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

Hepatitis B Virus Infection

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HSP90 and the chaperoning of cancer

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Nod1 Detects a Unique Muropeptide from Gram-Negative Bacterial Peptidoglycan

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Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.

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A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors

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Identification and Structural Characterization of the ATP/ADP-Binding Site in the Hsp90 Molecular Chaperone

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Structure of TPR Domain–Peptide Complexes

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

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Structure and mechanism of the Hsp90 molecular chaperone machinery

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Pathways of chaperone-mediated protein folding in the cytosol

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

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The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins

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NOD-LRR PROTEINS: Role in Host-Microbial Interactions and Inflammatory Disease

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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

Identification of CHIP, a Novel Tetratricopeptide Repeat-Containing Protein That Interacts with Heat Shock Proteins and Negatively Regulates Chaperone Functions

Ballinger, C. A., Connell, P. M., Wu, Y., Hu, Z., Thompson, L. J., Yin, L.-Y., & Patterson, C. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.6.4535 · Cited by 943 · see citing works

The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation

Meacham, G. C., Patterson, C., Zhang, W., Younger, J. M., & Cyr, D. (2000) · Nature Cell Biology · doi:10.1038/35050509 · Cited by 839 · 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

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

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ER chaperones in mammalian development and human diseases

Ni, M., & Lee, A. S. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.04.045 · Cited by 736 · see citing works

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

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Mechanisms of Disease: oncogene addiction—a rationale for molecular targeting in cancer therapy

Weinstein, I. B., & Joe, A. K. (2006) · Nature Clinical Practice Oncology · doi:10.1038/ncponc0558 · Cited by 708 · 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

Gene expression signature-based chemical genomic prediction identifies a novel class of HSP90 pathway modulators

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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 597 · see citing works

PINK1 Protects against Oxidative Stress by Phosphorylating Mitochondrial Chaperone TRAP1

Pridgeon, J. W., Olzmann, J. A., Chin, L.-S., & Li, L. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050172 · Cited by 596 · see citing works

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

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CHIP Is a U-box-dependent E3 Ubiquitin Ligase

Jiang, J., Ballinger, C. A., Wu, Y., Dai, Q., Cyr, D., Höhfeld, J., & Patterson, C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101968200 · Cited by 592 · 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

Hsp90: Chaperoning signal transduction

Richter, K., & Büchner, J. (2001) · Journal of Cellular Physiology · doi:10.1002/jcp.1131 · Cited by 570 · 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

Drugging the Cancer Chaperone HSP90

Workman, P., Burrows, F. J., Neckers, L., & Rosen, N. X. (2007) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1391.012 · Cited by 525 · 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

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

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

Phase I Pharmacokinetic and Pharmacodynamic Study of 17-Allylamino, 17-Demethoxygeldanamycin in Patients With Advanced Malignancies

Banerji, U., O’Donnell, A. E., Scurr, M. R., Pacey, S., Stapleton, S., Asad, Y. J., Simmons, L., Maloney, A., Raynaud, F. I., Campbell, M. J., et al. (2005) · Journal of Clinical Oncology · doi:10.1200/jco.2005.00.612 · Cited by 490 · see citing works

The Heat Shock Protein 90 Antagonist Novobiocin Interacts with a Previously Unrecognized ATP-binding Domain in the Carboxyl Terminus of the Chaperone*

Marcu, M., Chadli, A., Bouhouche, I., Catelli, M., & Neckers, L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003701200 · Cited by 481 · 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

Polyubiquitination and Proteasomal Degradation of the p185c-B-2 Receptor Protein-tyrosine Kinase Induced by Geldanamycin

Mimnaugh, E. G., Chavany, C., & Neckers, L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.37.22796 · Cited by 466 · see citing works

Disruption of the Raf-1-Hsp90 Molecular Complex Results in Destabilization of Raf-1 and Loss of Raf-1-Ras Association

Schulte, T. W., Blagosklonny, M. V., Ingui, C., & Neckers, L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.41.24585 · Cited by 457 · 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

4,5-Diarylisoxazole Hsp90 Chaperone Inhibitors: Potential Therapeutic Agents for the Treatment of Cancer

