Structural and Functional Analysis of the Middle Segment of Hsp90: Implications for ATP Hydrolysis and Client Protein and Cochaperone Interactions

The CCP4 suite: programs for protein crystallography

Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,317

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,723

Refinement of Macromolecular Structures by the Maximum-Likelihood Method

Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,796

SCOP: A structural classification of proteins database for the investigation of sequences and structures

Murzin, A. G., Brenner, S. E., Hubbard, T., & Chothia, C. (1995) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80134-2 · Cited by 6,435

Automated MAD and MIR structure solution

Terwilliger, T. C., & Berendzen, J. (1999) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444999000839 · Cited by 3,032

Structure of the 30S ribosomal subunit

Wimberly, B. T., Brodersen, D. E., Clemons, W. M., Morgan-Warren, R. J., Carter, A. P., Vonrhein, C., Hartsch, T., & Ramakrishnan, V. (2000) · Nature · doi:10.1038/35030006 · Cited by 2,035

[27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods

Fortelle, E. D. L., & Bricogne, G. (1997) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(97)76073-7 · Cited by 1,892

Maximum-likelihood density modification

Terwilliger, T. C. (2000) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444900005072 · Cited by 1,637

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

Investigation of the Hsp90 C-terminal Binding Site, Novel Inhibitors and Isoform-Dependent Client Proteins

Peterson, L. B. (2012) · KU ScholarWorks (The University of Kansas) · Cited by 4

Nitration-driven structural changes in Hsp90 linked to gain of pathological functions

Chatterjee, T., Taboada, A., Logan, I. E., Paul, P. N., Huerta, M., Reardon, P. N., Radí, R., Zeida, A., & Franco, M. C. (2025) · Biochemical Journal · doi:10.1042/bcj20253230 · Cited by 3

Structural Basis of Parasitic HSP90 ATPase Inhibition by Small Molecules

Tassone, G., Mazzorana, M., & Pozzi, C. (2022) · Pharmaceuticals · doi:10.3390/ph15111341 · Cited by 3

Structural basis of the key residue W320 responsible for Hsp90 conformational change

Peng, S., Matts, R. L., & Deng, J. (2022) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2022.2146197 · Cited by 3

Molecular Chaperones and Their Applications

Valsala, G., Sugathan, S., Bharathan, H., & MacRae, T. H. (2020) · Springer eBooks · doi:10.1007/978-981-15-5136-9_21 · Cited by 3

17-AAG promotes the degradation of HSP90 client METTL3 to suppress MYC RNA m6A modification and expression in colorectal cancer

Meng, H., Jalal, M., Wang, H., Wang, Y., Feng, Y., Zheng, P., Liu, X., & Huang, S. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.149421 · Cited by 2

The essential co-chaperone Sgt1 regulates client dwell time in the Hsp90 chaperone cycle

Engler, S., Delhommel, F., Dodt, C., López, A., Faust, O., Elimelech, A. R., Napolitano, V., Popowicz, G. M., Rosenzweig, R., Sattler, M., et al. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.12.002 · Cited by 4

NMR assignment of human HSP90 N-terminal domain bound to a long residence time resorcinol ligand

Henot, F., Crublet, E., Frech, M., & Boisbouvier, J. (2022) · Biomolecular NMR Assignments · doi:10.1007/s12104-022-10089-0 · Cited by 2

Conformational Analysis of the Loop-to-Helix Transition of the α-Helix3 Plastic Region in the N-Terminal Domain of Human Hsp90α by a Computational Biochemistry Approach

Gohda, K. (2022) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.2c00984 · Cited by 2

Structural Basis of Hsp90 Function

Prodromou, C., & Pearl, L. H. (2013) · Royal Society of Chemistry eBooks · doi:10.1039/9781849739689-00037 · Cited by 3

Investigating the influence of environment on the evolution of Hsp90 using comprehensive fitness maps [preprint]

Flynn, J. M., Rossouw, A., Cote-Hammarlof, P. A., Fragata, I., Mavor, D., Hollins, C., Bank, C., & Bolon, D. N. A. (2019) · eScholarship@UMassChan · Cited by 2

Hsp90 Structure and Function in Cancer

Faridi, N., & Ghahghaei, A. (2018) · Gene Cell and Tissue · doi:10.5812/gct.81887 · Cited by 2

