메뉴 건너뛰기




Volumn 100, Issue 10, 2009, Pages 1523-1529

Targeting HSP90 for cancer therapy

Author keywords

AKT; BCR ABL; EGFR; Heat shock proteins; HER 2; Tumour suppressor genes; VEGF

Indexed keywords

BORTEZOMIB; ERLOTINIB; ESTROGEN RECEPTOR; GEFITINIB; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; HYBRID PROTEIN; HYPOXIA INDUCIBLE FACTOR 1; IMATINIB; TAMOXIFEN; TANESPIMYCIN; TRASTUZUMAB; ANTINEOPLASTIC AGENT;

EID: 66149125584     PISSN: 00070920     EISSN: 15321827     Source Type: Journal    
DOI: 10.1038/sj.bjc.6605066     Document Type: Short Survey
Times cited : (269)

References (59)
  • 1
    • 4143095430 scopus 로고    scopus 로고
    • Altered Hsp90 function in cancer: A unique therapeutic opportunity
    • Bagatell R (2004) Altered Hsp90 function in cancer: a unique therapeutic opportunity. Mol Cancer Ther 3: 1021 - 1030
    • (2004) Mol Cancer Ther , vol.3 , pp. 1021-1030
    • Bagatell, R.1
  • 3
    • 26444482073 scopus 로고    scopus 로고
    • Pharmacokinetic-pharmacodynamic relationships for the heat shock protein 90 molecular chaperone inhibitor 17-allylamino, 17-demethoxygeldanamycin in human ovarian cancer xenograft models
    • Banerji U, Walton M, Raynaud F, Grimshaw R, Kelland L, Valenti M, Judson I, Workman P (2005) Pharmacokinetic-pharmacodynamic relationships for the heat shock protein 90 molecular chaperone inhibitor 17-allylamino, 17-demethoxygeldanamycin in human ovarian cancer xenograft models. Clin Cancer Res 11: 7023-7032
    • (2005) Clin Cancer Res , vol.11 , pp. 7023-7032
    • Banerji, U.1    Walton, M.2    Raynaud, F.3    Grimshaw, R.4    Kelland, L.5    Valenti, M.6    Judson, I.7    Workman, P.8
  • 4
    • 33749461709 scopus 로고    scopus 로고
    • Heat shock protein 90 inhibition in imatinib-resistant gastrointestinal stromal tumor
    • Bauer S, Yu LK, Demetri GD, Fletcher JA (2006) Heat shock protein 90 inhibition in imatinib-resistant gastrointestinal stromal tumor. Cancer Res 66: 9153-9161
    • (2006) Cancer Res , vol.66 , pp. 9153-9161
    • Bauer, S.1    Yu, L.K.2    Demetri, G.D.3    Fletcher, J.A.4
  • 7
    • 2342625412 scopus 로고    scopus 로고
    • Ubiquitination and proteasomal degradation of nucleophosmin-anaplastic lymphoma kinase induced by 17-allylamino- demethoxygeldanamycin: Role of the co-chaperone carboxyl heat shock protein 70-interacting protein
    • Bonvini P (2004) Ubiquitination and proteasomal degradation of nucleophosmin-anaplastic lymphoma kinase induced by 17-allylamino- demethoxygeldanamycin: role of the co-chaperone carboxyl heat shock protein 70-interacting protein. Cancer Res 64: 3256 - 3264
    • (2004) Cancer Res , vol.64 , pp. 3256-3264
    • Bonvini, P.1
  • 10
    • 34548658230 scopus 로고    scopus 로고
    • Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis
    • Dai C, Whitesell L, Rogers AB, Lindquist S (2007) Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis. Cell 130: 1005-1018
    • (2007) Cell , vol.130 , pp. 1005-1018
    • Dai, C.1    Whitesell, L.2    Rogers, A.B.3    Lindquist, S.4
  • 11
    • 33947677849 scopus 로고    scopus 로고
    • Overcoming resistance to tyrosine kinase inhibitors (TKIs) through inhibition of Heat Shock Protein 90 (Hsp90) chaperone function in patients with metastatic GIST: Results of a Phase I Trial of IPI-504, a water-soluble Hsp90 inhibitor
