited by stress protein Hsp70
    • COI: 1:CAS:528:DC%2BD2sXhtl2qsL3M, PID: 17694514
    • Afanasyeva EA, Komarova EY, Larsson LG, Bahram F, Margulis BA, Guzhova IV (2007) Drug-induced Myc-mediated apoptosis of cancer cells is inhibited by stress protein Hsp70. Int J Cancer 121(12):2615–2621
    • (2007) Int J Cancer , vol.121 , Issue.12 , pp. 2615-2621
    • Afanasyeva, E.A.1    Komarova, E.Y.2    Larsson, L.G.3    Bahram, F.4    Margulis, B.A.5    Guzhova, I.V.6
  • 4
    • 0036819191 scopus 로고    scopus 로고
    • Lipid interaction differentiates the constitutive and stress-induced heat shock proteins Hsc70 and Hsp70
    • COI: 1:CAS:528:DC%2BD3sXksVyluw%3D%3D, PID: 12653477
    • Arispe N, Doh M, De Maio A (2002) Lipid interaction differentiates the constitutive and stress-induced heat shock proteins Hsc70 and Hsp70. Cell Stress Chaperones 7(4):330–338
    • (2002) Cell Stress Chaperones , vol.7 , Issue.4 , pp. 330-338
    • Arispe, N.1    Doh, M.2    De Maio, A.3
  • 5
    • 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, Stevenson MA, Chen LB, Finberg RW, Koo GC, Calderwood SK (2000) HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine. Nat Med 6(4):435–442
    • (2000) Nat Med , vol.6 , Issue.4 , pp. 435-442
    • Asea, A.1    Kraeft, S.K.2    Kurt-Jones, E.A.3    Stevenson, M.A.4    Chen, L.B.5    Finberg, R.W.6    Koo, G.C.7    Calderwood, S.K.8
  • 6
    • 0037177825 scopus 로고    scopus 로고
    • Novel signal transduction pathway utilized by extracellular HSP70:role of toll-like receptor (TLR) 2 and TLR4
    • Asea A, Rehli M, Kabingu E, Boch JA, Bare O, Auron PE, Stevenson MA, Calderwood SK (2002) Novel signal transduction pathway utilized by extracellular HSP70:role of toll-like receptor (TLR) 2 and TLR4. J Biol Chem 277(17):15028–15034
    • (2002) J Biol Chem , vol.277 , Issue.17 , pp. 15028-15034
    • Asea, A.1    Rehli, M.2    Kabingu, E.3    Boch, J.A.4    Bare, O.5    Auron, P.E.6    Stevenson, M.A.7    Calderwood, S.K.8
  • 7
    • 0037783960 scopus 로고    scopus 로고
    • Stress-induced release of HSC70 from human tumors
    • COI: 1:CAS:528:DC%2BD3sXkvVCgtr4%3D, PID: 12826079
    • Barreto A, Gonzalez JM, Kabingu E, Asea A, Fiorentino S (2003) Stress-induced release of HSC70 from human tumors. Cell Immunol 222(2):97–104
    • (2003) Cell Immunol , vol.222 , Issue.2 , pp. 97-104
    • Barreto, A.1    Gonzalez, J.M.2    Kabingu, E.3    Asea, A.4    Fiorentino, S.5
  • 8
    • 0035070198 scopus 로고    scopus 로고
    • CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin
    • COI: 1:CAS:528:DC%2BD3MXis1ehurc%3D, PID: 11290339
    • Basu S, Binder RJ, Ramalingam T, Srivastava PK (2001) CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin. Immunity 14(3):303–313
    • (2001) Immunity , vol.14 , Issue.3 , pp. 303-313
    • Basu, S.1    Binder, R.J.2    Ramalingam, T.3    Srivastava, P.K.4
  • 9
    • 0037144808 scopus 로고    scopus 로고
    • CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes
    • COI: 1:CAS:528:DC%2BD38Xns1equr0%3D, PID: 12356871
    • Becker T, Hartl FU, Wieland F (2002) CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes. J Cell Biol 158(7):1277–1285