Brough, P. A., Aherne, W., Barril, X., Borgognoni, J., Boxall, K. J., Cansfield, J. E., Cheung, K.-M. J., Collins, I., Davies, N. G. M., Drysdale, M. J., et al. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm701018h · Cited by 449 · see citing works

Regulation of Tumor Cell Mitochondrial Homeostasis by an Organelle-Specific Hsp90 Chaperone Network

Kang, B. H., Plescia, J., Dohi, T., Rosa, J., Doxsey, S., & Altieri, D. C. (2007) · Cell · doi:10.1016/j.cell.2007.08.028 · Cited by 445 · 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

Chaperoned Ubiquitylation—Crystal Structures of the CHIP U Box E3 Ubiquitin Ligase and a CHIP-Ubc13-Uev1a Complex

Zhang, M., Windheim, M., Roe, S. M., Peggie, M. W., Cohen, P., Prodromou, C., & Pearl, L. H. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.09.023 · Cited by 420 · 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

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

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SGT1 Encodes an Essential Component of the Yeast Kinetochore Assembly Pathway and a Novel Subunit of the SCF Ubiquitin Ligase Complex

Kitagawa, K., Skowyra, D., Elledge, S. J., Harper, J. W., & Hieter, P. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80184-7 · Cited by 387 · see citing works

The HSP90 family of genes in the human genome: Insights into their divergence and evolution

Chen, B., Piel, W. H., Gui, L., Bruford, E. A., & Monteiro, A. (2005) · Genomics · doi:10.1016/j.ygeno.2005.08.012 · Cited by 383 · see citing works

Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling

Demand, J., Alberti, S., Patterson, C., & Höhfeld, J. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00487-0 · Cited by 377 · 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

High HSP90 Expression Is Associated with Decreased Survival in Breast Cancer

Pick, E., Kluger, Y., Giltnane, J. M., Moeder, C. B., Camp, R. L., Rimm, D. L., & Kluger, H. M. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-4511 · Cited by 357 · 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

DT-Diaphorase Expression and Tumor Cell Sensitivity to 17-Allylamino,17-demethoxygeldanamycin, an Inhibitor of Heat Shock Protein 90

Kèlland, L. R., Sharp, S. Y., Rogers, P., Myers, T. G., & Workman, P. (1999) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/91.22.1940 · Cited by 350 · see citing works

Rational design of shepherdin, a novel anticancer agent

Plescia, J., Salz, W., Xia, F., Pennati, M., Zaffaroni, N., Daidone, M. G., Meli, M., Dohi, T., Fortugno, P., Nefedova, Y., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.03.035 · Cited by 342 · see citing works

Combination of Trastuzumab and Tanespimycin (17-AAG, KOS-953) Is Safe and Active in Trastuzumab-Refractory HER-2–Overexpressing Breast Cancer: A Phase I Dose-Escalation Study

Modi, S., Stopeck, A., Gordon, M. S., Mendelson, D. S., Solit, D. B., Bagatell, R., Ma, W., Wheler, J. J., Rosen, N. X., Norton, L., et al. (2007) · Journal of Clinical Oncology · doi:10.1200/jco.2007.11.7960 · Cited by 335 · see citing works

Hepadnavirus assembly and reverse transcription require a multi‐component chaperone complex which is incorporated into nucleocapsids

Hu, J.-M., Toft, D., & Seeger, C. (1997) · EMBO Journal · doi:10.1093/emboj/16.1.59 · Cited by 328 · see citing works

Inhibitors of the heat shock response: Biology and pharmacology

Powers, M. V., & Workman, P. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.05.040 · Cited by 320 · see citing works

Inhibitors of the HSP90 Molecular Chaperone: Current Status

Sharp, S. Y., & Workman, P. (2006) · Advances in cancer research · doi:10.1016/s0065-230x(06)95009-x · Cited by 311 · see citing works

V600E B-Raf requires the Hsp90 chaperone for stability and is degraded in response to Hsp90 inhibitors

Grbovic, O. M., Basso, A. D., Sawai, A., Ye, Q., Friedlander, P. A., Solit, D. B., & Rosen, N. X. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609973103 · Cited by 308 · 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

A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells

Chiosis, G., Timaul, M. N., Lucas, B. S., Münster, P. N., Zheng, F. F., Sepp‐Lorenzino, L., & Rosen, N. X. (2001) · Chemistry & Biology · doi:10.1016/s1074-5521(01)00015-1 · Cited by 289 · see citing works

Inhibition of signal transduction by the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin results in cytostasis and apoptosis.