    • Demetri GD, George S, Morgan JA, van den Abbeele A, Quigley MT, Fletcher JA, Normandt E, Patterson J, Adams J, Grayzel D (2006) Overcoming resistance to tyrosine kinase inhibitors (TKIs) through inhibition of Heat Shock Protein 90 (Hsp90) chaperone function in patients with metastatic GIST: results of a Phase I Trial of IPI-504, a water-soluble Hsp90 inhibitor. EJC Suppl 4: 173
    • (2006) EJC Suppl , vol.4 , pp. 173
    • Demetri, G.D.1    George, S.2    Morgan, J.A.3    van den Abbeele, A.4    Quigley, M.T.5    Fletcher, J.A.6    Normandt, E.7    Patterson, J.8    Adams, J.9    Grayzel, D.10
  • 12
    • 0036530301 scopus 로고    scopus 로고
    • VEGF(165) promotes survival of leukemic cells by Hsp90-mediated induction of Bcl-2 expression and apoptosis inhibition
    • Dias S, Shmelkov SV, Lam G, Rafii S (2002) VEGF(165) promotes survival of leukemic cells by Hsp90-mediated induction of Bcl-2 expression and apoptosis inhibition. Blood 99: 2532-2540
    • (2002) Blood , vol.99 , pp. 2532-2540
    • Dias, S.1    Shmelkov, S.V.2    Lam, G.3    Rafii, S.4
  • 13
    • 0035810142 scopus 로고    scopus 로고
    • Activity of a specific inhibitor of the BCR-ABL tyrosine kinase in the blast crisis of chronic myeloid leukemia and acute lymphoblastic leukemia with the Philadelphia chromosome
    • Druker BJ, Sawyers CL, Kantarjian H, Resta DJ, Reese SF, Ford JM, Capdeville R, Talpaz M (2001) Activity of a specific inhibitor of the BCR-ABL tyrosine kinase in the blast crisis of chronic myeloid leukemia and acute lymphoblastic leukemia with the Philadelphia chromosome. NEngl J Med 344: 1038 - 1042
    • (2001) NEngl J Med , vol.344 , pp. 1038-1042
    • Druker, B.J.1    Sawyers, C.L.2    Kantarjian, H.3    Resta, D.J.4    Reese, S.F.5    Ford, J.M.6    Capdeville, R.7    Talpaz, M.8
  • 15
    • 0031835957 scopus 로고    scopus 로고
    • Regulation of transcription by hypoxia requires a multiprotein complex that includes hypoxia-inducible factor 1, an adjacent transcription factor, and p300/CREB binding protein
    • Ebert BL, Bunn HF (1998) Regulation of transcription by hypoxia requires a multiprotein complex that includes hypoxia-inducible factor 1, an adjacent transcription factor, and p300/CREB binding protein. Mol Cell Biol 18: 4089-4096
    • (1998) Mol Cell Biol , vol.18 , pp. 4089-4096
    • Ebert, B.L.1    Bunn, H.F.2
  • 17
    • 34548075217 scopus 로고    scopus 로고
    • Hydroxamic acid analogue histone deacetylase inhibitors attenuate estrogen receptor-alpha levels and transcriptional activity: A result of hyperacetylation and inhibition of chaperone function of heat shock protein 90
    • Fiskus W, Ren Y, Mohapatra A, Bali P, Mandawat A, Rao R, Herger B, Yang Y, Atadja P, Wu J, Bhalla K (2007) Hydroxamic acid analogue histone deacetylase inhibitors attenuate estrogen receptor-alpha levels and transcriptional activity: a result of hyperacetylation and inhibition of chaperone function of heat shock protein 90. Clin Cancer Res 13: 4882-4890
    • (2007) Clin Cancer Res , vol.13 , pp. 4882-4890
    • Fiskus, W.1    Ren, Y.2    Mohapatra, A.3    Bali, P.4    Mandawat, A.5    Rao, R.6    Herger, B.7    Yang, Y.8    Atadja, P.9    Wu, J.10    Bhalla, K.11
  • 19
    • 0030003813 scopus 로고    scopus 로고
