메뉴 건너뛰기




Volumn 65, Issue 4, 2011, Pages 239-243

Molecular chaperones: Toward new therapeutic tools

Author keywords

Cancer; Chaperones; Neurodegenerative disease; Neuroprotection

Indexed keywords

17 ALLYLAMINO DEMETHOXY GELDANAMYCIN; ANTINEOPLASTIC AGENT; CATHEPSIN; CHAPERONE; CISPLATIN; DOXORUBICIN; GELDANAMYCIN; HEAT SHOCK PROTEIN 100; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HYPOXIA INDUCIBLE FACTOR 1; HYPOXIA INDUCIBLE FACTOR 1ALPHA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MET TYROSINE KINASE; METALLOPROTEIN; NITRIC OXIDE SYNTHASE; PACLITAXEL; PROTEASOME INHIBITOR; PROTEIN KINASE; PROTEIN MSH2; PROTEIN P53; PROTEIN TYROSINE KINASE; PURINE SCAFFOLD INHIBITOR; RADICICOL; SMALL HEAT SHOCK PROTEIN; TIN CHLORIDE; TRICHOSTATIN A; UNCLASSIFIED DRUG; UNINDEXED DRUG; VASCULOTROPIN;

EID: 79960430517     PISSN: 07533322     EISSN: 19506007     Source Type: Journal    
DOI: 10.1016/j.biopha.2011.04.025     Document Type: Review
Times cited : (42)

References (55)
  • 1
    • 40849140683 scopus 로고    scopus 로고
    • Protective effects of heat shock protein 27 in a model of ALS occur in the early stages of disease progression
    • Sharp P.S., et al. Protective effects of heat shock protein 27 in a model of ALS occur in the early stages of disease progression. Neurobiol Dis 2008, 30(1):42-55.
    • (2008) Neurobiol Dis , vol.30 , Issue.1 , pp. 42-55
    • Sharp, P.S.1
  • 2
    • 40849092480 scopus 로고    scopus 로고
    • Heat shock proteins, endothelin, and peripheral neuronal injury
    • Klass M.G., et al. Heat shock proteins, endothelin, and peripheral neuronal injury. Neurosci Lett 2008, 433(3):188-193.
    • (2008) Neurosci Lett , vol.433 , Issue.3 , pp. 188-193
    • Klass, M.G.1
  • 3
    • 70149124059 scopus 로고    scopus 로고
    • Induction of heat shock protein 70 reduces the alteration of striatal electrical activity caused by mitochondrial impairment
    • Tantucci M., et al. Induction of heat shock protein 70 reduces the alteration of striatal electrical activity caused by mitochondrial impairment. Neuroscience 2009, 163(3):735-740.
    • (2009) Neuroscience , vol.163 , Issue.3 , pp. 735-740
    • Tantucci, M.1
  • 4
    • 0035363805 scopus 로고    scopus 로고
    • Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease
    • Sittler A., et al. Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease. Hum Mol Genet 2001, 10(12):1307-1315.
    • (2001) Hum Mol Genet , vol.10 , Issue.12 , pp. 1307-1315
    • Sittler, A.1
  • 5
    • 27744517366 scopus 로고    scopus 로고
    • Heat shock proteins as emerging therapeutic targets
    • Soti C., et al. Heat shock proteins as emerging therapeutic targets. Br J Pharmacol 2005, 146(6):769-780.
    • (2005) Br J Pharmacol , vol.146 , Issue.6 , pp. 769-780
    • Soti, C.1
  • 6
    • 70450216770 scopus 로고    scopus 로고
    • Heat shock proteins in glioblastomas
    • Yang I., Fang S., Parsa A.T. Heat shock proteins in glioblastomas. Neurosurg Clin N Am 2010, 21(1):111-123.
    • (2010) Neurosurg Clin N Am , vol.21 , Issue.1 , pp. 111-123
    • Yang, I.1    Fang, S.2    Parsa, A.T.3
  • 7
    • 21744445069 scopus 로고    scopus 로고
    • Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications
    • Ciocca D.R., Calderwood S.K. Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications. Cell Stress Chaperones 2005, 10(2):86-103.