Role of Heat Shock Protein 90 in Autoimmune Inflammatory Rheumatic Diseases

Štorkánová, H., & Tomčík, M. (2019) · Heat shock proteins · doi:10.1007/978-3-030-02254-9_5 · Cited by 2

Inhibition of the Molecular Chaperone Heat Shock Protein 90 in Cancer: Consequences for the Regulation of Survival Signaling and Induction of Cell Death

Clarke, P. A., Powers, M. V., & Workman, P. (2006) · Wiley eBooks · doi:10.1002/9783527619665.ch37 · Cited by 2

Towards a Complete Structure of Hsp90

Bracher, A., & Hartl, F. U. (2005) · Structure · doi:10.1016/j.str.2005.03.004 · Cited by 2

Genome-wide identification and analysis of the abiotic stress responsiveness of the heat shock protein 90 gene family in Medicago sativa L

Liu, H., Zhang, Y., Li, X., Zhao, L., Ma, X., He, F., Li, M., Wang, X., Long, R., Kang, J., et al. (2025) · BMC Plant Biology · doi:10.1186/s12870-025-07520-8 · Cited by 1

An isotype-specific phosphorylation of Hsp90 rewires co-chaperone regulations

Banerjee, T., Moroni, E., Riedl, M., Colombo, G., & Büchner, J. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113292 · Cited by 1

Role of Heat Shock Protein 90 in Diabetes and Pancreatic Cancer Management

Sushma, P. S., Momin, S., & Srivani, G. (2019) · Springer eBooks · doi:10.1007/978-981-32-9393-9_11 · Cited by 1

General Structural and Functional Features of Molecular Chaperones

Edkins, A. L., & Boshoff, A. (2013) · Springer eBooks · doi:10.1007/978-94-007-7438-4_2 · Cited by 1

Small-Molecule Inhibitors of Protein–Protein Interactions as Therapeutics

Poluri, K. M., Gulati, K., Tripathi, D. K., & Nagar, N. (2023) · Springer eBooks · doi:10.1007/978-981-99-2423-3_7 · Cited by 1

Understanding of ATP-lid conformational dynamics in the N-terminal domain of Hsp90 and its mutants by use of a computational biochemistry approach

Gohda, K. (2025) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2025.2487202 · Cited by 1

Benzbromarone interferes with the interaction between Hsp90 and Aha1 by interacting with both of them

Zhong, Y., Li, S., Xu, Z., Gao, J., Ma, Q., Gao, T., Tang, J., Xiong, M., Xu, Y., Dai, H., et al. (2025) · Communications Biology · doi:10.1038/s42003-025-08189-3 · Cited by 1

Crystal Structures of N-terminal Domain of Human Hsp90 With ATP Analogues Reveal The Functional Regulation of Hsp90*

Li, J., Sun, L.-H., Xu, C., Yu, F., Zhou, H., Tang, L., & He, J. (2012) · PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS · doi:10.3724/sp.j.1206.2011.00611 · Cited by 2

Targeting Heat Shock Proteins in Multiple Myeloma

Kale, V. P., Phadtare, S., Amin, S., & Pandey, M. K. (2019) · Heat shock proteins · doi:10.1007/978-3-030-03952-3_12 · Cited by 1

The Hsp90 Chaperone Machinery Acts at Protein Folding Clefts to Regulate Both Signaling Protein Function and Protein Quality Control

Pratt, W. B., Morishima, Y., & Osawa, Y. (2007) · Springer eBooks · doi:10.1007/978-1-4020-6401-2_1 · Cited by 1

Regulation of the heat shock response by thiol-reactive compounds in the yeast Saccharomyces cerevisiae

Wang, Y. (2012) · Digital Commons-TMC (Texas Medical Center) · Cited by 1

A Peptide Encoded by Long Non-coding RNA NEAT1 Suppresses Cancer Growth through Interfering RAF-HSP90β Complex StabilityPreprint

Dong, Z., Chen, X.-J., Li, J., Laster, K. V., Zhang, H., Huang, Y., Liu, F., Zhou, L., Liu, K., & Huang, C. (2023) · Research Square · doi:10.21203/rs.3.rs-3608223/v1 · Cited by 1

The Role of Molecular Chaperones in the ER Associated Degradation of the Cystic Fibrosis Transmembrane Conductance Regulator in the Budding Yeast S. cerevisiae

Youker, R. T. (2006) · D-Scholarship@Pitt (University of Pittsburgh) · Cited by 1

The Role of Molecular Chaperones in Yeast Cell Wall Integrity and Identification of Chaperone Modulators that Interfere with Simian Virus 40 Replication

Wright, C. M. (2007) · D-Scholarship@Pitt (University of Pittsburgh)

Estudio del valor patogénico de la expresión y ruta de señalización de KIT e IGF1R en Sarcoma de Ewing: ¿nuevas posibles dianas terapeúticas?