Hostein, I., Robertson, D. M., Di-Stefano, F., Workman, P., & Clarke, P. A. (2001) · PubMed · Cited by 284 · see citing works

RAR1 Positively Controls Steady State Levels of Barley MLA Resistance Proteins and Enables Sufficient MLA6 Accumulation for Effective Resistance

Bieri, S., Mauch, S., Shen, Q., et al. (2004) · The Plant Cell · doi:10.1105/tpc.104.026682 · Cited by 284 · see citing works

Structures of GRP94-Nucleotide Complexes Reveal Mechanistic Differences between the hsp90 Chaperones

Dollins, D. E., Warren, J. J., Immormino, R. M., & Gewirth, D. T. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.08.024 · Cited by 282 · see citing works

Targeting of the protein chaperone, HSP90, by the transformation suppressing agent, radicicol

Sharma, S. V., Agatsuma, T., & Nakano, H. (1998) · Oncogene · doi:10.1038/sj.onc.1201790 · Cited by 279 · 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

Structure-Activity Relationships in Purine-Based Inhibitor Binding to HSP90 Isoforms

Wright, L. M., Barril, X., Dymock, B. W., Sheridan, L., Surgenor, A. E., Beswick, M., Drysdale, M., Collier, A. J., Massey, A., Davies, N., et al. (2004) · Chemistry & Biology · doi:10.1016/j.chembiol.2004.03.033 · Cited by 268 · 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

Role of molecular chaperones in steroid receptor action.

Pratt, W., Galigniana, M., Morishima, Y., & Murphy, P. J. M. (2004) · Essays in Biochemistry · doi:10.1042/bse0400041 · Cited by 259 · see citing works

p185erbB2 Binds to GRP94 in Vivo

Chavany, C., Mimnaugh, E. G., Miller, P. E., Bitton, R. J., Nguyen, P., Trepel, J. B., Whitesell, L. J., Schnur, R. C., Moyer, J. D., & Neckers, L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.9.4974 · Cited by 257 · 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

Activated B-RAF Is an Hsp90 Client Protein That Is Targeted by the Anticancer Drug 17-Allylamino-17-Demethoxygeldanamycin

Dias, S. D. R., Friedlos, F., Light, Y., Springer, C. J., Workman, P., & Marais, R. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-2632 · Cited by 246 · see citing works

Stable Association of hsp90 and p23, but Not hsp70, with Active Human Telomerase

Forsythe, H. L., Jarvis, J. L., Turner, J. W., Elmore, L. W., & Holt, S. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100055200 · Cited by 245 · see citing works

Combinatorial attack on multistep oncogenesis by inhibiting the Hsp90 molecular chaperone

Workman, P. (2003) · Cancer Letters · doi:10.1016/j.canlet.2003.08.032 · Cited by 245 · 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

Hsp90 and Cdc37 – a chaperone cancer conspiracy

Pearl, L. H. (2004) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2004.12.011 · Cited by 241 · 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

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

Development of 17-allylamino-17-demethoxygeldanamycin hydroquinone hydrochloride (IPI-504), an anti-cancer agent directed against Hsp90

Sydor, J. R., Normant, E., Pien, C. S., Porter, J. R., Ge, J., Grenier, L., Pak, R. H., Ali, J. A., Dembski, M. S., Hudak, J., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608372103 · Cited by 231 · see citing works

Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co‐chaperone p23

Young, J. C., & Hartl, F. U. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5930 · Cited by 230 · see citing works

Novel, Potent Small-Molecule Inhibitors of the Molecular Chaperone Hsp90 Discovered through Structure-Based Design