    • Characterization of the transforming activity of p80, a hyperpho-sphorylated protein in a Ki-1 lymphoma cell line with chromosomal translocation t(2;5)
    • Fujimoto J, Shiota M, Iwahara T, Seki N, Satoh H, Mori S, Yamamoto T (1996) Characterization of the transforming activity of p80, a hyperpho-sphorylated protein in a Ki-1 lymphoma cell line with chromosomal translocation t(2;5). Proc Natl Acad Sci USA 93: 4181-4186
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4181-4186
    • Fujimoto, J.1    Shiota, M.2    Iwahara, T.3    Seki, N.4    Satoh, H.5    Mori, S.6    Yamamoto, T.7
  • 20
    • 1642541150 scopus 로고    scopus 로고
    • 17-Allylamino-17- demethoxygeldanamycin (17-AAG) is effective in down-regulating mutated, constitutively activated KIT protein in human mast cells
    • Fumo G, Akin C, Metcalfe DD, Neckers L (2004) 17-Allylamino-17- demethoxygeldanamycin (17-AAG) is effective in down-regulating mutated, constitutively activated KIT protein in human mast cells. Blood 103: 1078-1084
    • (2004) Blood , vol.103 , pp. 1078-1084
    • Fumo, G.1    Akin, C.2    Metcalfe, D.D.3    Neckers, L.4
  • 21
    • 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
    • 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
  • 24
    • 0344822643 scopus 로고    scopus 로고
    • The tyrosine kinase NPM-ALK, associated with anaplastic large cell lymphoma, binds the intracellular domain of the surface receptor CD30 but is not activated by CD30 stimulation
    • Hubinger G, Scheffrahn I, Muller E, Bai R, Duyster J, Morris SW, Schrezenmeier H, Bergmann L (1999) The tyrosine kinase NPM-ALK, associated with anaplastic large cell lymphoma, binds the intracellular domain of the surface receptor CD30 but is not activated by CD30 stimulation. Exp Hematol 27: 1796-1805
    • (1999) Exp Hematol , vol.27 , pp. 1796-1805
    • Hubinger, G.1    Scheffrahn, I.2    Muller, E.3    Bai, R.4    Duyster, J.5    Morris, S.W.6    Schrezenmeier, H.7    Bergmann, L.8
  • 25
    • 0027391629 scopus 로고
    • Small heat shock proteins are molecular chaperones
    • Jakob U, Gaestel M, Engel K, Buchner J (1993) Small heat shock proteins are molecular chaperones. J Biol Chem 268: 1517-1520
    • (1993) J Biol Chem , vol.268 , pp. 1517-1520
    • Jakob, U.1    Gaestel, M.2    Engel, K.3    Buchner, J.4
  • 26
    • 38149015503 scopus 로고    scopus 로고
    • PI3K/PTEN signaling in tumorigenesis and angiogenesis
    • Jiang BH, Liu LZ (2008) PI3K/PTEN signaling in tumorigenesis and angiogenesis. Biochim Biophys Acta 1784: 150-158
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 150-158
    • Jiang, B.H.1    Liu, L.Z.2
  • 28
    • 0037338707 scopus 로고    scopus 로고
    • Bidirectional signaling between the estrogen receptor and the epidermal growth factor receptor
    • Levin ER (2003) Bidirectional signaling between the estrogen receptor and the epidermal growth factor receptor. Mol Endocrinol 17: 309-317
    • (2003) Mol Endocrinol , vol.17 , pp. 309-317
    • Levin, E.R.1
  • 29
    • 0034615701 scopus 로고    scopus 로고
    • Disruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation
    • Lewis J, Devin A, Miller A, Lin Y, Rodriguez Y, Neckers L, Liu ZG (2000) Disruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation. J Biol Chem 275: 10519-10526
    • (2000) J Biol Chem , vol.275 , pp. 10519-10526
