메뉴 건너뛰기




Volumn 49, Issue 16, 2006, Pages 4953-4960

Structural and quantum chemical studies of 8-aryl-sulfanyl adenine class Hsp90 inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE DERIVATIVE; ANTINEOPLASTIC AGENT; BROMINE; CHAPERONE; CHLORINE; HALIDE; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; IODINE; POLYCYCLIC AROMATIC HYDROCARBON DERIVATIVE; PU H64; PU H71;

EID: 33746914732     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm060297x     Document Type: Article
Times cited : (93)

References (45)
  • 1
    • 0035989680 scopus 로고    scopus 로고
    • HSP90 as a new therapeutic target for cancer therapy: The story unfolds
    • Maloney, A.; Workman, P. HSP90 as a new therapeutic target for cancer therapy: the story unfolds. Expert Opin. Biol. Ther. 2002, 2, 3-24.
    • (2002) Expert Opin. Biol. Ther. , vol.2 , pp. 3-24
    • Maloney, A.1    Workman, P.2
  • 2
    • 12344291243 scopus 로고    scopus 로고
    • Hsp90 and Cdc37 - A chaperone cancer conspiracy
    • Pearl, L. H. Hsp90 and Cdc37-a chaperone cancer conspiracy. Curr. Opin. Genet. Dev. 2005, 15, 55-61.
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 55-61
    • Pearl, L.H.1
  • 3
    • 7944225978 scopus 로고    scopus 로고
    • Independent ATPase activity of Hsp90 subunits creates a flexible assembly platform
    • McLaughlin, S. H.; Ventouras, L. A.; Lobbezoo, B.; Jackson, S. E. Independent ATPase activity of Hsp90 subunits creates a flexible assembly platform. J. Mol. Biol. 2004, 344, 813-826.
    • (2004) J. Mol. Biol. , vol.344 , pp. 813-826
    • McLaughlin, S.H.1    Ventouras, L.A.2    Lobbezoo, B.3    Jackson, S.E.4
  • 4
    • 4444291743 scopus 로고    scopus 로고
    • The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle
    • Richter, K.; Walter, S.; Buchner, J. The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle. J. Mol. Biol. 2004, 342, 1403-1413.
    • (2004) J. Mol. Biol. , vol.342 , pp. 1403-1413
    • Richter, K.1    Walter, S.2    Buchner, J.3
  • 5
    • 24044518180 scopus 로고    scopus 로고
    • Structure of unliganded GRP94, the endoplasmic reticulum Hsp90: Basis for nucleotide-induced conformational change
    • Dollins, D. E.; Immormino, R. M.; Gewirth, D. T. Structure of unliganded GRP94, the endoplasmic reticulum Hsp90: Basis for nucleotide-induced conformational change. J. Biol Chem. 2005, 280, 30438-30447.
    • (2005) J. Biol. Chem. , vol.280 , pp. 30438-30447
    • Dollins, D.E.1    Immormino, R.M.2    Gewirth, D.T.3
  • 6
    • 8544249185 scopus 로고    scopus 로고
    • Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone
    • Immormino, R. M.; Dollins, D. E.; Shaffer, P. L.; Soldano, K. L.; Walker, M. A.; et al. Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone. J. Biol. Chem. 2004, 279, 46162-46171.
    • (2004) J. Biol. Chem. , vol.279 , pp. 46162-46171
    • Immormino, R.M.1    Dollins, D.E.2    Shaffer, P.L.3    Soldano, K.L.4    Walker, M.A.5
  • 7
    • 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.; O'Brien, R.; Ladbury, J. E.; Piper, P. W.; et al. Identification and structural characterization of the ATP/ ADP-binding site in the Hsp90 molecular chaperone. Cell 1997, 90, 65-75.
