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

Genome Structures and Evolution Analysis of Hsp90 Gene Family in Brassica napus Reveal the Possible Roles of Members in Response to Salt Stress and the Infection of Sclerotinia sclerotiorum

Wang, L., Liu, F., Ju, L., Xue, B., Wang, Y., Wang, D., & Hou, D. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2022.854034 · Cited by 19

Dolichol phosphate mannose synthase: a Glycosyltransferase with Unity in molecular diversities

Banerjee, D. K., Zhang, Z., Baksi, K., & Serrano-Negrón, J. E. (2017) · Glycoconjugate Journal · doi:10.1007/s10719-017-9777-4 · Cited by 19

Identification of Isoform-Selective Ligands for the Middle Domain of Heat Shock Protein 90 (Hsp90)

Mak, O. W., Raina, C., Reynisson, J., & Leung, I. K. H. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20215333 · Cited by 19

Binding of Proteolytically Processed Phospholipase D from Streptomyces chromofuscus to Phosphatidylcholine Membranes Facilitates Vesicle Aggregation and Fusion

Stieglitz, K. A., Seaton, B. A., & Roberts, M. F. (2001) · Biochemistry · doi:10.1021/bi011338o · Cited by 19

Mechanism of JNK signal regulation by placental HSP70 and HSP90 in endothelial cell during preeclampsia

Padmini, E., Uthra, V., & Lavanya, S. (2012) · Toxicology Mechanisms and Methods · doi:10.3109/15376516.2012.673091 · Cited by 18

How Selective are Hsp90 Inhibitors for Cancer Cells over Normal Cells?

Wang, Y., Koay, Y. C., & McAlpine, S. R. (2017) · ChemMedChem · doi:10.1002/cmdc.201600595 · Cited by 18

Hsp90 Inhibition Reduces TLR5 Surface Expression and NF-κB Activation in Human Myeloid Leukemia THP-1 Cells

Na, B. H., Hoang, T. X., & Kim, J. Y. (2018) · BioMed Research International · doi:10.1155/2018/4319369 · Cited by 18

Functional characterization of orchardgrass endoplasmic reticulum-resident Hsp90 (DgHsp90) as a chaperone and an ATPase

Cha, J., Jung, M. H., Ermawati, N., Su’udi, M., Rho, G., Han, C., Lee, K. H., & Son, D. (2009) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2009.06.008 · Cited by 18

Screening of genes related to ovary development in Chinese shrimp Fenneropenaeus chinensis by suppression subtractive hybridization

Xie, Y., Li, F., Wang, B., Li, S., Wang, D., Jiang, H., Zhang, C., Yu, K., & Xiang, J. (2010) · Comparative Biochemistry and Physiology Part D Genomics and Proteomics · doi:10.1016/j.cbd.2010.02.001 · Cited by 18

Targeting HSP90/Survivin using a cell permeable structure based peptido-mimetic shepherdin in retinoblastoma

Venkatesan, N., Kanwar, J. R., Deepa, P. R., NavaneethaKrishnan, S., Joseph, C., & Krishnakumar, S. (2016) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2016.04.011 · Cited by 18

EVIDENCE THAT THE NOVOBIOCIN‐SENSITIVE ATP‐BINDING SITE OF THE HEAT SHOCK PROTEIN 90 (HSP90) IS NECESSARY FOR ITS AUTOPHOSPHORYLATION

Langer, T., Schlatter, H., & Fasold, H. (2002) · Cell Biology International · doi:10.1006/cbir.2002.0882 · Cited by 19

Selective nitration of Hsp90 acts as a metabolic switch promoting tumor cell proliferation

Logan, I. E., Nguyen, K. T., Chatterjee, T., Manivannan, B., Paul, N. P., Kim, S., Sixta, E., Bastian, L. P., Marean‐Reardon, C. L., Karajannis, M. A., et al. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103249 · Cited by 17

Diabetes upregulates the expression of HSP90 and downregulates HSP70 in the liver of diabetic rats

Amawi, K. F., Almazari, I., Alsarhan, A. A., Alhamad, H., & Alkhatib, A. J. (2019) · Comparative Clinical Pathology · doi:10.1007/s00580-019-02902-5 · Cited by 17

