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

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

Transformation of intact yeast cells treated with alkali cations

Ito, H., Fukuda, Y., Murata, K., & Kimura, A. (1983) · Journal of Bacteriology · doi:10.1128/jb.153.1.163-168.1983 · Cited by 7,518 · see citing works

New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites

Gietz, R. D., & Sugino, A. (1988) · Gene · doi:10.1016/0378-1119(88)90185-0 · Cited by 2,901 · see citing works

The Hsp70 and Hsp60 Chaperone Machines

Bukau, B., & Horwich, A. L. (1998) · Cell · doi:10.1016/s0092-8674(00)80928-9 · Cited by 2,816 · 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

Fluorographic detection of radioactivity in polyacrylamide gols with the water-soluble fluor, sodium salicylate

Chamberlain, J. P. (1979) · Analytical Biochemistry · doi:10.1016/0003-2697(79)90716-4 · Cited by 1,970 · see citing works

Methods in Yeast Genetics: A Laboratory Course Manual

Rose, M. D., Winston, F., & Hieter, P. (1990) · Medical Entomology and Zoology · Cited by 1,894 · see citing works

Crystal Structure of an Hsp90–Geldanamycin Complex: Targeting of a Protein Chaperone by an Antitumor Agent

Stebbins, C. E., Russo, A. A., Schneider, C. B., Rosen, N. X., Hartl, F. U., & Pavletich, N. P. (1997) · Cell · doi:10.1016/s0092-8674(00)80203-2 · Cited by 1,370 · see citing works

Methods in Yeast Genetics — A Laboratory Course Manual

Radford, A. D. (1991) · Biochemical Education · doi:10.1016/0307-4412(91)90039-b · Cited by 1,258 · see citing works

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., & Pearl, L. H. (1997) · Cell · doi:10.1016/s0092-8674(00)80314-1 · Cited by 1,258 · see citing works

An atypical topoisomerase II from archaea with implications for meiotic recombination

Bergerat, A., de Massy, B., Gadelle, D., Varoutas, P.-C., Nicolas, A. G., & Forterre, P. (1997) · Nature · doi:10.1038/386414a0 · Cited by 948 · see citing works

hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures.

Borkovich, K. A., Farrelly, F. W., Finkelstein, D. B., Taulien, J., & Lindquist, S. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.9.3919 · Cited by 641 · see citing works

The Amino-terminal Domain of Heat Shock Protein 90 (hsp90) That Binds Geldanamycin Is an ATP/ADP Switch Domain That Regulates hsp90 Conformation

Grenert, J. P., Sullivan, W. P., Fadden, P., Haystead, T., Clark, J., Mimnaugh, E. G., Krutzsch, H. C., Ochel, H.-J., Schulte, T. W., Sausville, E. A., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.38.23843 · Cited by 568 · 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

Hip, a novel cochaperone involved in the eukaryotic hsc70/hsp40 reaction cycle

Höfeld, J., Minami, Y., & Hartl, F. U. (1995) · Cell · doi:10.1016/0092-8674(95)90099-3 · Cited by 440 · 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

The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj‐1 have distinct roles in recognition of a non‐native protein and protein refolding.

Freeman, B. C., & Morimoto, R. I. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00660.x · Cited by 424 · 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 · cited 1× · see citing works

Supervising the fold: functional principles of molecular chaperones

Büchner, J. (1996) · The FASEB Journal · doi:10.1096/fasebj.10.1.8566529 · Cited by 418 · see citing works

Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90

Schneider, C. B., Sepp‐Lorenzino, L., Nimmesgern, E., Ouerfelli, O., Danishefsky, S. J., Rosen, N. X., & Hartl, F. U. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.25.14536 · Cited by 405 · see citing works

The Role of ATP in the Functional Cycle of the DnaK Chaperone System

McCarty, J. S., Buchberger, A., Reinstein, J., & Bukau, B. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0284 · Cited by 382 · see citing works

Transient Interaction of Hsp90 with Early Unfolding Intermediates of Citrate Synthase

Jakob, U., Lilie, H., Meyer, I., & Büchner, J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7288 · Cited by 360 · see citing works

The 43-kilodalton N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs

Ali, J. A., Jackson, A. P., Howells, A. J., & Maxwell, A. (1993) · Biochemistry · doi:10.1021/bi00061a033 · Cited by 304 · 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

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

Tumor rejection antigen gp96/grp94 is an ATPase: implications for protein folding and antigen presentation.