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5
  • 8
    • 0034711270 scopus 로고    scopus 로고
    • The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone
    • Marcu, M. G.; Chadli, A.; Bouhouche, I.; Catelli, M.; Neckers, L. M. The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone. J. Biol. Chem. 2000, 275, 37181-37186.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37181-37186
    • Marcu, M.G.1    Chadli, A.2    Bouhouche, I.3    Catelli, M.4    Neckers, L.M.5
  • 10
    • 0031895351 scopus 로고    scopus 로고
    • The hsp90-based chaperone system: Involvement in signal transduction from a variety of hormone and growth factor receptors
    • Pratt, W. B. The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors. Proc. Soc. Exp. Biol. Med. 1998, 217, 420-434.
    • (1998) Proc. Soc. Exp. Biol. Med. , vol.217 , pp. 420-434
    • Pratt, W.B.1
  • 11
    • 17044403753 scopus 로고    scopus 로고
    • Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding
    • Huai, Q.; Wang, H.; Liu, Y.; Kim, H. Y.; Toft, D.; et al. Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding. Structure (London) 2005, 13, 579-590.
    • (2005) Structure (London) , vol.13 , pp. 579-590
    • Huai, Q.1    Wang, H.2    Liu, Y.3    Kim, H.Y.4    Toft, D.5
  • 12
    • 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.; et al. Structural and functional analysis of the middle segment of hsp90. Implications for ATP hydrolysis and client protein and cochaperone interactions. Mol. Cell 2003, 11, 647-658.
    • (2003) Mol. Cell , vol.11 , pp. 647-658
    • Meyer, P.1    Prodromou, C.2    Hu, B.3    Vaughan, C.4    Roe, S.M.5
  • 14
    • 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, NJ, U.S.) 2003, 228, 111-133.
    • (2003) Exp. Biol. Med. (Maywood, NJ, U.S.) , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 15
    • 0035808455 scopus 로고    scopus 로고
    • Hsp90 regulates p50(cdc37) function during the biogenesis of the active conformation of the heme-regulated eIF2 alpha kinase
    • Shao, J.; Grammatikakis, N.; Scroggins, B. T.; Uma, S.; Huang, W.; et al. Hsp90 regulates p50(cdc37) function during the biogenesis of the active conformation of the heme-regulated eIF2 alpha kinase. J. Biol. Chem. 2001, 276, 206-214.
    • (2001) J. Biol. Chem. , vol.276 , pp. 206-214
    • Shao, J.1    Grammatikakis, N.2    Scroggins, B.T.3    Uma, S.4    Huang, W.5
  • 16
    • 0031590456 scopus 로고    scopus 로고
    • Geldanamycin-induced destabilization of Raf-1 involves the proteasome
    • Schulte, T. W.; An, W. G.; Neckers, L. M. Geldanamycin-induced destabilization of Raf-1 involves the proteasome. Biochem. Biophys. Res. Commun. 1997, 239, 655-659.
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 655-659
    • Schulte, T.W.1    An, W.G.2    Neckers, L.M.3
  • 17
    • 0035071607 scopus 로고    scopus 로고
    • A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells
    • Chiosis, G.; Timaul, M. N.; Lucas, B.; Munster, P. N.; Zheng, F. F.; et al. A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells. Chem. Biol. 2001, 8, 289-299.
    • (2001) Chem. Biol. , vol.8 , pp. 289-299
    • Chiosis, G.1    Timaul, M.N.2    Lucas, B.3    Munster, P.N.4    Zheng, F.F.5
  • 18
    • 23244451884 scopus 로고    scopus 로고
    • Preferential sensitization of tumor cells to radiation by heat shock protein 90 inhibitor geldanamycin
    • Matsumoto, Y.; Machida, H.; Kubota, N. Preferential sensitization of tumor cells to radiation by heat shock protein 90 inhibitor geldanamycin. J. Radiat. Res. (Tokyo) 2005, 46, 215-221.
    • (2005) J. Radiat. Res. (Tokyo) , vol.46 , pp. 215-221
    • Matsumoto, Y.1    Machida, H.2    Kubota, N.3
  • 19
    • 0141596326 scopus 로고    scopus 로고
    • Clinical development of 17-allylamino, 17-demethoxygeldanamycin
    • Sausville, E. A.; Tomaszewski, J. E.; Ivy, P. Clinical development of 17-allylamino, 17-demethoxygeldanamycin. Curr. Cancer Drug Targets 2003, 3, 377-383.
