Hsp90: Structure and Function

Structure of the N-terminal Domain of GRP94

Soldano, K. L., Jivan, A., Nicchitta, C. V., & Gewirth, D. T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308661200 · Cited by 140

Pathogenesis of and Therapeutic Strategies to Ameliorate the Transthyretin Amyloidoses

Sekijima, Y., Kelly, J. W., & Ikeda, S. (2008) · Current Pharmaceutical Design · doi:10.2174/138161208786404155 · Cited by 139

Development of Novobiocin Analogues That Manifest Anti-proliferative Activity against Several Cancer Cell Lines

Burlison, J. A., Avila, C., Vielhauer, G. A., Lubbers, D. J., Holzbeierlein, J. M., & Blagg, B. S. J. (2008) · The Journal of Organic Chemistry · doi:10.1021/jo702191a · Cited by 138

Two Structures of Cyclophilin 40

Taylor, P., Dornan, J., Carrello, A., Minchin, R. F., Ratajczak, T., & Walkinshaw, M. D. (2001) · Structure · doi:10.1016/s0969-2126(01)00603-7 · Cited by 137

Crystal structure of tRNA(m1G37)methyltransferase: insights into tRNA recognition

Ahn, H. J., Kim, H., Yoon, H., et al. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg269 · Cited by 137

The Molecular Chaperone Hsp90 Modulates Intermediate Steps of Amyloid Assembly of the Parkinson-related Protein α-Synuclein

Falsone, S. F., Kungl, A. J., Rek, A., Cappai, R., & Zangger, K. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.057240 · Cited by 137

Rab11a and HSP90 Regulate Recycling of Extracellular α-Synuclein

Liu, J., Zhang, J., Shi, M. Y., Quinn, T. J., Bradner, J. M., Beyer, R., Chen, S., & Zhang, J. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.6202-08.2009 · Cited by 137

Crystal Structure and Activity of Human p23, a Heat Shock Protein 90 Co-chaperone

Weaver, A. J., Sullivan, W. P., Felts, S. J., Owen, B. A. L., & Toft, D. O. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003410200 · Cited by 136

Human Sgt1 Binds HSP90 through the CHORD-Sgt1 Domain and Not the Tetratricopeptide Repeat Domain*

Lee, Y.-T., Jacob, J., Michowski, W., Nowotny, M., Kuźnicki, J., & Chazin, W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400215200 · Cited by 136

Hsp90 regulates tau pathology through co-chaperone complexes in Alzheimer's disease

Salminen, A., Ojala, J. O., Kaarniranta, K., Hiltunen, M., & Soininen, H. S. (2010) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2010.10.006 · Cited by 131

Structural and functional coupling of Hsp90‐ and Sgt1‐centred multi‐protein complexes

Zhang, M., Botër, M., Li, K., Kadota, Y., Panaretou, B., Prodromou, C., Shirasu, K., & Pearl, L. H. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.190 · Cited by 131

HSP90-buffered genetic variation is common in Arabidopsis thaliana

Sangster, T. A., Salathia, N., Lee, H. N., Watanabe, E., Schellenberg, K., Morneau, K., Wang, H., Undurraga, S., Queitsch, C., & Lindquist, S. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712210105 · Cited by 131

A fragment of secreted Hsp90α carries properties that enable it to accelerate effectively both acute and diabetic wound healing in mice

Cheng, C.-F., Sahu, D., Tsen, F., Zhao, Z., Fan, J., Kim, R., Wang, X., O’Brien, K., Li, Y., Kuang, Y.-T., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci46475 · Cited by 130

A postgenomic view of the heat shock proteins in kinetoplastids

Folgueira, C., & Requena, J. M. (2007) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2007.00069.x · Cited by 129

The role of FKBP5 in cancer aetiology and chemoresistance

Li, L., Lou, Z., & Wang, L. (2010) · British Journal of Cancer · doi:10.1038/sj.bjc.6606014 · Cited by 129

The client protein p53 adopts a molten globule–like state in the presence of Hsp90

Park, S. J., Borin, B. N., Martinez-Yamout, M. A., & Dyson, H. J. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2045 · Cited by 128

Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53

Hagn, F., Lagleder, S., Retzlaff, M., Rohrberg, J., Demmer, O., Richter, K., Buchner, J., & Kessler, H. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2114 · Cited by 127

Structural Studies on the Co-chaperone Hop and Its Complexes with Hsp90

Onuoha, S. C., Coulstock, E. T., Grossmann, J. G., & Jackson, S. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.02.013 · Cited by 127

HDAC6 regulates androgen receptor hypersensitivity and nuclear localization via modulating Hsp90 acetylation in castration-resistant prostate cancer.