    • (2005) Cell Stress Chaperones , vol.10 , Issue.2 , pp. 86-103
    • Ciocca, D.R.1    Calderwood, S.K.2
  • 8
    • 77649118928 scopus 로고    scopus 로고
    • Recombinant Fv-Hsp70 protein mediates neuroprotection after focal cerebral ischemia in rats
    • Zhan X., et al. Recombinant Fv-Hsp70 protein mediates neuroprotection after focal cerebral ischemia in rats. Stroke 2010, 41(3):538-543.
    • (2010) Stroke , vol.41 , Issue.3 , pp. 538-543
    • Zhan, X.1
  • 9
    • 77953576838 scopus 로고    scopus 로고
    • Targeting HSP70: the second potentially druggable heat shock protein and molecular chaperone?
    • Powers M.V., et al. Targeting HSP70: the second potentially druggable heat shock protein and molecular chaperone?. Cell Cycle 2010, 9(8):1542-1550.
    • (2010) Cell Cycle , vol.9 , Issue.8 , pp. 1542-1550
    • Powers, M.V.1
  • 11
    • 33747512168 scopus 로고    scopus 로고
    • The distinctive role of small heat shock proteins in oncogenesis
    • Laudanski K., Wyczechowska D. The distinctive role of small heat shock proteins in oncogenesis. Arch Immunol Ther Exp (Warsz) 2006, 54(2):103-111.
    • (2006) Arch Immunol Ther Exp (Warsz) , vol.54 , Issue.2 , pp. 103-111
    • Laudanski, K.1    Wyczechowska, D.2
  • 13
    • 33644835965 scopus 로고    scopus 로고
    • Heat shock proteins in cancer: chaperones of tumorigenesis
    • Calderwood S.K., et al. Heat shock proteins in cancer: chaperones of tumorigenesis. Trends Biochem Sci 2006, 31(3):164-172.
    • (2006) Trends Biochem Sci , vol.31 , Issue.3 , pp. 164-172
    • Calderwood, S.K.1
  • 14
    • 7444231693 scopus 로고    scopus 로고
    • Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets
    • Spiess C., et al. Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets. Trends Cell Biol 2004, 14(11):598-604.
    • (2004) Trends Cell Biol , vol.14 , Issue.11 , pp. 598-604
    • Spiess, C.1
  • 15
    • 44549085390 scopus 로고    scopus 로고
    • Chaperonins: the hunt for the Group II mechanism
    • Bigotti M.G., Clarke A.R. Chaperonins: the hunt for the Group II mechanism. Arch Biochem Biophys 2008, 474(2):331-339.
    • (2008) Arch Biochem Biophys , vol.474 , Issue.2 , pp. 331-339
    • Bigotti, M.G.1    Clarke, A.R.2
  • 16
    • 22144490883 scopus 로고    scopus 로고
    • [Heat shock proteins as molecular chaperones]
    • Arrigo A.P. [Heat shock proteins as molecular chaperones]. Med Sci (Paris) 2005, 21(6-7):619-625.
    • (2005) Med Sci (Paris) , vol.21 , Issue.6-7 , pp. 619-625
    • Arrigo, A.P.1
  • 17
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt W.B., Toft D.O. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp Biol Med (Maywood) 2003, 228(2):111-133.
    • (2003) Exp Biol Med (Maywood) , vol.228 , Issue.2 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 18
    • 0142186172 scopus 로고    scopus 로고
    • Aging and molecular chaperones
    • Soti C., Csermely P. Aging and molecular chaperones. Exp Gerontol 2003, 38(10):1037-1040.
    • (2003) Exp Gerontol , vol.38 , Issue.10 , pp. 1037-1040
    • Soti, C.1    Csermely, P.2
  • 19
    • 0033575998 scopus 로고    scopus 로고
    • Hot-tub therapy for type 2 diabetes mellitus
    • Hooper P.L. Hot-tub therapy for type 2 diabetes mellitus. N Engl J Med 1999, 341(12):924-925.
