Structure and in vivo function of Hsp90

Hsp90 as a capacitor for morphological evolution

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

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

Whitesell, L., Mimnaugh, E. G., De Costa, B., Myers, C. E., & Neckers, L. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8324 · Cited by 1,444

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

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

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

Prodromou, C., Roe, S. M., O’Brien, R., Ladbury, J. E., Piper, P. W., & Pearl, L. H. (1997) · Cell · doi:10.1016/s0092-8674(00)80314-1 · Cited by 1,258

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

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

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

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

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

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

Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function

Cheetham, M. E., & Caplan, A. J. (1998) · Cell Stress and Chaperones · doi:10.1379/1466-1268(1998)003 · Cited by 604

Untitled work

Yang (2021) · doi:10.1038/s41598-020-79139-8 · Cited by 5,035

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

Pratt, W. B., & Toft, D. O. (2003) · Experimental Biology and Medicine · doi:10.1177/153537020322800201 · Cited by 1,497

Folding of Newly Translated Proteins In Vivo: The Role of Molecular Chaperones

Frydman, J. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.603 · Cited by 1,184

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

Intestinal epithelial cells secrete exosome–like vesicles

van Niel, G., Raposo, G., Candalh, C., Boussac, M., Hershberg, R. M., Cerf–Bensussan, N., & Heyman, M. (2001) · Gastroenterology · doi:10.1053/gast.2001.26263 · Cited by 698

Heat shock protein genes and their functional significance in fish

Basu, N., Todgham, A. E., Ackerman, P. A., Bibeau, M. R., Nakano, K., Schulte, P. M., & Iwama, G. K. (2002) · Gene · doi:10.1016/s0378-1119(02)00687-x · Cited by 653

Hsp70 and Hsp90—a relay team for protein folding

Wegele, H., Müller, L., & Büchner, J. (2004) · Springer eBooks · doi:10.1007/s10254-003-0021-1 · Cited by 609

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 602

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

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

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

Heat Shock Proteins 70 and 90 Inhibit Early Stages of Amyloid β-(1–42) Aggregation in Vitro

Evans, C. G., Wisén, S., & Gestwicki, J. E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606192200 · Cited by 396

&cestflwr; The Hsp90 family of proteins in Arabidopsis thaliana

Krishna, P., & Gloor, G. B. (2001) · Cell Stress and Chaperones · doi:10.1379/1466-1268(2001)006 · Cited by 360

Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability

Randow, F., & Seed, B. (2001) · Nature Cell Biology · doi:10.1038/ncb1001-891 · Cited by 316

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

Hsp90: Structure and Function

Jackson, S. (2012) · Topics in current chemistry · doi:10.1007/128_2012_356 · Cited by 347

Regulation of survivin function by Hsp90

Fortugno, P., Beltrami, E., Plescia, J., Fontana, J. T., Pradhan, D., Marchisio, P. C., Sessa, W. C., & Altieri, D. C. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2434345100 · Cited by 316

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 294

Fatal Attraction: Nonself Recognition and Heterokaryon Incompatibility in Filamentous Fungi

Glass, N. L., & Kaneko, I. (2003) · Eukaryotic Cell · doi:10.1128/ec.2.1.1-8.2003 · Cited by 271

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 270

The regulatory mechanism of Hsp90α secretion and its function in tumor malignancy

Wang, X., Song, X., Zhuo, W., Fu, Y., Shi, H., Liang, Y., Tong, M., Chang, G., & Luo, Y. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908151106 · Cited by 267

Epidermal Growth Factor Receptors Harboring Kinase Domain Mutations Associate with the Heat Shock Protein 90 Chaperone and Are Destabilized following Exposure to Geldanamycins

Shimamura, T., Lowell, A. M., Engelman, J. A., & Shapiro, G. I. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-0933 · Cited by 260

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 246

Combinatorial drug design targeting multiple cancer signaling networks controlled by mitochondrial Hsp90

Kang, B. H., Plescia, J., Song, H. Y., Meli, M., Colombo, G., Beebe, K. E., Scroggins, B. T., Neckers, L., & Altieri, D. C. (2009) · Journal of Clinical Investigation · doi:10.1172/jci37613 · Cited by 239

Stimulation of the weak ATPase activity of human Hsp90 by a client protein 1 1Edited by G. von Heijne