Ai, J., Wang, Y., Dar, J. A., Liu, J., Liu, L., Nelson, J. B., & Wang, Z. (2009) · Molecular Endocrinology · doi:10.1210/me.2009-0188 · Cited by 126 · cited 1×

Structural Basis for Assembly of Hsp90-Sgt1-CHORD Protein Complexes: Implications for Chaperoning of NLR Innate Immunity Receptors

Zhang, M., Kadota, Y., Prodromou, C., Shirasu, K., & Pearl, L. H. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.05.010 · Cited by 126

Charged linker sequence modulates eukaryotic heat shock protein 90 (Hsp90) chaperone activity

Tsutsumi, S., Mollapour, M., Prodromou, C., Lee, C., Panaretou, B., Yoshida, S., Mayer, M. P., & Neckers, L. Μ. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1114414109 · Cited by 126

Differential Effects of Mitochondrial Heat Shock Protein 60 and Related Molecular Chaperones to Prevent Intracellular β-Amyloid-induced Inhibition of Complex IV and Limit Apoptosis

Veereshwarayya, V., Kumar, P., Rosen, K. M., Mestril, R., & Querfurth, H. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602533200 · Cited by 125

Cdc37 goes beyond Hsp90 and kinases

MacLean, M. J., & Picard, D. (2003) · Cell Stress and Chaperones · doi:10.1379/1466-1268(2003)008<0114:cgbhak>2.0.co;2 · Cited by 125

ASNA-1 Positively Regulates Insulin Secretion in C. elegans and Mammalian Cells

Kao, G., Nordenson, C., Still, M., Rönnlund, A., Tuck, S., & Naredi, P. L. J. (2007) · Cell · doi:10.1016/j.cell.2006.12.031 · Cited by 124

N-terminal domain of human Hsp90 triggers binding to the cochaperone p23

Karagöz, G. E., Duarte, A. M. S., Ippel, H., Uetrecht, C., Sinnige, T., van Rosmalen, M., Hausmann, J., Heck, A. J. R., Boelens, R., & Rüdiger, S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1011867108 · Cited by 124

The accumulation of three specific proteins related to glucose‐regulated proteins in a temperature‐sensitive hamster mutant cell line K12

Lee, A. S. (1981) · Journal of Cellular Physiology · doi:10.1002/jcp.1041060113 · Cited by 124

Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation.

Harst, A., Lin, H.-Y., & Obermann, W. (2005) · Biochemical Journal · doi:10.1042/bj20041283 · Cited by 121

FK506-binding protein 52 is essential to uterine reproductive physiology controlled by the progesterone receptor A isoform

Yang, Z., Wolf, I. M., Chen, H., Periyasamy, S., Chen, Z., Yong, W., Shi, S., Zhao, W., Xu, J., Srivastava, A., et al. (2006) · Molecular Endocrinology · doi:10.1210/me.2006-0024 · Cited by 119 · cited 1×

Discovery and Design of Novel HSP90 Inhibitors Using Multiple Fragment‐based Design Strategies

Huth, J. R., Park, C., Petros, A. M., Kunzer, A. R., Wendt, M. D., Wang, X., Lynch, C. L., Mack, J. C., Swift, K. M., Judge, R. A., et al. (2007) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2007.00535.x · Cited by 119

C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle 1 1Edited by R. Huber

Weikl, T., Muschler, P., Richter, K., Veit, T., Reinstein, J., & Büchner, J. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4157 · Cited by 119

Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms

Johnson, J. L., & Brown, C. (2009) · Cell Stress and Chaperones · doi:10.1007/s12192-008-0058-9 · Cited by 119