    • (1999) N Engl J Med , vol.341 , Issue.12 , pp. 924-925
    • Hooper, P.L.1
  • 20
    • 77950189338 scopus 로고    scopus 로고
    • Heat shock proteins, cell survival and drug resistance: the mitochondrial chaperone TRAP1, a potential novel target for ovarian cancer therapy
    • Landriscina M., et al. Heat shock proteins, cell survival and drug resistance: the mitochondrial chaperone TRAP1, a potential novel target for ovarian cancer therapy. Gynecol Oncol 2010, 117(2):177-182.
    • (2010) Gynecol Oncol , vol.117 , Issue.2 , pp. 177-182
    • Landriscina, M.1
  • 21
    • 13744256921 scopus 로고    scopus 로고
    • Membrane fluidization triggers membrane remodeling which affects the thermotolerance in Escherichia coli
    • Shigapova N., et al. Membrane fluidization triggers membrane remodeling which affects the thermotolerance in Escherichia coli. Biochem Biophys Res Commun 2005, 328(4):1216-1223.
    • (2005) Biochem Biophys Res Commun , vol.328 , Issue.4 , pp. 1216-1223
    • Shigapova, N.1
  • 22
    • 0037293568 scopus 로고    scopus 로고
    • Nitric oxide, superoxide, and peroxynitrite in myocardial ischaemia-reperfusion injury and preconditioning
    • Ferdinandy P., Schulz R. Nitric oxide, superoxide, and peroxynitrite in myocardial ischaemia-reperfusion injury and preconditioning. Br J Pharmacol 2003, 138(4):532-543.
    • (2003) Br J Pharmacol , vol.138 , Issue.4 , pp. 532-543
    • Ferdinandy, P.1    Schulz, R.2
  • 23
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D., Weinberg R.A. The hallmarks of cancer. Cell 2000, 100(1):57-70.
    • (2000) Cell , vol.100 , Issue.1 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 24
    • 77955088992 scopus 로고    scopus 로고
    • Multi-chaperone-peptide-rich mixture from colo-carcinoma cells elicits potent anticancer immunity
    • Huang C., et al. Multi-chaperone-peptide-rich mixture from colo-carcinoma cells elicits potent anticancer immunity. Cancer Epidemiol 2010.
    • (2010) Cancer Epidemiol
    • Huang, C.1
  • 25
    • 77149141379 scopus 로고    scopus 로고
    • Hsp90 as a therapeutic target in patients with oesophageal carcinoma
    • Ekman S., et al. Hsp90 as a therapeutic target in patients with oesophageal carcinoma. Expert Opin Ther Targets 2010, 14(3):317-328.
    • (2010) Expert Opin Ther Targets , vol.14 , Issue.3 , pp. 317-328
    • Ekman, S.1
  • 26
    • 77950615028 scopus 로고    scopus 로고
    • Mitochondrial Hsp90 chaperones as novel molecular targets in prostate cancer
    • Altieri D.C. Mitochondrial Hsp90 chaperones as novel molecular targets in prostate cancer. Future Oncol 2010, 6(4):487-489.
    • (2010) Future Oncol , vol.6 , Issue.4 , pp. 487-489
    • Altieri, D.C.1
  • 27
    • 77649147755 scopus 로고    scopus 로고
    • Heat shock cognate protein 70 is essential for Akt signaling in endothelial function
    • Shiota M., et al. Heat shock cognate protein 70 is essential for Akt signaling in endothelial function. Arterioscler Thromb Vasc Biol 2010, 30(3):491-497.
    • (2010) Arterioscler Thromb Vasc Biol , vol.30 , Issue.3 , pp. 491-497
    • Shiota, M.1
  • 28
    • 65549085219 scopus 로고    scopus 로고
    • Heat shock protein inhibitors and vaccines as new agents in cancer treatment
    • Karapanagiotou E.M., Syrigos K., Saif M.W. Heat shock protein inhibitors and vaccines as new agents in cancer treatment. Expert Opin Investig Drugs 2009, 18(2):161-174.
    • (2009) Expert Opin Investig Drugs , vol.18 , Issue.2 , pp. 161-174
    • Karapanagiotou, E.M.1    Syrigos, K.2    Saif, M.W.3
  • 29
    • 34548189523 scopus 로고    scopus 로고
    • Extracellular heat shock protein 90: a role for a molecular chaperone in cell motility and cancer metastasis
    • Tsutsumi S., Neckers L. Extracellular heat shock protein 90: a role for a molecular chaperone in cell motility and cancer metastasis. Cancer Sci 2007, 98(10):1536-1539.