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

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

HEAT SHOCK RESPONSE AND AGEING: MECHANISMS AND APPLICATIONS

Verbeke, P., Fonager, J., Clark, B. F. C., & Rattan, S. I. S. (2001) · Cell Biology International · doi:10.1006/cbir.2001.0789 · Cited by 220

Hsp90 inhibitors: Small molecules that transform the Hsp90 protein folding machinery into a catalyst for protein degradation

Blagg, B. S. J., & Kerr, T. D. (2005) · Medicinal Research Reviews · doi:10.1002/med.20052 · Cited by 191

HSP90AB1: Helping the good and the bad

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

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

Heat Shock Protein 90 in Plants: Molecular Mechanisms and Roles in Stress Responses

Xu, Z., Li, Z., Chen, Y., Chen, M., Li, L., & Ma, Y. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms131215706 · Cited by 173

Induction of Hsp90 protein expression in malignant melanomas and melanoma metastases

Becker, B., Multhoff, G., Farkas, B., Wild, P. J., Landthaler, M., Stolz, W., & VOGT, T. M. (2004) · Experimental Dermatology · doi:10.1111/j.0906-6705.2004.00114.x · Cited by 167

Hsp90: an emerging target for breast cancer therapy

Beliakoff, J., & Whitesell, L. J. (2004) · Anti-Cancer Drugs · doi:10.1097/01.cad.0000136876.11928.be · Cited by 154

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

Synthesis and biological activities of novel 17-aminogeldanamycin derivatives

Tian, Z., Liu, Y., Zhang, D., Wang, Z., Dong, S. D., Carreras, C. W., Zhou, Y., Rastelli, G., Santi, D. V., & Myles, D. C. (2004) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2004.07.053 · Cited by 151

Constantly Updated Knowledge of Hsp90

Terasawa, K. (2005) · The Journal of Biochemistry · doi:10.1093/jb/mvi056 · Cited by 151

Structural Basis for Depletion of Heat Shock Protein 90 Client Proteins by Deguelin

Oh, S. H., Woo, J. K., Yazici, Y. D., Myers, J. N., Kim, W.-Y., Jin, Q., Hong, S., Park, H., Suh, Y., Kim, K.-W., et al. (2007) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djm007 · Cited by 146

Involvement of Tumor Necrosis Factor Receptor-associated Protein 1 (TRAP1) in Apoptosis Induced by β-Hydroxyisovalerylshikonin

Masuda, Y., Shima, G., Aiuchi, T., Horie, M., Hori, K., Nakajo, S., Kajimoto, S., Shibayama‐Imazu, T., & Nakaya, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404256200 · Cited by 142

Deranged Expression of Molecular Chaperones in Brains of Patients with Alzheimer's Disease

Yoo, B. C., Kim, S. H., Cairns, N. J., Fountoulakis, M., & Lübec, G. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.4109 · Cited by 137

JlpA of Campylobacter jejuni interacts with surface-exposed heat shock protein 90alpha and triggers signalling pathways leading to the activation of NF-kappaB and p38 MAP kinase in epithelial cells

Jin, S., Song, Y. C., Emili, A., Sherman, P. M., & Chan, V. L. (2003) · Cellular Microbiology · doi:10.1046/j.1462-5822.2003.00265.x · Cited by 134

The dietary bioflavonoid, quercetin, selectively induces apoptosis of prostate cancer cells by down‐regulating the expression of heat shock protein 90

Aalinkeel, R., Bindukumar, B., Reynolds, J. L., Sykes, D. E., Mahajan, S. D., Chadha, K. C., & Schwartz, S. A. (2008) · The Prostate · doi:10.1002/pros.20845 · Cited by 137

The Evolutionary History of Kinetoplastids and Their Kinetoplasts

Simpson, A. G. B., Lukeš, J., & Roger, A. J. (2002) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a004032 · Cited by 131

Plasma Heat Shock Protein 90alpha as a Biomarker for the Diagnosis of Liver Cancer: An Official, Large-scale, and Multicenter Clinical Trial

Fu, Y., Xu, X., Huang, D., Cui, D., Liu, L., Liu, J., He, Z., Liu, J., Zheng, S., & Luo, Y. (2017) · EBioMedicine · doi:10.1016/j.ebiom.2017.09.007 · Cited by 131

Overexpression of AtHsp90.2, AtHsp90.5 and AtHsp90.7 in Arabidopsis thaliana enhances plant sensitivity to salt and drought stresses