Dymock, B. W., Barril, X., Brough, P. A., Cansfield, J. E., Massey, A. J., McDonald, E., Hubbard, R. E., Surgenor, A. E., Roughley, S. D., Webb, P., et al. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm050355z · Cited by 227 · see citing works

Involvement of Hsp90 in Assembly and Nuclear Import of Influenza Virus RNA Polymerase Subunits

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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

The identification, synthesis, protein crystal structure and in vitro biochemical evaluation of a new 3,4-diarylpyrazole class of Hsp90 inhibitors

Cheung, K.-M. J., Matthews, T. P., James, K. E., Rowlands, M., Boxall, K. J., Sharp, S. Y., Maloney, A., Roe, S. M., Prodromou, C., Pearl, L. H., et al. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.05.046 · Cited by 219 · see citing works

Arabidopsis RAR1 Exerts Rate-Limiting Control of R Gene–Mediated Defenses against Multiple Pathogens

Muskett, P. R., Kahn, K., Austin, M. J., et al. (2002) · The Plant Cell · doi:10.1105/tpc.001040 · Cited by 215 · see citing works

Arabidopsis SGT1b Is Required for SCFTIR1-Mediated Auxin Response

Gray, W. M., Muskett, P. R., Chuang, H.-W., & Parker, J. E. (2003) · The Plant Cell · doi:10.1105/tpc.010884 · Cited by 214 · 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

Phase I Trial of 17-Allylamino-17-Demethoxygeldanamycin in Patients with Advanced Cancer

Solit, D. B., Ivy, S. P., Kopil, C., Sikorski, R. P., Morris, M. J., Slovin, S. F., Kelly, W. K., Delacruz, A., Curley, T., Heller, G., et al. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-1863 · Cited by 212 · 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

Structural and Functional Analysis of SGT1 Reveals That Its Interaction with HSP90 Is Required for the Accumulation of Rx, an R Protein Involved in Plant Immunity

Botër, M., Amigues, B., Peart, J. R., Breuer, C., Kadota, Y., Casais, C., Moore, G. R., Kleanthous, C., Ochsenbein, F., Shirasu, K., et al. (2007) · The Plant Cell · doi:10.1105/tpc.107.050427 · Cited by 204 · see citing works

The Stress Response: Implications for the Clinical Development of Hsp90 Inhibitors

Whitesell, L. J., Bagatell, R., & Falsey, R. R. (2003) · Current Cancer Drug Targets · doi:10.2174/1568009033481787 · Cited by 203 · see citing works

Hsp70 Molecular Chaperones: Emerging Roles in Human Disease and Identification of Small Molecule Modulators

Brodsky, J. L., & Chiosis, G. (2006) · Current Topics in Medicinal Chemistry · doi:10.2174/156802606777811997 · Cited by 202 · see citing works

ErbB2 Degradation Mediated by the Co-chaperone Protein CHIP

Zhou, P., Fernandes, N. D., Dodge, I. L., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209640200 · Cited by 201 · see citing works

Structure, function, and mechanism of the Hsp90 molecular chaperone

Pearl, L. H., & Prodromou, C. (2001) · Advances in protein chemistry · doi:10.1016/s0065-3233(01)59005-1 · Cited by 199 · 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

Gene expression profiling of human colon cancer cells following inhibition of signal transduction by 17-allylamino-17-demethoxygeldanamycin, an inhibitor of the hsp90 molecular chaperone

Clarke, P. A., Hostein, I., Banerji, U., Stefano, F. D., Maloney, A., Walton, M., Judson, I. R., & Workman, P. (2000) · Oncogene · doi:10.1038/sj.onc.1203753 · Cited by 194 · see citing works

Requirement of Heat Shock Protein 90 for Human Hepatitis B Virus Reverse Transcriptase Function

Hu, J., Flores, D., Toft, D. O., Wang, X., & Nguyen, D. H. A. (2004) · Journal of Virology · doi:10.1128/jvi.78.23.13122-13131.2004 · Cited by 181 · see citing works

Identification of Potent Water Soluble Purine-Scaffold Inhibitors of the Heat Shock Protein 90

He, H., Zatorska, D., Kim, J., Aguirre, J., Llauger, L., She, Y., Wu, N. F., Immormino, R. M., Gewirth, D. T., & Chiosis, G. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm0508078 · Cited by 178 · 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

