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

The Molecular Chaperone Sse1 and the Growth Control Protein Kinase Sch9 Collaborate to Regulate Protein Kinase A Activity in Saccharomyces cerevisiae

Trott, A. E., Shaner, L. M., & Morano, K. A. (2005) · Genetics · doi:10.1534/genetics.105.043109 · Cited by 55

Transformation of the Non-Selective Aminocyclohexanol-Based Hsp90 Inhibitor into a Grp94-Seletive Scaffold

Mishra, S. J., Ghosh, S., Stothert, A. R., Dickey, C. A., & Blagg, B. S. J. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00747 · Cited by 55

Hsp90 Chaperone Activity Requires the Full-length Protein and Interaction among Its Multiple Domains

Johnson, B. D., Chadli, A., Felts, S. J., Bouhouche, I., CATELLI, M. G., & Toft, D. O. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005195200 · Cited by 55

Study of the development of chemoresistance in melanoma cell lines using proteome analysis

Sinha, P. K., Poland, J., Kohl, S., Schnölzer, M., Helmbach, H., Hütter, G., Lage, H., & Schadendorf, D. (2003) · Electrophoresis · doi:10.1002/elps.200305456 · Cited by 54

A comparison of Hsp90α and Hsp90β interactions with cochaperones and substrates

Taherian, A., Krone, P. H., & Ovsenek, N. (2008) · Biochemistry and Cell Biology · doi:10.1139/o07-154 · Cited by 52

Role of p50/CDC37 in Hepadnavirus Assembly and Replication

Wang, X., Grammatikakis, N., & Hu, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202198200 · Cited by 52

A Chemical Surface Modification of Chitosan by Glycoconjugates To Enhance the Cell−Biomaterial Interaction

Wang, Y.-C., Kao, S., & Hsieh, H. (2003) · Biomacromolecules · doi:10.1021/bm0256294 · Cited by 52

Molecular characterization and phylogenetic evaluation of the hsp90 gene from selected nematodes.

Skantar, A. M., & Carta, L. K. (2004) · PubMed Central · Cited by 52

Cdc37 is essential for chromosome segregation and cytokinesis in higher eukaryotes

Lange, B. M. H., Rebollo, E., Herold, A., & González, C. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf531 · Cited by 52

Expression analysis of heat shock genes in the skin, spleen and blood of common carp(Cyprinus carpio)after cadmium exposure and hypothermia

Ferencz, Á., Juhász, R., Butnariu, M., Deér, A. K., Varga, I., & Nemcsók, J. (2012) · Acta Biologica Hungarica · doi:10.1556/abiol.63.2012.1.2 · Cited by 51

Cns1 Is an Activator of the Ssa1 ATPase Activity

Hainzl, O., Wegele, H., Richter, K., & Büchner, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402189200 · Cited by 51

Cloning of an orange-spotted grouper Epinephelus coioides heat shock protein 90AB (HSP90AB) and characterization of its expression in response to nodavirus

Chen, Y.-M., Kuo, C., Wang, T., Shie, P.-S., Wang, W.-C., Huang, S.-L., Tsai, T.-J., Chen, P.-P., Chen, J.-C., & Chen, T.-Y. (2010) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2010.02.004 · Cited by 50

Mass Spectrometry for Proteomics-Based Investigation of Oxidative Stress and Heat Shock Proteins

Sokolowska, I., Woods, A. G., Wagner, J. S., Dorler, J., Wormwood, K. L., Thome, J., & Darie, C. C. (2011) · ACS symposium series · doi:10.1021/bk-2011-1083.ch013 · Cited by 49

Genome-wide identification and expression analysis of HSP90 gene family in Nicotiana tabacum

Song, Z., Pan, F., Yang, C., Jia, H., HouLong, J., He, F., NaJia, L., Lu, X., & Zhang, H. (2019) · BMC Genetics · doi:10.1186/s12863-019-0738-8 · Cited by 49

