Cited by 222Heat shock proteins researchUbiquitin and proteasome pathwaysHistone Deacetylase Inhibitors Research

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HSP90 Inhibitors: Current Development and Potential in Cancer Therapy

Sidera, Katerina, Patsavoudi, Evangelia·2013·Recent Patents on Anti-Cancer Drug Discovery

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Abstract

In the last decade, the molecular chaperone HSP90 has emerged as an important target in cancer therapeutics and has subsequently become the focus of several drug discovery and development efforts. The first-in-class HSP90 inhibitor 17-AAG entered into Phase I clinical trial in 1999. Today 13 HSP90 inhibitors representing multiple drug classes, with different modes of action, are undergoing clinical evaluation. The present review will highlight the involvement of HSP90 in regulating and maintaining the transformed phenotype, provide an overview on current HSP90 inhibitors and further update on the most relevant patents which have recently appeared in the literature. Keywords: Cancer therapeutics, cell surface, chaperoning, drug discovery, HSP90, signal transduction.

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“These effects are generally based on the activity of inhibitors of chaperone proteins which plays a central role in protein quality control (Sidera and Patsavoudi 2014), or the activation of pro-apoptotic pathways and inhibition of pro-survival signals that are relevant to the downstream UPR…”
The Alpha Isoform of Heat Shock Protein 90 and the Co-chaperones p23 and Cdc37 Promote Opioid Anti-nociception in the Brain
Lei, W., Duron, D. I., Stine, C., Mishra, S. J., Blagg, B. S. J., & Streicher, J. M. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00294 · Cited by 23
“First generation non-selective Hsp90 inhibitors like 17-AAG failed clinical trials due to liver toxicity (Sidera and Patsavoudi, 2014).”
Background
Y‐632 inhibits heat shock protein 90 (Hsp90) function by disrupting the interaction between Hsp90 and Hsp70/Hsp90 organizing protein, and exerts antitumor activity in vitro and in vivo
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“findings have strong implications for the management of cancer pain because Hsp90 inhibitors are being developed as novel cancer therapeutics.(35) These findings suggest that Hsp90”
Background
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Huang, R., Ayine‐Tora, D. M., Rosdi, M. N. M., Li, Y., Reynisson, J., & Leung, I. K. H. (2016) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2016.11.059 · Cited by 21
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“Promoting the degradation of Hsp90 oncogenic client proteins by inhibiting Hsp90 is considered as a promising new anticancer strategy [44,45].”
Background
The Potential of Targeting P53 and HSP90 Overcoming Acquired MAPKi-Resistant Melanoma
Hsieh, C., & Shen, C. (2019) · Current Treatment Options in Oncology · doi:10.1007/s11864-019-0622-9 · Cited by 20
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“A number of HSP90 inhibitors have entered pre-clinical and clinical studies.(7) Of Abbreviations: BAG3, Bcl-2-associated athanogene domain 3; CHX, cycloheximide.”
Background
Cooperative treatment effectiveness of ATR and HSP90 inhibition in Ewing’s sarcoma cells
Marx, C., Schaarschmidt, M. U., Kirkpatrick, J. M., Marx-Blümel, L., Halilovic, M., Westermann, M., Hoelzer, D., Meyer, F. B., Geng, Y., Buder, K., et al. (2021) · Cell & Bioscience · doi:10.1186/s13578-021-00571-y · Cited by 18
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“, ganetispib (Synta) or AUY922 (Novartis) (reviewed in [14,52,53] and references therein).”
Background
Functional maturation of cytochromes P450 3A4 and 2D6 relies on GAPDH- and Hsp90-Dependent heme allocation
Islam, S., Jayaram, D. T., Biswas, P., & Stuehr, D. J. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.105633 · Cited by 16
“Similar concerns hold regarding the impact of chronic Hsp90 inhibition, given that Hsp90 is a target in anti-cancer pharmaceutical development and clinical trials (35, 36).”
Background
Modified biphenyl Hsp90 C-terminal inhibitors for the treatment of cancer
Forsberg, L. K., Liu, W., Holzbeierlein, J. M., & Blagg, B. S. J. (2017) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2017.07.030 · Cited by 16
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“We finally investigated whether resistance to PU-H71 could be overcome by treatment with two alternative, structurally distinct ATP-competitive HSP90 inhibitors that are currently in clinical development, the geldanamycin derivative tanespimycin (also known as 17-AAG) and the second-generation triazole ganetespib (als…”
BackgroundInfluential
Design, synthesis, and anticancer activity of C8-substituted-4′-thionucleosides as potential HSP90 inhibitors
Qu, S., Mulamoottil, V. A., Nayak, A., Ryu, S., Hou, X., Song, J., Yu, J., Sahu, P. K., Zhao, L., Choi, S., et al. (2016) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2016.05.041 · Cited by 15
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Medium-Throughput Detection of Hsp90/Cdc37 Protein–Protein Interaction Inhibitors Using a Split Renilla Luciferase-Based Assay
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“Unfortunately, its derivatives, including 17-AAG (17-N-allyloamino-17demethoxygeldanamycin), failed in the clinic partly due to high toxicity.(24,25) Synthetic second-generation Hsp90 inhibitors, such as luminespib, have shown more favorable results.”