Hsp90: A Novel Target for Cancer Therapy

Solit, D. B., & Rosen, N. X. (2006) · Current Topics in Medicinal Chemistry · doi:10.2174/156802606777812068 · Cited by 171 · 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

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

Comparison of 17-dimethylaminoethylamino-17-demethoxy-geldanamycin (17DMAG) and 17-allylamino-17-demethoxygeldanamycin (17AAG) in vitro: effects on Hsp90 and client proteins in melanoma models

Smith, V., Sausville, E. A., Camalier, R. F., et al. (2005) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-004-0947-2 · Cited by 156 · see citing works

F-box proteins: the key to protein degradation

Ho, M. S.-C., Tsai, P.-I., & Chien, C. (2006) · Journal of Biomedical Science · doi:10.1007/s11373-005-9058-2 · Cited by 155 · see citing works

GRP94 Is Essential for Mesoderm Induction and Muscle Development Because It Regulates Insulin-like Growth Factor Secretion

Wanderling, S. S., Simen, B. B., Ostrovsky, O., Ahmed, N. T., Vogen, S. M., Gidalevitz, T., & Argon, Y. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-03-0275 · Cited by 154 · 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

Surface charge and hydrophobicity determine ErbB2 binding to the Hsp90 chaperone complex

Xu, W., Yuan, X., Xiang, Z., Mimnaugh, E. G., Marcu, M. G., & Neckers, L. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb885 · Cited by 152 · see citing works

CK2 Controls Multiple Protein Kinases by Phosphorylating a Kinase-Targeting Molecular Chaperone, Cdc37

Miyata, Y., & Nishida, E. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.9.4065-4074.2004 · Cited by 149 · see citing works

New Efficient Synthesis of Resorcinylic Macrolides via Ynolides: Establishment of Cycloproparadicicol as Synthetically Feasible Preclinical Anticancer Agent Based on Hsp90 as the Target

Yang, Z.-Q., Geng, X., Solit, D. B., et al. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0484348 · Cited by 148 · see citing works

SGT1 is essential for Nod1 activation

Correia, J. D. S., Miranda, Y., Leonard, N., & Ulevitch, R. J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610926104 · Cited by 145 · see citing works

p23 and HSP20/α‐crystallin proteins define a conserved sequence domain present in other eukaryotic protein families

Ranea, J. A. G., Mirey, G., Camonis, J., & Valencia, A. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03321-5 · Cited by 144 · see citing works

Inhibition of the heat shock protein 90 molecular chaperone in vitro and in vivo by novel, synthetic, potent resorcinylic pyrazole/isoxazole amide analogues

Sharp, S. Y., Prodromou, C., Boxall, K. J., et al. (2007) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-07-0149 · Cited by 144 · see citing works

Herpes Simplex Virus Type 1 DNA Polymerase Requires the Mammalian Chaperone Hsp90 for Proper Localization to the Nucleus

Burch, A. D., & Weller, S. K. (2005) · Journal of Virology · doi:10.1128/jvi.79.16.10740-10749.2005 · Cited by 142 · see citing works

Gene and Protein Expression Profiling of Human Ovarian Cancer Cells Treated with the Heat Shock Protein 90 Inhibitor 17-Allylamino-17-Demethoxygeldanamycin

Maloney, A., Clarke, P. A., Naaby‐Hansen, S., Stein, R. C., Koopman, J.-O., Akpan, A., Yang, A., Zvelebil, M., Cramer, R., Stimson, L., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-2968 · Cited by 138 · 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

Antiviral activity and RNA polymerase degradation following Hsp90 inhibition in a range of negative strand viruses

Connor, J. H., McKenzie, M. O., Parks, G. D., & Lyles, D. S. (2007) · Virology · doi:10.1016/j.virol.2006.12.026 · Cited by 135 · see citing works

U‐box protein carboxyl terminus of Hsc70‐interacting protein (CHIP) mediates poly‐ubiquitylation preferentially on four‐repeat Tau and is involved in neurodegeneration of tauopathy