Modulating molecular chaperone Hsp90 functions through reversible acetylation

Aoyagi, S., & Archer, T. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2005.09.003 · Cited by 118

A Novel Class of Small Molecule Inhibitors of Hsp90

Yi, F., & Regan, L. (2008) · ACS Chemical Biology · doi:10.1021/cb800162x · Cited by 116

A non-toxic Hsp90 inhibitor protects neurons from Aβ-induced toxicity

Ansar, S., Burlison, J. A., Hadden, M. K., Yu, X. M., Desino, K. E., Bean, J. L., Neckers, L., Audus, K. L., Michaelis, M. L., & Blagg, B. S. J. (2007) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2007.01.017 · Cited by 114

Structural and Quantum Chemical Studies of 8-Aryl-sulfanyl Adenine Class Hsp90 Inhibitors

Immormino, R. M., Kang, Y., Chiosis, G., & Gewirth, D. T. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm060297x · Cited by 113

Two endoplasmic reticulum (ER)/ER Golgi intermediate compartment-based lysine acetyltransferases post-translationally regulate BACE1 levels

Ko, M. H., & Puglielli, L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m804901200 · Cited by 111

Balance between Folding and Degradation for Hsp90-Dependent Client Proteins: A Key Role for CHIP

Kundrat, L., & Regan, L. (2010) · Biochemistry · doi:10.1021/bi100386w · Cited by 109

The ATPase Cycle of the Endoplasmic Chaperone Grp94

Frey, S., Leskovar, A., Reinstein, J., & Büchner, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704647200 · Cited by 109

Phosphorylation of Serine 13 Is Required for the Proper Function of the Hsp90 Co-chaperone, Cdc37

Shao, J., Prince, T. L., Hartson, S. D., & Matts, R. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c300330200 · Cited by 109

Intracellular protozoan parasites of humans: the role of molecular chaperones in development and pathogenesis.

Shonhai, A., Maier, A., Przyborski, J., & Blatch, G. (2011) · Protein Peptide Letters · doi:10.2174/092986611794475002 · Cited by 109

FKBP51 and Cyp40 are positive regulators of androgen-dependent prostate cancer cell growth and the targets of FK506 and cyclosporin A

Periyasamy, S., Hinds, T., Shemshedini, L., Shou, W., & Sanchez, E. R. (2010) · Oncogene · doi:10.1038/onc.2009.458 · Cited by 108

A Protein Associated with Toll-Like Receptor 4 (PRAT4A) Regulates Cell Surface Expression of TLR4

Wakabayashi, Y., Kobayashi, M., Akashi‐Takamura, S., Tanimura, N., Konno, K., Takahashi, K., Ishii, T., Mizutani, T., Iba, H., Kouro, T., et al. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.3.1772 · Cited by 108

ATP-binding Properties of Human Hsp90

Scheibel, T., Neuhofen, S., Weikl, T., Mayr, C., Reinstein, J., Vogel, P. D., & Büchner, J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.30.18608 · Cited by 108

Designed TPR Modules as Novel Anticancer Agents

Cortajarena, A. L., Fang, Y., & Regan, L. (2008) · ACS Chemical Biology · doi:10.1021/cb700260z · Cited by 108

Chaperones and proteases: Cellular fold-controlling factors of proteins in neurodegenerative diseases and aging

Hinault, M., Ben‐Zvi, A., & Goloubinoff, P. (2006) · Journal of Molecular Neuroscience · doi:10.1385/jmn:30:3:249 · Cited by 107

Identification of Residues on Hsp70 and Hsp90 Ubiquitinated by the Cochaperone CHIP

Kundrat, L., & Regan, L. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.11.017 · Cited by 107

Tyrosine Phosphorylation of HSP90 within the P2X7 Receptor Complex Negatively Regulates P2X7 Receptors

Adinolfi, E., Kim, M., Young, M. T., Virgilio, F. D., & Surprenant, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301508200 · Cited by 106

Mechanistic studies of Sansalvamide A-amide: An allosteric modulator of Hsp90

Vasko, R. C., Rodriguez, R. A., Cunningham, C. N., Ardi, V. C., Agard, D. A., & McAlpine, S. R. (2010) · ACS Medicinal Chemistry Letters · doi:10.1021/ml900003t · Cited by 105