Song, H., Zhao, R., Fan, P., Wang, X., Chen, X., & Li, Y. (2009) · Planta · doi:10.1007/s00425-008-0886-y · Cited by 120

Opposite Perceptual and Sensorimotor Responses to a Size-Weight Illusion

Grandy, M. S., & Westwood, D. A. (2006) · Journal of Neurophysiology · doi:10.1152/jn.00851.2005 · Cited by 119

Molecular chaperones and the art of recognizing a lost cause

McClellan, A. J., & Frydman, J. (2001) · Nature Cell Biology · doi:10.1038/35055162 · Cited by 118

A biochemical rationale for the anticancer effects of Hsp90 inhibitors: Slow, tight binding inhibition by geldanamycin and its analogues

Gooljarsingh, L. T., Fernandes, C., Yan, K., Zhang, H., Grooms, M. H., Johanson, K., Sinnamon, R. H., Kirkpatrick, R. B., Kerrigan, J. J., Lewis, T. S., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602650103 · Cited by 118

Heat shock proteins and kidney disease: perspectives of HSP therapy

Chebotareva, N. V., Bobkova, I. N., & Shilov, E. (2017) · Cell Stress and Chaperones · doi:10.1007/s12192-017-0790-0 · Cited by 116

The chaperone MeHSP90 recruits MeWRKY20 and MeCatalase1 to regulate drought stress resistance in cassava

Wei, Y., Liu, W., Hu, W., Yu, Y., & Shi, H. (2019) · New Phytologist · doi:10.1111/nph.16346 · Cited by 111

The Influence of ATP and p23 on the Conformation of hsp90

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

EARLY EVOLUTIONARY HISTORY OF DINOFLAGELLATES AND APICOMPLEXANS (ALVEOLATA) AS INFERRED FROM HSP90 AND ACTIN PHYLOGENIES1

Leander, B. S., & Keeling, P. J. (2004) · Journal of Phycology · doi:10.1111/j.1529-8817.2004.03129.x · Cited by 107

Acute thermal stress and various heavy metals induce tissue-specific pro-or anti-apoptotic events via the p38-MAPK signal transduction pathway in Mytilus galloprovincialis (Lam.)

Kefaloyianni, E., Gourgou, E., Ferle, V., Kotsakis, E., Gaitanaki, C., & Beis, I. D. (2005) · Journal of Experimental Biology · doi:10.1242/jeb.01924 · Cited by 110

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

In Vitro Reconstitution of Functional Hepadnavirus Reverse Transcriptase with Cellular Chaperone Proteins

Hu, J., Toft, D. O., Anselmo, D., & Wang, X. (2002) · Journal of Virology · doi:10.1128/jvi.76.1.269-279.2002 · Cited by 106

Auditing the pharmacological accounts for Hsp90 molecular chaperone inhibitors: unfolding the relationship between pharmacokinetics and pharmacodynamics.

Workman, P. (2003) · PubMed · Cited by 105

Design, Synthesis, and Biological Evaluation of Novel Deguelin-Based Heat Shock Protein 90 (HSP90) Inhibitors Targeting Proliferation and Angiogenesis

Chang, D.-J., An, H., Kim, K.-S., Kim, H. H., Jung, J., Lee, J. M., Kim, N., Han, Y. T., Yun, H., Lee, S.-J., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm301488q · Cited by 102

Association of Extracellular Membrane Vesicles with Cutaneous Wound Healing

Than, U. T. T., Guanzon, D., Leavesley, D. I., & Parker, T. J. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18050956 · Cited by 103

Heat-shock protein 90 inhibitors as novel cancer chemotherapeutic agents

Neckers, L., & Neckers, K. (2002) · Expert Opinion on Emerging Drugs · doi:10.1517/14728214.7.2.277 · Cited by 104

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

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

Protein Kinase A-dependent Translocation of Hsp90α Impairs Endothelial Nitric-oxide Synthase Activity in High Glucose and Diabetes

Lei, H., Venkatakrishnan, A., Yu, S., & Kazlauskas, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608985200 · Cited by 98

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

Hsp90 Regulates Activation of Interferon Regulatory Factor 3 and TBK-1 Stabilization in Sendai Virus-infected Cells

Yang, K. S., Shi, H., Qi, R., Sun, S., Tang, Y., Zhang, B., & Wang, C. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-09-0853 · Cited by 94

Hsp104 Interacts with Hsp90 Cochaperones in Respiring Yeast

Abbas‐Terki, T., Donzé, O., Briand, P.-A., & Picard, D. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.22.7569-7575.2001 · Cited by 94

