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Volumn 53, Issue 20, 2010, Pages 7280-7286

ATPases as drug targets: Insights from heat shock proteins 70 and 90

Author keywords

[No Author keywords available]

Indexed keywords

15 DEOXYSPERGUALIN; 5 (2,4 DIHYDROXY 5 ISOPROPYLPHENYL) 4 (4 MORPHOLINOMETHYLPHENYL) 3 ISOXAZOLECARBOXYLIC ACID ETHYLAMIDE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATASE INHIBITOR; ANTINEOPLASTIC AGENT; BEP NVP 800; BIIB 021; BIIB 0221; DMT 003052; GALACTOLIPID; GELDANAMYCIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; IPI 493; NVP BEP 800; PHENYLETHYNESULFONAMIDE; RADICICOL; SNX 5422; STA 9090; SULFONAMIDE; TANESPIMYCIN; TANESPIMYCIN HYDROQUINONE; UNCLASSIFIED DRUG; VER 155008; XL 888; ADENOSINE TRIPHOSPHATE; PROTEIN BINDING;

EID: 77958516062     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm100342z     Document Type: Review
Times cited : (60)

References (59)
  • 1
    • 0036718795 scopus 로고    scopus 로고
    • ATPases as drug targets: Learning from their structure
    • Chene, P. ATPases as drug targets: learning from their structure Nat. Rev. Drug Discovery 2002, 1 (9) 665-673
    • (2002) Nat. Rev. Drug Discovery , vol.1 , Issue.9 , pp. 665-673
    • Chene, P.1
  • 2
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • Whitesell, L.; Lindquist, S. L. HSP90 and the chaperoning of cancer Nat. Rev. Cancer 2005, 5 (10) 761-772
    • (2005) Nat. Rev. Cancer , vol.5 , Issue.10 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 3
    • 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, E. G.; Xu, W.; Vos, M.; Yuan, X.; Isaacs, J. S.; Bisht, K. S.; Gius, D.; Neckers, L. Simultaneous inhibition of hsp 90 and the proteasome promotes protein ubiquitination, causes endoplasmic reticulum-derived cytosolic vacuolization, and enhances antitumor activity Mol. Cancer Ther. 2004, 3 (5) 551-566
    • (2004) Mol. Cancer Ther. , vol.3 , Issue.5 , 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
  • 4
    • 35348890981 scopus 로고    scopus 로고
    • Drugging the cancer chaperone HSP90: Combinatorial therapeutic expolitation on oncogene addiction and tumor stress
    • Workman, P.; Burrows, F.; Neckers, L.; Rosen, N. Drugging the cancer chaperone HSP90: combinatorial therapeutic expolitation on oncogene addiction and tumor stress Ann. N.Y. Acad. Sci. 2007, 1113 (Stress Responses in Biology and Medicine) 202-216
    • (2007) Ann. N.Y. Acad. Sci. , vol.1113 , pp. 202-216
    • Workman, P.1    Burrows, F.2    Neckers, L.3    Rosen, N.4
  • 5
    • 51449093764 scopus 로고    scopus 로고
    • Targeting Hsp90: Small-molecule inhibitors and their clinical development
    • Taldone, T.; Gozman, A.; Maharaj, R.; Chiosis, G. Targeting Hsp90: small-molecule inhibitors and their clinical development Curr. Opin. Pharmacol. 2008, 8 (4) 370-374
    • (2008) Curr. Opin. Pharmacol. , vol.8 , Issue.4 , pp. 370-374
    • Taldone, T.1    Gozman, A.2    Maharaj, R.3    Chiosis, G.4
  • 7
    • 62449226171 scopus 로고    scopus 로고
    • Acquired resistance to 17-allylamino-17-demethoxygeldanamycin (tanespimycin) in glioblastoma cells
    • Gaspar, N.; Sharp, S. Y.; Pacey, S.; Jones, D.; Walton, M.; Vassal, G.; Eccles, S.; Pearson, A.; Workman, P. Acquired resistance to 17-allylamino-17- demethoxygeldanamycin (tanespimycin) in glioblastoma cells Cancer Res. 2009, 69 (5) 1966-1975
    • (2009) Cancer Res. , vol.69 , Issue.5 , pp. 1966-1975
    • Gaspar, N.1    Sharp, S.Y.2    Pacey, S.3    Jones, D.4    Walton, M.5    Vassal, G.6    Eccles, S.7    Pearson, A.8    Workman, P.9
  • 14
    • 62149135294 scopus 로고    scopus 로고
    • Discovery and development of heat shock protein 90 inhibitors
    • Taldone, T.; Sun, W.; Chiosis, G. Discovery and development of heat shock protein 90 inhibitors Bioorg. Med. Chem. 2009, 17 (6) 2225-2235
    • (2009) Bioorg. Med. Chem. , vol.17 , Issue.6 , pp. 2225-2235
    • Taldone, T.1    Sun, W.2    Chiosis, G.3
  • 16