The aminocoumarins: biosynthesis and biology

Heide, L. E. (2009) · Natural Product Reports · doi:10.1039/b808333a · Cited by 105

Preclinical Characterization of Mitochondria-Targeted Small Molecule Hsp90 Inhibitors, Gamitrinibs, in Advanced Prostate Cancer

Kang, B. H., Siegelin, M. D., Plescia, J., Raskett, C. M., Garlick, D. S., Dohi, T., Lian, J. B., Stein, G. S., Languino, L. R., & Altieri, D. C. (2010) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-10-1818 · Cited by 105

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., & Gewirth, D. T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405253200 · Cited by 104

Advances in the discovery and development of heat-shock protein 90 inhibitors for cancer treatment

Patel, H., Modi, S., Chiosis, G., & Taldone, T. (2011) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2011.563296 · Cited by 103

Molecular Chaperones as Rational Drug Targets for Parkinsons Disease Therapeutics

Kalia, S. K., Kalia, L. V., & McLean, P. J. (2010) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152710793237386 · Cited by 103

Independent ATPase Activity of Hsp90 Subunits Creates a Flexible Assembly Platform

McLaughlin, S. H., Ventouras, L.-A., Lobbezoo, B., & Jackson, S. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.09.055 · Cited by 102

Proteomics-Determined Differences in the Concanavalin-A-Fractionated Proteome of Hippocampus and Inferior Parietal Lobule in Subjects with Alzheimer’s Disease and Mild Cognitive Impairment: Implications for Progression of AD

Owen, J. B., Domenico, F. D., Rukhsana Sultana, A., Marzia Perluigi, A., Cini, C., Pierce, W. M. J., & Butterfield, D. A. (2008) · Journal of Proteome Research · doi:10.1021/pr800667a · Cited by 102

Bridging the gap: From protein misfolding to protein misfolding diseases

Luheshi, L. M., & Dobson, C. M. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.06.030 · Cited by 101

CRINEPT-TROSY NMR reveals p53 core domain bound in an unfolded form to the chaperone Hsp90

Rüdiger, S., Freund, S. M. V., Veprintsev, D. B., & Fersht, A. R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.132393699 · Cited by 100

The ATPase Cycle of the Mitochondrial Hsp90 Analog Trap1

Leskovar, A., Wegele, H., Werbeck, N. D., Büchner, J., & Reinstein, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709516200 · Cited by 100

Assessment of the ATP Binding Properties of Hsp90

Jakob, U., Scheibel, T., Bose, S., Reinstein, J., & Büchner, J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.17.10035 · Cited by 99

Immunoelectron Microscopy Provides Evidence That Tumor Necrosis Factor Receptor-Associated Protein 1 (TRAP-1) Is a Mitochondrial Protein Which also Localizes at Specific Extramitochondrial Sites

Cechetto, J. D., & Gupta, R. S. (2000) · Experimental Cell Research · doi:10.1006/excr.2000.4983 · Cited by 98

Chaperone-mediated autophagy dysfunction in the pathogenesis of neurodegeneration

Koga, H., & Cuervo, A. M. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.07.006 · Cited by 98

The chlorate‐resistant and photomorphogenesis‐defective mutant cr88 encodes a chloroplast‐targeted HSP90

Cao, D., Froehlich, J. E., Zhang, H., & Cheng, C. (2003) · The Plant Journal · doi:10.1046/j.1365-313x.2003.016011.x · Cited by 98

Chaperoning steroidal physiology: Lessons from mouse genetic models of Hsp90 and its cochaperones

Sánchez, E. R. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.11.006 · Cited by 98

Toxoplasma gondii Hsp90 is a Potential Drug Target Whose Expression and Subcellular Localization are Developmentally Regulated

Echeverría, P. C., Matrajt, M., Harb, O. S., Zappia, M. P., Costas, M. A., Roos, D. S., Dubremetz, J., & Angel, S. O. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.05.031 · Cited by 97

Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation

Nathan, D. F., Vos, M. H., & Lindquist, S. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.4.1409 · Cited by 96

Triggering Aggresome Formation

Zaarur, N., Meriin, A. B., Gabai, V. L., & Sherman, M. Y. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802216200 · Cited by 95