    • (2003) Curr. Cancer Drug Targets , vol.3 , pp. 377-383
    • Sausville, E.A.1    Tomaszewski, J.E.2    Ivy, P.3
  • 20
    • 0034771555 scopus 로고    scopus 로고
    • The Hsp90 inhibitor geldanamycin selectively sensitizes Bcr-Abl-expressing leukemia cells to cytotoxic chemotherapy
    • Blagosklonny, M. V.; Fojo, T.; Bhalla, K. N.; Kim, J. S.; Trepel, J. B.; et al. The Hsp90 inhibitor geldanamycin selectively sensitizes Bcr-Abl-expressing leukemia cells to cytotoxic chemotherapy. Leukemia 2001, 15, 1537-1543.
    • (2001) Leukemia , vol.15 , pp. 1537-1543
    • Blagosklonny, M.V.1    Fojo, T.2    Bhalla, K.N.3    Kim, J.S.4    Trepel, J.B.5
  • 21
    • 0033502429 scopus 로고    scopus 로고
    • Geldanamycin as a potential anti-cancer agent: Its molecular target and biochemical activity
    • Neckers, L.; Schulte, T. W.; Mimnaugh, E. Geldanamycin as a potential anti-cancer agent: its molecular target and biochemical activity. Invest. New Drugs 1999, 17, 361-373.
    • (1999) Invest. New Drugs , vol.17 , pp. 361-373
    • Neckers, L.1    Schulte, T.W.2    Mimnaugh, E.3
  • 22
    • 0031844350 scopus 로고    scopus 로고
    • Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin
    • Schulte, T. W.; Akinaga, S.; Soga, S.; Sullivan, W.; Stensgard, B.; et al. Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin. Cell Stress Chaperones 1998, 3, 100-108.
    • (1998) Cell Stress Chaperones , vol.3 , pp. 100-108
    • Schulte, T.W.1    Akinaga, S.2    Soga, S.3    Sullivan, W.4    Stensgard, B.5
  • 23
    • 3042637928 scopus 로고    scopus 로고
    • Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms
    • Wright, L.; Barril, X.; Dymock, B.; Sheridan, L.; Surgenor, A.; et al. Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms. Chem. Biol. 2004, 11, 775-785.
    • (2004) Chem. Biol. , vol.11 , pp. 775-785
    • Wright, L.1    Barril, X.2    Dymock, B.3    Sheridan, L.4    Surgenor, A.5
  • 24
    • 0035071607 scopus 로고    scopus 로고
    • A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells
    • Chiosis, G.; Timaul, M. N.; Lucas, B.; Munster, P. N.; Zheng, F. F.; et al. A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells. Chem. Biol. 2001, 8, 289-299.
    • (2001) Chem. Biol. , vol.8 , pp. 289-299
    • Chiosis, G.1    Timaul, M.N.2    Lucas, B.3    Munster, P.N.4    Zheng, F.F.5
  • 25
    • 3042553538 scopus 로고    scopus 로고
    • Targeting wide-range oncogenic transformation via PU24FCl, a specific inhibitor of tumor Hsp90
    • Vilenchik, M.; Solit, D.; Basso, A.; Huezo, H.; Lucas, B.; et al. Targeting wide-range oncogenic transformation via PU24FCl, a specific inhibitor of tumor Hsp90. Chem. Biol. 2004, 11, 787-797.
    • (2004) Chem. Biol. , vol.11 , pp. 787-797
    • Vilenchik, M.1    Solit, D.2    Basso, A.3    Huezo, H.4    Lucas, B.5
  • 26
    • 0036836964 scopus 로고    scopus 로고
    • Development of a purine-scaffold novel class of Hsp90 binders that inhibit the proliferation of cancer cells and induce the degradation of Her2 tyrosine kinase
    • Chiosis, G.; Lucas, B.; Shtil, A.; Huezo, H.; Rosen, N. Development of a purine-scaffold novel class of Hsp90 binders that inhibit the proliferation of cancer cells and induce the degradation of Her2 tyrosine kinase. Bioorg. Med. Chem. 2002, 10, 3555-3564.