Crystal Structures of Histone and p53 Methyltransferase SmyD2 Reveal a Conformational Flexibility of the Autoinhibitory C-Terminal Domain

Jiang, Y., Sirinupong, N., Brunzelle, J. S., & Yang, Z. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021640 · Cited by 49

Inhibiting Heat Shock Protein 90 Protects Nucleus Pulposus-Derived Stem/Progenitor Cells From Compression-Induced Necroptosis and Apoptosis

Hu, B., Zhang, S., Liu, W., Wang, P., Chen, S., Lv, X., Shi, D., Ma, K., Wang, B., Wu, Y., et al. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00685 · Cited by 48

Volatile organic compounds cytotoxicity and expression of HSP72, HSP90 and GRP78 stress proteins in cultured human cells

Croute, F., Poinsot, J., Gaubin, Y., Beau, B., Simon, V., Murat, J. C., & Soleilhavoup, J. P. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(02)00271-9 · Cited by 48

Novel Hsp90 inhibitor NVP-AUY922 radiosensitizes prostate cancer cells

Gandhi, N. S., Wild, A. T., Chettiar, S. T., Aziz, K., Katō, Y., Gajula, R. P., Williams, R. D., Cades, J., Annadanam, A., Song, D. Y., et al. (2013) · Cancer Biology & Therapy · doi:10.4161/cbt.23626 · Cited by 47

Identification of immunity‐related genes in the burying beetle Nicrophorus vespilloides by suppression subtractive hybridization

Vogel, H., Badapanda, C., & Vilcinskas, A. (2011) · Insect Molecular Biology · doi:10.1111/j.1365-2583.2011.01109.x · Cited by 47

Qri2/Nse4, a component of the essential Smc5/6 DNA repair complex

Hu, B., Liao, C., Millson, S. H., Mollapour, M., Prodromou, C., Pearl, L. H., Piper, P. W., & Panaretou, B. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04531.x · Cited by 47

The Hsp90 Co-Chaperones Cdc37 and Sti1 Interact Physically and Genetically

Abbas‐Terki, T., Briand, P.-A., Donzé, O., & Picard, D. (2002) · Biological Chemistry · doi:10.1515/bc.2002.152 · Cited by 47

Design strategies to target crystallographic waters applied to the Hsp90 molecular chaperone

Kung, P., Sinnema, P.-J., Richardson, P., Hickey, M. J., Gajiwala, K. S., Wang, F., Huang, B., McClellan, G. A., Wang, J., Maegley, K. A., et al. (2011) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.04.130 · Cited by 45

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 45

Investigating the protein-protein interactions of the yeast Hsp90 chaperone system by two-hybrid analysis: potential uses and limitations of this approach

Millson, S. H., Truman, A. W., Wolfram, F., King, V., Panaretou, B., Prodromou, C., Pearl, L. H., & Piper, P. W. (2004) · Cell Stress and Chaperones · doi:10.1379/csc-29r1.1 · Cited by 46

Study of Therapy Resistance in Cancer Cells with Functional Proteome Analysis

Poland, J., Schadendorf, D., Lage, H., Schnölzer, M., Celis, J. E., & Sinha, P. K. (2002) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.2002.037 · Cited by 46

Machinery of protein folding and unfolding

Zhang, X., Beuron, F., & Freemont, P. S. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00315-9 · Cited by 46

Rational Biosynthetic Engineering for Optimization of Geldanamycin Analogues

Kim, W.-C., Lee, D., Hong, S. S., Zhu, N., Shin, J. C., Roh, S. H., Wu, C., Choi, O., Lee, K., Shen, Y., et al. (2009) · ChemBioChem · doi:10.1002/cbic.200800763 · Cited by 45

The NS1 protein of influenza a virus interacts with heat shock protein Hsp90 in human alveolar basal epithelial cells: Implication for virus-induced apoptosis

