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

Global analysis of protein expression in yeast

Ghaemmaghami, S., Huh, W.-K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., & Weissman, J. S. (2003) · Nature · doi:10.1038/nature02046 · Cited by 3,750 · see citing works

Hsp90 as a capacitor for morphological evolution

Rutherford, S. L., & Lindquist, S. (1998) · Nature · doi:10.1038/24550 · Cited by 2,270 · see citing works

The Heat Shock Response: Life on the Verge of Death

Richter, K., Haslbeck, M., & Büchner, J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.006 · Cited by 2,045 · 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

Steroid Receptor Interactions with Heat Shock Protein and Immunophilin Chaperones*

Pratt, W. B., & Toft, D. O. (1997) · Endocrine Reviews · doi:10.1210/edrv.18.3.0303 · Cited by 1,791 · see citing works

Regulation of Signaling Protein Function and Trafficking by the hsp90/hsp70-Based Chaperone Machinery 1

Pratt, W., & Toft, D. (2003) · Experimental biology and medicine · doi:10.1177/153537020322800201 · Cited by 1,539 · see citing works

Targeting the dynamic HSP90 complex in cancer

Trepel, J. B., Mollapour, M., Giaccone, G., & Neckers, L. (2010) · Nature reviews. Cancer · doi:10.1038/nrc2887 · Cited by 1,523 · see citing works

Hsp90 as a capacitor of phenotypic variation

Queitsch, C., Sangster, T. A., & Lindquist, S. (2002) · Nature · doi:10.1038/nature749 · Cited by 1,372 · see citing works

Repression of Heat Shock Transcription Factor HSF1 Activation by HSP90 (HSP90 Complex) that Forms a Stress-Sensitive Complex with HSF1

Zou, J., Guo, Y., Guettouche, T., Smith, D. F., & Voellmy, R. W. (1998) · Cell · doi:10.1016/s0092-8674(00)81588-3 · Cited by 1,232 · see citing works

Structure of TPR Domain–Peptide Complexes

Scheufler, C., Brinker, A., Bourenkov, G., Pegoraro, S., Moroder, L., Bartunik, H., Hartl, F. U., & Moarefi, I. (2000) · Cell · doi:10.1016/s0092-8674(00)80830-2 · Cited by 1,188 · see citing works

HDAC6 Regulates Hsp90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor

Kovacs, J. J., Murphy, P. J. M., Gaillard, S., Zhao, X., Wu, J.-T., Nicchitta, C. V., Yoshida, M., Toft, D. O., Pratt, W. B., & Yao, T.-P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.021 · Cited by 1,153 · see citing works

Dynamic activation of endothelial nitric oxide synthase by Hsp90

García‐Cardeña, G., Fan, R., Shah, V. H., Sorrentino, R., Cirino, G., Papapetropoulos, A., & Sessa, W. C. (1998) · Nature · doi:10.1038/33934 · Cited by 1,029 · see citing works

The 90-kDa Molecular Chaperone Family

Csermely, P., Schnaider, T., Sőti, C., Prohászka, Z., & Nardai, G. (1998) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(98)00013-8 · Cited by 1,024 · see citing works

Modulation of Akt kinase activity by binding to Hsp90

Sato, S., Fujita, N., & Tsuruo, T. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.170276797 · Cited by 967 · 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

Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70

Young, J. C., Hoogenraad, N. J., & Hartl, F. U. (2003) · Cell · doi:10.1016/s0092-8674(02)01250-3 · Cited by 915 · see citing works

The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR‐mediated protein–protein interactions

Das, A. K., Cohen, P. T. W., & Barford, D. (1998) · The EMBO Journal · doi:10.1093/emboj/17.5.1192 · Cited by 832 · see citing works

Heat Shock Factor 1 Is a Powerful Multifaceted Modifier of Carcinogenesis

Dai, C., Whitesell, L. J., Rogers, A. B., & Lindquist, S. L. (2007) · Cell · doi:10.1016/j.cell.2007.07.020 · Cited by 827 · see citing works

Hsp90

Young, J. C., Moarefi, I., & Hartl, F. U. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200104079 · Cited by 826 · 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

Heat-shock protein 90, a chaperone for folding and regulation

Picard, D. (2002) · Cellular and Molecular Life Sciences · doi:10.1007/pl00012491 · Cited by 797 · see citing works

Reduced levels of hsp90 compromise steroid receptor action in vivo

Picard, D., Khursheed, B., Garabedian, M. J., Fortin, M. G., Lindquist, S., & Yamamoto, K. R. (1990) · Nature · doi:10.1038/348166a0 · Cited by 787 · see citing works

GHKL, an emergent ATPase/kinase superfamily

DUTTA, R., & Inouye, M. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01503-0 · Cited by 767 · see citing works

Inhibition of Histone Deacetylase 6 Acetylates and Disrupts the Chaperone Function of Heat Shock Protein 90

Bali, P., Pranpat, M., Bradner, J., Balasis, M., Fiskus, W., Guo, F., Rocha, K., Kumaraswamy, S., Boyapalle, S., Atadja, P., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500186200 · Cited by 755 · see citing works

SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells

Hamamoto, R., Furukawa, Y., Morita, M., Iimura, Y., Pittella-Silva, F., Li, M., Yagyu, R., & Nakamura, Y. (2004) · Nature Cell Biology · doi:10.1038/ncb1151 · Cited by 738 · 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

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

Steroid Receptor Interactions with Heat Shock Protein and Immunophilin Chaperones

Pratt, W. B. (1997) · Endocrine Reviews · doi:10.1210/er.18.3.306 · Cited by 641 · see citing works

Hsp90 isoforms: functions, expression and clinical importance

Sreedhar, A. S., Kalmár, É., Csermely, P., & Shen, Y.-F. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00229-7 · Cited by 624 · see citing works

Hsp90 Cochaperone Aha1 Downregulation Rescues Misfolding of CFTR in Cystic Fibrosis

Wang, X., Venable, J. D., LaPointe, P., Hutt, D. M., Koulov, A. V., Coppinger, J. A., Gürkan, C., Kellner, W. A., Matteson, J., Plutner, H., et al. (2006) · Cell · doi:10.1016/j.cell.2006.09.043 · Cited by 601 · see citing works

In Vivo Function of Hsp90 Is Dependent on ATP Binding and ATP Hydrolysis

Obermann, W. M. J., Sondermann, H., Russo, A. A., Pavletich, N. P., & Hartl, F. U. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.4.901 · Cited by 593 · see citing works

Functional proteomic screens reveal an essential extracellular role for hsp90α in cancer cell invasiveness

Eustace, B. K., Sakurai, T., Stewart, J. K., Yimlamai, D., Unger, C., Zehetmeier, C., Lain, B., Torella, C., Henning, S. W., Beste, G., et al. (2004) · Nature Cell Biology · doi:10.1038/ncb1131 · Cited by 590 · see citing works

The Hsp90 Chaperone Machinery

Wandinger, S. K., Richter, K., & Büchner, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800007200 · Cited by 548 · see citing works

Activation of the ATPase Activity of Hsp90 by the Stress-Regulated Cochaperone Aha1

Panaretou, B., Siligardi, G., Meyer, P., Maloney, A., Sullivan, J. K., Singh, S., Millson, S. H., Clarke, P. A., Naaby‐Hansen, S., Stein, R. C., et al. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00785-2 · Cited by 544 · see citing works

Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3

Gamerdinger, M., Hajieva, P., Kaya, A. M., Wolfrum, U., Hartl, F. U., & Behl, C. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.29 · Cited by 522 · see citing works

HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis

Takahashi, A., Casais, C., Ichimura, K., & Shirasu, K. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2033934100 · Cited by 494 · see citing works

Diverse Cellular Functions of the Hsp90 Molecular Chaperone Uncovered Using Systems Approaches

McClellan, A. J., Xia, Y., Deutschbauer, A. M., Davis, R. W., Gerstein, M., & Frydman, J. (2007) · Cell · doi:10.1016/j.cell.2007.07.036 · Cited by 474 · see citing works

Structural Analysis of E. coli hsp90 Reveals Dramatic Nucleotide-Dependent Conformational Rearrangements

Shiau, A. K., Harris, S. F., Southworth, D. R., & Agard, D. A. (2006) · Cell · doi:10.1016/j.cell.2006.09.027 · Cited by 455 · see citing works

Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)‐domain co‐chaperones

Prodromou, C., Siligardi, G., O'brien, R., Woolfson, D., Regan, L., Panaretou, B., Ladbury, J., Piper, P., & Pearl, L. H. (1999) · EMBO Journal · doi:10.1093/emboj/18.3.754 · Cited by 455 · see citing works

A crucial function of SGT1 and HSP90 in inflammasome activity links mammalian and plant innate immune responses

Mayor, A., Martinon, F., Smedt, T. D., Pétrilli, V., & Tschopp, J. (2007) · Nature Immunology · doi:10.1038/ni1459 · Cited by 438 · see citing works

Regulatory Role of SGT1 in Early R Gene-Mediated Plant Defenses

Austin, M. J., Muskett, P. R., Kahn, K., Feys, B. J., Jones, J. D. G., & Parker, J. E. (2002) · Science · doi:10.1126/science.1067747 · Cited by 421 · see citing works

Heat-shock protein hsp90 governs the activity of pp60v-src kinase.