    • (2002) J Cell Biol , vol.158 , Issue.7 , pp. 1277-1285
    • Becker, T.1    Hartl, F.U.2    Wieland, F.3
  • 10
    • 77952990863 scopus 로고    scopus 로고
    • Anti-cancer therapies that utilize cell penetrating peptides
    • COI: 1:CAS:528:DC%2BC3cXmsVamt7Y%3D
    • Bitler BG, Schroeder JA (2010) Anti-cancer therapies that utilize cell penetrating peptides. Recent Patent Anticancer Drug Discov 5(2):99–108
    • (2010) Recent Patent Anticancer Drug Discov , vol.5 , Issue.2 , pp. 99-108
    • Bitler, B.G.1    Schroeder, J.A.2
  • 11
    • 84857771152 scopus 로고    scopus 로고
    • Potential efficacy of cell-penetrating peptides for nucleic acid and drug delivery in cancer
    • COI: 1:CAS:528:DC%2BC3MXhsVKmtrjL, PID: 21840374
    • Bolhassani A (2011) Potential efficacy of cell-penetrating peptides for nucleic acid and drug delivery in cancer. Biochim Biophys Acta 1816(2):232–246
    • (2011) Biochim Biophys Acta , vol.1816 , Issue.2 , pp. 232-246
    • Bolhassani, A.1
  • 12
    • 13844256698 scopus 로고    scopus 로고
    • Tat peptide-mediated cellular delivery: back to basics
    • COI: 1:CAS:528:DC%2BD2MXhslWnsr4%3D, PID: 15722164
    • Brooks H, Lebleu B, Vivès E (2005) Tat peptide-mediated cellular delivery: back to basics. Adv Drug Deliv Rev 57(4):559–577
    • (2005) Adv Drug Deliv Rev , vol.57 , Issue.4 , pp. 559-577
    • Brooks, H.1    Lebleu, B.2    Vivès, E.3
  • 13
    • 34447550254 scopus 로고    scopus 로고
    • Extracellular heat shock proteins in cell signaling
    • COI: 1:CAS:528:DC%2BD2sXotlaisLs%3D, PID: 17499247
    • Calderwood SK, Mambula SS, Gray PJ Jr, Theriault JR (2007) Extracellular heat shock proteins in cell signaling. FEBS Lett 581(19):3689–3694
    • (2007) FEBS Lett , vol.581 , Issue.19 , pp. 3689-3694
    • Calderwood, S.K.1    Mambula, S.S.2    Gray, P.J.3    Theriault, J.R.4
  • 14
    • 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, Vincent J, Bruchard M, Remy-Martin JP 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(2):457–571
    • (2010) J Clin Invest , vol.120 , Issue.2 , pp. 457-571
    • Chalmin, F.1    Ladoire, S.2    Mignot, G.3    Vincent, J.4    Bruchard, M.5    Remy-Martin, J.P.6
  • 15
    • 0041816277 scopus 로고    scopus 로고
    • Antennapedia and HIV transactivator of transcription (TAT) “protein transductiondomains” promote endocytosis of high molecular weight cargo upon binding to cell surface glycosaminoglycans
    • COI: 1:CAS:528:DC%2BD3sXntVWqtL4%3D, PID: 12837762
    • Console S, Marty C, García-Echeverría C, Schwendener R, Ballmer-Hofer K (2003) Antennapedia and HIV transactivator of transcription (TAT) “protein transductiondomains” promote endocytosis of high molecular weight cargo upon binding to cell surface glycosaminoglycans. J Biol Chem 278(37):35109–35114
    • (2003) J Biol Chem , vol.278 , Issue.37 , pp. 35109-35114
    • Console, S.1    Marty, C.2    García-Echeverría, C.3    Schwendener, R.4    Ballmer-Hofer, K.5
  • 17
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia homeodomain translocates through biological membranes
    • COI: 1:CAS:528:DyaK2cXlt1Oqt7Y%3D, PID: 8144628
    • Derossi D, Joliot AH, Chassaing G, Prochiantz A (1994) The third helix of the Antennapedia homeodomain translocates through biological membranes. J Biol Chem 269(14):10444–10450