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: Cellular functions and molecular mechanism
    • Mayer, M. P.; Bukau, B. Hsp70 chaperones: cellular functions and molecular mechanism Cell. Mol. Life Sci. 2005, 62 (6) 670-684
    • (2005) Cell. Mol. Life Sci. , vol.62 , Issue.6 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 17
  • 18
    • 0642377466 scopus 로고    scopus 로고
    • More than folding: Localized functions of cytosolic chaperones
    • Young, J. C.; Barral, J. M.; Ulrich, H. F. More than folding: localized functions of cytosolic chaperones Trends Biochem. Sci. 2003, 28 (10) 541-547
    • (2003) Trends Biochem. Sci. , vol.28 , Issue.10 , pp. 541-547
    • Young, J.C.1    Barral, J.M.2    Ulrich, H.F.3
  • 19
    • 0034515269 scopus 로고    scopus 로고
    • Heat shock protein 70 is required for the survival of cancer cells
    • Nylandsted, J.; Brand, K.; Jaattela, M. Heat shock protein 70 is required for the survival of cancer cells Ann. N.Y. Acad. Sci. 2000, 926, 122-125
    • (2000) Ann. N.Y. Acad. Sci. , vol.926 , pp. 122-125
    • Nylandsted, J.1    Brand, K.2    Jaattela, M.3
  • 20
    • 0037115547 scopus 로고    scopus 로고
    • Eradication of glioblastoma, and breast and colon carcinoma xenografts by Hsp70 depletion
    • Nylandsted, J.; Wick, W.; Hirt, U. A.; Brand, K.; Rohde, M.; Leist, M.; Weller, M.; Jaattela, M. Eradication of glioblastoma, and breast and colon carcinoma xenografts by Hsp70 depletion Cancer Res. 2002, 62 (24) 7139-7142
    • (2002) Cancer Res. , vol.62 , Issue.24 , pp. 7139-7142
    • Nylandsted, J.1    Wick, W.2    Hirt, U.A.3    Brand, K.4    Rohde, M.5    Leist, M.6    Weller, M.7    Jaattela, M.8
  • 22
    • 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
    • Guo, F.; Rocha, K.; Bali, P.; Pranpat, M.; Fiskus, W.; Boyapalle, S.; Kumaraswamy, S.; Balasis, M.; Greedy, B.; Armitage, E. S.; Lawrence, N.; Bhalla, K. 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. 2005, 65 (22) 10536-10544
    • (2005) Cancer Res. , vol.65 , Issue.22 , pp. 10536-10544
    • Guo, F.1    Rocha, K.2    Bali, P.3    Pranpat, M.4    Fiskus, W.5    Boyapalle, S.6    Kumaraswamy, S.7    Balasis, M.8    Greedy, B.9    Armitage, E.S.10    Lawrence, N.11    Bhalla, K.12
  • 23
    • 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, V. L.; Budagova, K. R.; Sherman, M. Y. 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 2005, 24 (20) 3328-3338
    • (2005) Oncogene , vol.24 , Issue.20 , pp. 3328-3338
    • Gabai, V.L.1    Budagova, K.R.2    Sherman, M.Y.3
  • 24
    • 32944454483 scopus 로고    scopus 로고
    • Targeting heat shock response to sensitize cancer cells to proteasome and Hsp90 inhibitors
    • Zaarur, N.; Gabai, V. L.; Porco, J. A., Jr.; Calderwood, S.; Sherman, M. Y. Targeting heat shock response to sensitize cancer cells to proteasome and Hsp90 inhibitors Cancer Res. 2006, 66 (3) 1783-1791
    • (2006) Cancer Res. , vol.66 , Issue.3 , pp. 1783-1791
    • Zaarur, N.1    Gabai, V.L.2    Porco Jr., J.A.3    Calderwood, S.4    Sherman, M.Y.5
  • 25
    • 50349096803 scopus 로고    scopus 로고
    • Dual targeting of HSC70 and HSP72 inhibits HSP90 function and induces tumor-specific apoptosis
    • Powers, M. V.; Clarke, P. A.; Workman, P. Dual targeting of HSC70 and HSP72 inhibits HSP90 function and induces tumor-specific apoptosis Cancer Cell 2008, 14 (3) 250-262
    • (2008) Cancer Cell , vol.14 , Issue.3 , pp. 250-262
    • Powers, M.V.1    Clarke, P.A.2    Workman, P.3
  • 26
    • 77953734857 scopus 로고    scopus 로고
    • Heat shock protein 70 (Hsp70) as an emerging drug target
    • Evans, C. G.; Chang, L.; Gestwicki, J. E. Heat shock protein 70 (Hsp70) as an emerging drug target J. Med. Chem. 2010, 53 (12) 4585-4602
    • (2010) J. Med. Chem. , vol.53 , Issue.12 , pp. 4585-4602
    • Evans, C.G.1    Chang, L.2    Gestwicki, J.E.3
  • 27
    • 77953576838 scopus 로고    scopus 로고
    • Targeting HSP70: The second potentially druggable heat shock protein and molecular chaperone?