Xu, Y., & Lindquist, S. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.15.7074 · Cited by 416 · see citing works

An Acetylation Site in the Middle Domain of Hsp90 Regulates Chaperone Function

Scroggins, B. T., Robzyk, K., Wang, D., Marcu, M. G., Tsutsumi, S., Beebe, K., Cotter, R. J., Felts, S., Toft, D., Karnitz, L., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.008 · Cited by 413 · see citing works

THE SELECTION OF S. CEREVISIAE MUTANTS DEFECTIVE IN THE START EVENT OF CELL DIVISION

Reed, S. I. (1980) · Genetics · doi:10.1093/genetics/95.3.561 · Cited by 393 · 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

Glucose depletion accounts for the induction of two transformation-sensitive membrane proteinsin Rous sarcoma virus-transformed chick embryo fibroblasts.

Shiu, R. P. C., Pouysségur, J., & Pastan, I. H. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.9.3840 · Cited by 376 · see citing works

The hsp90-related Protein TRAP1 Is a Mitochondrial Protein with Distinct Functional Properties

Felts, S. J., Owen, B. A. L., Nguyen, P., Trepel, J. B., Donner, D. B., & Toft, D. O. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.5.3305 · Cited by 371 · 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

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

Hop Modulates hsp70/hsp90 Interactions in Protein Folding

Johnson, B. D., Schumacher, R. J., Ross, E. D., & Toft, D. O. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.6.3679 · Cited by 358 · see citing works

The Hsp90‐binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo

Riggs, D. L., Roberts, P. J., Chirillo, S. C., Cheung‐Flynn, J., Prapapanich, V., Ratajczak, T., Gaber, R., Picard, D., & Smith, D. F. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg108 · Cited by 353 · see citing works

The Mechanism of Hsp90 Regulation by the Protein Kinase-Specific Cochaperone p50cdc37

Roe, S. M., Ali, M. M. U., Meyer, P., Vaughan, C. K., Panaretou, B., Piper, P. W., Prodromou, C., & Pearl, L. H. (2004) · Cell · doi:10.1016/s0092-8674(03)01027-4 · Cited by 351 · see citing works

Hsp90 and Environmental Stress Transform the Adaptive Value of Natural Genetic Variation

Jarosz, D. F., & Lindquist, S. (2010) · Science · doi:10.1126/science.1195487 · Cited by 346 · see citing works

Molecular Chaperone Hsp90 Associates with Resistance Protein N and Its Signaling Proteins SGT1 and Rar1 to Modulate an Innate Immune Response in Plants

Liu, Y., Burch‐Smith, T. M., Schiff, M., Feng, S., & Dinesh‐Kumar, S. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310029200 · Cited by 346 · see citing works

Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90

Heßling, M., Richter, K., & Büchner, J. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1565 · Cited by 343 · see citing works

Domain Mapping Studies Reveal That the M Domain of hsp90 Serves as a Molecular Scaffold to Regulate Akt-Dependent Phosphorylation of Endothelial Nitric Oxide Synthase and NO Release

Fontana, J. T., Fulton, D. J., Chen, Y., Fairchild, T. A., McCabe, T. J. D., Fujita, N., Tsuruo, T., & Sessa, W. C. (2002) · Circulation Research · doi:10.1161/01.res.0000016837.26733.be · Cited by 340 · see citing works

Identification of Functional Domains of the Aryl Hydrocarbon Receptor

Fukunaga, B. N., Probst, M. R., Reisz-Porszasz, S., & Hankinson, O. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.49.29270 · Cited by 338 · see citing works

Hop as an Adaptor in the Heat Shock Protein 70 (Hsp70) and Hsp90 Chaperone Machinery

Chen, S., & Smith, D. F. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.52.35194 · Cited by 334 · see citing works

S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities

Martı́nez-Ruiz, A., Villanueva, L., de Orduña, C. G., López‐Ferrer, D., Higueras, M. Á., Tarín, C., Rodríguez‐Crespo, I., Vázquez, J., & Lamas, S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407294102 · Cited by 330 · see citing works

Update on Hsp90 Inhibitors in Clinical Trial

Kim, Y., Alarcon, S., Lee, S., Lee, M.-J., Giaccone, G., Neckers, L., & Trepel, J. (2009) · Current Topics in Medicinal Chemistry · doi:10.2174/156802609789895728 · Cited by 311 · see citing works

Altered Hsp90 function in cancer: A unique therapeutic opportunity

Bagatell, R., & Whitesell, L. J. (2004) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.1021.3.8 · Cited by 301 · see citing works

Dynamics of heat shock protein 90–progesterone receptor binding and the disactivation loop model for steroid receptor complexes

Smith, D. F. (1993) · Molecular Endocrinology · doi:10.1210/me.7.11.1418 · Cited by 300 · see citing works

Structure of an Hsp90-Cdc37-Cdk4 Complex

Vaughan, C. K., Gohlke, U., Sobott, F., Good, V. M., Ali, M. M. U., Prodromou, C., Robinson, C. V., Saibil, H. R., & Pearl, L. H. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.07.016 · Cited by 293 · see citing works

HSP90 and Its R2TP/Prefoldin-like Cochaperone Are Involved in the Cytoplasmic Assembly of RNA Polymerase II

Boulon, S., Pradet‐Balade, B., Verheggen, C., Molle, D., Boireau, S., Georgieva, M., Azzag, K., Robert, M.-C., Ahmad, Y., Neel, H., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.08.023 · Cited by 289 · see citing works

Extracellular heat shock protein‐90α: linking hypoxia to skin cell motility and wound healing

Li, W., Li, Y., Guan, S., Fan, J., Cheng, C.-F., Bright, A. M., Chinn, C., Chen, M., & Woodley, D. T. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601579 · Cited by 280 · see citing works

Enhanced SMYD3 expression is essential for the growth of breast cancer cells

Hamamoto, R., Pittella-Silva, F., Tsuge, M., Nishidate, T., Katagiri, T., Nakamura, Y., & Furukawa, Y. (2006) · Cancer Science · doi:10.1111/j.1349-7006.2006.00146.x · Cited by 275 · see citing works

Regulation of Hsp90 ATPase Activity by the Co-chaperone Cdc37p/p50

Siligardi, G., Panaretou, B., Meyer, P., Singh, S., Woolfson, D. N., Piper, P. W., Pearl, L. H., & Prodromou, C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201287200 · Cited by 272 · 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

Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistancePreprint

Geller, R., Vignuzzi, M., Andino, R., & Frydman, J. (2007) · Genes & Development · doi:10.1101/gad.1505307 · Cited by 260 · see citing works

Protein Phosphatase 5 Is a Major Component of Glucocorticoid Receptor·hsp90 Complexes with Properties of an FK506-binding Immunophilin

Silverstein, A. M., Galigniana, M. D., Chen, M.-S., Owens-Grillo, J. K., Chinkers, M., & Pratt, W. B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.26.16224 · Cited by 258 · see citing works

Histone Deacetylase 6 and Heat Shock Protein 90 Control the Functions of Foxp3 + T-Regulatory Cells

de Zoeten, E. F., Wang, L., Butler, K. V., Beier, U. H., Akimova, T., Sai, H., Bradner, J. E., Mazitschek, R., Kozikowski, A. P., Matthias, P., et al. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05155-11 · Cited by 257 · see citing works

The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis

Mickler, M., Heßling, M., Ratzke, C., Büchner, J., & Hugel, T. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1557 · Cited by 254 · see citing works

Role of the Myosin Assembly Protein UNC-45 as a Molecular Chaperone for Myosin

Barral, J. M., Hutagalung, A. H., Brinker, A., Hartl, F. U., & Epstein, H. F. (2002) · Science · doi:10.1126/science.1066648 · Cited by 252 · see citing works

Expression and characterization of human FKBP52, an immunophilin that associates with the 90-kDa heat shock protein and is a component of steroid receptor complexes.