Li, Z., & Srivastava, P. K. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05983.x · Cited by 287 · 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

Model-free methods of analyzing domain motions in proteins from simulation: A comparison of normal mode analysis and molecular dynamics simulation of lysozyme

Hayward, S., Kitao, A., & Berendsen, H. J. C. (1997) · Proteins Structure Function and Bioinformatics · doi:10.1002/(sici)1097-0134(199703)27:3 · Cited by 282 · 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

Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells

Whitesell, L. J., & Cook, P. (1996) · Molecular Endocrinology · doi:10.1210/mend.10.6.8776730 · Cited by 263 · 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

hsp82 Is an Essential Protein That Is Required in Higher Concentrations for Growth of Cells at Higher Temperatures

Borkovich, K. A., Farrelly, F. W., FINKELSTEIN, D. B., et al. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.9.3919-3930.1989 · Cited by 255 · 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

Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases.

Nadeau, K. C., Das, A., & Walsh, C. T. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54100-4 · Cited by 245 · see citing works

Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence

Scheibel, T., Weikl, T., & Buchner, J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.4.1495 · Cited by 243 · see citing works

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. (1997) · Nature Structural Biology · doi:10.1038/nsb0697-477 · Cited by 239 · see citing works

Nucleotides and Two Functional States of hsp90

Sullivan, W., Stensgard, B. A., Caucutt, G., Bartha, B. B., McMahon, N., Alnemri, E. S., Litwack, G., & Toft, D. O. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.12.8007 · Cited by 235 · 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

The Second Step of ATP Binding to DnaK Induces Peptide Release

Theyssen, H., Schuster, H.-P., Packschies, L., et al. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0606 · Cited by 218 · see citing works

The hsp90-binding Antibiotic Geldanamycin Decreases Raf Levels and Epidermal Growth Factor Signaling without Disrupting Formation of Signaling Complexes or Reducing the Specific Enzymatic Activity of Raf Kinase

Stancato, L. F., Silverstein, A. M., Owens-Grillo, J. K., Chow, Y., Jove, R., & Pratt, W. B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.7.4013 · Cited by 201 · 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

Heat-induced Chaperone Activity of HSP90

Yonehara, M., Minami, Y., Kawata, Y., Nagai, J., & Yahara, I. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.5.2641 · Cited by 194 · see citing works

Folding of the Glucocorticoid Receptor by the Reconstituted hsp90-based Chaperone Machinery

Dittmar, K. D., & Pratt, W. B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.20.13047 · Cited by 183 · 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

The Cyclosporin A-binding Immunophilin CyP-40 and the FK506-binding Immunophilin hsp56 Bind to a Common Site on hsp90 and Exist in Independent Cytosolic Heterocomplexes with the Untransformed Glucocorticoid Receptor

Owens-Grillo, J. K., Hoffmann, K., Hutchison, K. A., Yem, A. W., Deibel, M. R., Handschumacher, R. E., & Pratt, W. B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.35.20479 · Cited by 168 · see citing works

The 90-kDa heat shock protein (hsp-90) possesses an ATP binding site and autophosphorylating activity.

Csermely, P., & Kahn, C. R. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)67740-9 · Cited by 148 · see citing works

How Potassium Affects the Activity of the Molecular Chaperone Hsc70

Wilbanks, S. M., & McKay, D. B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.5.2251 · Cited by 138 · 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

ATP induces a conformational change of the 90-kDa heat shock protein (hsp90).

Csermely, P., Kajtár, J., Hollósi, M., Jalsovszky, G., Holly, S., Kahn, C. R., Gergely, P., Söti, C., Mihály, K., & Somogyi, J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53939-9 · Cited by 133 · see citing works

Modulation of the ATPase Activity of the Molecular Chaperone DnaK by Peptides and the DnaJ and GrpE Heat Shock Proteins

Jordan, R. L., & McMacken, R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.9.4563 · Cited by 131 · see citing works

Geldanamycin-stimulated destabilization of mutated p53 is mediated by the proteasome in vivo

Whitesell, L. J., Sutphin, P. D., An, W. G., Schulte, T. W., Blagosklonny, M. V., & Neckers, L. (1997) · Oncogene · doi:10.1038/sj.onc.1201120 · Cited by 127 · see citing works

How Potassium Affects the Activity of the Molecular Chaperone Hsc70

O’Brien, M. C., & McKay, D. B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.5.2247 · Cited by 116 · see citing works

Interaction of Endoplasmic Reticulum Chaperone GRP94 with Peptide Substrates Is Adenine Nucleotide-independent

Wearsch, P. A., & Nicchitta, C. V. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.8.5152 · Cited by 116 · 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

Cdc37: a protein kinase chaperone?