    • (1994) J Biol Chem , vol.269 , Issue.14 , pp. 10444-10450
    • Derossi, D.1    Joliot, A.H.2    Chassaing, G.3    Prochiantz, A.4
  • 18
    • 33750504883 scopus 로고    scopus 로고
    • Formation of transmembrane ionic channels of primary amphipathic cell-penetrating peptides. Consequences on the mechanism of cell penetration
    • COI: 1:CAS:528:DC%2BD28XhtFKmtLjO, PID: 17011511
    • Deshayes S, Plénat T, Charnet P, Divita G, Molle G, Heitz F (2006) Formation of transmembrane ionic channels of primary amphipathic cell-penetrating peptides. Consequences on the mechanism of cell penetration. Biochim Biophys Acta 1758(11):1846–1851
    • (2006) Biochim Biophys Acta , vol.1758 , Issue.11 , pp. 1846-1851
    • Deshayes, S.1    Plénat, T.2    Charnet, P.3    Divita, G.4    Molle, G.5    Heitz, F.6
  • 19
    • 65549133368 scopus 로고    scopus 로고
    • Delivery of macromolecules using arginine-rich cell-penetrating peptides: ways to overcome endosomal entrapment
    • COI: 1:CAS:528:DC%2BD1MXhtVWru7bF, PID: 19125334
    • El-Sayed A, Futaki S, Harashima H (2009) Delivery of macromolecules using arginine-rich cell-penetrating peptides: ways to overcome endosomal entrapment. AAPS J 11(1):13–22
    • (2009) AAPS J , vol.11 , Issue.1 , pp. 13-22
    • El-Sayed, A.1    Futaki, S.2    Harashima, H.3
  • 20
    • 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(1):2
    • (2004) Cancer Cell Int , vol.4 , Issue.1 , pp. 2
    • Evdonin, A.L.1    Guzhova, I.V.2    Margulis, B.A.3    Medvedeva, N.D.4
  • 21
    • 0035937124 scopus 로고    scopus 로고
    • Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery
    • COI: 1:CAS:528:DC%2BD3MXhs1KmtL0%3D, PID: 11084031
    • Futaki S, Suzuki T, Ohashi W, Yagami T, Tanaka S, Ueda K, Sugiura Y (2001) Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery. J Biol Chem 276(8):5836–5840
    • (2001) J Biol Chem , vol.276 , Issue.8 , pp. 5836-5840
    • Futaki, S.1    Suzuki, T.2    Ohashi, W.3    Yagami, T.4    Tanaka, S.5    Ueda, K.6    Sugiura, Y.7
  • 23
    • 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, Asea A, Gross C, Schroeder JA, Multhoff G (2005) Heat shock protein 70 surface-positive tumor exosomes stimulate migratory and cytolytic activity of natural killer cells. Cancer Res 65(12):5238–5247
    • (2005) Cancer Res , vol.65 , Issue.12 , pp. 5238-5247
    • Gastpar, R.1    Gehrmann, M.2    Bausero, M.A.3    Asea, A.4    Gross, C.5    Schroeder, J.A.6    Multhoff, G.7
  • 24
    • 1242314233 scopus 로고    scopus 로고
    • Heat shock protein 70-reactivity is associated with increased cell surface density of CD94/CD56 on primary natural killer cells
    • COI: 1:CAS:528:DC%2BD2cXitlOis74%3D, PID: 15115287
    • Gross C, Schmidt-Wolf IG, Nagaraj S, Gastpar R, Ellwart J, Kunz-Schughart LA, Multhoff G (2003) Heat shock protein 70-reactivity is associated with increased cell surface density of CD94/CD56 on primary natural killer cells. Cell Stress Chaperones 8(4):348–360
    • (2003) Cell Stress Chaperones , vol.8 , Issue.4 , pp. 348-360
    • Gross, C.1    Schmidt-Wolf, I.G.2    Nagaraj, S.3    Gastpar, R.4    Ellwart, J.5    Kunz-Schughart, L.A.6    Multhoff, G.7