Peattie, D. A., Harding, M. W., Fleming, M. A., DeCenzo, M. T., Lippke, J. A., Livingston, D. J., & Benasutti, M. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.22.10974 · Cited by 251 · see citing works

The Assembly of Progesterone Receptor-hsp90 Complexes Using Purified Proteins*

Kosano, H., Stensgard, B., Charlesworth, M., McMahon, N., & Toft, D. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.49.32973 · Cited by 251 · see citing works

Under cover: causes, effects and implications of Hsp90‐mediated genetic capacitance

Sangster, T. A., Lindquist, S., & Queitsch, C. (2004) · BioEssays · doi:10.1002/bies.20020 · Cited by 251 · see citing works

Chaperoning of Glucocorticoid Receptors

Pratt, W. B., Morishima, Y., Murphy, M. N., & Harrell, M. (2005) · Springer eBooks · doi:10.1007/3-540-29717-0_5 · Cited by 247 · 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

Asymmetric Activation of the Hsp90 Dimer by Its Cochaperone Aha1

Retzlaff, M., Hagn, F., Mitschke, L., Heßling, M., Gugel, F., Kessler, H., Richter, K., & Büchner, J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.01.006 · Cited by 244 · see citing works

Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery

Meyer, P., Prodromou, C., Liao, C., Hu, B., Roe, S., Vaughan, C., Vlašić, I., Panaretou, B., Piper, P., & Pearl, L. H. (2004) · EMBO Journal · doi:10.1038/sj.emboj.7600141 · Cited by 244 · see citing works

Stimulation of the weak ATPase activity of human hsp90 by a client protein.

McLaughlin, S., Smith, H. W., & Jackson, S. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5245 · Cited by 244 · 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

Hepatitis C virus RNA replication is regulated by FKBP8 and Hsp90

Okamoto, T., Nishimura, Y., Ichimura, T., Suzuki, K., Miyamura, T., Suzuki, T., Moriishi, K., & Matsuura, Y. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601367 · Cited by 241 · see citing works

The Importance of ATP Binding and Hydrolysis by Hsp90 in Formation and Function of Protein Heterocomplexes*

Grenert, J. P., Johnson, B. D., & Toft, D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.25.17525 · Cited by 238 · see citing works

Aha1 Binds to the Middle Domain of Hsp90, Contributes to Client Protein Activation, and Stimulates the ATPase Activity of the Molecular Chaperone

Lotz, G. P., Lin, H., Harst, A., & Obermann, W. M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212761200 · Cited by 236 · 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

Insights into the catalytic mechanism of peptidyl prolyl cis/trans isomerases

Fanghänel, J. (2004) · Frontiers in bioscience · doi:10.2741/1494 · Cited by 232 · see citing works

Characterization of the AhR−hsp90−XAP2 Core Complex and the Role of the Immunophilin-Related Protein XAP2 in AhR Stabilization

Meyer, B. K., & Perdew, G. H. (1999) · Biochemistry · doi:10.1021/bi982223w · Cited by 232 · 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

Arabidopsis ROF1 (FKBP62) modulates thermotolerance by interacting with HSP90.1 and affecting the accumulation of HsfA2‐regulated sHSPs

Meiri, D., & Breiman, A. (2009) · The Plant Journal · doi:10.1111/j.1365-313x.2009.03878.x · Cited by 229 · see citing works

Ligand Discrimination by TPR Domains

Brinker, A., Scheufler, C., von der Muelbe, F., Fleckenstein, B. T., Herrmann, C., Jung, G., Moarefi, I., & Hartl, F. U. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109002200 · Cited by 227 · 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

Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle.

Southworth, D., & Agard, D. (2008) · Molecules and Cells · doi:10.1016/j.molcel.2008.10.024 · Cited by 225 · see citing works

A Cyclophilin Function in Hsp90-Dependent Signal Transduction

Duina, A. A., Foreman, H.-C. C., Marsh, J. A., Lindquist, S. L., & Gaber, R. F. (1996) · Science · doi:10.1126/science.274.5293.1713 · Cited by 224 · see citing works

Hsp90 Recognizes a Common Surface on Client Kinases

Citri, A., Harari, D., Shohat-Ophir, G., Ramakrishnan, P., Gan, J., Lavi, S., Eisenstein, M., Kimchi, A., Wallach, D., Pietrokovski, S., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512613200 · Cited by 222 · see citing works

Evidence for a Mechanism of Repression of Heat Shock Factor 1 Transcriptional Activity by a Multichaperone Complex

Guo, Y., Guettouche, T., Fenna, M., Boellmann, F., Pratt, W. B., Toft, D. O., Smith, D. F., & Voellmy, R. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105931200 · Cited by 221 · see citing works

Role of Acetylation and Extracellular Location of Heat Shock Protein 90α in Tumor Cell Invasion

Yang, Y., Rao, R., Shen, J., Tang, Y., Fiskus, W. C., Nechtman, J., Atadja, P. W., & Bhalla, K. N. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-0644 · Cited by 221 · see citing works

Identification of Hsp90 as a Stimulatory Host Factor Involved in Influenza Virus RNA Synthesis

Momose, F., Naito, T., Yano, K., Sugimoto, S., Morikawa, Y., & Nagata, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206822200 · Cited by 212 · see citing works

The hsp90 Chaperone Complex Regulates Intracellular Localization of the Dioxin Receptor

Kazlauskas, A., Sundström, S., Poellinger, L., & Pongratz, I. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.7.2594-2607.2001 · Cited by 211 · see citing works

The HSP90 chaperone complex, an emerging force in plant development and phenotypic plasticity

Sangster, T. A., & Queitsch, C. (2004) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2004.11.012 · Cited by 205 · see citing works

Hsp90-Dependent Activation of Protein Kinases Is Regulated by Chaperone-Targeted Dephosphorylation of Cdc37

Vaughan, C. K., Mollapour, M., Smith, J. R., Truman, A. W., Hu, B., Good, V. M., Panaretou, B., Neckers, L., Clarke, P. A., Workman, P., et al. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.07.021 · Cited by 202 · see citing works

Proposal for a role of the Hsp90/Hsp70-based chaperone machinery in making triage decisions when proteins undergo oxidative and toxic damage

Pratt, W. B., Morishima, Y., Peng, H., & Osawa, Y. (2010) · Experimental Biology and Medicine · doi:10.1258/ebm.2009.009250 · Cited by 201 · see citing works

Characterization of a Novel 23-Kilodalton Protein of Unactive Progesterone Receptor Complexes

Johnson, J. L., Beito, T. G., Krco, C. J., & Toft, D. O. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.3.1956 · Cited by 197 · see citing works

The Co-chaperone p23 Arrests the Hsp90 ATPase Cycle to Trap Client Proteins

McLaughlin, S. H., Sobott, F., Yao, Z.-P., Zhang, W., Nielsen, P. R., Grossmann, J. G., Laue, E. D., Robinson, C. V., & Jackson, S. E. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.11.085 · Cited by 196 · 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

Molecular Cloning of Human FKBP51 and Comparisons of Immunophilin Interactions with Hsp90 and Progesterone Receptor

Nair, S. C., Rimerman, R. A., Toran, E. J., Chen, S., Prapapanich, V., Butts, R. N., & Smith, D. F. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.2.594 · Cited by 196 · see citing works

Sti1 Is a Non-competitive Inhibitor of the Hsp90 ATPase

Richter, K., Muschler, P., Hainzl, O., Reinstein, J., & Büchner, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213094200 · Cited by 188 · see citing works

Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation

Zhao, R., Kakihara, Y., Gribun, A., Huen, J., Yang, G., Khanna, M., Costanzo, M., Brost, R. L., Boone, C. M., Hughes, T. R., et al. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200709061 · Cited by 185 · see citing works

The Human Double-stranded DNA-activated Protein Kinase Phosphorylates the 90-kDa Heat-shock Protein, hsp90α at Two NH2-terminal Threonine Residues

Lees‐Miller, S. P., & Anderson, C. W. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71488-9 · Cited by 182 · see citing works

Ancient heat shock gene is dispensable

Bardwell, J. C. A., & Craig, E. A. (1988) · Journal of Bacteriology · doi:10.1128/jb.170.7.2977-2983.1988 · Cited by 181 · see citing works

NLR sensors meet at the SGT1–HSP90 crossroad

Kadota, Y., Shirasu, K., & Guérois, R. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.12.005 · Cited by 181 · see citing works

Functional analysis of the hsp90-associated human peptidyl prolyl Cis/Trans isomerases FKBP51, FKBP52 and cyp40 1 1Edited by R. Huber

Pirkl, F., & Buchner, J. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4595 · Cited by 179 · 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

Assembly of progesterone receptor with heat shock proteins and receptor activation are ATP mediated events.

Smith, D. F., Stensgard, B. A., Welch, W. J., & Toft, D. O. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48438-4 · Cited by 174 · see citing works

Biological and Structural Basis for Aha1 Regulation of Hsp90 ATPase Activity in Maintaining Proteostasis in the Human Disease Cystic Fibrosis

Koulov, A. V., LaPointe, P., Lu, B., Razvi, A., Coppinger, J. A., Dong, M., Matteson, J., Laister, R. C., Arrowsmith, C. H., Yates, J. R., et al. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-12-1017 · Cited by 173 · see citing works

Hsp90 is regulated by a switch point in the C‐terminal domain

Retzlaff, M., Stahl, M., Eberl, H. C., Lagleder, S., Beck, J., Kessler, H., & Büchner, J. (2009) · EMBO Reports · doi:10.1038/embor.2009.153 · Cited by 171 · see citing works

The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies

Freeman, B. C., Felts, S. J., Toft, D. O., & Yamamoto, K. R. (2000) · Genes & Development · doi:10.1101/gad.14.4.422 · Cited by 168 · see citing works

Substrate Binding Drives Large-Scale Conformational Changes in the Hsp90 Molecular Chaperone

Street, T. O., Lavery, L. A., & Agard, D. A. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.01.029 · Cited by 166 · 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

Substrate Transfer from the Chaperone Hsp70 to Hsp90

Wegele, H., Wandinger, S. K., Schmid, A. B., Reinstein, J., & Büchner, J. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.12.008 · Cited by 162 · 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

Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90.