Hunter, T., & Poon, R. Y. C. (1997) · Trends in Cell Biology · doi:10.1016/s0962-8924(97)01027-1 · Cited by 111 · see citing works

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 · see citing works

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 · see citing works

Identifying the catalytic residue of the ATPase reaction of DNA gyrase.

Jackson, A. P., & Maxwell, A. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.11232 · Cited by 95 · see citing works

Autophosphorylation of grp94 (Endoplasmin)

Csermely, P., Miyata, Y., Schnaider, T., & Yahara, I. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.11.6381 · Cited by 79 · see citing works

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 76 · 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

Hsc70, immunoglobulin heavy chain binding protein, and Hsp90 differ in their ability to stimulate transport of precursor proteins into mammalian microsomes.

Wiech, H., Büchner, J., Zimmermann, M., Zimmermann, R., & Jakob, U. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53190-2 · Cited by 59 · see citing works

Expression of recombinant human casein kinase II and recombinant heat shock protein 90 in Escherichia coli and characterization of their interactions.

Shi, Y., Brown, E. D., & Walsh, C. T. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.7.2767 · Cited by 52 · see citing works

DNA topology: Topoisomerases keep it simple

Bates, A. D., & Maxwell, A. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00403-9 · Cited by 51 · see citing works

Geldanamycin Prevents Nuclear Translocation of Mutant p53

Dasgupta, G., & Momand, J. A. (1997) · Experimental Cell Research · doi:10.1006/excr.1997.3766 · Cited by 49 · see citing works

Plasma-membrane ATPase action affects several stress tolerances of Saccharomyces cerevisiae and Schizosaccharomyces pombe as well as the extent and duration of the heat shock response

Panaretou, B., & Piper, P. W. (1990) · Journal of General Microbiology · doi:10.1099/00221287-136-9-1763 · Cited by 48 · 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., et al. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.2.869-876.1993 · Cited by 48 · see citing works

83‐Kilodalton heat shock proteins of trypanosomes are potent peptide‐stimulated ATPases

Nadeau, K. C., Walsh, C. T., Bradley, M., Sullivan, M. A., & Engman, D. M. (1992) · Protein Science · doi:10.1002/pro.5560010802 · Cited by 43 · see citing works

Authentic temperature-regulation of a heat shock gene inserted into yeast on a high copy number vector

Cheng, L., Hirst, K. L., & Piper, P. W. (1992) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(92)90048-5 · Cited by 23 · see citing works

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

Nardai, G., Schnaider, T., Sőti, C., Ryan, M. T., Høj, P. B., Somogyi, J., & Csermely, P. (1996) · Journal of Biosciences · doi:10.1007/bf02703107 · Cited by 22 · see citing works

The HSP90 chaperone machinery

Schopf, F. H., Biebl, M. M., & Buchner, J. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.20 · Cited by 1,540 · 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

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

The high-affinity HSP90–CHIP complex recognizes and selectively degrades phosphorylated tau client proteins

Dickey, C. A., Kamal, A., Lundgren, K., Klosak, N., Bailey, R. M., Dunmore, J., Ash, P., Shoraka, S., Zlatkovic, J., Eckman, C. B., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci29715 · Cited by 642 · see citing works

HSP90 as a new therapeutic target for cancer therapy: the story unfolds

Maloney, A., & Workman, P. (2002) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2.1.3 · Cited by 531 · see citing works

The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones

Li, J., Soroka, J., & Buchner, J. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.09.003 · Cited by 498 · 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

The Hsp90 molecular chaperone: an open and shut case for treatment

Pearl, L. H., Prodromou, C., & Workman, P. (2008) · Biochemical Journal · doi:10.1042/bj20071640 · Cited by 447 · 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

Swe1Wee1-Dependent Tyrosine Phosphorylation of Hsp90 Regulates Distinct Facets of Chaperone Function

Mollapour, M., Tsutsumi, S., Donnelly, A. C., Beebe, K., Tokita, M. J., Lee, M.-J., Lee, S., Morra, G., Bourboulia, D., Scroggins, B. T., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.01.005 · Cited by 196 · see citing works

Minireview: The Intersection of Steroid Receptors with Molecular Chaperones: Observations and Questions

Smith, D. F., & Toft, D. O. (2008) · Molecular Endocrinology · doi:10.1210/me.2008-0089 · Cited by 173 · see citing works

A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p).