Hatakeyama, S., Matsumoto, M., Kamura, T., Murayama, M., Chui, D.-H., Planel, E., Takahashi, R., Nakayama, K. I., & Takashima, A. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02713.x · 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

CHIP Mediates Degradation of Smad Proteins and Potentially Regulates Smad-Induced Transcription

Li, L., Xin, H., Xu, X., Huang, M., Zhang, X., Chen, Y., Zhang, S., Fu, X.-Y., & Chang, Z. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.24.2.856-864.2004 · Cited by 118 · see citing works

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

Huth, J. R., Park, C., Petros, A. M., Kunzer, A. R., Wendt, M. D., Wang, X., Lynch, C. L., Mack, J. C., Swift, K. M., Judge, R. A., et al. (2007) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2007.00535.x · Cited by 116 · see citing works

7‘-Substituted Benzothiazolothio- and Pyridinothiazolothio-Purines as Potent Heat Shock Protein 90 Inhibitors

Zhang, L., Fan, J., VU, K. N., et al. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm051146h · Cited by 115 · see citing works

In vitro Biological Characterization of a Novel, Synthetic Diaryl Pyrazole Resorcinol Class of Heat Shock Protein 90 Inhibitors

Sharp, S. Y., Boxall, K. J., Rowlands, M., Prodromou, C., Roe, S. M., Maloney, A., Powers, M. V., Clarke, P. A., Box, G., Sanderson, S., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-3473 · Cited by 112 · see citing works

Sgt1p Contributes to Cyclic AMP Pathway Activity and Physically Interacts with the Adenylyl Cyclase Cyr1p/Cdc35p in Budding Yeast

Dubacq, C., Guérois, R., Courbeyrette, R., Kitagawa, K., & Mann, C. (2002) · Eukaryotic Cell · doi:10.1128/ec.1.4.568-582.2002 · Cited by 110 · 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

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

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

The Role of Hsp90N, a New Member of the Hsp90 Family, in Signal Transduction and Neoplastic Transformation

Grammatikakis, N., Vultur, A., Ramana, C. V., Siganou, A., Schweinfest, C. W., Watson, D. K., & Raptis, L. H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109200200 · Cited by 97 · see citing works

Hsp90 Inhibitors in the Clinic

Pacey, S., Banerj, U., Judson, I. R., & Workman, P. (2005) · Springer eBooks · doi:10.1007/3-540-29717-0_14 · Cited by 96 · see citing works

Antileukemic Activity of Shepherdin and Molecular Diversity of Hsp90 Inhibitors

Gyurkocza, B., Plescia, J., Raskett, C. M., Garlick, D. S., Lowry, P. A., Carter, B. Z., Andreeff, M., Meli, M., Colombo, G., & Altieri, D. C. (2006) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djj300 · 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

Chaperoning Checkpoint Kinase 1 (Chk1), an Hsp90 Client, with Purified Chaperones

Arlander, S. J. H., Felts, S. J., Wagner, J. M., Stensgard, B. A., Toft, D. O., & Karnitz, L. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508687200 · Cited by 92 · see citing works

Sgt1 Associates with Hsp90: an Initial Step of Assembly of the Core Kinetochore Complex

Bansal, P. K., Abdulle, R., & Kitagawa, K. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.18.8069-8079.2004 · Cited by 90 · 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

Structures of the N-Terminal and Middle Domains of E. coli Hsp90 and Conformation Changes upon ADP Binding

Huai, Q., Wang, H., Liu, Y., Kim, H.-Y., Toft, D. O., & Ke, H. (2005) · Structure · doi:10.1016/j.str.2004.12.018 · Cited by 86 · see citing works

The Hsp90 Capacitor, Developmental Remodeling, and Evolution: The Robustness of Gene Networks and the Curious Evolvability of Metamorphosis

Rutherford, S., Hirate, Y., & Swalla, B. J. (2007) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230701597782 · Cited by 86 · see citing works

Natural Product Origins of Hsp90 Inhibitors

Uehara, Y. (2003) · Current Cancer Drug Targets · doi:10.2174/1568009033481796 · Cited by 82 · see citing works

Expressed as the sole Hsp90 of yeast, the α and β isoforms of human Hsp90 differ with regard to their capacities for activation of certain client proteins, whereas only Hsp90β generates sensitivity to the Hsp90 inhibitor radicicol

Millson, S. H., Truman, A. W., Rácz, Á., Hu, B., Panaretou, B., Nuttall, J. M., Mollapour, M., Sőti, C., & Piper, P. W. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.05974.x · Cited by 80 · see citing works

Definition of the minimal fragments of Sti1 required for dimerization, interaction with Hsp70 and Hsp90 and in vivo functions.