Chadli, A., Bouhouche, I., Sullivan, W. J., Stensgard, B., McMahon, N., Catelli, M., & Toft, D. (2000) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.220430297 · Cited by 159 · see citing works

Conservation of Hsp90 macromolecular complexes in Saccharomyces cerevisiae.

Chang, H.-C., & Lindquist, S. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31486-2 · Cited by 158 · see citing works

The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90

Wandinger, S. K., Suhre, M. H., Wegele, H., & Büchner, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7600930 · Cited by 158 · see citing works

Drosophila Piwi functions in Hsp90-mediated suppression of phenotypic variation

Gangaraju, V. K., Yin, H., Weiner, M. M., Wang, J., Huang, X., & Lin, H. (2010) · Nature Genetics · doi:10.1038/ng.743 · Cited by 156 · see citing works

Mixed Hsp90–cochaperone complexes are important for the progression of the reaction cycle

Li, J., Richter, K., & Buchner, J. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1965 · Cited by 155 · see citing works

SBA1 Encodes a Yeast Hsp90 Cochaperone That Is Homologous to Vertebrate p23 Proteins

Fang, Y., Fliss, A., Rao, J., & Caplan, A. J. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.7.3727 · Cited by 154 · see citing works

Hsp90 Chaperones Wild-type p53 Tumor Suppressor Protein

Walerych, D., Kudla, G. R., Gutkowska, M., Wawrzynów, B., Muller, L., King, F. W., Helwak, A., Boros, J., Żylicz, M., & Żylicz, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407601200 · Cited by 153 · see citing works

Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery

Meyer, P., Prodromou, C., Liao, C., Hu, B., Roe, S., Vaughan, C., Vlašić, I., Panaretou, B., Piper, P., & Pearl, L. H. (2004) · EMBO Journal · doi:10.1038/sj.emboj.7600060 · Cited by 153 · see citing works

Noncatalytic Role of the FKBP52 Peptidyl-Prolyl Isomerase Domain in the Regulation of Steroid Hormone Signaling

Riggs, D. L., Cox, M. B., Tardif, H. L., Hessling, M., Buchner, J., & Smith, D. F. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00985-07 · Cited by 150 · see citing works

HSP40 Binding Is the First Step in the HSP90 Chaperoning Pathway for the Progesterone Receptor*

Hernández, M., Chadli, A., & Toft, D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111445200 · Cited by 149 · see citing works

Mapping the HSP90 binding region of the glucocorticoid receptor.

Howard, K. J., Holley, S., Yamamoto, K. R., & Distelhorst, C. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38489-3 · Cited by 145 · see citing works

Conserved Conformational Changes in the ATPase Cycle of Human Hsp90

Richter, K., Soroka, J., Skalniak, Ł., Leskovar, A., Heßling, M., Reinstein, J., & Büchner, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800540200 · Cited by 145 · see citing works

Src-mediated Phosphorylation of Hsp90 in Response to Vascular Endothelial Growth Factor (VEGF) Is Required for VEGF Receptor-2 Signaling to Endothelial NO Synthase

Duval, M., Bœuf, F. L., Huot, J., & Gratton, J. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-05-0467 · Cited by 140 · see citing works

Sti1 Is a Novel Activator of the Ssa Proteins

Wegele, H., Haslbeck, M., Reinstein, J., & Büchner, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301548200 · Cited by 138 · see citing works

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 · see citing works

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 · see citing works

Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system

Brychzy, A., Rein, T., Winklhofer, K. F., Hartl, F. U., Young, J. C., & Obermann, W. M. J. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg362 · Cited by 135 · see citing works

The Host Cell Chaperone Hsp90 Is Essential for Translocation of the Binary Clostridium botulinum C2 Toxin into the Cytosol

Haug, G., Leemhuis, J., Tiemann, D., Meyer, D., Aktories, K., & Barth, H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303980200 · Cited by 132 · see citing works

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 · see citing works

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 · see citing works

Sgt1p Is a Unique Co-chaperone That Acts as a Client Adaptor to Link Hsp90 to Skp1p

Catlett, M. G., & Kaplan, K. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603847200 · Cited by 126 · see citing works

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 122 · see citing works

Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle

Ratzke, C., Mickler, M., Hellenkamp, B., Büchner, J., & Hugel, T. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000916107 · Cited by 119 · see citing works

Cpr6 and Cpr7, Two Closely Related Hsp90-associated Immunophilins from Saccharomyces cerevisiae, Differ in Their Functional Properties

Mayr, C., Richter, K., Lilie, H., & Büchner, J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005251200 · Cited by 117 · see citing works

Dimerization of Hsp90 Is Required for in Vivo Function

Wayne, N., & Bolon, D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703844200 · Cited by 117 · see citing works

p23, a simple protein with complex activities

Felts, S. J., & Toft, D. O. (2003) · Cell Stress and Chaperones · doi:10.1379/1466-1268(2003)008 · Cited by 116 · see citing works

The chaperones Hsp90 and Cdc37 mediate the maturation and stabilization of protein kinase C through a conserved PXXP motif in the C-terminal tail.

Gould, C. M., Kannan, N., Taylor, S. S., & Newton, A. C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808436200 · Cited by 113 · see citing works

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 · see citing works

Association of the heat shock protein HSP90 with steroid hormone receptors and tyrosine kinase oncogene products

Ziemiecki, A., CATELLI, M. G., Joab, I., & Moncharmont, B. (1986) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(86)80424-7 · Cited by 107 · see citing works

Aryl hydrocarbon (Ah) receptor levels are selectively modulated by hsp90-associated immunophilin homolog XAP2

Meyer, B. K., Petrulis, J. R., & Perdew, G. H. (2000) · Cell Stress and Chaperones · doi:10.1379/1466-1268(2000)005 · Cited by 105 · see citing works

Specific Arabidopsis HSP90.2 alleles recapitulate RAR1 cochaperone function in plant NB-LRR disease resistance protein regulation

Hubert, D. A., He, Y., McNulty, B. C., Tornero, P., & Dangl, J. L. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904877106 · Cited by 99 · see citing works

Hsp90 Phosphorylation Is Linked to Its Chaperoning Function

Zhao, Y.-G., Gilmore, R., Leone, G. W., Coffey, M. C., Weber, B., & Lee, P. W. K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105562200 · Cited by 98 · see citing works

Protein Kinase CK2 in Health and Disease: CK2: The kinase controlling the Hsp90 chaperone machinery

Miyata, Y. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-9152-0 · Cited by 98 · see citing works

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 97 · see citing works

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 97 · see citing works

An unstructured C-terminal region of the hsp90 co-chaperone p23 is important for its chaperone function 1 1Edited by R. Huber

Weikl, T., Abelmann, K., & Buchner, J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3172 · Cited by 97 · see citing works

The Hsp90 Cochaperone p23 Is the Limiting Component of the Multiprotein Hsp90/Hsp70-based Chaperone System in Vivo Where It Acts to Stabilize the Client Protein·Hsp90 Complex

Morishima, Y., Kanelakis, K. C., Murphy, P. J. M., Lowe, E. R., Jenkins, G. J., Osawa, Y., Sunahara, R. K., & Pratt, W. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m309814200 · Cited by 97 · see citing works

Hsp90 Enhances Degradation of Oxidized Calmodulin by the 20 S Proteasome

Whittier, J. E., Xiong, Y., Rechsteiner, M., & Squier, T. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406048200 · Cited by 94 · see citing works

Identification of Amino Acids in the Tetratricopeptide Repeat and C-Terminal Domains of Protein Phosphatase 5 Involved in Autoinhibition and Lipid Activation

Kang, H., Sayner, S., Gross, K. L., Russell, L. C., & Chinkers, M. (2001) · Biochemistry · doi:10.1021/bi010999i · Cited by 94 · see citing works

Molecular Chaperone Hsp90 Is Important for Vaccinia Virus Growth in Cells

Hung, J., Chung, C.-S., & Chang, W. (2002) · Journal of Virology · doi:10.1128/jvi.76.3.1379-1390.2002 · Cited by 94 · see citing works

The Hsp90 Molecular Chaperone Modulates Multiple Telomerase Activities

Toogun, O. A., DeZwaan, D. C., & Freeman, B. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01417-07 · Cited by 93 · see citing works