  • 25
    • 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(2):132–139
    • (1997) Cell Stress Chaperones , vol.2 , Issue.2 , pp. 132-139
    • Guzhova, I.V.1    Darieva, Z.A.2    Melo, A.R.3    Margulis, B.A.4
  • 26
    • 0035964907 scopus 로고    scopus 로고
    • In vitro studies show that Hsp70 can be released by glia and that exogenous Hsp70 can enhance neuronal stress tolerance
    • COI: 1:CAS:528:DC%2BD3MXntV2js7w%3D, PID: 11578598
    • Guzhova I, Kislyakova K, Moskaliova O, Fridlanskaya I, Tytell M, Cheetham M, Margulis B (2001) In vitro studies show that Hsp70 can be released by glia and that exogenous Hsp70 can enhance neuronal stress tolerance. Brain Res 914(1–2):66–73
    • (2001) Brain Res , vol.914 , Issue.1-2 , pp. 66-73
    • Guzhova, I.1    Kislyakova, K.2    Moskaliova, O.3    Fridlanskaya, I.4    Tytell, M.5    Cheetham, M.6    Margulis, B.7
  • 27
    • 80053144772 scopus 로고    scopus 로고
    • Novel mechanism of Hsp70 chaperone-mediated prevention of polyglutamine aggregates in a cellular model of Huntington disease
    • COI: 1:CAS:528:DC%2BC3MXht1ajtbjJ, PID: 21775503
    • Guzhova IV, Lazarev VF, Kaznacheeva AV, Ippolitova MV, Muronetz VI, Kinev AV, Margulis BA (2011) Novel mechanism of Hsp70 chaperone-mediated prevention of polyglutamine aggregates in a cellular model of Huntington disease. Hum Mol Genet 20(20):3953–3963
    • (2011) Hum Mol Genet , vol.20 , Issue.20 , pp. 3953-3963
    • Guzhova, I.V.1    Lazarev, V.F.2    Kaznacheeva, A.V.3    Ippolitova, M.V.4    Muronetz, V.I.5    Kinev, A.V.6    Margulis, B.A.7
  • 28
    • 84881191318 scopus 로고    scopus 로고
    • Intracellular and extracellular Hsp70 chaperone as a target for cancer therapy
    • COI: 1:CAS:528:DC%2BC3sXht1SlsbnO, PID: 23845032
    • Guzhova IV, Shevtsov MA, Abkin SV, Pankratova KM, Margulis BA (2013) Intracellular and extracellular Hsp70 chaperone as a target for cancer therapy. Int J Hyperthermia 29(5):399–408
    • (2013) Int J Hyperthermia , vol.29 , Issue.5 , pp. 399-408
    • Guzhova, I.V.1    Shevtsov, M.A.2    Abkin, S.V.3    Pankratova, K.M.4    Margulis, B.A.5
  • 29
    • 33845989425 scopus 로고    scopus 로고
    • Complex formation of 70-kDa heat shock protein with acidic glycolipids and phospholipids
    • COI: 1:CAS:528:DC%2BD2sXmtVahsg%3D%3D, PID: 17204248
    • Harada Y, Sato C, Kitajima K (2007) Complex formation of 70-kDa heat shock protein with acidic glycolipids and phospholipids. Biochem Biophys Res Commun 353(3):655–660
    • (2007) Biochem Biophys Res Commun , vol.353 , Issue.3 , pp. 655-660
    • Harada, Y.1    Sato, C.2    Kitajima, K.3
  • 30
    • 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(2):257–266
    • (1989) J Cell Physiol , vol.138 , Issue.2 , pp. 257-266
    • Hightower, L.E.1    Guidon, P.T.2
  • 31
    • 0029878720 scopus 로고    scopus 로고
    • VMD—visual molecular dynamics
    • COI: 1:CAS:528:DyaK28Xis12nsrg%3D, PID: 8744570
    • Humphrey W, Dalke A, Schulten K (1996) VMD—visual molecular dynamics. J Mol Graph 14:33–38
    • (1996) J Mol Graph , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 32
    • 0142149065 scopus 로고    scopus 로고