Synthesis of Functionalized 2‐(4‐Hydroxyphenyl)‐3‐methylbenzofuran Allosteric Modulators of Hsp90 Activity

Sattin, S., Panza, M., Vasile, F., Berni, F., Goti, G., Tao, J., Moroni, E., Agard, D. A., Colombo, G., & Bernardi, A. (2016) · European Journal of Organic Chemistry · doi:10.1002/ejoc.201600420 · Cited by 17

Requirement of Peptidyl-Prolyl Cis/Trans isomerases and chaperones for cellular uptake of bacterial AB-type toxins

Ernst, K. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.938015 · Cited by 16

Identification, Characterization and Expression Profiling of Stress-Related Genes in Easter Lily (Lilium formolongi)

Howlader, J., Park, J., Robin, A. H. K., Sumi, K. R., & Nou, I. (2017) · Genes · doi:10.3390/genes8070172 · Cited by 16

The Role of HSP90 Chaperones in Stability and Plasticity of Ontogenesis of Plants under Normal and Stressful Conditions (Arabidopsis thaliana)

Kozeko, L. (2019) · Cytology and Genetics · doi:10.3103/s0095452719020063 · Cited by 16

Dietary non-protein energy source regulates antioxidant status and immune response of barramundi (Lates calcarifer)

Fu, Z., Yang, R., Chen, X., Qin, J. G., Gu, Z., & Ma, Z. (2019) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2019.11.018 · Cited by 16

Potentiation of angiogenic switch in capillary endothelial cells by cAMP: A cross-talk between up-regulated LLO biosynthesis and the HSP-70 expression

Martínez, J. A., Tavárez, J. J., Oliveira, C. M., & Banerjee, D. K. (2006) · Glycoconjugate Journal · doi:10.1007/s10719-006-7926-2 · Cited by 16

An Hsp90 modulator that exhibits a unique mechanistic profile

Ramsey, D. M., McConnell, J. R., Alexander, L. D., Tanaka, K. W., Vera, C. M., & McAlpine, S. R. (2012) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2012.03.012 · Cited by 15

cDNA cloning and expression analysis of two heat shock protein genes, Hsp90 and Hsp60, from a sterile Ulva pertusa (Ulvales, Chlorophyta)

Tominaga, H., Coury, D. A., Amano, H., Miki, W., & Kakinuma, M. (2012) · Fisheries Science · doi:10.1007/s12562-011-0451-7 · Cited by 15

Synthesis of potential allosteric modulators of Hsp90 by chemical glycosylation of Eupomatenoid-6

Morelli, L., Bernardi, A., & Sattin, S. (2014) · Carbohydrate Research · doi:10.1016/j.carres.2014.03.006 · Cited by 15

Cellular responses in the coral Stylophora pistillata exposed to eutrophication from fish mariculture

Kramarsky‐Winter, E., Downs, C. A., Downs, A., & Loya, Y. (2009) · Evolutionary ecology research · Cited by 15

A Mechanistic and Structural Analysis of the Inhibition of the 90-kDa Heat Shock Protein by the Benzoquinone and Hydroquinone Ansamycins

Reigan, P., Siegel, D. M., Guo, W., & Ross, D. (2011) · Molecular Pharmacology · doi:10.1124/mol.110.070086 · Cited by 15

The ATPases: a new family for a family-based drug design approach

Chêne, P. (2003) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.7.3.453 · Cited by 15

An Evaluation of Hsp90 as a Mediator of Cortical Patterning in Tetrahymena

Frankel, J., Williams, N. E., Nelsen, E. M., & Keeling, P. J. (2001) · Journal of Eukaryotic Microbiology · doi:10.1111/j.1550-7408.2001.tb00297.x · Cited by 15

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 · doi:10.1002/ange.200390300 · Cited by 15

Changes in activity and transcription of antioxidant enzymes and heat shock protein 90 in the water flea, Daphnia magna - exposed to mercury