Hsp90 phosphorylation, Wee1 and the cell cycle

Mollapour, M., Tsutsumi, S., & Neckers, L. (2010) · Cell Cycle · doi:10.4161/cc.9.12.12054 · Cited by 95

Celastrol Inhibits Hsp90 Chaperoning of Steroid Receptors by Inducing Fibrillization of the Co-chaperone p23

Chadli, A., Felts, S. J., Wang, Q., Sullivan, W. P., Botuyan, M. V., Fauq, A., Ramirez-Alvarado, M., & Mer, G. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.081018 · Cited by 94

The role of serine/threonine protein phosphatase type 5 (PP5) in the regulation of stress-induced signaling networks and cancer

Golden, T. A., Swingle, M. R., & Honkanen, R. E. (2008) · Cancer and Metastasis Reviews · doi:10.1007/s10555-008-9125-z · Cited by 94

FKBP51 – a selective modulator of glucocorticoid and androgen sensitivity

Stechschulte, L. A., & Sanchez, E. R. (2011) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2011.04.012 · Cited by 92 · cited 1×

Discovery of benzamide tetrahydro-4H-carbazol-4-ones as novel small molecule inhibitors of Hsp90

Barta, T. E., Veal, J. M., Rice, J. W., Partridge, J. M., Fadden, R. P., Ma, W., Jenks, M., Geng, L., Hanson, G. J., Huang, K. H., et al. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.05.023 · Cited by 91

Molecular chaperone‐mediated tau protein metabolism counteracts the formation of granular tau oligomers in human brain

Sahara, N., Maeda, S., Yoshiike, Y., Mizoroki, T., Yamashita, S., Murayama, M., Park, J. ‐., Saito, Y., Murayama, S., & Takashima, A. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21417 · Cited by 90

Application of Chemoproteomics to Drug Discovery: Identification of a Clinical Candidate Targeting Hsp90

Fadden, P., Huang, K. H., Veal, J. M., Steed, P. M., Barabasz, A. F., Foley, B. E., Hu, M., Partridge, J. M., Rice, J. W., Scott, A., et al. (2010) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.04.015 · Cited by 87

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. O., & Ke, H. (2005) · Structure · doi:10.1016/j.str.2004.12.018 · Cited by 86

Brain site‐specific gene expression analysis in Alzheimer's disease patients

Yokota, T., Mishra, M., Akatsu, H., Tani, Y., Miyauchi, T., Yamamoto, T., Kosaka, K., Nagai, Y., Sawada, T., & Heese, K. (2006) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.2006.01722.x · Cited by 86

Dynamic Interaction of Hsp90 with Its Client Protein p53

Park, S. J., Kostić, M., & Dyson, H. J. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.05.030 · Cited by 84

Hsp90 structure and function studied by NMR spectroscopy

Didenko, T., Duarte, A. M. S., Karagöz, G. E., & Rüdiger, S. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.11.009 · Cited by 83

Hsp90 charged-linker truncation reverses the functional consequences of weakened hydrophobic contacts in the N domain

Tsutsumi, S., Mollapour, M., Graf, C., Lee, C., Scroggins, B. T., Xu, W., Haslerova, L., Heßling, M., Konstantinova, A. A., Trepel, J. B., et al. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1682 · Cited by 83

Molecular chaperones and the biosynthesis of antigen receptors

Melnick, J., & Argon, Y. (1995) · Immunology Today · doi:10.1016/0167-5699(95)80167-7 · Cited by 83

Chaperoning Oncogenes: Hsp90 as a Target of Geldanamycin

Neckers, L. (2005) · Handbook of experimental pharmacology · doi:10.1007/3-540-29717-0_11 · Cited by 81

Protein Misfolding Diseases: Current and Emerging Principles and Therapies

Ramirez-Alvarado, M., Kelly, J. W., & Dobson, C. M. (2010) · Wiley eBooks · doi:10.1002/9780470572702 · Cited by 81

The peptide-binding activity of GRP94 is regulated by calcium

Biswas, C., Ostrovsky, O., Makarewich, C. A., Wanderling, S. S., Gidalevitz, T., & Argon, Y. (2007) · Biochemical Journal · doi:10.1042/bj20061867 · Cited by 81