    • Complexes of plasmid DNA with basic domain 47-57 of the HIV-1 Tat protein are transferred to mammalian cells by endocytosis-mediated pathways
    • COI: 1:CAS:528:DC%2BD3sXot1alsLo%3D, PID: 12882958
    • Ignatovich IA, Dizhe EB, Pavlotskaya AV, Akifiev BN, Burov SV, Orlov SV, Perevozchikov AP (2003) Complexes of plasmid DNA with basic domain 47-57 of the HIV-1 Tat protein are transferred to mammalian cells by endocytosis-mediated pathways. J Biol Chem 278(43):42625–42636
    • (2003) J Biol Chem , vol.278 , Issue.43 , pp. 42625-42636
    • Ignatovich, I.A.1    Dizhe, E.B.2    Pavlotskaya, A.V.3    Akifiev, B.N.4    Burov, S.V.5    Orlov, S.V.6    Perevozchikov, A.P.7
  • 33
    • 0038668000 scopus 로고    scopus 로고
    • Escaping cell death: survival proteins in cancer
    • PID: 10094811
    • Jäättelä M (1999) Escaping cell death: survival proteins in cancer. Exp Cell Res 248(1):30–43
    • (1999) Exp Cell Res , vol.248 , Issue.1 , pp. 30-43
    • Jäättelä, M.1
  • 34
    • 0032855497 scopus 로고    scopus 로고
    • Multifaceted activities of the HIV-1 transactivator of transcription, Tat
    • COI: 1:CAS:528:DyaK1MXmslWqs74%3D, PID: 10506122
    • Jeang KT, Xiao H, Rich EA (1999) Multifaceted activities of the HIV-1 transactivator of transcription, Tat. J Biol Chem 274(41):28837–28840
    • (1999) J Biol Chem , vol.274 , Issue.41 , pp. 28837-28840
    • Jeang, K.T.1    Xiao, H.2    Rich, E.A.3
  • 35
    • 52949148197 scopus 로고    scopus 로고
    • Cell penetrating peptides for in vivo molecular imaging applications
    • COI: 1:CAS:528:DC%2BD1cXhtlehsb%2FK, PID: 18781991
    • Kersemans V, Kersemans K, Cornelissen B (2008) Cell penetrating peptides for in vivo molecular imaging applications. Curr Pharm Des 14(24):2415–2447
    • (2008) Curr Pharm Des , vol.14 , Issue.24 , pp. 2415-2447
    • Kersemans, V.1    Kersemans, K.2    Cornelissen, B.3
  • 36
    • 58149193233 scopus 로고    scopus 로고
    • The SWISS-MODEL repository and associated resources
    • COI: 1:CAS:528:DC%2BD1cXhsFejtb7P, PID: 18931379
    • Kiefer F, Arnold K, Künzli M, Bordoli L, Schwede T (2009) The SWISS-MODEL repository and associated resources. Nucleic Acids Res 37:D387–D392
    • (2009) Nucleic Acids Res , vol.37 , pp. 387-392
    • Kiefer, F.1    Arnold, K.2    Künzli, M.3    Bordoli, L.4    Schwede, T.5
  • 37
    • 7644236153 scopus 로고    scopus 로고
    • Downstream caspases are novel targets for the antiapoptotic activity of the molecular chaperone hsp70
    • COI: 1:CAS:528:DC%2BD2cXhtVSgsrvM, PID: 15544164
    • Komarova EY, Afanasyeva EA, Bulatova MM, Cheetham ME, Margulis BA, Guzhova IV (2004) Downstream caspases are novel targets for the antiapoptotic activity of the molecular chaperone hsp70. Cell Stress Chaperones 9(3):265–275
    • (2004) Cell Stress Chaperones , vol.9 , Issue.3 , pp. 265-275
    • Komarova, E.Y.1    Afanasyeva, E.A.2    Bulatova, M.M.3    Cheetham, M.E.4    Margulis, B.A.5    Guzhova, I.V.6
  • 38
    • 0348062818 scopus 로고    scopus 로고
    • The SWISS-MODEL repository of annotated three-dimensional protein structure homology models
    • COI: 1:CAS:528:DC%2BD3sXhtVSrtbfL, PID: 14681401