    • Powers, M. V.; Jones, K.; Barillari, C.; Westwood, I.; van Montfort, R. L.; Workman, P. 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    Jones, K.2    Barillari, C.3    Westwood, I.4    Van Montfort, R.L.5    Workman, P.6
  • 30
    • 70349768075 scopus 로고    scopus 로고
    • A small molecule inhibitor of inducible heat shock protein 70
    • Leu, J. I.; Pimkina, J.; Frank, A.; Murphy, M. E.; George, D. L. A small molecule inhibitor of inducible heat shock protein 70 Mol. Cell 2009, 36 (1) 15-27
    • (2009) Mol. Cell , vol.36 , Issue.1 , pp. 15-27
    • Leu, J.I.1    Pimkina, J.2    Frank, A.3    Murphy, M.E.4    George, D.L.5
  • 31
    • 74249097474 scopus 로고    scopus 로고
    • Pharmacological targeting of the Hsp70 chaperone
    • Patury, S.; Miyata, Y.; Gestwicki, J. E. Pharmacological targeting of the Hsp70 chaperone Curr. Top. Med. Chem. 2009, 9 (15) 1337-1351
    • (2009) Curr. Top. Med. Chem. , vol.9 , Issue.15 , pp. 1337-1351
    • Patury, S.1    Miyata, Y.2    Gestwicki, J.E.3
  • 32
    • 10944263745 scopus 로고    scopus 로고
    • Small molecule modulators of endogenous and co-chaperone-stimulated Hsp70 ATPase activity
    • Fewell, S. W.; Smith, C. M.; Lyon, M. A.; Dumitrescu, T. P.; Wipf, P.; Day, B. W.; Brodsky, J. L. Small molecule modulators of endogenous and co-chaperone-stimulated Hsp70 ATPase activity J. Biol. Chem. 2004, 279 (49) 51131-51140
    • (2004) J. Biol. Chem. , vol.279 , Issue.49 , pp. 51131-51140
    • Fewell, S.W.1    Smith, C.M.2    Lyon, M.A.3    Dumitrescu, T.P.4    Wipf, P.5    Day, B.W.6    Brodsky, J.L.7
  • 33
    • 0035847010 scopus 로고    scopus 로고
    • Identification of an inhibitor of hsc70-mediated protein translocation and ATP hydrolysis
    • Fewell, S. W.; Day, B. W.; Brodsky, J. L. Identification of an inhibitor of hsc70-mediated protein translocation and ATP hydrolysis J. Biol. Chem. 2001, 276 (2) 910-914
    • (2001) J. Biol. Chem. , vol.276 , Issue.2 , pp. 910-914
    • Fewell, S.W.1    Day, B.W.2    Brodsky, J.L.3
  • 34
    • 39149117364 scopus 로고    scopus 로고
    • Identification of small molecules that modify the protein folding activity of heat shock protein 70
    • Wisen, S.; Gestwicki, J. E. Identification of small molecules that modify the protein folding activity of heat shock protein 70 Anal. Biochem. 2008, 374 (2) 371-377
    • (2008) Anal. Biochem. , vol.374 , Issue.2 , pp. 371-377
    • Wisen, S.1    Gestwicki, J.E.2
  • 35
    • 0035808322 scopus 로고    scopus 로고
    • The ATPase domain of hsp70 possesses a unique binding specificity for 3′-sulfogalactolipids
    • Mamelak, D.; Lingwood, C. The ATPase domain of hsp70 possesses a unique binding specificity for 3′-sulfogalactolipids J. Biol. Chem. 2001, 276 (1) 449-456
    • (2001) J. Biol. Chem. , vol.276 , Issue.1 , pp. 449-456
    • Mamelak, D.1    Lingwood, C.2
  • 36
    • 0037452541 scopus 로고    scopus 로고
    • 3′-Sulfogalactolipid binding specifically inhibits Hsp70 ATPase activity in vitro
    • Whetstone, H.; Lingwood, C. 3′-Sulfogalactolipid binding specifically inhibits Hsp70 ATPase activity in vitro Biochemistry 2003, 42 (6) 1611-1617
    • (2003) Biochemistry , vol.42 , Issue.6 , pp. 1611-1617
    • Whetstone, H.1    Lingwood, C.2
  • 37
    • 77958487220 scopus 로고    scopus 로고
    • version 2.2; Schrodinger LLC (120 West 45th Street, New York, NY 10036)
    • SiteMap, version 2.2; Schrodinger LLC (120 West 45th Street, New York, NY 10036), 2008.
