A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone

PROCHECK: a program to check the stereochemical quality of protein structures

Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581 · see citing works

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,011 · see citing works

Improved methods for building 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. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,650 · see citing works

X-PLOR Version 3.1: A System for X-ray Crystallography and NMR

Brünger, A. T. (1992) · Medical Entomology and Zoology · Cited by 3,439 · see citing works

Raster3D Version 2.0. A program for photorealistic molecular graphics

Merritt, E. A., & Murphy, M. E. P. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994006396 · Cited by 2,531 · see citing works

The crystal structure of the bacterial chaperonln GroEL at 2.8 Å

Braig, K., Otwinowski, Z., Hegde, R. S., Boisvert, D. C., Joachimiak, A., Horwich, A. L., & Sigler, P. B. (1994) · Nature · doi:10.1038/371578a0 · Cited by 1,321 · see citing works

Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK

Zhu, X., Zhao, X., Burkholder, W., Gragerov, A., Ogata, C., Gottesman, M., & Hendrickson, W. (1996) · Science · doi:10.1126/science.272.5268.1606 · Cited by 1,289 · see citing works

SURFNET: A program for visualizing molecular surfaces, cavities, and intermolecular interactions

Laskowski, R. A. (1995) · Journal of Molecular Graphics · doi:10.1016/0263-7855(95)00073-9 · Cited by 1,005 · see citing works

3D domain swapping: A mechanism for oligomer assembly

Bennett, M. J., Schlunegger, M. P., & Eisenberg, D. S. (1995) · Protein Science · doi:10.1002/pro.5560041202 · Cited by 765 · see citing works

Steroid receptors and their associated proteins

Smith, D. F., & Toft, D. O. (1993) · Molecular Endocrinology · doi:10.1210/mend.7.1.8446107 · Cited by 549 · see citing works

Hsp90 chaperones protein folding in vitro

Wiech, H., Büchner, J., Zimmermann, R., & Jakob, U. (1992) · Nature · doi:10.1038/358169a0 · Cited by 505 · see citing works

A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis

Sikorski, R. S., Boguski, M. S., Goebl, M. G., & Hieter, P. (1990) · Cell · doi:10.1016/0092-8674(90)90745-z · Cited by 499 · see citing works

Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4

Stepanova, L., Leng, X., Parker, S. B., & Harper, J. W. (1996) · Genes & Development · doi:10.1101/gad.10.12.1491 · Cited by 483 · see citing works

Common non-hormone binding component in non-transformed chick oviduct receptors of four steroid hormones

Joab, I., Radanyi, C., Renoir, M., Buchou, T., CATELLI, M. G., Binart, N., Mešter, J., & Baulieu, É.-É. (1984) · Nature · doi:10.1038/308850a0 · Cited by 434 · see citing works

Mutational Analysis of Hsp90 Function: Interactions with a Steroid Receptor and a Protein Kinase

Nathan, D. F., & Lindquist, S. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.7.3917 · Cited by 423 · see citing works

Chaperone Function of Hsp90-Associated Proteins

Bose, S., Weikl, T., Bügl, H., & Buchner, J. (1996) · Science · doi:10.1126/science.274.5293.1715 · Cited by 379 · see citing works

Molecular Chaperone Machines: Chaperone Activities of the Cyclophilin Cyp-40 and the Steroid Aporeceptor-Associated Protein p23

Freeman, B. C., Toft, D. O., & Morimoto, R. I. (1996) · Science · doi:10.1126/science.274.5293.1718 · Cited by 370 · see citing works

Phylogenetic analysis of the 90 kD heat shock family of protein sequences and an examination of the relationship among animals, plants, and fungi species.

Gupta, R. S. (1995) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a040281 · Cited by 316 · see citing works

Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system.

Stancato, L. F., Chow, Y. H., Hutchison, K. A., Perdew, G. H., Jove, R., & Pratt, W. B. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80600-0 · Cited by 300 · see citing works

Snap helix with knob and hole: Essential repeats in S. pombe nuclear protein nuc2 +

Hirano, T., Kinoshita, N., Morikawa, K., & Yanagida, M. (1990) · Cell · doi:10.1016/0092-8674(90)90746-2 · Cited by 295 · see citing works

Progesterone Receptor Structure and Function Altered by Geldanamycin, an hsp90-Binding Agent

Smith, D. F., Whitesell, L. J., Nair, S. C., Chen, S., Prapapanich, V., & Rimerman, R. A. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.12.6804 · Cited by 289 · see citing works

Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila

Cutforth, T. (1994) · Cell · doi:10.1016/0092-8674(94)90442-1 · Cited by 287 · see citing works

Identification of a 60-Kilodalton Stress-Related Protein, p60, which Interacts with hsp90 and hsp70

Smith, D. F., Sullivan, W. P., Marion, T. N., Zaitsu, K., Madden, B. J., McCormick, D., & Toft, D. O. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.2.869 · Cited by 269 · see citing works

A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90.