Background
Inhibiting spinal cord-specific hsp90 isoforms reveals a novel strategy to improve the therapeutic index of opioid treatment
Duron, D. I., Tanguturi, P., Campbell, C. S., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-65637-6 · Cited by 12
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“This kind of inhibitors are exhaustively described in a review([66]), and they have shown to sensitize cancer cells to lots of chemotherapies (in various cancer: breast, prostate, ovarian, melanoma, glioblastoma, leukemia, myeloma,.”
Background
The role of heat shock protein 90 in regulating pain, opioid signaling, and opioid antinociception
Streicher, J. M. (2019) · Vitamins and hormones · doi:10.1016/bs.vh.2019.05.010 · Cited by 12
HEXIM1 controls P-TEFb processing and regulates drug sensitivity in triple-negative breast cancer
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“Tumor cells often display increased abundance of Hsp90, which subsequently promotes tumor cell survival and transformation through effects on Akt, TNFα, NF-κB, and other oncogene or tumor suppressors, and overexpression of Hsp90 in breast cancer correlates with poor prognosis (Sidera and Patsavoudi, 2014).”
Background
Targeting EGFR and ALK in NSCLC: Current Evidence and Future Perspective
Bennati, C., Paglialunga, L., Ricciuti, B., Metro, G., Marcomigni, L., Gili, A., & Crinò, L. (2016) · Lung Cancer Management · doi:10.2217/lmt-2016-0005 · Cited by 14
Advances in research on the relationship between the LMNA gene and human diseases (Review)
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“Meng et al (111) and Sidera et al (112) demonstrated that TPX2 can modulate lamin A/C phosphorylation levels in ovarian cancer cells, thereby affecting their stability and inhibiting cellular processes.”
Background
PU-H71 (NSC 750424): a molecular masterpiece that targets HSP90 in cancer and beyond
Saber, S., Abdelhady, R., Elhemely, M. A., Elmorsy, E. A., Hamad, R. S., Abdel‐Reheim, M. A., El-kott, A. F., AlShehri, M. A., Morsy, K., Alsheri, A. S., et al. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1475998 · Cited by 11
“…of BCL6 by PU-H71 is thought to be mediated through multiple mechanisms including, reduced stability and increased degradation of the BCL6 protein (Sidera and Patsavoudi, 2014); disruption of the interaction between BCL6 and its transcriptional co-repressors, such as Silencing Mediator of…”
Rare ER protein misfolding-mistrafficking disorders: Therapeutic developments
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The in silico identification of potent anti-cancer agents by targeting the ATP binding site of the N-domain of HSP90
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“Some benzamides such as SNX-5422 (a pro-drug of active SNX2122) and SNX-2122 failed in clinical trials because of their ocular toxicity, resulting in irreversible retinal damage [10,11].”
Background
Introns control stochastic allele expression bias
Sands, B., Yun, S. R., & Mendenhall, A. (2021) · Nature Communications · doi:10.1038/s41467-021-26798-4 · Cited by 8
Heat Shock Proteins: Endogenous Modulators of Ferroptosis
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Maggot Extract Inhibits Cell Migration and Tumor Growth by Targeting HSP90AB1 in Ovarian Cancer
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“HSP90 is considered a potential target for cancer therapy [11,36].”
Background
Complex Crystal Structure Determination of Hsp90N-NVP-AUY922 and In Vitro Anti-NSCLC Activity of NVP-AUY922
He, C., Lv, Y., Guo, M., et al. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.847556 · Cited by 9
Bisphenol A Regulates the TNFR1 Pathway and Excessive ROS Mediated by miR-26a-5p/ADAM17 Axis to Aggravate Selenium Deficiency-Induced Necroptosis in Broiler Veins
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“Heat shock protein (HSP), a type of DAMP, is expressed at high levels during tissue injury to maintain normal cell function [46, 47].”
HSP90 Inhibition Attenuated Isoflurane-Induced Neurotoxicity in Mice and Human Neuroglioma Cells
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“Heat shock protein 90 (HSP90) is an evolutionarily conserved molecular chaperone crucial for maintaining cellular protein stability through interactions with various protein partners [16].”