    • (2007) Cancer Sci , vol.98 , Issue.10 , pp. 1536-1539
    • Tsutsumi, S.1    Neckers, L.2
  • 30
    • 4744371115 scopus 로고    scopus 로고
    • The heat-shock protein receptors: some answers and more questions
    • Binder R.J., Vatner R., Srivastava P. The heat-shock protein receptors: some answers and more questions. Tissue Antigens 2004, 64(4):442-451.
    • (2004) Tissue Antigens , vol.64 , Issue.4 , pp. 442-451
    • Binder, R.J.1    Vatner, R.2    Srivastava, P.3
  • 31
    • 2942716692 scopus 로고    scopus 로고
    • Functional proteomic screens reveal an essential extracellular role for hsp90 alpha in cancer cell invasiveness
    • Eustace B.K., et al. Functional proteomic screens reveal an essential extracellular role for hsp90 alpha in cancer cell invasiveness. Nat Cell Biol 2004, 6(6):507-514.
    • (2004) Nat Cell Biol , vol.6 , Issue.6 , pp. 507-514
    • Eustace, B.K.1
  • 32
    • 42049084486 scopus 로고    scopus 로고
    • A small molecule cell-impermeant Hsp90 antagonist inhibits tumor cell motility and invasion
    • Tsutsumi S., et al. A small molecule cell-impermeant Hsp90 antagonist inhibits tumor cell motility and invasion. Oncogene 2008, 27(17):2478-2487.
    • (2008) Oncogene , vol.27 , Issue.17 , pp. 2478-2487
    • Tsutsumi, S.1
  • 33
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
    • Kamal A., et al. A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 2003, 425(6956):407-410.
    • (2003) Nature , vol.425 , Issue.6956 , pp. 407-410
    • Kamal, A.1
  • 34
    • 0038069088 scopus 로고    scopus 로고
    • Geldanamycin and its 17-allylamino-17-demethoxy analogue antagonize the action of cisplatin in human colon adenocarcinoma cells: differential caspase activation as a basis for interaction
    • Vasilevskaya I.A., Rakitina T.V., O'Dwyer P.J. Geldanamycin and its 17-allylamino-17-demethoxy analogue antagonize the action of cisplatin in human colon adenocarcinoma cells: differential caspase activation as a basis for interaction. Cancer Res 2003, 63(12):3241-3246.
    • (2003) Cancer Res , vol.63 , Issue.12 , pp. 3241-3246
    • Vasilevskaya, I.A.1    Rakitina, T.V.2    O'Dwyer, P.J.3
  • 35
    • 20244367890 scopus 로고    scopus 로고
    • Bimoclomol: a non-toxic, hydroxylamine derivative with stress protein-inducing activity and cytoprotective effects
    • Vigh L., et al. Bimoclomol: a non-toxic, hydroxylamine derivative with stress protein-inducing activity and cytoprotective effects. Nat Med 1997, 3(10):1150-1154.
    • (1997) Nat Med , vol.3 , Issue.10 , pp. 1150-1154
    • Vigh, L.1
  • 36
    • 28044469532 scopus 로고    scopus 로고
    • Pharmacological induction of heat-shock proteins alleviates polyglutamine-mediated motor neuron disease
    • Katsuno M., et al. Pharmacological induction of heat-shock proteins alleviates polyglutamine-mediated motor neuron disease. Proc Natl Acad Sci U S A 2005, 102(46):16801-16806.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.46 , pp. 16801-16806
    • Katsuno, M.1
  • 37
    • 33746724745 scopus 로고    scopus 로고
    • Modulation of Hsp90 function in neurodegenerative disorders: a molecular-targeted therapy against disease-causing protein
    • Waza M., et al. Modulation of Hsp90 function in neurodegenerative disorders: a molecular-targeted therapy against disease-causing protein. J Mol Med 2006, 84(8):635-646.
    • (2006) J Mol Med , vol.84 , Issue.8 , pp. 635-646
    • Waza, M.1
  • 38
    • 33845874433 scopus 로고    scopus 로고
    • Brain CHIP: removing the culprits in neurodegenerative disease
    • Dickey C.A., et al. Brain CHIP: removing the culprits in neurodegenerative disease. Trends Mol Med 2007, 13(1):32-38.