    • Kopp J, Schwede T (2004) The SWISS-MODEL repository of annotated three-dimensional protein structure homology models. Nucleic Acids Res 32:D230–D234
    • (2004) Nucleic Acids Res , vol.32 , pp. 230-234
    • Kopp, J.1    Schwede, T.2
  • 39
    • 84863099046 scopus 로고    scopus 로고
    • Cell-penetrating peptides: breaking through to the other side
    • COI: 1:CAS:528:DC%2BC38XhtVShsb%2FM, PID: 22682515
    • Koren E, Torchilin VP (2012) Cell-penetrating peptides: breaking through to the other side. Trends Mol Med 18(7):385–393
    • (2012) Trends Mol Med , vol.18 , Issue.7 , pp. 385-393
    • Koren, E.1    Torchilin, V.P.2
  • 40
    • 0001185839 scopus 로고    scopus 로고
    • Accumulation of major stress protein 70 kDa protects myeloid and lymphoid cells from death by apoptosis
    • COI: 1:CAS:528:DyaK2sXmslOksbs%3D, PID: 14646550
    • Lasunskaia EB, Fridlianskaia II, Guzhova IV, Bozhkov VM, Margulis BA (1997) Accumulation of major stress protein 70 kDa protects myeloid and lymphoid cells from death by apoptosis. Apoptosis 2(2):156–163
    • (1997) Apoptosis , vol.2 , Issue.2 , pp. 156-163
    • Lasunskaia, E.B.1    Fridlianskaia, I.I.2    Guzhova, I.V.3    Bozhkov, V.M.4    Margulis, B.A.5
  • 41
    • 79952197259 scopus 로고    scopus 로고
    • Classes and prediction of cell penetrating peptides
    • COI: 1:CAS:528:DC%2BC3cXhsFyktbvP, PID: 21053118
    • Lindgren M, Langel U (2011) Classes and prediction of cell penetrating peptides. Methods Mol Biol 683:3–19
    • (2011) Methods Mol Biol , vol.683 , pp. 3-19
    • Lindgren, M.1    Langel, U.2
  • 42
    • 79959365312 scopus 로고    scopus 로고
    • Mechanisms of cellular uptake of cell-penetrating peptides
    • PID: 21687343
    • Madani F, Lindberg S, Langel U, Futaki S, Gräslund A (2011) Mechanisms of cellular uptake of cell-penetrating peptides. J Biophys 2011:414729
    • (2011) J Biophys , vol.2011 , pp. 414729
    • Madani, F.1    Lindberg, S.2    Langel, U.3    Futaki, S.4    Gräslund, A.5
  • 43
    • 34848889680 scopus 로고    scopus 로고
    • Mechanisms for Hsp70 secretion: crossing membranes without a leader
    • COI: 1:CAS:528:DC%2BD2sXhtFers77I, PID: 17920512
    • Mambula SS, Stevenson MA, Ogawa K, Calderwood SK (2007) Mechanisms for Hsp70 secretion: crossing membranes without a leader. Methods 43(3):168–175
    • (2007) Methods , vol.43 , Issue.3 , pp. 168-175
    • Mambula, S.S.1    Stevenson, M.A.2    Ogawa, K.3    Calderwood, S.K.4
  • 44
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays
    • COI: 1:STN:280:DyaL2c%2FovFSmtw%3D%3D, PID: 6606682
    • Mosmann T (1983) Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J Immunol Methods 65(1–2):55–63
    • (1983) J Immunol Methods , vol.65 , Issue.1-2 , pp. 55-63
    • Mosmann, T.1
  • 45
    • 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, Müller E, Meier T, Wilmanns W, Issels RD (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(2):272–279
    • (1995) Int J Cancer , vol.61 , Issue.2 , pp. 272-279
    • Multhoff, G.1    Botzler, C.2    Wiesnet, M.3    Müller, E.4    Meier, T.5    Wilmanns, W.6    Issels, R.D.7
  • 46
    • 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, Bastholm L, Elling F, Jäättelä M (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(14):7871–7876