Kim, H., Kim, J., & Lee, Y.-M. (2017) · Toxicology and Environmental Health Sciences · doi:10.1007/s13530-017-0335-z · Cited by 14

A small-molecule compound D6 overcomes EGFR-T790M-mediated resistance in non-small cell lung cancer

Tang, X., Cheng, L., Guo, L., Yan, Y., Su, F., Huang, D., Zhang, S., Liu, Z., Qian, M., Li, J., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-02906-4 · Cited by 14

Effects of low crude oil chronic exposure on the northern krill (Meganyctiphanes norvegica)

Moodley, L., Arnberg, M., Dunaevskaya, E., Seear, P. J., Bærheim, L., Nilsen, M., Ramanand, S. S., Øysæd, K. B., Westerlund, S. F. G., Jonsson, G., et al. (2017) · Journal of Experimental Marine Biology and Ecology · doi:10.1016/j.jembe.2017.07.003 · Cited by 13

Identification of Plasmodium falciparum heat shock 90 inhibitors via molecular docking

Everson, N., Bach, J., Hammill, J. T., Falade, M. O., Rice, A. L., Guy, R. K., & Eagon, S. (2021) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2021.127818 · Cited by 13

In Silico Prediction of the Dissociation Rate Constants of Small Chemical Ligands by 3D-Grid-Based VolSurf Method

Huang, S., Chen, L., Hu, M. Y., Zhang, D., Shi, T., Kuang, Z., Heng, Y., Xu, L., & Pan, X. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21072456 · Cited by 13

Heat shock proteins, Importance and expression in fishes

Wali, A., & Balkhi, M.-U. H. (2016) · European Journal of Biotechnology and Bioscience · Cited by 13

Cytotoxic activity to acute myeloid leukemia cells by Antp-TPR hybrid peptide targeting Hsp90

Horibe, T., Kawamoto, M., Kohno, M., & Kawakami, K. (2012) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2012.02.016 · Cited by 12

Liberation of the intramolecular interaction as the mechanism of heat‐induced activation of HSP90 molecular chaperone

Tanaka, E., Nemoto, T., & Ono, T. (2001) · European Journal of Biochemistry · doi:10.1046/j.0014-2956.2001.02458.x · Cited by 12

Heat shock protein 90 maintains the stability and function of transcription factor Broad Z7 by interacting with its Broad‐Complex‐Tramtrack‐Bric‐a‐brac domain

Cai, M., Li, X., Pei, X. ‐., Liu, W., Wang, J., & Zhao, X. (2014) · Insect Molecular Biology · doi:10.1111/imb.12118 · Cited by 11

Heat Shock Protein 90 Regulates the Stability of c-Jun in HEK293 Cells

Lu, C., Chen, D., Zhang, Z., Fang, F., Wu, Y., Luo, L., & Yin, Z. (2007) · Molecules and Cells · doi:10.1016/s1016-8478(23)07330-2 · Cited by 11

Discovery of indazole inhibitors for heat shock protein 90 as anti-cancer agents

La, M. T., Hoang, V.-H., Sahu, R., Nguyen, C.-T., Nam, G., Park, H., Park, M., Kim, Y. J., Kim, J. Y., Ann, J., et al. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116620 · Cited by 10

RNA-seq analysis and reconstruction of gene networks involved in response to salinity stress in quinoa (cv. Titicaca)

Hosseini, S. S., Ramezanpour, S. S., Soltanloo, H., & Seifati, S. E. (2023) · Scientific Reports · doi:10.1038/s41598-023-34534-9 · Cited by 10

Mactinin, a fragment of cytoskeletal α-actinin, is a novel inducer of heat shock protein (Hsp)-90 mediated monocyte activation

Luikart, S. D., Panoskaltsis‐Mortari, A., Hinkel, T., Perri, R. T., Gupta, K., Oegema, T. R., & Gupta, P. (2009) · BMC Cell Biology · doi:10.1186/1471-2121-10-60 · Cited by 10

Decomposition analysis of free energy profile for Hsp90-ADP association

Kawaguchi, K., Saito, H., & Nagao, H. (2015) · Molecular Simulation · doi:10.1080/08927022.2015.1102249 · Cited by 10