    • Lewis, J.1    Devin, A.2    Miller, A.3    Lin, Y.4    Rodriguez, Y.5    Neckers, L.6    Liu, Z.G.7
  • 30
    • 0035754080 scopus 로고    scopus 로고
    • To cycle or not to cycle: A critical decision in cancer
    • Malumbres M, Barbacid M (2001) To cycle or not to cycle: a critical decision in cancer. Nat Rev Cancer 1: 222-231
    • (2001) Nat Rev Cancer , vol.1 , pp. 222-231
    • Malumbres, M.1    Barbacid, M.2
  • 32
    • 4444311881 scopus 로고    scopus 로고
    • Simultaneous inhibition of hsp 90 and the proteasome promotes protein ubiquitination, causes endoplasmic reticulum-derived cytosolic vacuolization, and enhances antitumor activity
    • Mimnaugh EG, Xu W, Vos M, Yuan X, Isaacs JS, Bisht KS, Gius D, Neckers L (2004) Simultaneous inhibition of hsp 90 and the proteasome promotes protein ubiquitination, causes endoplasmic reticulum-derived cytosolic vacuolization, and enhances antitumor activity. Mol Cancer Ther 3: 551-566
    • (2004) Mol Cancer Ther , vol.3 , pp. 551-566
    • Mimnaugh, E.G.1    Xu, W.2    Vos, M.3    Yuan, X.4    Isaacs, J.S.5    Bisht, K.S.6    Gius, D.7    Neckers, L.8
  • 33
    • 34547616810 scopus 로고    scopus 로고
    • Selective suppression of lymphomas by functional loss of Hsfl in a p53-deficient mouse model for spontaneous tumors
    • Min JN, Huang L, Zimonjic DB, Moskophidis D, Mivechi NF (2007) Selective suppression of lymphomas by functional loss of Hsfl in a p53-deficient mouse model for spontaneous tumors. Oncogene 26: 5086 - 5097
    • (2007) Oncogene , vol.26 , pp. 5086-5097
    • Min, J.N.1    Huang, L.2    Zimonjic, D.B.3    Moskophidis, D.4    Mivechi, N.F.5
  • 34
    • 67349097679 scopus 로고    scopus 로고
    • Tanespimycin (an Hsp90 inhibitor) and trastuzumab is an active combination in patients (pts) with Her2-positive trastuzumab-refractory metastatic breast cancer (MBC): Phase 2 trial
    • Modi S, Stopeck A, Kinden H, Sugarman S, Ma W, Solit D, Kersey K, Johnson R, Hannah AL, Hudis C (2007a) Tanespimycin (an Hsp90 inhibitor) and trastuzumab is an active combination in patients (pts) with Her2-positive trastuzumab-refractory metastatic breast cancer (MBC): phase 2 trial. Breast Cancer Res Treat 106: S269-S270
    • (2007) Breast Cancer Res Treat , vol.106
    • Modi, S.1    Stopeck, A.2    Kinden, H.3    Sugarman, S.4    Ma, W.5    Solit, D.6    Kersey, K.7    Johnson, R.8    Hannah, A.L.9    Hudis, C.10
  • 36
    • 0035266132 scopus 로고    scopus 로고
    • Geldanamycin and its analogue 17-allylamino-17-demethoxygeldanamycin lowers Bcr-Abl levels and induces apoptosis and differentiation of Bcr-Abl-positive human leukemic blasts
    • Nimmanapalli R, O'Bryan E, Bhalla K (2001) Geldanamycin and its analogue 17-allylamino-17-demethoxygeldanamycin lowers Bcr-Abl levels and induces apoptosis and differentiation of Bcr-Abl-positive human leukemic blasts. Cancer Res 61: 1799-1804
    • (2001) Cancer Res , vol.61 , pp. 1799-1804
    • Nimmanapalli, R.1    O'Bryan, E.2    Bhalla, K.3
  • 37
    • 50349096803 scopus 로고    scopus 로고
    • Dual targeting of HSC70 and HSP72 inhibits HSP90 function and induces tumor-specific apoptosis
    • Powers MV, Clarke PA, Workman P (2008) Dual targeting of HSC70 and HSP72 inhibits HSP90 function and induces tumor-specific apoptosis. Cancer Cell 14: 250-262