    • (2000) Proc Natl Acad Sci U S A , vol.97 , Issue.14 , pp. 7871-7876
    • Nylandsted, J.1    Rohde, M.2    Brand, K.3    Bastholm, L.4    Elling, F.5    Jäättelä, M.6
  • 47
    • 84902089965 scopus 로고    scopus 로고
    • Exogenously delivered heat shock protein 70 displaces its endogenous analogue and sensitizes cancer cells to lymphocytes-mediated cytotoxicity
    • PID: 24797019
    • Shevtsov MA, Komarova EY, Meshalkina DA, Bychkova NV, Aksenov ND, Abkin SV, Margulis BA, Guzhova IV (2014) Exogenously delivered heat shock protein 70 displaces its endogenous analogue and sensitizes cancer cells to lymphocytes-mediated cytotoxicity. Oncotarget 5(10):3101–3114
    • (2014) Oncotarget , vol.5 , Issue.10 , pp. 3101-3114
    • Shevtsov, M.A.1    Komarova, E.Y.2    Meshalkina, D.A.3    Bychkova, N.V.4    Aksenov, N.D.5    Abkin, S.V.6    Margulis, B.A.7    Guzhova, I.V.8
  • 48
    • 15544373100 scopus 로고    scopus 로고
    • Extracellular HSP70 binding to surface receptors present on antigen presenting cells and endothelial/epithelial cells
    • PID: 15792802
    • Thériault JR, Mambula SS, Sawamura T, Stevenson MA, Calderwood SK (2005) Extracellular HSP70 binding to surface receptors present on antigen presenting cells and endothelial/epithelial cells. FEBS Lett 579(9):1951–1960
    • (2005) FEBS Lett , vol.579 , Issue.9 , pp. 1951-1960
    • Thériault, J.R.1    Mambula, S.S.2    Sawamura, T.3    Stevenson, M.A.4    Calderwood, S.K.5
  • 49
    • 33845446813 scopus 로고    scopus 로고
    • Role of scavenger receptors in the binding and internalization of heat shock protein 70
    • PID: 17142759
    • Thériault JR, Adachi H, Calderwood SK (2006) Role of scavenger receptors in the binding and internalization of heat shock protein 70. J Immunol 177(12):8604–8611
    • (2006) J Immunol , vol.177 , Issue.12 , pp. 8604-8611
    • Thériault, J.R.1    Adachi, H.2    Calderwood, S.K.3
  • 50
    • 33748648777 scopus 로고    scopus 로고
    • Cargo-dependent mode of uptake and bioavailability of TAT-containing proteins and peptides in living cells
    • PID: 16940149
    • Tunnemann G, Martin RM, Haupt S, Patsch C, Edenhofer F, Cardoso MC (2006) Cargo-dependent mode of uptake and bioavailability of TAT-containing proteins and peptides in living cells. FASEB J 20(11):1775–1784
    • (2006) FASEB J , vol.20 , Issue.11 , pp. 1775-1784
    • Tunnemann, G.1    Martin, R.M.2    Haupt, S.3    Patsch, C.4    Edenhofer, F.5    Cardoso, M.C.6
  • 51
    • 0022637881 scopus 로고
    • Heat shock-like protein is transferred from glia to axon
    • COI: 1:CAS:528:DyaL28Xms1Cruw%3D%3D, PID: 3947949
    • Tytell M, Greenberg SG, Lasek RJ (1986) Heat shock-like protein is transferred from glia to axon. Brain Res 363(1):161–164
    • (1986) Brain Res , vol.363 , Issue.1 , pp. 161-164
    • Tytell, M.1    Greenberg, S.G.2    Lasek, R.J.3
  • 52
    • 44849084963 scopus 로고    scopus 로고
    • Hsp70 translocates into the plasma membrane after stress and its release into extracellular environment in membrane-associated form that activates macrophages
    • COI: 1:CAS:528:DC%2BD1cXisl2jtLc%3D, PID: 18322243