Aligue, R., Akhavan‐Niak, H., & Russell, P. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06956.x · Cited by 261 · see citing works

A cellular protein that associates with the transforming protein of Rous sarcoma virus is also a heat-shock protein.

Oppermann, H., Levinson, W. E., & Bishop, J. M. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.2.1067 · Cited by 249 · see citing works

Binding of p23 and hsp90 during assembly with the progesterone receptor.

Johnson, J. L., & Toft, D. O. (1995) · Molecular Endocrinology · doi:10.1210/mend.9.6.8592513 · Cited by 233 · see citing works

A novel chaperone complex for steroid receptors involving heat shock proteins, immunophilins, and p23.

Johnson, J. L., & Toft, D. O. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31487-4 · Cited by 229 · see citing works

Role of the Protein Chaperone YDJ1 in Establishing Hsp90-Mediated Signal Transduction Pathways

Kimura, Y., Yahara, I., & Lindquist, S. L. (1995) · Science · doi:10.1126/science.7761857 · Cited by 228 · see citing works

Interaction of the Rous Sarcoma Virus Protein pp60 src with the Cellular Proteins pp50 and pp90

Brugge, J. S. (1986) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-70810-7_1 · Cited by 225 · see citing works

The 56-59-kilodalton protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70- and 90-kilodalton heat shock proteins

Sánchez, E. R., Faber, L. E., Henzel, W. J., & Pratt, W. B. (1990) · Biochemistry · doi:10.1021/bi00473a021 · Cited by 206 · see citing works

The specific DNA binding activity of the dioxin receptor is modulated by the 90 kd heat shock protein.

Wilhelmsson, A., Cuthill, S., Denis, M. G., Wikström, A., Gustafsson, J.-Å., & Poellinger, L. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb08081.x · Cited by 198 · see citing works

The cyclophilin component of the unactivated estrogen receptor contains a tetratricopeptide repeat domain and shares identity with p59 (FKBP59)

Ratajczak, T., Carrello, A., Mark, P. J., Warner, B., Simpson, R. J., Moritz, R. L., & House, A. K. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38636-3 · Cited by 187 · see citing works

A New Member of the hsp90 Family of Molecular Chaperones Interacts with the Retinoblastoma Protein during Mitosis and after Heat Shock

Chen, C., Chen, Y., Dai, K., Chen, P., Riley, D. J., & Lee, W. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.9.4691 · Cited by 183 · see citing works

Cyclophilin 40 (CyP-40), Mapping of Its hsp90 Binding Domain and Evidence That FKBP52 Competes with CyP-40 for hsp90 Binding

Ratajczak, T., & Carrello, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.6.2961 · Cited by 175 · see citing works

The Carboxy-Terminal Region of Mammalian HSP90 Is Required for Its Dimerization and Function In Vivo

Minami, Y., Kimura, Y., Kawasaki, H., Suzuki, K., & Yahara, I. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.2.1459-1464.1994 · Cited by 172 · see citing works

A Model of Protein Targeting Mediated by Immunophilins and Other Proteins That Bind to hsp90 via Tetratricopeptide Repeat Domains

Owens-Grillo, J. K., Czar, M. J., Hutchison, K. A., Hoffmann, K., Perdew, G. H., & Pratt, W. B. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.23.13468 · Cited by 163 · see citing works

The ability of the immunophilin FKBP59-HBI to interact with the 90-kDa heat shock protein is encoded by its tetratricopeptide repeat domain.

Radanyi, C., Chambraud, B., & Baulieu, E. E. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.23.11197 · Cited by 155 · see citing works

Conformational activation of a basic helix-loop-helix protein (MyoD1) by the C-terminal region of murine HSP90 (HSP84).