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 3555-3564
    • Chiosis, G.1    Lucas, B.2    Shtil, A.3    Huezo, H.4    Rosen, N.5
  • 27
    • 31544433450 scopus 로고    scopus 로고
    • Orally active purine-based inhibitors of the heat shock protein 90
    • Biamonte, M. A.; Shi, J.; Hong, K.; Hurst, D. C.; Zhang, L.; et al. Orally active purine-based inhibitors of the heat shock protein 90. J. Med. Chem. 2006, 49, 817-828.
    • (2006) J. Med. Chem. , vol.49 , pp. 817-828
    • Biamonte, M.A.1    Shi, J.2    Hong, K.3    Hurst, D.C.4    Zhang, L.5
  • 28
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
    • Kamal, A.; Thao, L.; Sensintaffar, J.; Zhang, L.; Boehm, M. F.; et al. A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 2003, 425, 407-410.
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1    Thao, L.2    Sensintaffar, J.3    Zhang, L.4    Boehm, M.F.5
  • 29
    • 21244505104 scopus 로고    scopus 로고
    • Novel, potent small-molecule inhibitors of the molecular chaperone Hsp90 discovered through structure-based design
    • Dymock, B. W.; Barril, X.; Brough, P. A.; Cansfield, J. E.; Massey, A.; et al. Novel, potent small-molecule inhibitors of the molecular chaperone Hsp90 discovered through structure-based design. J. Med. Chem. 2005, 48, 4212-4215.
    • (2005) J. Med. Chem. , vol.48 , pp. 4212-4215
    • Dymock, B.W.1    Barril, X.2    Brough, P.A.3    Cansfield, J.E.4    Massey, A.5
  • 30
    • 20444465254 scopus 로고    scopus 로고
    • Radester, a novel inhibitor of the Hsp90 protein folding machinery
    • Shen, G.; Blagg, B. S. Radester, a novel inhibitor of the Hsp90 protein folding machinery. Org. Lett. 2005, 7, 2157-2160.
    • (2005) Org. Lett. , vol.7 , pp. 2157-2160
    • Shen, G.1    Blagg, B.S.2
  • 31
    • 10044237881 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of a radicicol and geldanamycin chimera, radamide
    • Clevenger, R. C.; Blagg, B. S. Design, synthesis, and evaluation of a radicicol and geldanamycin chimera, radamide. Org. Lett. 2004, 6, 4459-4462.
    • (2004) Org. Lett. , vol.6 , pp. 4459-4462
    • Clevenger, R.C.1    Blagg, B.S.2
  • 32
    • 20644448390 scopus 로고    scopus 로고
    • The identification, synthesis, protein crystal structure and in vitro biochemical evaluation of a new 3,4-diarylpyrazole class of Hsp90 inhibitors
    • Cheung, K. M.; Matthews, T. P.; James, K.; Rowlands, M. G.; Boxall, K. J.; et al. The identification, synthesis, protein crystal structure and in vitro biochemical evaluation of a new 3,4-diarylpyrazole class of Hsp90 inhibitors. Bioorg. Med. Chem. Lett. 2005, 15, 3338-3343.
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 3338-3343
    • Cheung, K.M.1    Matthews, T.P.2    James, K.3    Rowlands, M.G.4    Boxall, K.J.5
  • 33
    • 13944270580 scopus 로고    scopus 로고
    • Crystal structures of human HSP90alpha-complexed with dihydroxyphenyl-pyrazoles
    • Kreusch, A.; Han, S.; Brinker, A.; Zhou, V.; Choi, H. S.; et al. Crystal structures of human HSP90alpha-complexed with dihydroxyphenyl-pyrazoles. Bioorg. Med. Chem. Lett. 2005, 15, 1475-1478.
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 1475-1478
    • Kreusch, A.1    Han, S.2    Brinker, A.3    Zhou, V.4    Choi, H.S.5
  • 34
    • 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, 665-673.