Martins, A. S. D. S. (2008) · Gredos (University of Salamanca) · doi:10.14201/gredos.22508

The Hsp 90 Family of Molecular Chaperones

Richter, K., Meinlschmidt, B., & Büchner, J. (2008) · Wiley eBooks · doi:10.1002/9783527610754.sf22

Chaperone Function in Vitro

Buchner, J., & Walter, S. (2008) · Protein Science Encyclopedia · doi:10.1002/9783527610754.sf15

Estudos estruturais e funcionais da Hsp90 de Leishmania braziliensis e suas co-chaperonas p23

da Silva, K. P. (2012) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.75.2012.tde-24072012-172313

An investigation on the interaction between Hsp90 and p53 in breast cancer: An in-silico approach

Pilla, S. P. (2012)

IDENTIFICATION OF NOVEL HEAT SHOCK RESPONSE MODULATORS FOR EXPERIMENTAL ANTI-MELANOMA INTERVENTION

Davis, A. L. (2015) · UA Campus Repository (The University of Arizona)

The Molecular Chaperone gp96/GRP94 Interacts with Toll-like Receptors and Integrins via Its C-terminal

Wu, S., Hong, F., Gewirth, D. T., Guo, B., Liu, B., & Li, Z. (2012)

Experimental Illumination of Comprehensive Fitness Landscapes: A Dissertation

Hietpas, R. T. (2013) · eScholarship@UMassChan · doi:10.13028/m2kk6j

A Hsp90 és az adipogenezis kapcsolatának vizsgálata

Nguyễn, M. T. (2014) · Semmelweis University Repository (Semmelweis University) · doi:10.14753/se.2014.1971

Chaperones and Proteases of Mitochondria: From Protein Folding and Degradation to Mitophagy

Voos, W., Rüb, C., & Bruderek, M. (2014) · Springer eBooks · doi:10.1007/978-1-4939-1130-1_12

Estudo estrutural da co-chaperona Aha1 (Activator of Hsp90 ATPase 1) de Leishmania braziliensis e da sua ação sobre o ciclo funcional da Hsp90

Seraphim, T. V. (2015) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.75.2015.tde-25112015-102054

Hsp90 molecular chaperone: structure, functions and participation in the cardio-vascular pathologies

Kroupskaya, I. V. (2009) · Biopolymers and Cell · doi:10.7124/bc.0007ef

Uncovering aR egion of Heat Shock Protein 90 Important for Client Binding in E. coli and Chaperone Function in Yeast

Genest, O., Reidy, M. J., Street, T. O., Hoskins, J. R., Camberg, J. L., Agard, D. A., Masison, D. C., & Wickner, S. (2013)

The Role of ER-localized HSP90 in Modulating the WUSCHEL-CLAVATA pathway and ER Stress Resistance in Arabidopsis thaliana

Chong, L. P. (2015) · TSpace (University of Toronto)

Utilizing a Microbial Natural Product to Investigate Cellular Circuitry Governing Fungal Drug Resistance and Morphogenesis

Shekhar‐Guturja, T. (2016) · TSpace (University of Toronto)

The Roles of Hsp90 and Calcineurin in Antifungal Drug Resistance

Singh, S. (2012) · TSpace (University of Toronto)

Estudo estrutural e funcional da co-chaperona SGT de Leishmania braziliensis

Coto, A. L. S. (2016) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.75.2016.tde-17112016-135653

Determining the Mechanisms of Resistance to Drug Combinations and their Fitness Effects in Candida albicans

Hill, J. A. (2014) · TSpace (University of Toronto)

Hch1p Acts Differently From Its Homologue, Aha1p, in Regulating Sensitivity of Hsp90 to Hsp90 Inhibitors in Yeast