The Hsp90 Cochaperone p23 Is Essential for Perinatal Survival

Grad, I., McKee, T., Ludwig, S. M., Hoyle, G. W., Ruíz, P., Wurst, W., Floß, T., Miller, C. A., & Picard, D. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00734-06 · Cited by 91 · see citing works

Molecular Interaction Network of the Hsp90 Chaperone System

Zhao, R., & Houry, W. A. (2007) · Springer eBooks · doi:10.1007/978-0-387-39975-1_3 · Cited by 90 · see citing works

Unc45b Forms a Cytosolic Complex with Hsp90 and Targets the Unfolded Myosin Motor Domain

Srikakulam, R., Liu, L., & Winkelmann, D. A. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002137 · Cited by 89 · see citing works

Global Functional Map of the p23 Molecular Chaperone Reveals an Extensive Cellular Network

Echtenkamp, F., Zelin, E., Oxelmark, E., Woo, J. I., Andrews, B., Garabedian, M. J., & Freeman, B. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.05.029 · Cited by 89 · see citing works

Extracellular HSP90: Conquering the cell surface

Sidera, K., & Patsavoudi, E. (2008) · Cell Cycle · doi:10.4161/cc.7.11.6054 · Cited by 88 · see citing works

The Cellular Chaperone Heat Shock Protein 90 Facilitates Flock House Virus RNA Replication in Drosophila Cells

Kampmueller, K. M., & Miller, D. J. (2005) · Journal of Virology · doi:10.1128/jvi.79.11.6827-6837.2005 · Cited by 88 · see citing works

Inhibition of Apoptosome Formation by Suppression of Hsp90β Phosphorylation in Tyrosine Kinase-Induced Leukemias

Kurokawa, M., Zhao, C., Reya, T., & Kornbluth, S. A. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00265-08 · Cited by 85 · 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

Structural Organization of Procaryotic and Eucaryotic Hsp90. INFLUENCE OF DIVALENT CATIONS ON STRUCTURE AND FUNCTION

Jakob, U., Meyer, I., Bügl, H., André, S., Bardwell, J. C. A., & Büchner, J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.24.14412 · Cited by 83 · see citing works

Hsp90 Affecting Chromatin Remodeling Might Explain Transgenerational Epigenetic Inheritance in Drosophila

Ruden, D. M., & Lu, X. (2008) · Current Genomics · doi:10.2174/138920208786241207 · Cited by 80 · see citing works

Influence of trehalose on the molecular chaperone activity of p26, a small heat shock/α-crystallin protein

Viner, R. I., & Clegg, J. S. (2001) · Cell Stress and Chaperones · doi:10.1379/1466-1268(2001)006 · Cited by 80 · see citing works

HtpG, the prokaryotic homologue of Hsp90, stabilizes a phycobilisome protein in the cyanobacterium Synechococcus elongatus PCC 7942

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 78 · see citing works

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 78 · see citing works

The Pih1-Tah1 Cochaperone Complex Inhibits Hsp90 Molecular Chaperone ATPase Activity

Eckert, K., Saliou, J., Monlezun, L., Vigouroux, A., Atmane, N., Caillat, C., Quevillon‐Chéruel, S., Madiona, K., Nicaise, M., Lazereg, S., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.138263 · Cited by 77 · see citing works

Defining the Requirements for Hsp40 and Hsp70 in the Hsp90 Chaperone Pathway*

Cintron, N. S., & Toft, D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605417200 · Cited by 77 · see citing works

Heat-shock Protein 90 Is Essential for Stabilization of the Hepatitis C Virus Nonstructural Protein NS3

Ujino, S., Yamaguchi, S., Shimotohno, K., & Takaku, H. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806452200 · Cited by 76 · see citing works

Expression of the estrogen receptor-associated immunophilins, cyclophilin 40 and FKBP52, in breast cancer

Ward, B. K., Mark, P., Ingram, D., Minchin, R., & Ratajczak, T. (1999) · Breast Cancer Research and Treatment · doi:10.1023/a:1006390804515 · Cited by 74 · see citing works

HSP90: The Rosetta stone for cellular protein dynamics?

DeZwaan, D. C., & Freeman, B. C. (2008) · Cell Cycle · doi:10.4161/cc.7.8.5723 · Cited by 73 · see citing works

CDC37 is required for p60v-src activity in yeast.

Dey, B., Lightbody, J. J., & Boschelli, F. (1996) · Molecular Biology of the Cell · doi:10.1091/mbc.7.9.1405 · Cited by 73 · see citing works

Hsp 70/Hsp 90 organizing protein as a nitrosylation target in cystic fibrosis therapy

Marozkina, N. V., Yemen, S., Borowitz, M., Liu, L., Plapp, M., Sun, F., Islam, R. M., Erdmann-Gilmore, P., Townsend, R. R., Lichti, C. F., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909128107 · Cited by 72 · see citing works

Structural and functional analysis of SGT1–HSP90 core complex required for innate immunity in plants

Kadota, Y., Amigues, B., Ducassou, L., Madaoui, H., Ochsenbein, F., Guérois, R., & Shirasu, K. (2008) · EMBO Reports · doi:10.1038/embor.2008.185 · Cited by 68 · see citing works

Heat shock protein 90 facilitates formation of the HBV capsid via interacting with the HBV core protein dimers

Shim, H. Y., Quan, X., Yi, Y., & Jung, G. (2010) · Virology · doi:10.1016/j.virol.2010.11.005 · Cited by 67 · see citing works

Hsp90 Is Essential for Restoring Cellular Functions of Temperature-sensitive p53 Mutant Protein but Not for Stabilization and Activation of Wild-type p53

Müller, P., Češková, P., & Vojtesek, B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m412767200 · Cited by 67 · see citing works

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

Mollapour, M., Tsutsumi, S., Kim, Y. S., Trepel, J., & Neckers, L. (2011) · Oncotarget · doi:10.18632/oncotarget.272 · Cited by 66 · see citing works

Hsp90 increases LIM kinase activity by promoting its homo‐dimerization

Li, R., Soosairajah, J., Harari, D., Citri, A., Price, J. T., Ng, H. L., Morton, C. J., Parker, M. W., Yarden, Y., & Bernard, O. (2006) · The FASEB Journal · doi:10.1096/fj.05-5258fje · Cited by 65 · see citing works

Role of CypA and Hsp90 in membrane translocation mediated by anthrax protective antigen

Dmochewitz, L., Lillich, M., Kaiser, E., Jennings, L. D., Lang, A. E., Büchner, J., Fischer, G. S., Aktories, K., Collier, R. J., & Barth, H. (2010) · Cellular Microbiology · doi:10.1111/j.1462-5822.2010.01539.x · Cited by 65 · 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 60 · see citing works

FK506-binding protein 52 phosphorylation: a potential mechanism for regulating steroid hormone receptor activity

Cox, M. B., Riggs, D. L., Hessling, M., Schumacher, F., Buchner, J., & Smith, D. F. (2007) · Molecular Endocrinology · doi:10.1210/me.2006-0547 · Cited by 60 · see citing works

P59 (FK506 binding protein 59) interaction with heat shock proteins is highly conserved and may involve proteins other than steroid receptors

Tai, P. K. K., Chang, H., Albers, M. W., Schreiber, S. L., Toft, D. O., & Faber, L. E. (1993) · Biochemistry · doi:10.1021/bi00085a015 · Cited by 58 · see citing works

The Bcl-2 Regulator FKBP38-Calmodulin-Ca2+ Is Inhibited by Hsp90

Edlich, F., Erdmann, F., Jarczowski, F., Moutty, M.-C., Weiwad, M., & Fischer, G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611594200 · Cited by 57 · see citing works

Intracellular localization of the 90 kDA heat shock protein (HSP90α) determined by expression of a EGFP—HSP90α‐fusion protein in unstressed and heat stressed 3T3 cells

Langer, T., Rosmus, S., & Fasold, H. (2003) · Cell Biology International · doi:10.1016/s1065-6995(02)00256-1 · Cited by 54 · see citing works

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

Scroggins, B. T., & Neckers, L. (2007) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2.10.1403 · Cited by 52 · see citing works

Effect of Mutation of the Tetratricopeptide Repeat and Asparatate-Proline 2 Domains of Sti1 on Hsp90 Signaling and Interaction in Saccharomyces cerevisiae

Flom, G. A., Weekes, J., Williams, J. J., & Johnson, J. L. (2005) · Genetics · doi:10.1534/genetics.105.045815 · Cited by 52 · see citing works

The Non-canonical Hop Protein from Caenorhabditis elegans Exerts Essential Functions and Forms Binary Complexes with Either Hsc70 or Hsp90

Gaiser, A. M., Brandt, F., & Richter, K. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.06.051 · Cited by 52 · see citing works