    • (2008) Cancer Cell , vol.14 , pp. 250-262
    • Powers, M.V.1    Clarke, P.A.2    Workman, P.3
  • 38
    • 34447507818 scopus 로고    scopus 로고
    • Inhibitors of the heat shock response: Biology and pharmacology
    • Powers MV, Workman P (2007) Inhibitors of the heat shock response: biology and pharmacology. FEBS Lett 581: 3758-3769
    • (2007) FEBS Lett , vol.581 , pp. 3758-3769
    • Powers, M.V.1    Workman, P.2
  • 39
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt WB, Toft DO (2003) Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp Biol Med (Maywood, NJ) 228: 111-133
    • (2003) Exp Biol Med (Maywood, NJ) , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 40
    • 15744402283 scopus 로고    scopus 로고
    • Cotreatment with suberanoylanilide hydroxamic acid and 17-allylamino 17-demethoxygeldanamycin synergistically induces apoptosis in Bcr-Abl+ Cells sensitive and resistant to STI571 (imatinib mesylate) in association with down-regulation of Bcr-Abl, abrogation of signal transducer and activator of transcription 5 activity, and Bax conformational change
    • Rahmani M, Reese E, Dai Y, Bauer C, Kramer LB, Huang M, Jove R, Dent P, Grant S (2005) Cotreatment with suberanoylanilide hydroxamic acid and 17-allylamino 17-demethoxygeldanamycin synergistically induces apoptosis in Bcr-Abl+ Cells sensitive and resistant to STI571 (imatinib mesylate) in association with down-regulation of Bcr-Abl, abrogation of signal transducer and activator of transcription 5 activity, and Bax conformational change. Mol Pharmacol 67: 1166-1176
    • (2005) Mol Pharmacol , vol.67 , pp. 1166-1176
    • Rahmani, M.1    Reese, E.2    Dai, Y.3    Bauer, C.4    Kramer, L.B.5    Huang, M.6    Jove, R.7    Dent, P.8    Grant, S.9
  • 42
    • 0034718540 scopus 로고    scopus 로고
    • Modulation of Akt kinase activity by binding to Hsp90
    • Sato S, Fujita N, Tsuruo T (2000) Modulation of Akt kinase activity by binding to Hsp90. Proc Natl Acad Sci USA 97: 10832-10837
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10832-10837
    • Sato, S.1    Fujita, N.2    Tsuruo, T.3
  • 43
    • 33749316418 scopus 로고    scopus 로고
    • The epidermal growth factor receptor pathway: A model for targeted therapy
    • Scaltriti M, Baselga J (2006) The epidermal growth factor receptor pathway: a model for targeted therapy. Clin Cancer Res 12: 5268-5272
    • (2006) Clin Cancer Res , vol.12 , pp. 5268-5272
    • Scaltriti, M.1    Baselga, J.2
  • 45
    • 34548785473 scopus 로고    scopus 로고
    • Non-oncogene addiction and the stress phenotype of cancer cells
    • Solimini NL, Luo J, Elledge SJ (2007) Non-oncogene addiction and the stress phenotype of cancer cells. Cell 130: 986-988
    • (2007) Cell , vol.130 , pp. 986-988
    • Solimini, N.L.1    Luo, J.2    Elledge, S.J.3
  • 46
    • 37649024109 scopus 로고    scopus 로고
    • Development and application of Hsp90 inhibitors
    • Solit DB, Chiosis G (2008) Development and application of Hsp90 inhibitors. Drug Discov Today 13: 38-43
    • (2008) Drug Discov Today , vol.13 , pp. 38-43
    • Solit, D.B.1    Chiosis, G.2
  • 48
    • 0034751220 scopus 로고    scopus 로고
    • Estrogen receptor and breast cancer
    • Sommer S, Fuqua SA (2001) Estrogen receptor and breast cancer. Sem Cancer Biol 11: 339-352