Zhang, C., Yang, Y., Zhou, X., Yang, Z., Liu, X., Cao, Z., Song, H., He, Y., & Huang, P. (2011) · Virology Journal · doi:10.1186/1743-422x-8-181 · Cited by 50

Conformational Dynamics of the Molecular Chaperone Hsp90 in Complexes with a Co-chaperone and Anticancer Drugs

Phillips, J. J., Yao, Z., Zhang, W., McLaughlin, S. H., Laue, E. D., Robinson, C. V., & Jackson, S. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.04.059 · Cited by 45

Targeting a highly conserved domain in bacterial histidine kinases to generate inhibitors with broad spectrum activity

Fihn, C. A., & Carlson, E. E. (2021) · Current Opinion in Microbiology · doi:10.1016/j.mib.2021.03.007 · Cited by 43

FSHD2- and BAMS-associated mutations confer opposing effects on SMCHD1 function

Gurzau, A. D., Chen, K., Xue, S., Dai, W., Lucet, I. S., Ly, T. T. N., Reversade, B., Blewitt, M. E., & Murphy, J. M. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003104 · Cited by 42

Both the N‐ and C‐terminal chaperone sites of Hsp90 participate in protein refolding

Minami, M., Nakamura, M., Emori, Y., & Minami, Y. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02145.x · Cited by 43

High Affinity Binding of Hsp90 Is Triggered by Multiple Discrete Segments of Its Kinase Clients

Scroggins, B. T., Prince, T. L., Shao, J., Uma, S., Huang, W., Guo, Y., Yun, B.-G., Hedman, K., Matts, R. L., & Hartson, S. D. (2003) · Biochemistry · doi:10.1021/bi035001t · Cited by 43

Regulation of the Atrial Natriuretic Peptide Receptor by Heat Shock Protein 90 Complexes

Kumar, R., Grammatikakis, N., & Chinkers, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010480200 · Cited by 42

Platycodin D potentiates proliferation inhibition and apoptosis induction upon AKT inhibition via feedback blockade in non-small cell lung cancer cells

Li, T., Chen, X., Chen, X., Ma, D., Leung, C. H., & Lu, J. (2016) · Scientific Reports · doi:10.1038/srep37997 · Cited by 45

Bulk isolation of immune response-related genes by expressed sequenced tags of Japanese flounder leucocytes stimulated with Con A/PMA

Nam, B., Hırono, I., & Aoki, T. (2003) · Fish & Shellfish Immunology · doi:10.1006/fsim.2002.0448 · Cited by 42

Structure-based design of 7-carbamate analogs of geldanamycin

Rastelli, G., Tian, Z., Wang, Z., Myles, D. C., & Liu, Y. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.08.013 · Cited by 42

Differences in conformational dynamics within the Hsp90 chaperone family reveal mechanistic insights

Graf, C., Lee, C., Meier-Andrejszki, L. E., Nguyễn, M. T., & Mayer, M. P. (2014) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2014.00004 · Cited by 41

Role of Hsp90 in Biogenesis of the β-Cell ATP-sensitive Potassium Channel Complex

Yan, F.-F., Pratt, E. B., Chen, P., Wang, F., Skach, W. R., David, L. L., & Shyng, S. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-02-0116 · Cited by 41

Molecularly Targeted Agents as Radiosensitizers in Cancer Therapy—Focus on Prostate Cancer

Alcorn, S. R., Walker, A. J., Gandhi, N. S., Narang, A. K., Wild, A. T., Hales, R. K., Herman, J. M., Song, D. Y., DeWeese, T. L., Antonarakis, E. S., et al. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140714800 · Cited by 39

Heat Shock Protein Genes in Fish

Kayhan, F. E., & Duman, B. S. (2010) · Turkish Journal of Fisheries and Aquatic Sciences · doi:10.4194/trjfas.2010.0218 · Cited by 39