Tailored Quinolines Demonstrate Flexibility to Exert Antitumor Effects through Varied Mechanisms-A Medicinal Perspective

Sharma, S., Singh, A., Sharma, S., Sharma, R., Singh, J., Kinarivala, N., Nepali, K., & Liou, J. (2020) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/1871520620666200908104303 · Cited by 10

Novel nontoxic heat shock protein 90 inhibitors having selective antiproliferative effect

Orosz, A., Szabó, A., Szeman, G., Janáky, T., Somlai, C., Penke, B., Bodor, A., & Perczel, A. (2006) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2006.01.015 · Cited by 10

Heat shock protein 90 regulates the stability of MEKK3 in HEK293 cells

Fang, S., Fu, J., Yuan, X., Han, C., Shi, L., Xin, Y., Luo, L., & Yin, Z. (2009) · Cellular Immunology · doi:10.1016/j.cellimm.2009.05.012 · Cited by 8

An Hsp90 Inhibitor, Geldanamycin, as a Brassinosteroid Antagonist: Evidence from Salt‐Exposed Roots of Vigna radiata

AMZALLAG, G. N., & Goloubinoff, P. (2003) · Plant Biology · doi:10.1055/s-2003-40725 · Cited by 9

Ligand-independent activation of the P2X7 receptor by Hsp90 inhibition stimulates motor neuron apoptosis

Strayer, A. L., Dennys, C. N., Ricart, K. C., Bae, N., Beckman, J. S., Franco, M. C., & Estévez, Á. G. (2019) · Experimental Biology and Medicine · doi:10.1177/1535370219853798 · Cited by 10

Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity

Hu, H., Wang, Q., Du, J., Liu, Z., Ding, Y., Xue, H., Zhou, C., Feng, L., & Zhang, N. (2021) · Molecules · doi:10.3390/molecules26071943 · Cited by 8

Protein Misfolding, Chaperone Networks, and the Heat Shock Response in the Nervous System

Voisine, C., Orton, K., & Morimoto, R. I. (2007) · Elsevier eBooks · doi:10.1016/b978-012369509-3.50007-x · Cited by 8

Cellular stress response biomarkers for toxicity potential assessment of treated wastewater complex mixtures

Etteieb, S., Tarhouni, J., & Isoda, H. (2018) · Water and Environment Journal · doi:10.1111/wej.12361 · Cited by 8

Apoptosis and Angiogenesis in Varicose Veins Using Gene Expression Profiling

Chang, M., Chiang, P.-T., Chung, Y.-C., Ho, S.-Y., Lin, S., Lin, S., & Neoh, C.-A. (2009) · Fooyin Journal of Health Sciences · doi:10.1016/s1877-8607(10)60005-7 · Cited by 8

Identification of Hsp90 as a species independent H5N1 avian influenza A virus PB2 interacting protein

Jirakanwisal, K., Srisutthisamphan, K., Thepparit, C., Suptawiwat, O., Auewarakul, P., Paemanee, A., Roytrakul, S., & Smith, D. R. (2015) · Comparative Immunology Microbiology and Infectious Diseases · doi:10.1016/j.cimid.2015.10.001 · Cited by 8

Heat-Shock Protein 90-Targeted Nano Anticancer Therapy.

Rochani, A. K., Girija, A. R., Borah, A., Maekawa, T., & Kumar, D. S. (2016) · Journal of Pharmacy and Science · doi:10.1016/j.xphs.2015.10.007 · Cited by 8

The split Renilla luciferase complementation assay is useful for identifying the interaction of Epstein-Barr virus protein kinase BGLF4 and a heat shock protein Hsp90

Wang, J., Guo, W., Long, C., Zhou, H., Wang, H., & Sun, X. (2016) · Acta Virologica · doi:10.4149/av_2016_01_62 · Cited by 8

Hsp90 mediates the balance of nitric oxide and superoxide anion in the lungs of rats with acute pulmonary thromboembolism

Zhang, X., Jin, Y., Xia, L., Tao, X., Bai, M., & Zhang, J. (2008) · International Immunopharmacology · doi:10.1016/j.intimp.2008.09.012 · Cited by 7