3-(5-chloro-2,4-dihydroxyphenyl)-Pyrazole-4-carboxamides as inhibitors of the Hsp90 molecular chaperone

Brough, P. A., Barril, X., Beswick, M., Dymock, B. W., Drysdale, M. J., Wright, L. M., Grant, K., Massey, A. J., Surgenor, A. E., & Workman, P. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.08.091 · Cited by 81

Role of SGT1 in the regulation of plant R gene signalling

Muskett, P. R., & Parker, J. E. (2003) · Microbes and Infection · doi:10.1016/s1286-4579(03)00183-7 · Cited by 80

HtpG, the prokaryotic homologue of Hsp90, stabilizes a phycobilisome protein in the cyanobacterium Synechococcus elongatus PCC 7942: Interaction of HtpG with an in vivo substrate

SATO, T. A., Minagawa, S., Kojima, E., Okamoto, N., & Nakamoto, H. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07139.x · Cited by 79

Heat Shock Protein-90 (Hsp90) Acts as a Repressor of Peroxisome Proliferator-Activated Receptor-α (PPARα) and PPARβ Activity

Sumanasekera, W. K., Tien, E. S., Davis, J. W., Turpey, R., Perdew, G. H., & Heuvel, J. P. V. (2003) · Biochemistry · doi:10.1021/bi0347353 · Cited by 79

Impact of Heat-Shock Protein 90 on Cancer Metastasis

Tsutsumi, S., Beebe, K. E., & Neckers, L. (2009) · Future Oncology · doi:10.2217/fon.09.30 · Cited by 79

Biochemical and Structural Studies of the Interaction of Cdc37 with Hsp90

Zhang, W., Hirshberg, M., McLaughlin, S. H., Lazar, G. A., Grossmann, J. G., Nielsen, P. R., Sobott, F., Robinson, C. V., Jackson, S., & Laue, E. D. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.05.007 · Cited by 79

Structure-based discovery of a new class of Hsp90 inhibitors

Barril, X., Brough, P. A., Drysdale, M., Hubbard, R. E., Massey, A. J., Surgenor, A. E., & Wright, L. M. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.08.092 · Cited by 78

The Ah Receptor Is a Sensitive Target of Geldanamycin-Induced Protein Turnover

Chen, H.-S., Singh, S. S., & Perdew, G. H. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0398 · Cited by 78

Conformational Diversity in the TPR Domain-Mediated Interaction of Protein Phosphatase 5 with Hsp90

Cliff, M. J., Harris, R., Barford, D., Ladbury, J. E., & Williams, M. A. (2006) · Structure · doi:10.1016/j.str.2005.12.009 · Cited by 76

Direct stoichiometric evidence that the untransformed Mr 300,000, 9S, glucocorticoid receptor is a core unit derived from a larger heteromeric complex

Bresnick, E. H., Dalman, F. C., & Pratt, W. B. (1990) · Biochemistry · doi:10.1021/bi00454a028 · Cited by 76

Osmolyte‐induced conformational changes in the Hsp90 molecular chaperone

Street, T. O., Krukenberg, K. A., Rösgen, J., Bolen, D. W., & Agard, D. A. (2009) · Protein Science · doi:10.1002/pro.282 · Cited by 76

NMR Chemical Shift Perturbation Study of the N‐Terminal Domain of Hsp90 upon Binding of ADP, AMP‐PNP, Geldanamycin, and Radicicol

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Inhibition of HSP90 in Trypanosoma cruzi Induces a Stress Response but No Stage Differentiation

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Heat shock proteins in neurodegenerative diseases: Pathogenic roles and therapeutic implications

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Intrinsic Inhibition of the Hsp90 ATPase Activity

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Dihydroxyphenylisoindoline Amides as Orally Bioavailable Inhibitors of the Heat Shock Protein 90 (Hsp90) Molecular Chaperone

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Structure of Unliganded GRP94, the Endoplasmic Reticulum Hsp90

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Purine-Scaffold Hsp90 Inhibitors

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Crystal structures of human HSP90α-complexed with dihydroxyphenylpyrazoles