Hsp90 can accommodate the simultaneous binding of the FKBP52 and HOP proteins

Hildenbrand, Z. L., Molugu, S. K., Herrera, N., Ramirez, C., Xiao, C., & Bernal, R. A. (2011) · Oncotarget · doi:10.18632/oncotarget.225 · Cited by 38

Heat Shock Protein 90 Stabilizes Nucleolin to Increase mRNA Stability in Mitosis

Wang, S., Li, H., Hsu, T., Chen, S., Wu, C.-J., Chang, W., & Hung, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.310979 · Cited by 39

Heat Shock Protein 90 Is Important for Sp1 Stability during Mitosis

Wang, S., Chuang, J., Yeh, S.-H., Wang, Y.-T., Liu, Y., Chang, W., & Hung, J. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.02.040 · Cited by 38

Substrate-binding characteristics of proteins in the 90 kDa heat shock protein family

Nemoto, T., Toshio, O. N. O., & Tanaka, K. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3540663 · Cited by 38

Synthesis and evaluation of biotinylated sansalvamide A analogs and their modulation of Hsp90

Kunicki, J. B., Petersen, M. N., Alexander, L. D., Ardi, V. C., McConnell, J. R., & McAlpine, S. R. (2011) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.06.083 · Cited by 37

Hsp90 C-Terminal Inhibitors Exhibit Antimigratory Activity by Disrupting the Hsp90α/Aha1 Complex in PC3-MM2 Cells

Ghosh, S., Shinogle, H. E., Garg, G., Vielhauer, G. A., Holzbeierlein, J. M., Dobrowsky, R. T., & Blagg, B. S. J. (2014) · ACS Chemical Biology · doi:10.1021/cb5008713 · Cited by 37

Molecular Characterization and Expression of a Heat Shock Protein Gene (HSP90) from the Carmine Spider Mite,Tetranychus cinnabarinus(Boisduval)

Feng, H., Wang, L., Liu, Y., He, L., Li, M., Lu, W., & Xue, C. (2010) · Journal of Insect Science · doi:10.1673/031.010.11201 · Cited by 36

Effects of dietary soybean isoflavones on non-specific immune responses and hepatic antioxidant abilities and mRNA expression of two heat shock proteins (HSPs) in juvenile golden pompano Trachinotus ovatus under pH stress

Zhou, C., Lin, H., Huang, Z., Wang, J., Wang, Y., & Yu, W. (2015) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2015.10.036 · Cited by 35

Quantum Chemical Calculations and Mutational Analysis Suggest Heat Shock Protein 90 Catalyzes Trans-Cis Isomerization of Geldanamycin

Lee, Y. S., Marcu, M. G., & Neckers, L. (2004) · Chemistry & Biology · doi:10.1016/j.chembiol.2004.05.010 · Cited by 35

Global Protein Shotgun Expression Profiling of Proliferating MCF-7 Breast Cancer Cells

Sandhu, C., Connor, M. K., Kislinger, T., Slingerland, J. M., & Emili, A. (2005) · Journal of Proteome Research · doi:10.1021/pr0498842 · Cited by 35

Comprehensive Analysis of Protein Glycation Reveals Its Potential Impacts on Protein Degradation and Gene Expression in Human Cells

Sun, F., Suttapitugsakul, S., Xiao, H., & Wu, R. (2019) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-019-02197-4 · Cited by 35

Protein–Protein Interactions and Multi-component Complexes of Aminoacyl-tRNA Synthetases

Kim, J. H., Han, J. M., & Kim, S. (2013) · Topics in current chemistry · doi:10.1007/128_2013_479 · Cited by 34

Regulation of Phospholipase C-β Activity by Phosphatidic Acid: Isoform Dependence, Role of Protein Kinase C, and G Protein Subunits

Litosch, I. (2003) · Biochemistry · doi:10.1021/bi026414h · Cited by 32

Geldanamycin induction of grp78 requires activation of reactive oxygen species via ER stress responsive elements in 9L rat brain tumour cells