Oncogenic Mutations Reduce the Stability of Src Kinase

Falsone, S. F., Leptihn, S., Osterauer, A., Haslbeck, M., & Büchner, J. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.08.091 · Cited by 51 · see citing works

The Hsp82 molecular chaperone promotes a switch between unextendable and extendable telomere states

DeZwaan, D. C., Toogun, O. A., Echtenkamp, F., & Freeman, B. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1616 · Cited by 48 · see citing works

Hsp90 Inhibitors Disrupt Mitochondrial Homeostasis in Cancer Cells

Neckers, L., Kern, A., & Tsutsumi, S. (2007) · Chemistry & Biology · doi:10.1016/j.chembiol.2007.11.002 · Cited by 47 · see citing works

Cdc37 Interacts with the Glycine-Rich Loop of Hsp90 Client Kinases

Terasawa, K., Yoshimatsu, K., Iemura, S., Natsume, T., Tanaka, K., & Minami, Y. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.9.3378-3389.2006 · Cited by 46 · see citing works

Molecular Chaperone Functions in Protein Folding and Proteostasis

Kim, Y., Hipp, M. S., Bracher, A., Hayer-Hartl, M. K., & Hartl, F. U. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060208-092442 · Cited by 1,468 · see citing works

In vivo aspects of protein folding and quality control

Balchin, D., Hayer-Hartl, M. K., & Hartl, F. U. (2016) · Science · doi:10.1126/science.aac4354 · Cited by 1,432 · see citing works

Chaperone machines for protein folding, unfolding and disaggregation

Saibil, H. R. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3658 · Cited by 1,174 · see citing works

Recent advances in the development of protein–protein interactions modulators: mechanisms and clinical trials

Lu, H., Zhou, Q., He, J., Jiang, Z., Peng, C., Tong, R., & Shi, J. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00315-3 · Cited by 891 · see citing works

The heat‐shock protein/chaperone network and multiple stress resistance

Jacob, P., Heribert Hirt, A., & Bendahmane, A. (2016) · Plant Biotechnology Journal · doi:10.1111/pbi.12659 · Cited by 766 · 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

Protein quality control and elimination of protein waste: The role of the ubiquitin–proteasome system

Amm, I., Sommer, T., & Wolf, D. H. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.06.031 · Cited by 493 · see citing works

Structure, Function and Regulation of the Hsp90 Machinery

Büchner, J., & Li, J. (2013) · Biomedical Journal · doi:10.4103/2319-4170.113230 · Cited by 421 · see citing works

Hsp90 and Hsp70 chaperones: Collaborators in protein remodeling

Genest, O., Wickner, S., & Doyle, S. M. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.rev118.002806 · Cited by 384 · 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

Structure, Function, and Regulation of the Hsp90 MachineryPreprint

Biebl, M. M., & Büchner, J. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a034017 · Cited by 308 · see citing works

RISC assembly: Coordination between small RNAs and Argonaute proteins

Kobayashi, H., & Tomari, Y. (2015) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2015.08.007 · Cited by 306 · see citing works

How Hsp70 Molecular Machines Interact with Their Substrates to Mediate Diverse Physiological Functions

Clérico, E. M., Tilitsky, J. M., Meng, W., & Gierasch, L. M. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.02.004 · Cited by 299 · see citing works

Features of protein–protein interactions that translate into potent inhibitors: topology, surface area and affinity

Smith, M. C. P., & Gestwicki, J. E. (2012) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2012.10 · Cited by 285 · see citing works

Firefly luciferase mutants as sensors of proteome stress

Gupta, R., Kasturi, P., Bracher, A., Loew, C., Zheng, M., Villella, A., Garza, D., Hartl, F. U., & Raychaudhuri, S. (2011) · Nature Methods · doi:10.1038/nmeth.1697 · Cited by 219 · see citing works

C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances

Müller, P., Růčková, E., Halada, P., Coates, P. J., Hrstka, R., Lane, D. P., & Vojtěšek, B. (2012) · Oncogene · doi:10.1038/onc.2012.314 · Cited by 226 · see citing works

Hsp90 interaction with clients

Karagöz, G. E., & Rüdiger, S. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2014.12.002 · Cited by 203 · see citing works

Anatomy of RISC : how do small RNAs and chaperones activate Argonaute proteins?

Nakanishi, K. (2016) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1356 · Cited by 195 · see citing works

HSP90 inhibitors and cancer: Prospects for use in targeted therapies (Review)

Li, Z., & Luo, Y. (2022) · Oncology Reports · doi:10.3892/or.2022.8443 · Cited by 179 · see citing works

Heat shock proteins as potential targets for protective strategies in neurodegeneration

Kampinga, H. H., & Bergink, S. (2016) · The Lancet Neurology · doi:10.1016/s1474-4422(16)00099-5 · Cited by 172 · see citing works

Modulation of the Hsp90 Chaperone Cycle by a Stringent Client Protein

Lorenz, O. R., Freiburger, L., Rutz, D. A., Krause, M., Zierer, B. K., Alvira, S., Cuéllar, J., Valpuesta, J. M., Madl, T., Sattler, M., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.02.003 · Cited by 151 · see citing works

Hsp90 Breaks the Deadlock of the Hsp70 Chaperone System

Luengo, T. M., Kityk, R., Mayer, M. P., & Rüdiger, S. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.03.028 · Cited by 151 · see citing works

Emerging Functions of Human IFIT Proteins in Cancer

Pidugu, V. K., Pidugu, H. B., Wu, M., Liu, C., & Lee, T.-C. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00148 · Cited by 151 · see citing works

Transcriptional response to stress in the dynamic chromatin environment of cycling and mitotic cells

Vihervaara, A., Sergelius, C., Vasara, J., Blom, M. A. H., Elsing, A. N., Roos‐Mattjus, P., & Sistonen, L. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1305275110 · Cited by 149 · see citing works

GIGANTEA is a co-chaperone which facilitates maturation of ZEITLUPE in the Arabidopsis circadian clock

Cha, J., Kim, J., Kim, T.-S., Zeng, Q., Wang, L., Lee, S. Y., Kim, W.-Y., & Somers, D. (2017) · Nature Communications · doi:10.1038/s41467-016-0014-9 · Cited by 126 · see citing works

Anticancer Inhibitors of Hsp90 Function

Garg, G., Khandelwal, A., & Blagg, B. S. J. (2016) · Advances in cancer research · doi:10.1016/bs.acr.2015.12.001 · Cited by 147 · 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

The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation

Bhattacharya, K., Weidenauer, L., Luengo, T. M., Pieters, E. C., Echeverría, P. C., Bernasconi, L., Wider, D., Sadian, Y., Koopman, M. B., Villemin, M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19783-w · Cited by 140 · see citing works

Conformational Switching of the Molecular Chaperone Hsp90 via Regulated Phosphorylation

Soroka, J., Wandinger, S. K., Mäusbacher, N., Schreiber, T., Richter, K., Daub, H., & Buchner, J. (2012) · Molecular Cell · doi:10.1016/j.molcel.2011.12.031 · Cited by 139 · 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 132 · see citing works

Asymmetric Hsp90 N Domain SUMOylation Recruits Aha1 and ATP-Competitive Inhibitors

Mollapour, M., Bourboulia, D., Beebe, K. E., Woodford, M. R., Polier, S., Hoang, A., Chelluri, R. R., Li, Y., Guo, A., Lee, M.-J., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2013.12.007 · Cited by 129 · see citing works

HSF1 deficiency and impaired HSP90‐dependent protein folding are hallmarks of aneuploid human cells

Donnelly, N., Passerini, V., Dürrbaum, M., Stingele, S., & Štorchová, Z. (2014) · The EMBO Journal · doi:10.15252/embj.201488648 · Cited by 126 · see citing works

A script to highlight hydrophobicity and charge on protein surfaces

Hagemans, D., van Belzen, I. A. E. M., Luengo, T. M., & Rüdiger, S. (2015) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2015.00056 · Cited by 128 · see citing works

Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast

Genest, O., Reidy, M., Street, T. O., Hoskins, J. R., Camberg, J. L., Agard, D. A., Masison, D. C., & Wickner, S. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.11.017 · Cited by 118 · see citing works

Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein

Kellner, R., Hofmann, H., Barducci, A., Wunderlich, B., Nettels, D., & Schuler, B. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1407086111 · Cited by 122 · see citing works

Heat shock protein 90 controls HIV-1 reactivation from latency

Anderson, I., Low, J. S., Weston, S. M., Weinberger, M., Zhyvoloup, A., Labokha, A. A., Corazza, G., Kitson, R. R. A., Moody, C. J., Marcello, A., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1320178111 · Cited by 116 · see citing works

The charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function

Jahn, M., Rehn, A., Pelz, B., Hellenkamp, B., Richter, K., Rief, M., Büchner, J., & Hugel, T. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1414073111 · Cited by 110 · see citing works

Selective targeting of the stress chaperome as a therapeutic strategy

Taldone, T., Ochiana, S. O., Patel, P. D., & Chiosis, G. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2014.09.001 · Cited by 111 · see citing works

Natural Product Inspired N‐Terminal Hsp90 Inhibitors: From Bench to Bedside?