    • Vega VL, Rodriguez-Silva M, Frey T, Gehrmann M, Diaz JC, Steinem C, Multhoff G, Arispe N, De Maio A (2008) Hsp70 translocates into the plasma membrane after stress and its release into extracellular environment in membrane-associated form that activates macrophages. J Immunol 180(6):4299–4307
    • (2008) J Immunol , vol.180 , Issue.6 , pp. 4299-4307
    • Vega, V.L.1    Rodriguez-Silva, M.2    Frey, T.3    Gehrmann, M.4    Diaz, J.C.5    Steinem, C.6    Multhoff, G.7    Arispe, N.8    De Maio, A.9
  • 53
    • 77955713312 scopus 로고    scopus 로고
    • A new feature of the stress response: increase in endocytosis mediated by Hsp70
    • COI: 1:CAS:528:DC%2BC3cXpvV2jtrY%3D, PID: 20043217
    • Vega VL, Charles W, De Maio A (2010) A new feature of the stress response: increase in endocytosis mediated by Hsp70. Cell Stress Chaperones 15(5):517–527
    • (2010) Cell Stress Chaperones , vol.15 , Issue.5 , pp. 517-527
    • Vega, V.L.1    Charles, W.2    De Maio, A.3
  • 54
    • 0024810651 scopus 로고
    • Inhibition of antigen-induced lymphocyte proliferation by Tat protein from HIV-1
    • COI: 1:CAS:528:DyaK3cXps1yjtw%3D%3D, PID: 2556795
    • Viscidi RP, Mayur K, Lederman HM, Frankel AD (1989) Inhibition of antigen-induced lymphocyte proliferation by Tat protein from HIV-1. Science 246(4937):1606–1608
    • (1989) Science , vol.246 , Issue.4937 , pp. 1606-1608
    • Viscidi, R.P.1    Mayur, K.2    Lederman, H.M.3    Frankel, A.D.4
  • 56
    • 84889970066 scopus 로고    scopus 로고
    • Recent progress of cell-penetrating peptides as new carriers for intracellular cargo delivery
    • COI: 1:CAS:528:DC%2BC2cXhtVymsb0%3D, PID: 24291335
    • Wang F, Wang Y, Zhang X, Zhang W, Guo S, Jin F (2014) Recent progress of cell-penetrating peptides as new carriers for intracellular cargo delivery. J Control Release 174:126–136
    • (2014) J Control Release , vol.174 , pp. 126-136
    • Wang, F.1    Wang, Y.2    Zhang, X.3    Zhang, W.4    Guo, S.5    Jin, F.6
  • 57
    • 0037474523 scopus 로고    scopus 로고
    • Intracellular delivery of HSP70 using HIV-1 Tat protein transduction domain
    • COI: 1:CAS:528:DC%2BD3sXjtFemtA%3D%3D, PID: 12535640
    • Wheeler DS, Dunsmore KE, Wong HR (2003) Intracellular delivery of HSP70 using HIV-1 Tat protein transduction domain. Biochem Biophys Res Commun 301(1):54–59
    • (2003) Biochem Biophys Res Commun , vol.301 , Issue.1 , pp. 54-59
    • Wheeler, D.S.1    Dunsmore, K.E.2    Wong, H.R.3
  • 58
    • 11844293998 scopus 로고    scopus 로고
    • The cationic cell-penetrating peptide CPP TAT derived from the HIV-1 protein Tat is rapidly transported into living fibroblasts: optical, biophysical and metabolic evidence
    • COI: 1:CAS:528:DC%2BD2cXhtVOjtrfL, PID: 15628854
    • Ziegler A, Nervi P, Durrenberger M, Seelig J (2005) The cationic cell-penetrating peptide CPP TAT derived from the HIV-1 protein Tat is rapidly transported into living fibroblasts: optical, biophysical and metabolic evidence. Biochemistry 44(1):138–148
    • (2005) Biochemistry , vol.44 , Issue.1 , pp. 138-148
    • Ziegler, A.1    Nervi, P.2    Durrenberger, M.3    Seelig, J.4


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