    • (2008) SiteMap
  • 38
    • 65249117514 scopus 로고    scopus 로고
    • Identifying and characterizing binding sites and assessing druggability
    • Halgren, T. A. Identifying and characterizing binding sites and assessing druggability J. Chem. Inf. Model. 2009, 49, 377-389
    • (2009) J. Chem. Inf. Model. , vol.49 , pp. 377-389
    • Halgren, T.A.1
  • 39
    • 67650999672 scopus 로고    scopus 로고
    • Lessons for fragment library design: Analysis of output from multiple screening campaigns
    • Chen, I. J.; Hubbard, R. E. Lessons for fragment library design: analysis of output from multiple screening campaigns J. Comput.-Aided Mol. Des. 2009, 23, 603-620
    • (2009) J. Comput.-Aided Mol. Des. , vol.23 , pp. 603-620
    • Chen, I.J.1    Hubbard, R.E.2
  • 40
    • 17144373303 scopus 로고    scopus 로고
    • Druggability indices for protein targets derived from NMR-based screening data
    • Hajduk, P. J.; Huth, J. R.; Fesik, S. W. Druggability indices for protein targets derived from NMR-based screening data J. Med. Chem. 2005, 48 (7) 2518-2525
    • (2005) J. Med. Chem. , vol.48 , Issue.7 , pp. 2518-2525
    • Hajduk, P.J.1    Huth, J.R.2    Fesik, S.W.3
  • 41
    • 36248956723 scopus 로고    scopus 로고
    • The SeeDs approach: Integrating fragments into drug discovery
    • Hubbard, R. E.; Davis, B.; Chen, I.; Drysdale, M. J. The SeeDs approach: integrating fragments into drug discovery Curr. Top. Med. Chem. 2007, 7 (16) 1568-1581
    • (2007) Curr. Top. Med. Chem. , vol.7 , Issue.16 , pp. 1568-1581
    • Hubbard, R.E.1    Davis, B.2    Chen, I.3    Drysdale, M.J.4
  • 44
    • 0034602451 scopus 로고    scopus 로고
    • C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle
    • Weikl, T.; Muschler, P.; Richter, K.; Veit, T.; Reinstein, J.; Buchner, J. C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle J. Mol. Biol. 2000, 303 (4) 583-592
    • (2000) J. Mol. Biol. , vol.303 , Issue.4 , pp. 583-592
    • Weikl, T.1    Muschler, P.2    Richter, K.3    Veit, T.4    Reinstein, J.5    Buchner, J.6
  • 45
    • 0028584378 scopus 로고
    • ATPase kinetics of recombinant bovine 70 kDa heat shock cognate protein and its amino-terminal ATPase domain
    • Ha, J. H.; McKay, D. B. ATPase kinetics of recombinant bovine 70 kDa heat shock cognate protein and its amino-terminal ATPase domain Biochemistry 1994, 33 (48) 14625-14635
    • (1994) Biochemistry , vol.33 , Issue.48 , pp. 14625-14635
    • Ha, J.H.1    McKay, D.B.2
  • 46
    • 33746286154 scopus 로고    scopus 로고
    • Spectroscopic and thermodynamic measurements of nucleotide-induced changes in the human 70-kDa heat shock cognate protein
    • Borges, J. C.; Ramos, C. H. Spectroscopic and thermodynamic measurements of nucleotide-induced changes in the human 70-kDa heat shock cognate protein Arch. Biochem. Biophys. 2006, 452 (1) 46-54
    • (2006) Arch. Biochem. Biophys. , vol.452 , Issue.1 , pp. 46-54
    • Borges, J.C.1    Ramos, C.H.2
  • 47
    • 0031569356 scopus 로고    scopus 로고
    • Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain
    • Sriram, M.; Osipiuk, J.; Freeman, B.; Morimoto, R.; Joachimiak, A. Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain Structure 1997, 5 (3) 403-414
    • (1997) Structure , vol.5 , Issue.3 , pp. 403-414
    • Sriram, M.1    Osipiuk, J.2    Freeman, B.3    Morimoto, R.4    Joachimiak, A.5
  • 48
    • 0035936826 scopus 로고    scopus 로고
    • Structure of a Bag/Hsc70 complex: Convergent functional evolution of Hsp70 nucleotide exchange factors