Khandelwal, A., Crowley, V. M., & Blagg, B. S. J. (2015) · Medicinal Research Reviews · doi:10.1002/med.21351 · Cited by 109 · see citing works

Heat Shock Protein 70 (HSP70) Induction: Chaperonotherapy for Neuroprotection after Brain Injury

Kim, J. Y., Barua, S., Huang, M., Park, J., Yenari, M. A., & Lee, J. E. (2020) · Cells · doi:10.3390/cells9092020 · Cited by 109 · 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

Protein–Protein Interactions in the Molecular Chaperone Network

Freilich, R., Arhar, T., Abrams, J. L., & Gestwicki, J. E. (2018) · Accounts of Chemical Research · doi:10.1021/acs.accounts.8b00036 · Cited by 107 · see citing works

Small-molecule inhibitor targeting the Hsp90-Cdc37 protein-protein interaction in colorectal cancer

Wang, L., Zhang, L., Li, L., Jiang, J., Zheng, Z., Shang, J., Wang, C., Chen, W., Bao, Q., Xu, X., et al. (2019) · Science Advances · doi:10.1126/sciadv.aax2277 · Cited by 110 · see citing works

The heat shock response and small molecule regulators

Kurop, M. K., Huyen, C. M., Kelly, J. H., & Blagg, B. S. J. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113846 · Cited by 106 · see citing works

Heat Shock Protein (HSP) Drug Discovery and Development: Targeting Heat Shock Proteins in Disease

Shrestha, L., Bolaender, A., Patel, H., & Taldone, T. (2016) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026616666160413141911 · Cited by 105 · see citing works

HSP90 Molecular Chaperones, Metabolic Rewiring, and Epigenetics: Impact on Tumor Progression and Perspective for Anticancer Therapy

Condelli, V., Crispo, F., Pietrafesa, M., Lettini, G., Matassa, D. S., Esposito, F., Landriscina, M., & Maddalena, F. (2019) · Cells · doi:10.3390/cells8060532 · Cited by 105 · see citing works

ATP‐driven molecular chaperone machines

Clare, D. K., & Saibil, H. R. (2013) · Biopolymers · doi:10.1002/bip.22361 · Cited by 100 · see citing works

Heat Shock Protein 90 in Alzheimer’s Disease

Ou, J.-R., Tan, M., Xie, A., Yu, J., & Tan, L. (2014) · BioMed Research International · doi:10.1155/2014/796869 · Cited by 99 · see citing works

CHIP: A Co-chaperone for Degradation by the Proteasome

Edkins, A. L. (2014) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-319-11731-7_11 · Cited by 97 · see citing works

Norovirus antivirals: Where are we now?

Netzler, N. E., Tuipulotu, D. E., & White, P. A. (2018) · Medicinal Research Reviews · doi:10.1002/med.21545 · Cited by 95 · see citing works

Modulation of Amyloid States by Molecular ChaperonesPreprint

Wentink, A. S., Nussbaum-Krammer, C. I., & Bukau, B. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033969 · Cited by 91 · see citing works

Hsp90 inhibitors as senolytic drugs to extend healthy aging

Fuhrmann-Stroissnigg, H., Niedernhofer, L. J., & Robbins, P. D. (2018) · Cell Cycle · doi:10.1080/15384101.2018.1475828 · Cited by 92 · see citing works

Cytosolic Hsp90 Isoform-Specific Functions and Clinical Significance

Maiti, S., & Picard, D. (2022) · Biomolecules · doi:10.3390/biom12091166 · Cited by 92 · see citing works

Hsp90: Friends, clients and natural foes

Verma, S., Goyal, S., Jamal, S., Singh, A. P., & Grover, A. (2016) · Biochimie · doi:10.1016/j.biochi.2016.05.018 · Cited by 90 · see citing works

Computational Modeling of Allosteric Regulation in the Hsp90 Chaperones: A Statistical Ensemble Analysis of Protein Structure Networks and Allosteric Communications

Blacklock, K. M., & Verkhivker, G. M. (2014) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003679 · Cited by 90 · see citing works

Coordinated Conformational Processing of the Tumor Suppressor Protein p53 by the Hsp70 and Hsp90 Chaperone Machineries

Dahiya, V., Agam, G. N., Lawatscheck, J., Rutz, D. A., Lamb, D. C., & Büchner, J. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.03.026 · Cited by 92 · see citing works

Targeting heat-shock-protein 90 (Hsp90) by natural products: geldanamycin, a show case in cancer therapy

Franke, J., Eichner, S., Zeilinger, C., & Kirschning, A. (2013) · Natural Product Reports · doi:10.1039/c3np70012g · Cited by 88 · see citing works

Heat shock proteins as hallmarks of cancer: insights from molecular mechanisms to therapeutic strategies

Zuo, W., Pang, Q., Zhu, X., Yang, Q., Zhao, Q., He, G., Han, B., & Huang, W. (2024) · Journal of Hematology & Oncology · doi:10.1186/s13045-024-01601-1 · Cited by 88 · see citing works

The mitochondrial HSP90 paralog TRAP1 forms an OXPHOS-regulated tetramer and is involved in mitochondrial metabolic homeostasis

Joshi, A., Dai, L., Liu, Y. X., Lee, J., Ghahhari, N. M., Segala, G., Beebe, K. E., Jenkins, L. M. M., Lyons, G. C., Bernasconi, L., et al. (2020) · BMC Biology · doi:10.1186/s12915-020-0740-7 · Cited by 85 · see citing works

Prolyl Isomerization and Its Catalysis in Protein Folding and Protein Function

Schmidpeter, P. A. M., & Schmid, F. X. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.01.023 · Cited by 85 · see citing works

In Vivo Conformational Dynamics of Hsp90 and Its Interactors

Chavez, J. D., Schweppe, D. K., Eng, J. K., & Bruce, J. E. (2016) · Cell chemical biology · doi:10.1016/j.chembiol.2016.05.012 · Cited by 80 · see citing works

Genetics of glucocorticoid regulation and posttraumatic stress disorder -what do we know?

Castro-Vale, I., van Rossum, E. F. C., Machado, J. C., Mota-Cardoso, R., & Carvalho, D. (2016) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.02.005 · Cited by 85 · see citing works

Paralog Specific Hsp90 Inhibitors - A Brief History and a Bright Future

Gewirth, D. T. (2016) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026616666160413141154 · Cited by 80 · see citing works

Imbalances in the Hsp90 Chaperone Machinery: Implications for Tauopathies

Shelton, L. B., Koren, J., & Blair, L. J. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00724 · Cited by 78 · see citing works

Hsp90 protein interacts with phosphorothioate oligonucleotides containing hydrophobic 2′-modifications and enhances antisense activity

Liang, X., Shen, W., Sun, H., Kinberger, G. A., Prakash, T. P., Nichols, J. G., & Crooke, S. T. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw144 · Cited by 79 · see citing works

MicroRNA-126 regulates Hypoxia-Inducible Factor-1α which inhibited migration, proliferation, and angiogenesis in replicative endothelial senescence

Alique, M., Bodega, G., Giannarelli, C., Carracedo, J., & Ramı́rez, R. (2019) · Scientific Reports · doi:10.1038/s41598-019-43689-3 · Cited by 78 · see citing works

Physical Interaction between Bacterial Heat Shock Protein (Hsp) 90 and Hsp70 Chaperones Mediates Their Cooperative Action to Refold Denatured Proteins

Nakamoto, H., Fujita, K., Ohtaki, A., Watanabe, S., Narumi, S., Maruyama, T., Suenaga, E., Misono, T. S., Kumar, P. K. R., Goloubinoff, P., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.524801 · Cited by 78 · see citing works

Functional principles and regulation of molecular chaperones

Dahiya, V., & Büchner, J. (2018) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2018.10.001 · Cited by 75 · see citing works

Co-chaperones TIMP2 and AHA1 Competitively Regulate Extracellular HSP90:Client MMP2 Activity and Matrix Proteolysis

Baker-Williams, A. J., Hashmi, F., Budzyński, M. A., Woodford, M. R., Gleicher, S., Himanen, S. V., Makedon, A. M., Friedman, D., Cortes, S., Namek, S., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.07.045 · Cited by 75 · see citing works

LncRna CPS1-IT1 Suppresses Cell Proliferation, Invasion and Metastasis in Colorectal Cancer

Zhang, W., Yuan, W., Song, J., Wang, S., & Gu, X. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000485091 · Cited by 73 · see citing works

Chemical Tools to Investigate Mechanisms Associated with HSP90 and HSP70 in Disease

Shrestha, L., Patel, H. J., & Chiosis, G. (2016) · Cell chemical biology · doi:10.1016/j.chembiol.2015.12.006 · Cited by 71 · see citing works