    • (2007) Trends Mol Med , vol.13 , Issue.1 , pp. 32-38
    • Dickey, C.A.1
  • 39
    • 0842342532 scopus 로고    scopus 로고
    • The effect of treatment with BRX-220, a co-inducer of heat shock proteins, on sensory fibers of the rat following peripheral nerve injury
    • Kalmar B., et al. The effect of treatment with BRX-220, a co-inducer of heat shock proteins, on sensory fibers of the rat following peripheral nerve injury. Exp Neurol 2003, 184(2):636-647.
    • (2003) Exp Neurol , vol.184 , Issue.2 , pp. 636-647
    • Kalmar, B.1
  • 40
    • 58149402446 scopus 로고    scopus 로고
    • Hsp27 protects against ischemic brain injury via attenuation of a novel stress-response cascade upstream of mitochondrial cell death signaling
    • Stetler R.A., et al. Hsp27 protects against ischemic brain injury via attenuation of a novel stress-response cascade upstream of mitochondrial cell death signaling. J Neurosci 2008, 28(49):13038-13055.
    • (2008) J Neurosci , vol.28 , Issue.49 , pp. 13038-13055
    • Stetler, R.A.1
  • 41
    • 33646681219 scopus 로고    scopus 로고
    • Redox regulation of heat shock protein expression by signaling involving nitric oxide and carbon monoxide: relevance to brain aging, neurodegenerative disorders, and longevity
    • Calabrese V., et al. Redox regulation of heat shock protein expression by signaling involving nitric oxide and carbon monoxide: relevance to brain aging, neurodegenerative disorders, and longevity. Antioxid Redox Signal 2006, 8(3-4):444-477.
    • (2006) Antioxid Redox Signal , vol.8 , Issue.3-4 , pp. 444-477
    • Calabrese, V.1
  • 42
    • 36849005504 scopus 로고    scopus 로고
    • Exogenous delivery of heat shock protein 70 increases lifespan in a mouse model of amyotrophic lateral sclerosis
    • Gifondorwa D.J., et al. Exogenous delivery of heat shock protein 70 increases lifespan in a mouse model of amyotrophic lateral sclerosis. J Neurosci 2007, 27(48):13173-13180.
    • (2007) J Neurosci , vol.27 , Issue.48 , pp. 13173-13180
    • Gifondorwa, D.J.1
  • 43
    • 1942486792 scopus 로고    scopus 로고
    • Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice
    • Kieran D., et al. Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice. Nat Med 2004, 10(4):402-405.
    • (2004) Nat Med , vol.10 , Issue.4 , pp. 402-405
    • Kieran, D.1
  • 44
    • 4143152789 scopus 로고    scopus 로고
    • Radicicol activates heat shock protein expression and cardioprotection in neonatal rat cardiomyocytes
    • Griffin T.M., Valdez T.V., Mestril R. Radicicol activates heat shock protein expression and cardioprotection in neonatal rat cardiomyocytes. Am J Physiol Heart Circ Physiol 2004, 287(3):H1081-H1088.
    • (2004) Am J Physiol Heart Circ Physiol , vol.287 , Issue.3
    • Griffin, T.M.1    Valdez, T.V.2    Mestril, R.3
  • 45
    • 3943054801 scopus 로고    scopus 로고
    • Heat shock protein 90 transfection reduces ischemia-reperfusion-induced myocardial dysfunction via reciprocal endothelial NO synthase serine 1177 phosphorylation and threonine 495 dephosphorylation
    • Kupatt C., et al. Heat shock protein 90 transfection reduces ischemia-reperfusion-induced myocardial dysfunction via reciprocal endothelial NO synthase serine 1177 phosphorylation and threonine 495 dephosphorylation. Arterioscler Thromb Vasc Biol 2004, 24(8):1435-1441.