Armstrong, H. (2013) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r3tc7r

Structural bioinformatics studies and tool development related to drug discovery

Hatherley, R. (2016)

Caracterização de domínios da Hsp90 de Plasmodium falciparum e mapeamento da interação com a sua co-chaperona Aha4

Torricillas, M. D. S. (2019) · doi:10.11606/d.75.2019.tde-13052019-110021

The adaptive potential of the middle domain of yeast Hsp90Preprint

Cote-Hammarlof, P. A., Fragata, I., Flynn, J. M., Mavor, D., Zeldovich, K. B., Bank, C., & Bolon, D. N. A. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/832022

Defined Interactions of Protein Kinases with Hsp90 and Cdc37

Prince, T. L. (2005) · SHAREOK (University of Oklahoma; Oklahoma State University; Central Oklahoma University)

Como implicar a los bancos en la proteccion de los intereses del exportador

Osorio, F. P. (2000) · El Exportador

Mass spectrometric investigations of biomolecular machines

Blayney, M. J. (2010) · Research Online (University of Wollongong)

Efeito do consumo das proteínas, peptídeos e aminoácidos do soro do leite nas heat shock proteins (HSPs) e parâmetros relacionados em ratos

Moura, C. S. (2016) · doi:10.47749/t/unicamp.2016.975426

Hsp 90 Inhibitors

Blagg, B. S. J., & Hadden, M. K. (2010) · Wiley eBooks · doi:10.1002/0471266949.bmc212

Hsp90 Inhibitors

Blagg, B. S. J., Hadden, M. K., & Tarpley, R. S. (2021) · Wiley eBooks · doi:10.1002/0471266949.bmc212.pub2

Exploring the human Hsp70-Hop-Hsp90 system for Tau recognition

Moll, A. (2022) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-9131

Hsp90 Chaperones

Zierer, B. K., & Büchner, J. (2012) · Wiley eBooks · doi:10.1002/9780470015902.a0024154

Faculty Opinions recommendation of A methylated lysine is a switch point for conformational communication in the chaperone Hsp90.

Mollapour, M. (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.737482045.793572272

Caracterização da Hsp90 de Aedes aegypti e seus interatores SGT e complexo R2TP

Quel, N. G. (2019) · doi:10.47749/t/unicamp.2019.1233092

Synthesis and Crystallographic Investigation of a Series of Dicobalt Tetrahedrane Complexes Ligated by 2-Butyne-1,4-Diol. In Silico Evaluation of Their Efficiency as Anticancer Metallodrugs by Docking StudiesPreprint

Mohamed, A. S., Jourdain, I., Knorr, M., Elmi, A., Siddique, F., Chtita, S., Beffy, S., Carsten Strohmann, B., Schmidt, A., & Hussien, M. A. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4894082

Computational Elucidation of Possible Contributors to Formation and Stabilization of ATP ‐Lid Down‐Conformation in the N‐Terminal Domain of Hsp90

Gohda, K. (2025) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26849

HSP90B1 facilitates glioma radiotherapy resistance by regulating RhoC ubiquitin‒proteasome degradation

Xu, J., Guo, Y., Yang, J., Shang, G., Ning, W., Liu, D., Zhang, H., & Song, Y. (2025) · Genes & Diseases · doi:10.1016/j.gendis.2025.101756

Optogenetic Clustering of Human IRE1 Reveals Differential Regulation of Transcription and mRNA Splice Isoform Abundance by the UPRPreprint

Smith, J. W., Wilburn, D. B., & Belyy, V. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.16.665212

Temporal Interactome Mapping of Human Tau in Drosophila Reveals Progressive Mitochondrial Engagement and Porin/VDAC1-Dependent Modulation of Toxicity

Tsakiri, E. N., Samiotaki, M. K., Skoulakis, E. M. C., & Papanikolopoulou, K. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26199741

Direct optical activation of human IRE1 identifies unique patterns of transcriptional and post-transcriptional mRNA regulation in the unfolded protein response

Smith, J. W., Wilburn, D. B., & Belyy, V. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.111067

Using Phylogenetically Conserved Stress Responses to Discover Natural Products with Anticancer Activity

Turbyville, T. J. (2005) · UA Campus Repository (The University of Arizona)

Identification of Essential Functions of GRP94 in Metazoan Growth Control and Epithelial Homeostasis