    • Sondermann, H.; Scheufler, C.; Schneider, C.; Hohfeld, J.; Hartl, F. U.; Moarefi, I. Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors Science 2001, 291 (5508) 1553-1557
    • (2001) Science , vol.291 , Issue.5508 , pp. 1553-1557
    • Sondermann, H.1    Scheufler, C.2    Schneider, C.3    Hohfeld, J.4    Hartl, F.U.5    Moarefi, I.6
  • 49
    • 33646195474 scopus 로고
    • The hydrogen bond in molecular recognition
    • Fersht, A. R. The hydrogen bond in molecular recognition Trends Biochem. Sci. 1987, 12, 301-304
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 301-304
    • Fersht, A.R.1
  • 50
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou, C.; Roe, S. M.; OBrien, R.; Ladbury, J. E.; Piper, P. W.; Pearl, L. H. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone Cell 1997, 90 (1) 65-75
    • (1997) Cell , vol.90 , Issue.1 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    Obrien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 51
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins, C. E.; Russo, A. A.; Schneider, C.; Rosen, N.; Hartl, F. U.; Pavletich, N. P. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent Cell 1997, 89 (2) 239-250
    • (1997) Cell , vol.89 , Issue.2 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 52
    • 0037352446 scopus 로고    scopus 로고
    • Structural and functional analysis of the middle segment of hsp90: Implications for ATP hydrolysis and client protein and cochaperone interactions
    • Meyer, P.; Prodromou, C.; Hu, B.; Vaughan, C.; Roe, S. M.; Panaretou, B.; Piper, P. W.; Pearl, L. H. Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions Mol. Cell 2003, 11 (3) 647-658
    • (2003) Mol. Cell , vol.11 , Issue.3 , pp. 647-658
    • Meyer, P.1    Prodromou, C.2    Hu, B.3    Vaughan, C.4    Roe, S.M.5    Panaretou, B.6    Piper, P.W.7    Pearl, L.H.8
  • 56
    • 70350547754 scopus 로고    scopus 로고
    • Short peptides derived from the BAG-1 C-terminus inhibit the interaction between BAG-1 and HSC70 and decrease breast cancer cell growth
    • Sharp, A.; Cutress, R. I.; Johnson, P. W.; Packham, G.; Townsend, P. A. Short peptides derived from the BAG-1 C-terminus inhibit the interaction between BAG-1 and HSC70 and decrease breast cancer cell growth FEBS Lett. 2009, 583 (21) 3405-3411
    • (2009) FEBS Lett. , vol.583 , Issue.21 , pp. 3405-3411
    • Sharp, A.1    Cutress, R.I.2    Johnson, P.W.3    Packham, G.4    Townsend, P.A.5
  • 57
    • 61449261930 scopus 로고    scopus 로고
    • Death by chaperone: HSP90, HSP70 or both?
    • Powers, M. V.; Clarke, P. A.; Workman, P. Death by chaperone: HSP90, HSP70 or both? Cell Cycle 2009, 8 (4) 518-526
    • (2009) Cell Cycle , vol.8 , Issue.4 , pp. 518-526
    • Powers, M.V.1    Clarke, P.A.2    Workman, P.3
  • 58
    • 74849095191 scopus 로고    scopus 로고
    • Drugging the heat shock factor 1 pathway: Exploitation of the critical cancer cell dependence on the guardian of the proteome
    • de Billy, E.; Powers, M. V.; Smith, J. R.; Workman, P. Drugging the heat shock factor 1 pathway: exploitation of the critical cancer cell dependence on the guardian of the proteome Cell Cycle 2009, 8 (23) 3806-3808
    • (2009) Cell Cycle , vol.8 , Issue.23 , pp. 3806-3808
    • De Billy, E.1    Powers, M.V.2    Smith, J.R.3    Workman, P.4
  • 59
    • 24944497371 scopus 로고    scopus 로고
    • Features of selective kinase inhibitors
    • Knight, Z. A.; Shokat, K. M. Features of selective kinase inhibitors Chem. Biol. 2005, 12 (6) 621-637
    • (2005) Chem. Biol. , vol.12 , Issue.6 , pp. 621-637
    • Knight, Z.A.1    Shokat, K.M.2


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