    • (2004) Arterioscler Thromb Vasc Biol , vol.24 , Issue.8 , pp. 1435-1441
    • Kupatt, C.1
  • 46
    • 58149381759 scopus 로고    scopus 로고
    • Rescuing cardiac malfunction: the roles of the chaperone-like small heat shock proteins
    • Chung E., Leinwand L.A. Rescuing cardiac malfunction: the roles of the chaperone-like small heat shock proteins. Circ Res 2008, 103(12):1351-1353.
    • (2008) Circ Res , vol.103 , Issue.12 , pp. 1351-1353
    • Chung, E.1    Leinwand, L.A.2
  • 47
    • 65549134708 scopus 로고    scopus 로고
    • HSP 70 and atherosclerosis - protector or activator?
    • Bielecka-Dabrowa A., et al. HSP 70 and atherosclerosis - protector or activator?. Expert Opin Ther Targets 2009, 13(3):307-317.
    • (2009) Expert Opin Ther Targets , vol.13 , Issue.3 , pp. 307-317
    • Bielecka-Dabrowa, A.1
  • 48
    • 0027407468 scopus 로고
    • Heat shock and recovery protects renal allografts from warm ischemic injury and enhances HSP72 production
    • Perdrizet G.A., et al. Heat shock and recovery protects renal allografts from warm ischemic injury and enhances HSP72 production. Transplant Proc 1993, 25(1 Pt 2):1670-1673.
    • (1993) Transplant Proc , vol.25 , Issue.1 PART 2 , pp. 1670-1673
    • Perdrizet, G.A.1
  • 49
    • 76149134396 scopus 로고    scopus 로고
    • Immunomodulation with heat shock protein DiaPep277 to preserve beta cell function in type 1 diabetes - an update
    • Fischer B., et al. Immunomodulation with heat shock protein DiaPep277 to preserve beta cell function in type 1 diabetes - an update. Expert Opin Biol Ther 2010, 10(2):265-272.
    • (2010) Expert Opin Biol Ther , vol.10 , Issue.2 , pp. 265-272
    • Fischer, B.1
  • 50
    • 33750364777 scopus 로고    scopus 로고
    • Heat shock proteins induce T cell regulation of chronic inflammation
    • Hauet-Broere F., et al. Heat shock proteins induce T cell regulation of chronic inflammation. Ann Rheum Dis 2006, 65(Suppl.3):piii65-piii68.
    • (2006) Ann Rheum Dis , vol.65 , Issue.SUPPL. 3
    • Hauet-Broere, F.1
  • 51
    • 20944432903 scopus 로고    scopus 로고
    • Heat shock protein 27 expression in patients with chronic liver damage
    • Federico A., et al. Heat shock protein 27 expression in patients with chronic liver damage. Immunobiology 2005, 209(10):729-735.
    • (2005) Immunobiology , vol.209 , Issue.10 , pp. 729-735
    • Federico, A.1
  • 52
    • 77955199612 scopus 로고    scopus 로고
    • Heat shock proteins: cellular and molecular mechanisms in the central nervous system
    • Stetler R.A., et al. Heat shock proteins: cellular and molecular mechanisms in the central nervous system. Prog Neurobiol 2010, 92(2):184-211.
    • (2010) Prog Neurobiol , vol.92 , Issue.2 , pp. 184-211
    • Stetler, R.A.1
  • 53
    • 58149168845 scopus 로고    scopus 로고
    • Subcellular stress response and induction of molecular chaperones and folding proteins after transient global ischemia in rats
    • Truettner J.S., et al. Subcellular stress response and induction of molecular chaperones and folding proteins after transient global ischemia in rats. Brain Res 2009, 1249:9-18.
    • (2009) Brain Res , vol.1249 , pp. 9-18
    • Truettner, J.S.1
  • 54
    • 34047274469 scopus 로고    scopus 로고
    • Lens epithelium-derived growth factor is an Hsp70-2 regulated guardian of lysosomal stability in human cancer
    • Daugaard M., et al. Lens epithelium-derived growth factor is an Hsp70-2 regulated guardian of lysosomal stability in human cancer. Cancer Res 2007, 67(6):2559-2567.
    • (2007) Cancer Res , vol.67 , Issue.6 , pp. 2559-2567
    • Daugaard, M.1
  • 55
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • Pearl L.H., Prodromou C. Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu Rev Biochem 2006, 75:271-294.
    • (2006) Annu Rev Biochem , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.