Co-selected mutations in VCP: a novel mechanism of resistance to VCP inhibitors
Bastola, P., & CHIEN, J. R. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0049-9 · Cited by 9
Current Application of Nanoparticle Drug Delivery Systems to the Treatment of Anaplastic Thyroid Carcinomas
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C‐Terminal Hsp90 Inhibitors Overcome MEK and BRAF Inhibitor Resistance in Melanoma
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KARADEMİR, D., & Özgür, A. (2023) · Medical Oncology · doi:10.1007/s12032-023-02107-5 · Cited by 8
Geldanamycin induces apoptosis in human gastric carcinomas by affecting multiple oncogenic kinases that have synergic effects with TNF-related apoptosis-inducing ligand
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“Therefore, Hsp90 is important in cell proliferation, cell cycle progression, apoptosis and other features of malignant phenotypes, such as invasion, angiogenesis and metastasis (2,4).”
Mechanism of a Novel Camptothecin-Deoxycholic Acid Derivate Induced Apoptosis against Human Liver Cancer HepG2 Cells and Human Colon Cancer HCT116 Cells
Xiao, L., Xu, J., Weng, Q., et al. (2019) · Recent Patents on Anti-Cancer Drug Discovery · doi:10.2174/1574892814666191016162346 · Cited by 8
Mechanism of Inhibition of Hsp90 Dimerization by Gyrase B Inhibitor Coumermycin A1 (C–A1) Revealed by Molecular Dynamics Simulations and Thermodynamic Calculations
Cele, F. N., Kumalo, H. M., & Soliman, M. E. S. (2016) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-016-0743-8 · Cited by 8
17-DMAG disrupted the autophagy flux leading to the apoptosis of acute lymphoblastic leukemia cells by inducing heat shock cognate protein 70
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Gajjala, P. R., Singh, P., Odayar, V., Ediga, H. H., McCormack, F. X., & Madala, S. K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032850 · Cited by 8
“Currently, more than 10 HSP90 inhibitors that belong to multiple drug classes are in the advanced stages of clinical trials for cancer [77,78].”
Background
Dipyridamole interacts with the N-terminal domain of HSP90 and antagonizes the function of the chaperone in multiple cancer cell lines
Gao, J., Zhou, C., Zhong, Y., Li, S., Luo, X., Su, H., Li, M., Xu, Y., Zhang, N., & Zhou, H. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115376 · Cited by 7
Single-cell RNA-seq analyses inform necroptosis-associated myeloid lineages influence the immune landscape of pancreas cancer
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“Tremendous preclinical evidence has proved the rationale for targeting Hsp90 and dozens of Hsp90 inhibitors, including 17-DMAG, IPI-504, NVP-AUY922, BIIB021 and STA-9090, have been discovered accordingly and are currently in phase I-III clinical trials across multiple tumor types [15-17].”
Construction and in vitro/in vivo evaluation of 17-allylamino-17-demethoxygeldanamycin (17AAG)-loaded PEGylated nanostructured lipid carriers
Wang, Z., Wang, J., Yang, S., et al. (2015) · Drug Development and Industrial Pharmacy · doi:10.3109/03639045.2015.1031138 · Cited by 7
Effect of a heat shock protein 90-specific inhibitor on the proliferation and apoptosis induced by VEGF-C in cervical cancer cells
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“GA is a naturally occurring benzoquinone ansamycin, which binds specifically to the N‑terminal ATP binding domain of Hsp90 (21), and causes the destabilization and degradation of numerous Hsp90 target proteins.”
SNX-2112, an Hsp90 inhibitor, suppresses cervical cancer cells proliferation, migration, and invasion by inhibiting the Akt/mTOR signaling pathway
Fu, L.-S., Qiu, H., Liu, M., Hu, L., Wang, Y., Zhang, P.-C., Li, M., Wang, Y., & Liu, Z. (2020) · Medicinal Chemistry Research · doi:10.1007/s00044-020-02534-3 · Cited by 6
“2017), most of which are involved in cellular signaling and adaptation to various stress responses (Sidera and Patsavoudi 2014).”