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Structure of the ATP‐binding domain of Plasmodium falciparum Hsp90

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Malaria Heat Shock Proteins: Drug Targets that Chaperone other Drug Targets

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Binding of Hsp90 to Tau Promotes a Conformational Change and Aggregation of Tau Protein

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Different Poses for Ligand and Chaperone in Inhibitor-Bound Hsp90 and GRP94: Implications for Paralog-Specific Drug Design

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Localization of Sites of Interaction between p23 and Hsp90 in Solution

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Apo‐Hsp90 coexists in two open conformational states in solution

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An essential role for ATP binding and hydrolysis in the chaperone activity of GRP94 in cells

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Targeted inhibition of mitochondrial Hsp90 suppresses localised and metastatic prostate cancer growth in a genetic mouse model of disease

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Inhibition of Hsp90 with Synthetic Macrolactones: Synthesis and Structural and Biological Evaluation of Ring and Conformational Analogs of Radicicol

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Development of a High Throughput Drug Screening Assay for the Detection of Changes in Tau Levels - Proof of Concept with HSP90 inhibitors

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Casein kinase 2 phosphorylation of Hsp90 threonine 22 modulates chaperone function and drug sensitivity

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Stress response pathways in protozoan parasites

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Heterogeneity and dynamics in the assembly of the Heat Shock Protein 90 chaperone complexes

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Gp93, the Drosophila GRP94 ortholog, is required for gut epithelial homeostasis and nutrient assimilation-coupled growth control

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Molecular Chaperones and Regulation of Tau Quality Control: Strategies for Drug Discovery in Tauopathies

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The Human Cdc37·Hsp90 Complex Studied by Heteronuclear NMR Spectroscopy

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Neuroprotective activity and evaluation of Hsp90 inhibitors in an immortalized neuronal cell line

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A Compound That Inhibits the HOP–Hsp90 Complex Formation and Has Unique Killing Effects in Breast Cancer Cell Lines

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pH-Dependent Conformational Changes in Bacterial Hsp90 Reveal a Grp94-Like Conformation at pH 6 That Is Highly Active in Suppression of Citrate Synthase Aggregation

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Molecular Characterization of Macbecin as an Hsp90 Inhibitor

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Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide

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A common conformationally coupled ATPase mechanism for yeast and human cytoplasmic HSP90s

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Compartmentalized cancer drug discovery targeting mitochondrial Hsp90 chaperones

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Heat shock protein 90: translation from cancer to Alzheimer's disease treatment?

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HSP90 manages the ends

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The p23 molecular chaperone promotes functional telomerase complexes through DNA dissociation

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The HSP90-SGT1-RAR1 molecular chaperone complex: A core modulator in plant immunity

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Novel suppressors of α-synuclein toxicity identified using yeast

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Approaches for defining the Hsp90-dependent proteome

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Heat shock protein 90 from neglected protozoan parasites

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Endoplasmic reticulum quality control regulates the fate of transthyretin variants in the cell

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Post-translational modification of heat-shock protein 90: impact on chaperone function

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Design, synthesis, and evaluation of small molecule Hsp90 probes

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Molecular cloning of the 82-kDa heat shock protein (HSP90) of Toxoplasma gondii associated with the entry into and growth in host cells

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Alternate Strategies of Hsp90 Modulation for the Treatment of Cancer and Other Diseases

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Cross-Monomer Substrate Contacts Reposition the Hsp90 N-Terminal Domain and Prime the Chaperone Activity

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An AlphaScreen™-Based High-Throughput Screen to Identify Inhibitors of Hsp90-Cochaperone Interaction

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Cdc37 Regulation of the Kinome: When to Hold ‘Em and When to Fold ‘Em

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α-Synuclein Promotes the Recruitment of Tau to Protein Inclusions in Oligodendroglial Cells: Effects of Oxidative and Proteolytic Stress

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Carbamazepine promotes Her-2 protein degradation in breast cancer cells by modulating HDAC6 activity and acetylation of Hsp90

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Fragment‐based Identification of Hsp90 Inhibitors

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Hsp90 (Heat Shock Protein 90) Inhibitor Occupancy Is a Direct Determinant of Client Protein Degradation and Tumor Growth Arrest in Vivo