Flom, G. A., Behal, R. H., Rosen, L., Cole, D. G., & Johnson, J. L. (2007) · Biochemical Journal · doi:10.1042/bj20070084 · Cited by 80 · see citing works

Heat shock protein-90 inhibitors: a chronicle from geldanamycin to today's agents.

Chiosis, G., Lopes, E. C., & Solit, D. B. (2006) · PubMed · Cited by 79 · see citing works

Biochemical and Structural Studies of the Interaction of Cdc37 with Hsp90

Zhang, W., Hirshberg, M., McLaughlin, S. H., Lazar, G. A., Grossmann, J. G., Nielsen, P. R., Sobott, F., Robinson, C. V., Jackson, S., & Laue, E. D. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.05.007 · Cited by 78 · see citing works

The Biochemical Role of the Heat Shock Protein 90 Chaperone Complex in Establishing Human Telomerase Activity

Keppler, B. R., Grady, A. T., & Jarstfer, M. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511067200 · Cited by 75 · see citing works

Structure of Unliganded GRP94, the Endoplasmic Reticulum Hsp90

Dollins, D. E., Immormino, R. M., & Gewirth, D. T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503761200 · Cited by 74 · see citing works

Geldanamycin, a Ligand of Heat Shock Protein 90, Inhibits the Replication of Herpes Simplex Virus Type 1 In Vitro

Li, Y., Tao, P., Liu, Y.-Z., & Jiang, J. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.3.867-872.2004 · Cited by 73 · see citing works

Inhibitors of the HSP90 Molecular Chaperone: Attacking the Master Regulator in Cancer

McDonald, E., Workman, P., & Jones, K. A. (2006) · Current Topics in Medicinal Chemistry · doi:10.2174/156802606777812004 · Cited by 72 · see citing works

Iron chelation study in a normal human hepatocyte cell line suggests that tumor necrosis factor receptor‐associated protein 1 (TRAP1) regulates production of reactive oxygen species

Im, C., Lee, J., Zheng, Y. H., & Seo, J. (2006) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21064 · Cited by 68 · see citing works

Interaction of Hsp90 with the Nascent Form of the Mutant Epidermal Growth Factor Receptor EGFRvIII

Lavictoire, S. J., Parolin, D. A. E., Klimowicz, A., Kelly, J. F., & Lorimer, I. A. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209494200 · Cited by 67 · see citing works

Derrubone, an Inhibitor of the Hsp90 Protein Folding Machinery

Hadden, M. K., Galam, L., Gestwicki, J. E., et al. (2007) · Journal of Natural Products · doi:10.1021/np070190s · Cited by 66 · see citing works

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

Proisy, N., Sharp, S. Y., Boxall, K. J., Connelly, S., Roe, S. M., Prodromou, C., Slawin, A. M. Z., Pearl, L. H., Workman, P., & Moody, C. J. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2006.09.015 · Cited by 66 · see citing works

Definition of Protein Kinase Sequence Motifs That Trigger High Affinity Binding of Hsp90 and Cdc37

Prince, T. L., & Matts, R. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406882200 · Cited by 64 · see citing works

Post-translational Disruption of the ΔF508 Cystic Fibrosis Transmembrane Conductance Regulator (CFTR)-Molecular Chaperone Complex with Geldanamycin Stabilizes ΔF508 CFTR in the Rabbit Reticulocyte Lysate

Fuller, W., & Cuthbert, A. W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006278200 · Cited by 62 · see citing works

Identification of new biomarkers for clinical trials of Hsp90 inhibitors

Zhang, H., Chung, D., Yang, Y., et al. (2006) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-05-0537 · Cited by 61 · see citing works

Yeast is selectively hypersensitised to heat shock protein 90 (Hsp90)-targetting drugs with heterologous expression of the human Hsp90β, a property that can be exploited in screens for new Hsp90 chaperone inhibitors

Piper, P. W., Panaretou, B., Millson, S. H., Trumana, A., Mollapour, M., Pearl, L. H., & Prodromou, C. (2003) · Gene · doi:10.1016/s0378-1119(02)01102-2 · Cited by 53 · see citing works

Conformational dynamics of the molecular chaperone Hsp90 in complexes with a co-chaperone and anticancer drugs.