Maynard, J. C. (2009) · DukeSpace (Duke University)

Antibodies Against SARS-CoV-2 Nucleocapsid Protein Possess Autoimmune Properties

Rak, A. Y., Zabrodskaya, Y. A., Wong, P.-F., & Николаевна, И.-С. И. (2025) · Antibodies · doi:10.3390/antib15010002

Structural basis of HSP90C, a highly active chloroplastic HSP90 chaperone from A. thalianaPreprint

Rocca, R. L., Chenuel, T., Bergonzi, C., Maes, A., Pozza, A., & Meyer, P. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.05.697646

HSP90α promotes fowl adenovirus serotype 4 replication in LMH cells via interacting with hexon

Zhai, S., Zhang, X., Liu, K., Gao, H., Yu, L., Li, J., Yang, X., Zhao, J., & Zeng, W. A. N. G. (2026) · Avian Pathology · doi:10.1080/03079457.2025.2611109

Comparative analysis of the impact of Heat shock protein 90 kDa or Cdc37 mutation on the yeast proteome

Rios, E. I., & Johnson, J. L. (2026) · Cell Stress and Chaperones · doi:10.1016/j.cstres.2026.100164

C-H fonctionnalisation de purines : synthèse d’inhibiteurs potentiels de la HSP90

Sahnoun, S. (2011) · theses.fr (ABES) · doi:10.70675/39de54cdzed42z410bz84c5zaf41b61046db

Rôle des facteurs d'assemblage et du système HSP90/R2TP dans la biogenèse des particules C/D snoRNP et U4 snRNP

Bizarro, J. (2013) · theses.fr (ABES) · doi:10.70675/7ea370b3z86e5z4d67zb563z470e005ed8ec

Formation et régulation du complexe polymérase du virus de la rougeole

Bloyet, L.-M. (2015) · theses.fr (ABES) · doi:10.70675/39007b42zbb49z41b5zb5ffz4d00c60c4b16

Investigating the role of extended CBC complexes in RNA metabolism

Benbahouche, N. E. H. (2015) · theses.fr (ABES) · doi:10.70675/74b23280z7279z4ccfzb8ffzc6a45316012a

La protéine HSP90 : expression et ciblage dans les hémopathies malignes

Flandrin‐Gresta, P. (2012) · theses.fr (ABES) · doi:10.70675/c7c4c69bz12d5z4cc5zad16z0af4fefb9fb8

Étude du rôle du complexe SMN dans l’assemblage de RNP non codantes ubiquitaires : la SRP, les RNP C/D et H/ACA dont la télomérase, et étude du taux des facteurs d’assemblage de la télomérase dans les cellules cancéreuses

Dodré, M. (2014) · theses.fr (ABES) · doi:10.70675/b97d6973z95aaz4364z8030z3b86fc1d910d

Functional characterization of the TRRAP pseudokinase and its chaperone TTT during transcriptional regulation in colorectal cancer

Detilleux, D. (2018) · theses.fr (ABES) · doi:10.70675/6edd4ae0z525dz45f7zb1c5z3ade9c6098dc

Développements méthodologiques en spectrométrie de masse structurale pour la caractérisation de complexes biologiques multiprotéiques

Bourguet, M. (2019) · theses.fr (ABES) · doi:10.70675/ba485de5zaaacz49c6z9687z91bc6a719799

Etude des principes d’assemblage et de maturation des kinases de la famille des PIKKs chez Schizosaccharomyces pombe

Toullec, D. (2020) · theses.fr (ABES) · doi:10.70675/a7933611z0027z41dfz8436za664ba25bd4a

HSP90 une cible thérapeutique dynamique : modulation des conformations peuplées par la liaison de ligands

Henot, F. (2022) · theses.fr (ABES) · doi:10.70675/dcb06c1dz5e32z4f84zb791z3f4f67b79e05

Unperturbed hydration structure involves ADP recognition in the N‐terminal domain of human heat shock protein 90α

Hirano, Y., Kusaka, K., Ose, T., Kurihara, K., Aburai, K., Saito, J., & Tamada, T. (2026) · Protein Science · doi:10.1002/pro.70619

Structural basis of HSP90C, a highly active chloroplastic HSP90 chaperone from Arabidopsis thaliana