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Macrocyclic Inhibitors of Hsp90

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Inhibition of HSP90 with Pochoximes: SAR and Structure‐Based Insights

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Evolutionary Origins of Hsp90 Chaperones and a Deep Paralogy in their Bacterial Ancestors

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Analysis of the Structure and Synthesis of GRP94, an Abundant Stress Protein of the Endoplasmic Reticulum

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Heat shock protein-90-induced microglial clearance of exogenous amyloid-β1–42 in rat hippocampus in vivo

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Hsp90 can accommodate the simultaneous binding of the FKBP52 and HOP proteins

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Bending Tau into Shape: The Emerging Role of Peptidyl-Prolyl Isomerases in Tauopathies

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The Hsp90 co-chaperone p23 of Toxoplasma gondii: Identification, functional analysis and dynamic interactome determination

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Agrobacterium tumefaciens VirC2 enhances T-DNA transfer and virulence through its C-terminal ribbon–helix–helix DNA-binding fold

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Grp94 is Tyr-phosphorylated by Fyn in the lumen of the endoplasmic reticulum and translocates to Golgi in differentiating myoblasts

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Crystallographic structure of the tetratricopeptide repeat domain of Plasmodium falciparum FKBP35 and its molecular interaction with Hsp90 C‐terminal pentapeptide

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Discovery and development of purine-scaffold Hsp90 inhibitors

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Interaction between tau and alpha-synuclein proteins is impaired in the presence of P301L tau mutation

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Hsp90 Maintains the Stability and Function of the Tau Phosphorylating Kinase GSK3β

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The Role of p23, Hop, Immunophilins, and Other Co-chaperones in Regulating Hsp90 Function

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Detection of the ATPase Activity of the Molecular Chaperones Hsp90 and Hsp72 Using the Transcreener™ ADP Assay Kit

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HOP is a monomer: Investigation of the oligomeric state of the co‐chaperone HOP

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A Plasmodium homologue of cochaperone p23 and its differential expression during the replicative cycle of the malaria parasite

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3D DOSY-TROSY to determine the translational diffusion coefficient of large protein complexes

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Potent Triazolothione Inhibitor of Heat‐Shock Protein‐90

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Folding and stability of the ligand‐binding domain of the glucocorticoid receptor

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Hsp90 in non-mammalian metazoan model systems

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Heat shock protein 90β: A novel mediator of vitamin D action

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Strategies for Stalling Malignancy: Targeting Cancers Addiction to Hsp90

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Protein phosphatase 5 is required for Hsp90 function during proteotoxic stresses in Trypanosoma brucei

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Association of protein kinase CK2 with eukaryotic translation initiation factor eIF-2 and with grp94/endoplasmin

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A Library of Noviosylated Coumarin Analogues

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Inhibition of Hsp90 with Resorcylic Acid Macrolactones: Synthesis and Binding Studies

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Heterologous Desensitization of Opioid-stimulated Ca2+ Increase by Bradykinin or ATP in NG108-15 Cells

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Cyclophilin 40: An Hsp90-cochaperone associated with apo-steroid receptors

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Characterization of the 90 kDa heat shock protein (HSP90)-associated ATP/GTPase

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NMR Backbone Assignment of the N-terminal Domain of Human HSP90

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Letter to the Editor: Backbone resonance assignments of the 25kD N-terminal ATPase domain from the Hsp90 chaperone

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Association of protein kinase CK2 with eukaryotic translation initiation factor eIF-2 and with grp94/endoplasmin

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Substrates for Protein Kinase CK2 in Insulin Receptor Preparations from Rat Liver Membranes: Identification of a 210-kDa Protein Substrate as the Dimeric Form of Endoplasmin

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Identification of cyclophilin-40-interacting proteins reveals potential cellular function of cyclophilin-40

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Analyzing the aggregation of polyglutamine-expansion proteins and its modulation by molecular chaperones

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Proteomic profiling of phosphoproteins and glycoproteins responsive to wild-type alpha-synuclein accumulation and aggregation

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Detecting HSP90 Phosphorylation

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Heat shock proteins reduce aggregation and facilitate degradation of tau protein

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