Potential Hsp90 Inhibitors: A Novel Target for Cancer Therapy

K, R. B. P. (2015) · Chemotherapy Open access · doi:10.4172/2167-7700.1000146 · Cited by 7

Probing the role of Arg97 in Heat shock protein 90 N-terminal domain from the parasite Leishmania braziliensis through site-directed mutagenesis on the human counterpart

Tassone, G., Mangani, S., Botta, M., & Pozzi, C. (2018) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2018.09.005 · Cited by 7

3D-QSAR studies on PU3 analogues by comparative molecular field analysis

Liu, H.-C., Lyu, P. C., Leong, M. K., Tsai, K., & Hsiue, G. (2003) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2003.11.024 · Cited by 7

HSP90 and checkpoint-dependent lengthening of the G2 phase observed in plant cells under hypoxia and cold

Gim�nez-Abi�n, M. I., Rozal�n, A. E., Carballo, J. A., Botella, L. M., Pincheira, J., L�pez-S�ez, J. F., & de la Torre, C. (2004) · PROTOPLASMA · doi:10.1007/s00709-003-0022-6 · Cited by 7

Plant Hsp90 and Its Partner Proteins

Krishna, P. (2000) · Journal of Plant Biochemistry and Biotechnology · doi:10.1007/bf03263085 · Cited by 7

Involvement of Calcium-Mediated Reactive Oxygen Species in Inductive GRP78 Expression by Geldanamycin in 9L Rat Brain Tumor Cells

Sun, F., Shyu, H., Lee, M., Lee, M.-S., & Lai, Y. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140919169 · Cited by 6

Heat Shock Protein and their Significance in Fish Health

Demeke, A., & Tassew, A. (2016) · Cited by 6

Geldanamycin administration reduces the amount of primordial germ cells in the mouse embryo

Lejong, M., Choa-Duterre, M., Vanmuylder, N., & Louryan, S. (2018) · Morphologie · doi:10.1016/j.morpho.2018.05.001 · Cited by 6

Genetic Variations of Heat Shock Protein 84 in Mice Mediate Cellular Glucocorticoid Response

Zhao, Y., Shen, H., Chen, X., Xiong, R., Li, P., Liu, P., Yang, N., & Zhou, Y. (2010) · Cellular Physiology and Biochemistry · doi:10.1159/000303039 · Cited by 6

Isolation and quantification of the heat shock protein 90 alpha and beta isoforms from rat liver

Langer, T., & Fasold, H. (2001) · PROTOPLASMA · doi:10.1007/bf01288360 · Cited by 6

The Region Adjacent to the Highly Immunogenic Site and Shielded by the Middle Domain Is Responsible for Self-Oligomerization/Client Binding of the HSP90 Molecular Chaperone

Nemoto, T., Fukuma, Y., Yamada, S., Kobayakawa, T., Ono, T., & Ohara‐Nemoto, Y. (2004) · Biochemistry · doi:10.1021/bi036235f · Cited by 6

Genome-wide identification and characterization of HSP90 family gene in cotton and their potential role in salt stress tolerance

Hao, Z. Y., Feng, Q., Man, X. Y., Qi, D. Q., Yu, Q., Yang, Z. W., Elbagory, M., Kasem, E. S., Yasir, M., & Rong, J. Y. (2025) · Frontiers in Plant Science · doi:10.3389/fpls.2025.1574604 · Cited by 6

Recent progress in the development of HSP90 inhibitors: structure–activity relationship and biological evaluation studies

Kumar, A., Rai, A., Rangra, N. K., Singh, T. G., Ugwuagbo, S. C., & Bhatia, R. (2025) · Molecular Diversity · doi:10.1007/s11030-025-11314-3 · Cited by 4

Theoretical study of conformational transition of CDK4 by association of cyclin D3

Kawaguchi, K., Arwansyah, M. S., Kataoka, T., & Nagao, H. (2019) · Molecular Physics · doi:10.1080/00268976.2018.1563725 · Cited by 5