Lai, M.-T., Huang, K.-L., Chang, W., & Lai, Y. (2003) · Cellular Signalling · doi:10.1016/s0898-6568(03)00004-4 · Cited by 32

Heat shock protein 90 (Hsp90) regulates the stability of transforming growth factor β-activated kinase 1 (TAK1) in interleukin-1β-induced cell signaling

Shi, L., Zhang, Z., Fang, S., Xu, J., Liu, J., Shen, J., Fang, F., Luo, L., & Yin, Z. (2008) · Molecular Immunology · doi:10.1016/j.molimm.2008.07.019 · Cited by 34

Bovine sperm HSP-70 molecules: a potential cryo-tolerance marker associated with semen quality and fertility rate

Pardede, B. P., Kusumawati, A., Pangestu, M., & Purwantara, B. (2023) · Frontiers in Veterinary Science · doi:10.3389/fvets.2023.1167594 · Cited by 31

Inhibitors of the Plasmodium falciparum Hsp90 towards Selective Antimalarial Drug Design: The Past, Present and Future

Stofberg, M. L., Caillet, C., de Villiers, M., & Zininga, T. (2021) · Cells · doi:10.3390/cells10112849 · Cited by 32

The Human TPR Protein TTC4 Is a Putative Hsp90 Co-Chaperone Which Interacts with CDC6 and Shows Alterations in Transformed Cells

Crevel, G., Bennett, D. C., & Cotterill, S. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001737 · Cited by 31

Heat Shock Proteins at the Crossroads between Cancer and Alzheimer’s Disease

Wang, H., Tan, M., Lu, R.-C., Yu, J., & Tan, L. (2014) · BioMed Research International · doi:10.1155/2014/239164 · Cited by 32

Resolving Hot Spots in the C-Terminal Dimerization Domain that Determine the Stability of the Molecular Chaperone Hsp90

Ciglia, E., Vergin, J., Reimann, S., Smits, S. H. J., Schmitt, L., Groth, G., & Gohlke, H. (2014) · PLoS ONE · doi:10.1371/journal.pone.0096031 · Cited by 30

Development of radamide analogs as Grp94 inhibitors

Muth, A., Crowley, V. M., Khandelwal, A., Mishra, S. J., Zhao, J., Hall, J., & Blagg, B. S. J. (2014) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2014.05.075 · Cited by 30

Vectors for N- or C-terminal positioning of the yeast Gal4p DNA binding or activator domains

Millson, S. H., Truman, A. W., & Piper, P. W. (2003) · BioTechniques · doi:10.2144/03351bm06 · Cited by 30

Depletion of Hsp90β Induces Multiple Defects in B Cell Receptor Signaling

Shinozaki, F., Minami, M., Chiba, T., Suzuki, M. M., Yoshimatsu, K., Ichikawa, Y., Terasawa, K., Emori, Y., Matsumoto, K., Kurosaki, T., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600891200 · Cited by 31

Effect of E(sev) and Su(Raf) Hsp83 Mutants and Trans-heterozygotes on Bristle Trait Means and Variation in Drosophila melanogaster

Milton, C. C., Batterham, P., McKenzie, J. A., & Hoffmann, A. A. (2005) · Genetics · doi:10.1534/genetics.104.038463 · Cited by 30

PKCϵ Is a Unique Regulator for hsp90β Gene in Heat Shock Response

Wu, J., Xiao, L., Cheng, X.-K., Cui, L., Wu, N., & Shen, Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305537200 · Cited by 30

Formulation and in vitro efficacy of liposomes containing the Hsp90 inhibitor 6BrCaQ in prostate cancer cells

Sauvage, F., Franzè, S., Bruneau, A., Alami, M., Denis, S., Nicolas, V., Lesieur, S., Legrand, F., BARRATT, G. M., Messaoudi, S., et al. (2015) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2015.12.053 · Cited by 29

