Elucidation of the Hsp90 C-terminal inhibitor binding site.
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Anshuman Dixit | Gennady M Verkhivker | Sudhakar Voruganti | A. Dixit | B. Blagg | R. Matts | S. Hartson | Brian S J Blagg | Robert L Matts | Laura B Peterson | Liang Sun | Palgunan Kalyanaraman | Steve D Hartson | L. Peterson | Liang Sun | Sudhakar Voruganti | Palgunan Kalyanaraman
[1] Giulio Rastelli,et al. Exploring the Binding Site of C-Terminal Hsp90 Inhibitors , 2010, J. Chem. Inf. Model..
[2] B. Blagg,et al. Hsp90 inhibition: elimination of shock and stress. , 2010, Bioorganic & medicinal chemistry letters.
[3] J. Buchner,et al. Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle , 2010, Proceedings of the National Academy of Sciences.
[4] R. Scannevin,et al. Corrections to Heat Shock Protein 90: Inhibitors in Clinical Trials , 2010 .
[5] B. Blagg,et al. KU135, a Novel Novobiocin-Derived C-Terminal Inhibitor of the 90-kDa Heat Shock Protein, Exerts Potent Antiproliferative Effects in Human Leukemic Cells , 2009, Molecular Pharmacology.
[6] Johannes Buchner,et al. Hsp90 is regulated by a switch point in the C‐terminal domain , 2009, EMBO reports.
[7] D. Agard,et al. Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide , 2009, Protein science : a publication of the Protein Society.
[8] David A Agard,et al. Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle. , 2008, Molecular cell.
[9] B. Blagg,et al. Novobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket. , 2008, Current medicinal chemistry.
[10] R. Buey,et al. Apo‐Hsp90 coexists in two open conformational states in solution , 2008, Biology of the cell.
[11] J. Reinstein,et al. Conserved Conformational Changes in the ATPase Cycle of Human Hsp90* , 2008, Journal of Biological Chemistry.
[12] Robert P Hanzlik,et al. Protein targets of reactive metabolites of thiobenzamide in rat liver in vivo. , 2008, Chemical research in toxicology.
[13] Friedrich Förster,et al. Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90. , 2008, Structure.
[14] A. Ferrari,et al. Structural Models and Binding Site Prediction of the C‐terminal Domain of Human Hsp90: A New Target for Anticancer Drugs , 2008, Chemical biology & drug design.
[15] L. Pearl,et al. The Hsp90 molecular chaperone: an open and shut case for treatment. , 2008, The Biochemical journal.
[16] B. Blagg,et al. Development of novobiocin analogues that manifest anti-proliferative activity against several cancer cell lines. , 2008, The Journal of organic chemistry.
[17] Rodrigo Lopez,et al. Clustal W and Clustal X version 2.0 , 2007, Bioinform..
[18] B. Blagg,et al. Hsp90: a novel target for the disruption of multiple signaling cascades. , 2007, Current cancer drug targets.
[19] B. Blagg,et al. High-throughput assay for the identification of Hsp90 inhibitors based on Hsp90-dependent refolding of firefly luciferase. , 2007, Bioorganic & medicinal chemistry.
[20] B. Blagg,et al. Synthesis and evaluation of coumermycin A1 analogues that inhibit the Hsp90 protein folding machinery. , 2006, Organic letters.
[21] L. Pearl,et al. Structure and mechanism of the Hsp90 molecular chaperone machinery. , 2006, Annual review of biochemistry.
[22] Paul Workman,et al. Inhibitors of the HSP90 molecular chaperone: attacking the master regulator in cancer. , 2006, Current topics in medicinal chemistry.
[23] L. Pearl,et al. Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex , 2006, Nature.
[24] D. Mok,et al. Modulation of Chaperone Function and Cochaperone Interaction by Novobiocin in the C-terminal Domain of Hsp90 , 2006, Journal of Biological Chemistry.
[25] Laxmikant V. Kalé,et al. Scalable molecular dynamics with NAMD , 2005, J. Comput. Chem..
[26] Xiao Ming Yu,et al. Hsp90 inhibitors identified from a library of novobiocin analogues. , 2005, Journal of the American Chemical Society.
[27] Xiao Ming Yu,et al. Syntheses of photolabile novobiocin analogues. , 2004, Bioorganic & medicinal chemistry letters.
[28] R. Matts,et al. Novobiocin induces a distinct conformation of Hsp90 and alters Hsp90-cochaperone-client interactions. , 2004, Biochemistry.
[29] P. Charifson,et al. Crystal Structures of Escherichia coli Topoisomerase IV ParE Subunit (24 and 43 Kilodaltons): a Single Residue Dictates Differences in Novobiocin Potency against Topoisomerase IV and DNA Gyrase , 2004, Antimicrobial Agents and Chemotherapy.
[30] L. Neckers,et al. The Heat Shock Protein 90 Antagonist Novobiocin Interacts with a Previously Unrecognized ATP-binding Domain in the Carboxyl Terminus of the Chaperone* , 2000, The Journal of Biological Chemistry.
[31] L. Neckers,et al. Novobiocin and related coumarins and depletion of heat shock protein 90-dependent signaling proteins. , 2000, Journal of the National Cancer Institute.
[32] D. Hanahan,et al. The Hallmarks of Cancer , 2000, Cell.
[33] V. Thulasiraman,et al. Molybdate inhibits hsp90, induces structural changes in its C-terminal domain, and alters its interactions with substrates. , 1999, Biochemistry.
[34] L. Pearl,et al. Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. , 1999, Journal of medicinal chemistry.
[35] Walter H.J. Ward,et al. The entropic penalty of ordered water accounts for weaker binding of the antibiotic novobiocin to a resistant mutant of DNA gyrase: a thermodynamic and crystallographic study. , 1997, Biochemistry.
[36] Neal Rosen,et al. Crystal Structure of an Hsp90–Geldanamycin Complex: Targeting of a Protein Chaperone by an Antitumor Agent , 1997, Cell.
[37] T. Blundell,et al. Comparative protein modelling by satisfaction of spatial restraints. , 1993, Journal of molecular biology.
[38] P. Thibault,et al. Fragmentation reactions of multiply-protonated peptides and implications for sequencing by tandem mass spectrometry with low-energy collision-induced dissociation. , 1993, Analytical chemistry.
[39] E. Myers,et al. Basic local alignment search tool. , 1990, Journal of molecular biology.
[40] B. Blagg,et al. Characterization of a novel novobiocin analogue as a putative C‐terminal inhibitor of heat shock protein 90 in prostate cancer cells , 2010, The Prostate.