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

Signal Transduction–Directed Cancer Treatments

Sausville, E. A., Elsayed, Y. A., Monga, M., & Kim, G. (2003) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.43.100901.135813 · Cited by 89

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 89

Hsf1 on a leash – controlling the heat shock response by chaperone titration

Masser, A. E., Ciccarelli, M., & Andréasson, C. (2020) · Experimental Cell Research · doi:10.1016/j.yexcr.2020.112246 · Cited by 83

Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle

Li, Z., Hartl, F. U., & Bracher, A. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2608 · Cited by 87

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

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

A fluorescence polarization assay for inhibitors of Hsp90

Howes, R., Barril, X., Dymock, B. W., Grant, K., Northfield, C. J., Robertson, A., Surgenor, A. E., Wayne, J., Wright, L., James, K. E., et al. (2006) · Analytical Biochemistry · doi:10.1016/j.ab.2005.12.023 · Cited by 84

Role of heat shock proteins (molecular chaperones) in intestinal mucosal protection

Otaka, M., Odashima, M., & Watanabe, S. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.07.028 · Cited by 84

Synthesis and Biological Evaluation of a New Class of Geldanamycin Derivatives as Potent Inhibitors of Hsp90

Brazidec, J. L., Kamal, A., Busch, D. J., Thao, L., Zhang, L., Timony, G. A., Grecko, R., Trent, K., Lough, R. E., Salazar, T., et al. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm0306125 · Cited by 84

Anchorage-independent growth of breast carcinoma cells is mediated by serum exosomes

Ochieng, J., Pratap, S., Khatua, A. K., & Sakwe, A. M. (2009) · Experimental Cell Research · doi:10.1016/j.yexcr.2009.03.010 · Cited by 80

Phosphorylation and hsp90 Binding Mediate Heat Shock Stabilization of p53

Wang, C., & Chen, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m206697200 · Cited by 75

Synthesis of sansalvamide A peptidomimetics: triazole, oxazole, thiazole, and pseudoproline containing compounds

Davis, M. R., Singh, E. K., Wahyudi, H., Alexander, L. D., Kunicki, J. B., Nazarova, L. A., Fairweather, K. A., Giltrap, A. M., Jolliffe, K. A., & McAlpine, S. R. (2011) · Tetrahedron · doi:10.1016/j.tet.2011.11.089 · Cited by 76

Signal Responsiveness of IκB Kinases Is Determined by Cdc37-assisted Transient Interaction with Hsp90

Hinz, M., Broemer, M., Arslan, S. Ç., Otto, A., Mueller, E., Dettmer, R., & Scheidereit, C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705785200 · Cited by 81

Radicicol-sensitive Peptide Binding to the N-terminal Portion of GRP94

Vogen, S. M., Gidalevitz, T., Biswas, C., Simen, B. B., Stein, E. M., Gulmen, F., & Argon, Y. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205323200 · Cited by 77

Total Synthesis as a Resource in the Discovery of Potentially Valuable Antitumor Agents: Cycloproparadicicol

Yamamoto, K., Garbaccio, R. M., Stachel, S. J., Solit, D. B., Chiosis, G., Rosen, N. X., & Danishefsky, S. J. (2003) · Angewandte Chemie International Edition · doi:10.1002/anie.200390329 · Cited by 75

Breast Cancer

Hondermarck, H. (2003) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r300003-mcp200 · Cited by 75

Hsp90—From signal transduction to cell transformation

Brown, M. A., Zhu, L., Schmidt, C., & Tucker, P. W. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.08.054 · Cited by 73

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

Regulation of Heat Shock Protein 90 ATPase Activity by Sequences in the Carboxyl Terminus*

Owen, B., Sullivan, W., Felts, S., & Toft, D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111450200 · Cited by 69

Macrocycles That Inhibit the Binding between Heat Shock Protein 90 and TPR-Containing Proteins

Ardi, V. C., Alexander, L. D., Johnson, V. A., & McAlpine, S. R. (2011) · ACS Chemical Biology · doi:10.1021/cb200203m · Cited by 69

Heat Shock Protein 90 (Hsp90) Expression and Breast Cancer

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Geldanamycin, an inhibitor of heat shock protein 90 (Hsp90) mediated signal transduction has anti‐inflammatory effects and interacts with glucocorticoid receptor in vivo

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