Regulatory mechanisms for amylolytic gene expression in the koji moldAspergillus oryzae

Gomi, K. (2019) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2019.1625265 · Cited by 72 · see citing works

Heat Shock Proteins and Inflammasomes

Martine, P., & Rébé, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20184508 · Cited by 72 · see citing works

The Hsp70–Hsp90 go-between Hop/Stip1/Sti1 is a proteostatic switch and may be a drug target in cancer and neurodegeneration

Bhattacharya, K., & Picard, D. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03962-z · Cited by 73 · see citing works

Cyclin-dependent kinase 7 (CDK7)-mediated phosphorylation of the CDK9 activation loop promotes P-TEFb assembly with Tat and proviral HIV reactivation

Mbonye, U. R., Wang, B., Gokulrangan, G., Shi, W., Yang, S., & Karn, J. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.001347 · Cited by 71 · see citing works

Inhibiting protein-protein interactions of Hsp90 as a novel approach for targeting cancer

Gupta, S. D., Bommaka, M. K., & Banerjee, A. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.05.073 · Cited by 71 · see citing works

Hsp90 Inhibitors Exhibit Resistance-Free Antiviral Activity against Respiratory Syncytial Virus

Geller, R., Andino, R., & Frydman, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056762 · Cited by 71 · see citing works

HSP 90 and co‐chaperones: a multitaskers’ view on plant hormone biology

Donato, M. D., & Geisler, M. M. (2019) · FEBS Letters · doi:10.1002/1873-3468.13499 · Cited by 66 · see citing works

Molecular mechanism and targeted therapy of Hsp90 involved in lung cancer: New discoveries and developments (Review)

Biaoxue, R., & Yang, S. (2017) · International Journal of Oncology · doi:10.3892/ijo.2017.4214 · Cited by 67 · see citing works

Hsp70/Hsp90 Organising Protein (Hop): Beyond Interactions with Chaperones and Prion Proteins

Baindur‐Hudson, S., Edkins, A. L., & Blatch, G. L. (2014) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-319-11731-7_3 · Cited by 67 · see citing works

Long noncoding RNA CPS1-IT1 suppresses the metastasis of hepatocellular carcinoma by regulating HIF-1α activity and inhibiting epithelial-mesenchymal transition

Wang, T., Yu, C., Lin, Y.-S., Chen, T., Yeh, C., Liang, K., Shieh, T., Chen, C., & Hsueh, C. (2016) · Oncotarget · doi:10.18632/oncotarget.9635 · Cited by 65 · see citing works

Heat shock proteins as a key defense mechanism in poultry production under heat stress conditions

Gouda, A., Tolba, S. A., Mahrose, K., Felemban, S. G., Khafaga, A. F., Khalifa, N. E., Jaremko, M., Moustafa, M., Alshaharni, M. O., Algopish, U., et al. (2024) · Poultry Science · doi:10.1016/j.psj.2024.103537 · Cited by 66 · see citing works

Chaperone Action at the Single-Molecule Level

Mashaghi, A., Krämer, G., Lamb, D. C., Mayer, M. P., & Tans, S. J. (2013) · Chemical Reviews · doi:10.1021/cr400326k · Cited by 65 · see citing works

The Hsp70 chaperone is a major player in stress-induced transposable element activation

Cappucci, U., Noro, F., Casale, A. M., Fanti, L., Berloco, M. F., Alagia, A. A., Grassi, L., Pera, L. L., Piacentini, L., & Pimpinelli, S. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1903936116 · Cited by 65 · see citing works

S100A6: molecular function and biomarker role

Wang, Y., Kang, X., Kang, X., & Yang, F. (2023) · Biomarker Research · doi:10.1186/s40364-023-00515-3 · Cited by 63 · see citing works

A global view of Hsp90 functions

Chiosis, G., Dickey, C. A., & Johnson, J. L. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2481 · Cited by 63 · see citing works

Learning from Nature: Advances in Geldanamycin- and Radicicol-Based Inhibitors of Hsp90

Kitson, R. R. A., & Moody, C. J. (2013) · The Journal of Organic Chemistry · doi:10.1021/jo4002849 · Cited by 64 · see citing works

Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle

Biebl, M. M., Lopez, A., Rehn, A., Freiburger, L., Lawatscheck, J., Blank, B., Sattler, M., & Buchner, J. (2021) · Nature Communications · doi:10.1038/s41467-021-21063-0 · Cited by 58 · see citing works

Molecular Chaperones of Leishmania : Central Players in Many Stress-Related and -Unrelated Physiological Processes

Requena, J. M., Montalvo, A. M., & Fraga, J. (2015) · BioMed Research International · doi:10.1155/2015/301326 · Cited by 63 · see citing works

Contributions of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity

Walton-Diaz, A., Khan, S., Bourboulia, D., Trepel, J., Neckers, L., & Mollapour, M. (2013) · Future Medicinal Chemistry · doi:10.4155/fmc.13.88 · Cited by 58 · see citing works

Keep your heart in shape: molecular chaperone networks for treating heart disease

Tarone, G., & Brancaccio, M. (2014) · Cardiovascular Research · doi:10.1093/cvr/cvu049 · Cited by 61 · see citing works

Features of the Chaperone Cellular Network Revealed through Systematic Interaction Mapping

Rizzolo, K., Huen, J., Kumar, A., Phanse, S., Vlasblom, J., Kakihara, Y., Zeineddine, H. A., Minić, Z., Snider, J. D., Wang, W., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.08.074 · Cited by 61 · see citing works

Hsp90 Is Essential under Heat Stress in the Bacterium Shewanella oneidensis

Honoré, F. A., Méjean, V., & Genest, O. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.03.082 · Cited by 59 · see citing works

Multifaceted roles of HEAT SHOCK PROTEIN 90 molecular chaperones in plant development

Tichá, T., Samakovli, D., Kuchařová, A., Vavrdová, T., & Šamaj, J. (2020) · Journal of Experimental Botany · doi:10.1093/jxb/eraa177 · Cited by 59 · see citing works

Prolyl Hydroxylase Domain Protein 2 (PHD2) Binds a Pro-Xaa-Leu-Glu Motif, Linking It to the Heat Shock Protein 90 Pathway

Song, D., Li, L.-S., Heaton-Johnson, K. J., Arsenault, P. R., Master, S. R., & Lee, F. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.440552 · Cited by 58 · see citing works

Hsp90@chromatin.nucleus: an emerging hub of a networker

Sawarkar, R., & Paro, R. (2013) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.11.007 · Cited by 55 · see citing works

Client Proteins and Small Molecule Inhibitors Display Distinct Binding Preferences for Constitutive and Stress-Induced HSP90 Isoforms and Their Conformationally Restricted Mutants

Prince, T. L., Kijima, T., Tatokoro, M., Lee, S., Tsutsumi, S., Yim, K. H., Rivas, C., Alarcon, S. V., Schwartz, H., Khamit-Kush, K. K., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0141786 · Cited by 56 · see citing works

High-Resolution Structural Analysis Shows How Tah1 Tethers Hsp90 to the R2TP Complex

Back, R., Dominguez, C., Rothé, B., Bobo, C., Beaufils, C., Moréra, S., Meyer, P., Charpentier, B., Branlant, C., Allain, F. H. ‐., et al. (2013) · Structure · doi:10.1016/j.str.2013.07.024 · Cited by 56 · see citing works

Heat shock protein 90 acts in brassinosteroid signaling through interaction with BES1/BZR1 transcription factor

Shigeta, T., Zaizen, Y., Sugimoto, Y., Nakamura, Y. K., Matsuo, T., & Okamoto, S. (2015) · Journal of Plant Physiology · doi:10.1016/j.jplph.2015.02.003 · Cited by 54 · see citing works

DCZ3112, a novel Hsp90 inhibitor, exerts potent antitumor activity against HER2-positive breast cancer through disruption of Hsp90-Cdc37 interaction

Chen, X., Liu, P., Wang, Q., Li, Y., Li, F., Fu, H., Zhu, J., Chen, Z., Zhu, W., Xie, C., et al. (2018) · Cancer Letters · doi:10.1016/j.canlet.2018.07.012 · Cited by 55 · 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

The ‘active life’ of Hsp90 complexes

Prodromou, C. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.07.020 · Cited by 171 · see citing works

“Tuning” the ATPase Activity of Hsp90

Prodromou, C., & Morgan, R. M. (2016) · Springer eBooks · doi:10.1007/978-3-319-24780-9_23 · Cited by 9 · see citing works

Aha-type co-chaperones: the alpha or the omega of the Hsp90 ATPase cycle?

LaPointe, P., Mercier, R., & Wolmarans, A. (2019) · Biological Chemistry · doi:10.1515/hsz-2019-0341 · Cited by 11 · see citing works

The chaperone Hsp90: changing partners for demanding clients

Röhl, A., Rohrberg, J., & Büchner, J. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.02.003 · Cited by 268 · see citing works