Millson, S. H., Truman, A. W., King, V., Prodromou, C., Pearl, L. H., & Piper, P. W. (2005) · Eukaryotic Cell · doi:10.1128/ec.4.5.849-860.2005 · Cited by 172 · see citing works

Threonine 22 Phosphorylation Attenuates Hsp90 Interaction with Cochaperones and Affects Its Chaperone Activity

Mollapour, M., Tsutsumi, S., Truman, A. W., Xu, W., Vaughan, C. K., Beebe, K., Konstantinova, A., Vourganti, S., Panaretou, B., Piper, P. W., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.02.011 · Cited by 165 · see citing works

The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle

Richter, K., Walter, S., & Buchner, J. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.07.064 · Cited by 159 · see citing works

The Middle Domain of Hsp90 Acts as a Discriminator between Different Types of Client Proteins

Hawle, P., Siepmann, M., Harst, A., Siderius, M., Reusch, H. P., & Obermann, W. M. J. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.02188-05 · Cited by 127 · see citing works

Heat shock protein 90 from <i>Escherichia coli</i> collaborates with the DnaK chaperone system in client protein remodeling

Genest, O., Hoskins, J. R., Camberg, J. L., Doyle, S. M., & Wickner, S. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1104703108 · Cited by 124 · see citing works

The Influence of ATP and p23 on the Conformation of hsp90

Sullivan, W. P., Owen, B. A. L., & Toft, D. O. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207754200 · Cited by 111 · see citing works

Dynamics of the regulation of Hsp90 by the co‐chaperone Sti1

Lee, C., Graf, C., Mayer, F. J., Richter, S. M., & Mayer, M. P. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.37 · Cited by 105 · see citing works

Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs

Leach, M. D., Klipp, E., Cowen, L. E., & Brown, A. J. P. (2012) · Nature Reviews Microbiology · doi:10.1038/nrmicro2875 · Cited by 107 · see citing works

Requirement of Hsp90 for centrosomal function reflects its regulation of Polo kinase stability

de Cárcer, G., do Carmo Avides, M., Lallena, M. J., Glover, D. M., & González, C. (2001) · The EMBO Journal · doi:10.1093/emboj/20.11.2878 · Cited by 90 · see citing works

p23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activity

Forafonov, F., Toogun, O. A., Grad, I., Suslova, E., Freeman, B. C., & Picard, D. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.02246-07 · Cited by 84 · see citing works

Hsp70 and Hsp90 of E. coli Directly Interact for Collaboration in Protein Remodeling

Genest, O., Hoskins, J. R., Kravats, A. N., Doyle, S. M., & Wickner, S. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.10.010 · Cited by 76 · see citing works

The Mechanism of Hsp90 ATPase Stimulation by Aha1

Wolmarans, A., Lee, B., Spyracopoulos, L., & LaPointe, P. (2016) · Scientific Reports · doi:10.1038/srep33179 · Cited by 72 · see citing works

Global proteomic analyses define an environmentally contingent Hsp90 interactome and reveal chaperone-dependent regulation of stress granule proteins and the R2TP complex in a fungal pathogen

O’Meara, T. R., O’Meara, M. J., Polvi, E. J., Pourhaghighi, M. R., Liston, S. D., Lin, Z.-Y., Veri, A. O., Emili, A., Gingras, A.-C., & Cowen, L. E. (2019) · PLoS Biology · doi:10.1371/journal.pbio.3000358 · Cited by 49 · see citing works

Cryo-EM structures reveal a multistep mechanism of Hsp90 activation by co-chaperone Aha1

Liu, Y., Sun, M., Myasnikov, A. G., Elnatan, D., Delaeter, N., Nguyenquang, M., & Agard, D. A. (2020) · doi:10.1101/2020.06.30.180695 · Cited by 37 · see citing works

The interplay between Bag-1, Hsp70, and Hsp90 reveals that inhibiting Hsp70 rebinding is essential for Glucocorticoid Receptor activity

Kirschke, E., Roe-Zurz, Z., Noddings, C., & Agard, D. (2020) · doi:10.1101/2020.05.03.075523 · Cited by 6 · see citing works

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

Evidence for chaperone heterocomplexes containing both Hsp90 and VCP

Prince, T. L., Shao, J., Matts, R. L., & Hartson, S. D. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.04.047 · Cited by 16 · see citing works