Rocca, R. L., Chenuel, T., Bergonzi, C., Maes, A., Pozza, A., & Meyer, P. (2026) · Journal of Molecular Biology · doi:10.1016/j.jmb.2026.169935

Hypoxia–ROS–HSP Triad Axis in Cancer: Mechanisms, Crosstalk, and Therapeutic Implications

Singh, M. K., Yun, H. R., Ranbhise, J. S., Han, S., Yeo, S. G., Quan, F., Kim, B., Kim, S. S., & Kang, I. (2026) · Cells · doi:10.3390/cells15191802

Plasmodium falciparum putative Hsp90 functionally complements yeast Hsp90 and is inhibited in an isoform-specific manner

Khamitkar, S. R., Bag, M., Kini, V. R., Singh, M., Sethi, B. K., & Bhattacharyya, S. (2026) · Frontiers in Parasitology · doi:10.3389/fpara.2026.1944050

Exploratory chromosome 14-focused transcriptomic profiling of PSEN1-associated familial Alzheimer's disease across brain regions

Pradeepkiran, J. A., Munikumar, M., More, P., Pradhan, D. P., Maddineni, J., Kosanam, M., Srichurnam, S., Malempati, T., Thota, A., & Sainath, S. B. (2026) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2026.141192

From productive coupling to catalytic commitment: An evolutionarily tuned interdomain connector in Leishmania Aha1 orchestrates Hsp90 activation

Dores-Silva, P. R., Seraphim, T. V., Minari, K., da Silva, I. R. F., Gomes, W. P. C., de Sousa, L. F., da Rocha, A. M. F., Barbosa, L. R. S., Joseph, J. S., & Borges, J. C. (2026) · FEBS Journal · doi:10.1111/febs.70776

BindingDB Entry 50042689: A chemical-biological study reveals C9-type iridoids as novel heat shock protein 90 (Hsp90) inhibitors.

BindingDB (2013) · UC San Diego · doi:10.7270/q2k938w3

BindingDB Entry 50005891: Design and synthesis of 2-amino-6-(1H,3H-benzo[de]isochromen-6-yl)-1,3,5-triazines as novel Hsp90 inhibitors.

BindingDB (2020) · UC San Diego · doi:10.7270/q2pr7zxr

BindingDB Entry 50006714: C-terminal modulators of heat shock protein of 90 kDa (HSP90): State of development and modes of action.

BindingDB (2021) · UC San Diego · doi:10.7270/q27w6gfn

BindingDB Entry 4677: Discovery and design of novel HSP90 inhibitors using multiple fragment-based design strategies.

BindingDB (2011) · UC San Diego · doi:10.7270/q25x27dh

BindingDB Entry 1948: Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms.

BindingDB (2007) · UC San Diego · doi:10.7270/q2rx99bc

BindingDB Entry 50018217: Natural heat shock protein 90 inhibitors in cancer and inflammation.

BindingDB (2024) · UC San Diego · doi:10.7270/q2cj8jnq

BindingDB Entry 50032408: ATPases as drug targets: insights from heat shock proteins 70 and 90.

BindingDB (2011) · UC San Diego · doi:10.7270/q25x2956

BindingDB Entry 50039098: Heat shock protein 90: inhibitors in clinical trials.

BindingDB (2012) · UC San Diego · doi:10.7270/q2gm889j

BindingDB Entry 50045229: Development of radamide analogs as Grp94 inhibitors.

BindingDB (2016) · UC San Diego · doi:10.7270/q2xk8h77

Hsp90-Mediated Maturation of Kinases and Nuclear Steroid Hormone Receptors: A Dissertation

Pursell, N. W. (2011) · doi:10.13028/dtnt-eg88

Structure and Functional Relationships of Hsp90

Prodromou, C., & Pearl, L. H. (2003) · Current Cancer Drug Targets · doi:10.2174/1568009033481877 · Cited by 262

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

Crystal structure and functional analysis of the middle segment of Hsp90: Implications for ATP hydrolysis and co-chaperone interactions.

Meyer, P., Prodromou, C., & Hu-B (2003) · UCL Discovery (University College London) · Cited by 2

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

Coordinated ATP Hydrolysis by the Hsp90 Dimer

Richter, K., Muschler, P., Hainzl, O., & Büchner, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103832200 · Cited by 207