Phillips, J., Yao, Z.-P., Zhang, W., McLaughlin, S., Laue, E., Robinson, C., & Jackson, S. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.04.059 · Cited by 50 · see citing works

Geldanamycin, a Potent and Specific Inhibitor of Hsp90, Inhibits Gene Expression and Replication of Human Cytomegalovirus

Basha, W., Kitagawa, R., Uhara, M., Imazu, H., 上地幸平, & Tanaka, J. (2005) · Antiviral chemistry & chemotherapy · doi:10.1177/095632020501600206 · Cited by 50 · see citing works

A novel class of Hsp90 inhibitors isolated by structure-based virtual screening

Park, H., Kim, Y., & Hahn, J. (2007) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2007.08.069 · Cited by 49 · see citing works

Regulation of Death-associated Protein Kinase

Zhang, L., Nephew, K. P., & Gallagher, P. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610430200 · Cited by 46 · see citing works

Hsp90 levels affect telomere length in yeast

Grandin, N., & Charbonneau, M. (2001) · Molecular Genetics and Genomics · doi:10.1007/s004380000398 · Cited by 44 · see citing works

Mammalian CHORD‐containing protein 1 is a novel heat shock protein 90‐interacting protein

Wu, J., Luo, S., Jiang, H., & Li, H. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.12.005 · Cited by 43 · see citing works

The messenger and the message: gp96 (GRP94)-peptide interactions in cellular immunity

Nicchitta, C. V., Carrick, D. M., & Baker-LePain, J. C. (2004) · Cell Stress and Chaperones · doi:10.1379/csc-62.1 · Cited by 43 · see citing works

Design, Synthesis, and StructureActivity Relationships for Chimeric Inhibitors of Hsp90

Shen, G., Wang, M., Welch, T. R., et al. (2006) · The Journal of Organic Chemistry · doi:10.1021/jo061054f · Cited by 39 · see citing works

Regulation of Proto-Oncogenic Dbl by Chaperone-Controlled, Ubiquitin-Mediated Degradation

Kamynina, E., Kauppinen, K. P., Duan, F., Muakkassa, N., & Manor, D. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01051-06 · Cited by 35 · see citing works

Chp‐1 and melusin, two CHORD containing proteins in vertebrates

Brancaccio, M., Menini, N., Bongioanni, D., et al. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00892-5 · Cited by 34 · see citing works

Geldanamycins Trigger a Novel Ron Degradative Pathway, Hampering Oncogenic Signaling

Germano, S., Barberis, D., Santoro, M. M., Penengo, L., Citri, A., Yarden, Y., & Gaudino, G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602014200 · Cited by 32 · see citing works

Chaperone-dependent E3 ligase CHIP ubiquitinates and mediates proteasomal degradation of soluble guanylyl cyclase

Xia, T., Dimitropoulou, C., Zeng, J., Antonova, G. N., Snead, C. M., Venema, R. C., Fulton, D. J., Qian, S. B., Patterson, C., Papapetropoulos, A., et al. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00579.2007 · Cited by 31 · see citing works

Hsp90 and Chromatin: Where is the Link?

Sangster, T. A., Queitsch, C., & Lindquist, S. L. (2003) · Cell Cycle · doi:10.4161/cc.2.3.400 · Cited by 29 · see citing works

Analysis of the CK2‐dependent phosphorylation of serine 13 in Cdc37 using a phospho‐specific antibody and phospho‐affinity gel electrophoresis

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Localization of HSP90 Binding Sites in the Human Hepatitis B Virus Polymerase

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