    • (2002) Nat. Rev. Drug Discovery , vol.1 , pp. 665-673
    • Chene, P.1
  • 35
    • 17444416142 scopus 로고    scopus 로고
    • Evaluation of 8-arylsulfanyl, 8-arylsulfoxyl, and 8-arylsulfonyl adenine derivatives as inhibitors of the heat shock protein 90
    • Llauger, L.; He, H.; Kim, J.; Aguirre, J.; Rosen, N.; et al. Evaluation of 8-arylsulfanyl, 8-arylsulfoxyl, and 8-arylsulfonyl adenine derivatives as inhibitors of the heat shock protein 90. J. Med. Chem. 2005, 48, 2892-2905.
    • (2005) J. Med. Chem. , vol.48 , pp. 2892-2905
    • Llauger, L.1    He, H.2    Kim, J.3    Aguirre, J.4    Rosen, N.5
  • 36
    • 30444447639 scopus 로고    scopus 로고
    • Identification of potent water soluble purine-scaffold inhibitors of the heat shock protein 90
    • He, H.; Zatorska, D.; Kim, J.; Aguirre, J.; Llauger, L.; et al. Identification of potent water soluble purine-scaffold inhibitors of the heat shock protein 90. J. Med. Chem. 2006, 49, 381-390.
    • (2006) J. Med. Chem. , vol.49 , pp. 381-390
    • He, H.1    Zatorska, D.2    Kim, J.3    Aguirre, J.4    Llauger, L.5
  • 37
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 1993, 26, 795-800.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 38
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones, T. A.; Zou, J. Y.; Cowan, S. W.; Kjeldgaard, M. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr., Sect. A 1991, 47, 110-119.
    • (1991) Acta Crystallogr., Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 39
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A. T.; Adams, P. D.; Clore, G. M.; DeLano, W. L.; Gros, P.; et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr., Sect. D 1998, 54, 905-921.
    • (1998) Acta Crystallogr., Sect. D , vol.54 , pp. 905-921
    • Brunger, A.T.1    Adams, P.D.2    Clore, G.M.3    DeLano, W.L.4    Gros, P.5
  • 40
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: A tool for high-throughput crystallography of protein-ligand complexes
    • Schuttelkopf, A. W.; van Aalten, D. M. PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr., Sect. D 2004, 60, 1355-1363.
    • (2004) Acta Crystallogr., Sect. D , vol.60 , pp. 1355-1363
    • Schuttelkopf, A.W.1    Van Aalten, D.M.2
  • 41
    • 0347383757 scopus 로고    scopus 로고
    • New tools and data for improving structures, using all-atom contacts
    • Academic Press: San Diego, CA
    • Richardson, J. S.; Arendall, W. B., 3rd; Richardson, D. C. New Tools and Data for Improving Structures, Using All-Atom Contacts. Methods in Enzymology. Academic Press: San Diego, CA, 2003; pp 385-412.
    • (2003) Methods in Enzymology , pp. 385-412
    • Richardson, J.S.1    Arendall III, W.B.2    Richardson, D.C.3
  • 42
    • 0037441653 scopus 로고    scopus 로고
    • Structure validation by Calpha geometry: Phi, psi and Cbeta deviation
    • Lovell, S. C.; Davis, I. W.; Arendall, W. B., 3rd; de Bakker, P. I.; Word, J. M.; et al. Structure validation by Calpha geometry: phi, psi and Cbeta deviation. Proteins 2003, 50, 437-450.
    • (2003) Proteins , vol.50 , pp. 437-450
    • Lovell, S.C.1    Davis, I.W.2    Arendall III, W.B.3    De Bakker, P.I.4    Word, J.M.5
  • 43
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A.; Teplyakov, A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 1997, 30, 1022-1025.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 44
    • 0030901877 scopus 로고    scopus 로고
    • A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone
    • Prodromou, C.; Roe, S. M.; Piper, P. W.; Pearl, L. H. A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone. Nat. Struct. Biol. 1997, 4, 477-482.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 477-482
    • Prodromou, C.1    Roe, S.M.2    Piper, P.W.3    Pearl, L.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.