Heat shock response and shape regulation during newt tail regeneration

Radugina, E. A., & Grigoryan, E. N. (2017) · Journal of Thermal Biology · doi:10.1016/j.jtherbio.2017.11.009 · Cited by 5

Stretch-Activated Atrial Natriuretic Peptide Secretion in Atria with Heat Shock Protein 70 Overexpression

Kim, S. H., Koh, G. Y., Cho, K. W., Park, W., & Seo, J. (2003) · Experimental Biology and Medicine · doi:10.1177/153537020322800211 · Cited by 5

Physiological Role of Heat Shock Proteins, Molecular Function and Stress Removal in Fishes

Sen, S. S., & Giri, S. S. (2017) · Heat shock proteins · doi:10.1007/978-3-319-73377-7_8 · Cited by 4

Higher Sensitivity of Peripheral Blood Lymphocytes to Endogenous Glucocorticoid in Renal Transplant Recipients Treated with Tacrolimus, as Compared to those Treated with Cyclosporine

Muhetaer, G., Takeuchi, H., Akizuki, S., Iwamoto, H., Shimazu, M., Unezaki, S., & Hirano, T. (2012) · Cell Medicine · doi:10.3727/215517912x639423 · Cited by 4

Microsatellite Repeats: Canaries in the Coalmine

Chatterjee, N., Santillan, B. A., & Wilson, J. H. (2013) · Springer eBooks · doi:10.1007/978-1-4614-6280-4_7 · Cited by 6

Heat Shock Proteins in Cardiovascular Stress

Geraldine, J., Mala, S., & Takeuchi, S. (2008) · Clinical medicine Cardiology · doi:10.4137/cmc.s876 · Cited by 4

Identifying functional interactions with molecular chaperones

Johnson, J. L., & Craig, E. A. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)51863-2 · Cited by 4

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

Les protéines de choc thermique ( heat shock proteins). I : Classification, structure, fonctions et implications dans les processus pathologiques.

Wirth, D., Gustin, P., Drion, P. V., Dessy‐Doize, C., & Christians, E. (2002) · Open Repository and Bibliography (University of Liège) · Cited by 4

Nitration in cancer signaling

Claassen, I., Adrita, N., Chandler, K. B., Black, S. M., Roberts, B. R., Estévez, Á. G., Beckman, J. S., & Franco, M. C. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104223 · Cited by 4

Role of heat shock proteins in renal function and adaptation to heat stress: Implications for global warming

Tran, T. T. T., Tran, K. V., Nguyen, T. D., Pham, N. T. T., & Nguyen, T. H. (2025) · World Journal of Nephrology · doi:10.5527/wjn.v14.i3.107571 · Cited by 3

The Hsp90 Chaperone Machinery: An Important Hub in Protein Interaction Networks

Radons, J. (2016) · Journal of Advances in Medicine and Medical Research · doi:10.9734/bjmmr/2016/24631 · Cited by 3

Lack of evidence that Pseudomonas aeruginosa AmpDh3‐PA0808 constitute a type VI secretion system effector–immunity pair

Colautti, J., Bullen, N. P., & Whitney, J. C. C. (2022) · Molecular Microbiology · doi:10.1111/mmi.15021 · Cited by 3

Analysis of Expression Pattern of Genome and Analysis of HSP90 Gene Family in Aeluropus littoralis under Salinity Stress

Hashemipetroudi, S. H., Nematzadeh, G., Mohammadi, S., & Kuhlmann, M. (2019) · Journal of Crop Breeding · doi:10.29252/jcb.11.31.134 · Cited by 3

Evaluating Dual Hsp90 and Hsp70 Inhibition as a Cancer Therapy

Buckton, L. K., Wang, Y., McConnell, J. R., & McAlpine, S. R. (2015) · Topics in medicinal chemistry · doi:10.1007/7355_2015_96 · Cited by 3

Heat Shock Proteins as Therapeutic Targets in Amyotrophic Lateral Sclerosis

Kalmár, B., & Greensmith, L. (2008) · Springer eBooks · doi:10.1007/978-1-4020-8231-3_4 · Cited by 3

Histidine Kinases

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