Shaknovich, R., Shue, G., & Kohtz, D. S. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.11.5059 · Cited by 154 · see citing works

Physical Interaction of Mammalian CDC37 with CDK4

Dai, K., Kobayashi, R., & Beach, D. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.36.22030 · Cited by 134 · see citing works

Interaction between casein kinase II and the 90-kDa stress protein, HSP90

Miyata, Y., & Yahara, I. (1995) · Biochemistry · doi:10.1021/bi00025a019 · Cited by 117 · see citing works

Heat Shock Protein 84 Forms a Complex with Mutant p53 Protein Predominantly within a Cytoplasmic Compartment of the Cell

Sepehrnia, B., Paz, I. B., Dasgupta, G., & Momand, J. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.25.15084 · Cited by 114 · see citing works

Analysis of native forms and isoform compositions of the mouse 90-kDa heat shock protein, HSP90

Minami, Y., Kawasaki, H., Miyata, Y., Suzuki, K., & Yahara, I. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99195-7 · Cited by 102 · see citing works

Purification of a Novel Calcium-independent Phospholipase A2 from Rabbit Kidney

Portilla, D., & Dai, G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.26.15451 · Cited by 85 · see citing works

Characterization of the protein-protein interactions determining the heat shock protein (hsp90.hsp70.hsp56) heterocomplex

Czar, M. J., Owens-Grillo, J. K., Dittmar, K. D., Hutchison, K. A., Zacharek, A. M., Leach, K. L., Deibel, M. R., & Pratt, W. B. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)78104-6 · Cited by 77 · see citing works

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 · see citing works

Immunofluorescence localization of the 90-kDa heat-shock protein to cytoskeleton.

Czar, M. J., Welsh, M. J., & Pratt, W. B. (1996) · PubMed · Cited by 75 · see citing works

Mutational analysis of Hsp90α dimerization and subcellular localization: dimer disruption does not impede ‘in vivo’ interaction with estrogen receptor

Meng, X., Devin, J., Sullivan, W. P., Toft, D. O., Baulieu, É.-É., & CATELLI, M. G. (1996) · Journal of Cell Science · doi:10.1242/jcs.109.7.1677 · Cited by 65 · see citing works

Cyclophilin-40: evidence for a dimeric complex with hsp90

Hoffmann, K., & Handschumacher, R. E. (1995) · Biochemical Journal · doi:10.1042/bj3070005 · Cited by 65 · see citing works

Mutational analysis of hsp90 binding to the progesterone receptor.

Sullivan, W. P., & Toft, D. O. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80738-8 · Cited by 64 · see citing works

The roles of residues Tyr150, Glu272, and His314 in class C β-lactamases

Dubus, A., Ledent, P., Lamotte‐Brasseur, J., & Frère, J. (1996) · Proteins Structure Function and Bioinformatics · doi:10.1002/(sici)1097-0134(199608)25:4 · Cited by 62 · see citing works

Expanding family

Boguski, M. S., Sikorski, R. S., Hieter, P., et al. (1990) · Nature · doi:10.1038/346114a0 · Cited by 35 · see citing works

HSP90 at the hub of protein homeostasis: emerging mechanistic insights

Taipale, M., Jarosz, D. F., & Lindquist, S. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2918 · Cited by 1,818 · see citing works

Structure and mechanism of the Hsp90 molecular chaperone machinery

Pearl, L. H., & Prodromou, C. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142738 · Cited by 1,103 · see citing works

Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin.

Roe, S. M., Prodromou, C., O'Brien, R., Ladbury, J. E., Piper, P. W., & Pearl, L. H. (1999) · Journal of Medicinal Chemistry · doi:10.1021/jm980403y · Cited by 1,004 · see citing works

Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex

Ali, M. M. U., Roe, S. M., Vaughan, C. K., Meyer, P., Panaretou, B., Piper, P. W., Prodromou, C., & Pearl, L. H. (2006) · Nature · doi:10.1038/nature04716 · Cited by 962 · see citing works

Navigating the Chaperone Network: An Integrative Map of Physical and Genetic Interactions Mediated by the Hsp90 Chaperone

Zhao, R., Davey, M., Hsu, Y.-C., Kaplanek, P., Tong, A., Parsons, A. B., Krogan, N., Cagney, G., Mai, D., Greenblatt, J., et al. (2005) · Cell · doi:10.1016/j.cell.2004.12.024 · Cited by 819 · see citing works

ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo

Panaretou, B., Prodromou, C., Roe, S. M., O'Brien, R., Ladbury, J. E., Piper, P. W., & Pearl, L. H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.16.4829 · Cited by 735 · see citing works

The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease

Hoter, A., El-Sabban, M. E., & Naim, H. Y. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092560 · Cited by 693 · see citing works

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. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00065-0 · Cited by 491 · see citing works

The ATPase cycle of Hsp90 drives a molecular ‘clamp’ via transient dimerization of the N‐terminal domains

Prodromou, C., Panaretou, B., Chohan, S., Siligardi, G., O'Brien, R., Ladbury, J. E., Roe, S. M., Piper, P. W., & Pearl, L. H. (2000) · The EMBO Journal · doi:10.1093/emboj/19.16.4383 · Cited by 492 · see citing works

<i>In vivo</i> functions of the <i>Saccharomyces cerevisiae</i> Hsp90 chaperone

Nathan, D. F., Vos, M. H., & Lindquist, S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.24.12949 · Cited by 364 · see citing works

Hsp90-Tau complex reveals molecular basis for specificity in chaperone action

Karagöz, G. E., Duarte, A. M. S., Akoury, E., Ippel, H., Biernat, J., Morán Luengo, T., Radli, M., Didenko, T., Nordhues, B. A., Veprintsev, D. B., et al. (2014) · Cell · doi:10.1016/j.cell.2014.01.037 · Cited by 318 · see citing works

Conformational dynamics of the molecular chaperone Hsp90

Krukenberg, K. A., Street, T. O., Lavery, L. A., & Agard, D. A. (2011) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583510000314 · Cited by 308 · see citing works

Structure and in vivo function of Hsp90

Pearl, L. H., & Prodromou, C. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)00047-0 · Cited by 317 · see citing works

Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle

Siligardi, G., Hu, B., Panaretou, B., Piper, P. W., Pearl, L. H., & Prodromou, C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410562200 · Cited by 207 · see citing works

HSP90AB1: Helping the good and the bad

Haase, M., & Fitze, G. (2016) · Gene · doi:10.1016/j.gene.2015.08.063 · Cited by 179 · see citing works

The Plasticity of the Hsp90 Co-chaperone System

Sahasrabudhe, P., Rohrberg, J., Biebl, M. M., Rutz, D. A., & Buchner, J. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.08.004 · Cited by 136 · see citing works

Structural basis for species-selective targeting of Hsp90 in a pathogenic fungus

Whitesell, L., Robbins, N., Huang, D. S., McLellan, C. A., Shekhar-Guturja, T., LeBlanc, E. V., Nation, C. S., Hui, R., Hutchinson, A., Collins, C., et al. (2019) · Nature Communications · doi:10.1038/s41467-018-08248-w · Cited by 124 · see citing works

Client binding shifts the populations of dynamic Hsp90 conformations through an allosteric network

Lopez, A., Dahiya, V., Delhommel, F., Freiburger, L., Stehle, R., Asami, S., Rutz, D., Blair, L., Buchner, J., & Sattler, M. (2021) · Science Advances · doi:10.1126/sciadv.abl7295 · Cited by 59 · see citing works

Simulation study of the function of domain swapping in the HSP90 chaperone cycle

Matsukura, L., & Miyashita, N. (2022) · Journal of Physics Conference Series · doi:10.1088/1742-6596/2207/1/012024

The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding

Woodford, M. R., Dunn, D. M., Blanden, A. R., Capriotti, D., Loiselle, D. R., Prodromou, C., Panaretou, B., Hughes, P. F., Smith, A. P., Ackerman, W., et al. (2016) · Nature Communications · doi:10.1038/ncomms12037 · Cited by 76 · see citing works

Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle

Li, J., Richter, K., Reinstein, J., & Büchner, J. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2502 · Cited by 130 · see citing works

Inhibition of GR‐mediated transcription by p23 requires interaction with Hsp90

Wochnik, G. M., Young, J. C., Schmidt, U., Holsboer, F., Hartl, F. U., & Rein, T. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00066-3 · Cited by 46 · see citing works

A novel chaperone-activity-reducing mechanism of the 90-kDa molecular chaperone HSP90

Itoh, H., Ogura, M., Komatsuda, A., Wakui, H., MIURA, A. B., & Tashima, Y. (1999) · Biochemical Journal · doi:10.1042/bj3430697 · Cited by 83 · see citing works