HSP90 Interacts with the Fibronectin N-terminal Domains and Increases Matrix Formation

Chakraborty, A., Boel, N. M.-E., & Edkins, A. L. (2020) · Cells · doi:10.3390/cells9020272 · Cited by 30

Hsp90 Activity Modulation by Plant Secondary Metabolites

Piaz, F. D., Terracciano, S., Tommasi, N. D., & Braca, A. (2015) · Planta Medica · doi:10.1055/s-0035-1546251 · Cited by 28

HSP90 as a regulator of extracellular matrix dynamics

Chakraborty, A., & Edkins, A. L. (2021) · Biochemical Society Transactions · doi:10.1042/bst20210374 · Cited by 28

Cloning and characterization of the HSP90 beta gene from Tanichthys albonubes Lin (Cyprinidae): effect of copper and cadmium exposure

Liu, H., Chen, H., Jing, J., & Ma, X. (2011) · Fish Physiology and Biochemistry · doi:10.1007/s10695-011-9556-2 · Cited by 27

HSP90β chaperoning SMURF1-mediated LATS proteasomal degradation in the regulation of bone formation

Qu, M., Gong, Y., Jin, Y., Gao, R., He, Q., Xu, Y., Shen, T., Mei, L., Xu, C., Hussain, M., et al. (2022) · Cellular Signalling · doi:10.1016/j.cellsig.2022.110523 · Cited by 26

Schizosaccharomyces pombe Hsp90/Git10 Is Required for Glucose/cAMP Signaling

Alaamery, M. A., & Hoffman, C. S. (2008) · Genetics · doi:10.1534/genetics.107.086165 · Cited by 26

Hsp90α Recruited by Sp1 Is Important for Transcription of 12(S)-Lipoxygenase in A431 Cells

Hung, J., Wu, C., Liao, P., & Chang, W. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504904200 · Cited by 26

Allosteric Regulation of Hsp90α’s Activity by Small Molecules Targeting the Middle Domain of the Chaperone

Zhou, C., Zhang, C., Zhu, H., Liu, Z., Su, H., Zhang, X., Chen, T., Zhong, Y., Hu, H., Xiong, M., et al. (2020) · iScience · doi:10.1016/j.isci.2020.100857 · Cited by 25

Molecular basis of the interaction of Hsp90 with its co‐chaperone Hop

Lott, A., Oroz, J., & Zweckstetter, M. (2020) · Protein Science · doi:10.1002/pro.3969 · Cited by 26

A client‐binding site of Cdc37

Terasawa, K., & Minami, Y. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04884.x · Cited by 25

Functional Proteomics of Breast Cancer for Signal Pathway Profiling and Target Discovery

Hondermarck, H., Dollé, L., Yazidi‐Belkoura, I. E., Vercoutter‐Edouart, A., Adriaenssens, É., & Lemoine, J. (2002) · Journal of Mammary Gland Biology and Neoplasia · doi:10.1023/a:1024086015542 · Cited by 25

Hsp90 Cochaperone Aha1 Is a Negative Regulator of the Saccharomyces MAL Activator and Acts Early in the Chaperone Activation Pathway

Ran, F., Gadura, N., & Michels, C. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.040600 · Cited by 24

Pnck induces ligand-independent EGFR degradation by probable perturbation of the Hsp90 chaperone complex

Deb, T. B., Zuo, A., Wang, Y., Barndt, R. J., Cheema, A. K., Sengupta, S., Coticchia, C. M., & Johnson, M. D. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00167.2010 · Cited by 25

Phosphorylation-dependent Interaction of the Asialoglycoprotein Receptor with Molecular Chaperones

Huang, T., Deng, H., Wolkoff, A. W., & Stockert, R. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204786200 · Cited by 24

Structural–Thermodynamic Relationships of Interactions in the N-Terminal ATP-Binding Domain of Hsp90

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