    • (2001) Sem Cancer Biol , vol.11 , pp. 339-352
    • Sommer, S.1    Fuqua, S.A.2
  • 49
    • 0034660856 scopus 로고    scopus 로고
    • Inhibition of Hsp90 function by ansamycins causes retinoblastoma gene product-dependent Gl arrest
    • Srethapakdi M, Liu F, Tavorath R, Rosen N (2000) Inhibition of Hsp90 function by ansamycins causes retinoblastoma gene product-dependent Gl arrest. Cancer Res 60: 3940-3946
    • (2000) Cancer Res , vol.60 , pp. 3940-3946
    • Srethapakdi, M.1    Liu, F.2    Tavorath, R.3    Rosen, N.4
  • 52
    • 0034650543 scopus 로고    scopus 로고
    • The geldanamycins are potent inhibitors of the hepatocyte growth factor/scatter factor-met-urokinase plasminogen activator-plasmin proteolytic network
    • Webb CP, Hose CD, Koochekpour S, Jeffers M, Oskarsson M, Sausville E, Monks A, Vande Woude GF (2000) The geldanamycins are potent inhibitors of the hepatocyte growth factor/scatter factor-met-urokinase plasminogen activator-plasmin proteolytic network. Cancer Res 60: 342 - 349
    • (2000) Cancer Res , vol.60 , pp. 342-349
    • Webb, C.P.1    Hose, C.D.2    Koochekpour, S.3    Jeffers, M.4    Oskarsson, M.5    Sausville, E.6    Monks, A.7    Vande Woude, G.F.8
  • 54
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • Whitesell L, Lindquist SL (2005) HSP90 and the chaperoning of cancer. Nat Rev Cancer 5: 761 - 772
    • (2005) Nat Rev Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 55
    • 0031909866 scopus 로고    scopus 로고
    • The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent
    • Whitesell L, Sutphin PD, Pulcini EJ, Martinez JD, Cook PH (1998) The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent. Mol Cell Biol 18: 1517-1524
    • (1998) Mol Cell Biol , vol.18 , pp. 1517-1524
    • Whitesell, L.1    Sutphin, P.D.2    Pulcini, E.J.3    Martinez, J.D.4    Cook, P.H.5
  • 56
    • 0033229880 scopus 로고    scopus 로고
    • HSF1 is required for extra-embryonic development, postnatal growth and protection during inflammatory responses in mice
    • Xiao X, Zuo X, Davis AA, McMillan DR, Curry BB, Richardson JA, Benjamin IJ (1999) HSF1 is required for extra-embryonic development, postnatal growth and protection during inflammatory responses in mice. EMBO J 18:5943-5952
    • (1999) EMBO J , vol.18 , pp. 5943-5952
    • Xiao, X.1    Zuo, X.2    Davis, A.A.3    McMillan, D.R.4    Curry, B.B.5    Richardson, J.A.6    Benjamin, I.J.7
  • 57
    • 34250162144 scopus 로고    scopus 로고
    • Targeting the molecular chaperone heat shock protein 90 provides a multifaceted effect on diverse cell signaling pathways of cancer cells
    • Xu W, Neckers L (2007) Targeting the molecular chaperone heat shock protein 90 provides a multifaceted effect on diverse cell signaling pathways of cancer cells. Clin Cancer Res 13: 1625 - 1629
    • (2007) Clin Cancer Res , vol.13 , pp. 1625-1629
    • Xu, W.1    Neckers, L.2
  • 58
    • 5044239107 scopus 로고    scopus 로고
    • Pathways of chaperone- mediated protein folding in the cytosol
    • Young JC, Agashe VR, Siegers K, Hard FU (2004) Pathways of chaperone- mediated protein folding in the cytosol. Nat Rev 5: 781 - 791
    • (2004) Nat Rev , vol.5 , pp. 781-791
    • Young, J.C.1    Agashe, V.R.2    Siegers, K.3    Hard, F.U.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.