Background
Integrin αvβ3 Induces HSP90 Inhibitor Resistance via FAK Activation in KRAS-Mutant Non-Small Cell Lung Cancer
Yoon, S., Yang, H., Ryu, H.-M., Lee, E., Jo, Y., Seo, S., Kim, D., Lee, C. H., Kim, W., Jung, K. H., et al. (2021) · Cancer Research and Treatment · doi:10.4143/crt.2021.651 · Cited by 6
An Insight to Heat Shock Protein 90: A Remedy for Multiple Problems
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HSP90 and Its Inhibitors for Cancer Therapy: Use of Nano-delivery System to Improve Its Clinical Application
Somu, P., & Paul, S. (2019) · Heat shock proteins · doi:10.1007/978-3-030-23158-3_8 · Cited by 5
Targeting Hsp90 with FS-108 circumvents gefitinib resistance in EGFR mutant non-small cell lung cancer cells
Wang, Y.-Q., Shen, A., Sun, J., Wang, X., Liu, H., Zhang, M., Chen, D.-Q., Xiong, B., Shen, J., Geng, M., et al. (2016) · Acta Pharmacologica Sinica · doi:10.1038/aps.2016.85 · Cited by 5
Recent progress and structural insights of potential Hsp90 inhibitors as anticancer agents
Singh, A., Maity, S., Devi, P., Rai, A., & Asati, V. (2025) · Molecular Diversity · doi:10.1007/s11030-025-11160-3 · Cited by 5
Heat shock protein 90α inhibitor, PU-H71 in combination with DHEA promoting apoptosis in triple-negative breast cancer cell line MDA-MB-231
Soudan, H., Saeed, H. M. S., Demellawy, M. E., Shalaby, M. A., Hassan, M., Elkewedi, M., & El-Nikhely, N. A. (2020) · Acta Biochimica Polonica · doi:10.18388/abp.2020_5418 · Cited by 4
“Cancer cells rely on the molecular chaperones to survive as well as to acquire and maintain their malignant phenotype through the proper folding of the client proteins responsible for these functions (Sidera & Patsavoudi, 2014).”
Background
Combination Treatment of Withalongolide a Triacetate with Cisplatin Induces Apoptosis by Targeting Translational Initiation, Migration, and Epithelial to Mesenchymal Transition in Head and Neck Squamous Cell Carcinoma
Subramanian, C., Spielbauer, K. K., Pearce, R. E., Kovatch, K. J., Prince, M. E., Timmermann, B. N., & Cohen, M. S. (2022) · Nutrients · doi:10.3390/nu14245398 · Cited by 4
Disruption of Proteostasis by Natural Products and Synthetic Compounds That Induce Pervasive Unfolding of Proteins: Therapeutic Implications
Vilaboa, N. E., López, J. A., de Mesa, M., Escudero-Duch, C., Winfield, N., Bayford, M., & Voellmy, R. W. (2023) · Pharmaceuticals · doi:10.3390/ph16040616 · Cited by 4
“Another approach, inhibition of major chaperone HSP90, has not produced potent anti-tumor responses in multiple clinical trials [7,8].”
Background
Computational Studies of Allosteric Regulation in the Hsp90 Molecular Chaperone: From Functional Dynamics and Protein Structure Networks to Allosteric Communications and Targeted Anti‐Cancer Modulators
Verkhivker, G. M. (2014) · Israel Journal of Chemistry · doi:10.1002/ijch.201300143 · Cited by 4
Molecular Chaperone Inhibitors
Moses, M. A., Zuehlke, A. D., & Neckers, L. (2018) · Springer eBooks · doi:10.1007/978-3-319-69042-1_2 · Cited by 5
HDN-1 induces cell differentiation toward apoptosis in promyelocytic leukemia cells depending on its selective effect on client proteins of Hsp90
Qi, X., Zhang, X., Liu, X., Tang, W., Dai, J., Chen, A., Lin, Q., Zhu, T., & Li, J. (2021) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2021.115459 · Cited by 4
The lonidamine derivative H2-gamendazole reduces cyst formation in polycystic kidney disease
Sundar, S. V., Zhou, J. X., Magenheimer, B. S., et al. (2022) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00095.2022 · 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
Therapeutic Potential of Heat Shock Protein 90 Inhibitors, Geldanamycin, and Analog Compounds in Precision Cancer Therapy
Alzebari, A. M., Qadir, A. M., Rafaat, M. S., et al. (2023) · BioMed Target Journal · doi:10.59786/bmtj.122 · Cited by 3
“Nevertheless, Infinity has discontinued the progress of this medication because of many limitations, such as unfavorable pharmaceutical characteristics, including limited solubility and challenges in administering the appropriate dosage 143 .”
Background
High-throughput screening system for inhibitors of human Heat Shock Factor 2
Smith, L. M., Bhattacharya, D., Williams, D. J., et al. (2015) · Cell Stress and Chaperones · doi:10.1007/s12192-015-0605-0 · Cited by 3
“The greatest successes in the hunt for inhibitors of the molecular chaperone system are several inhibitors of the major molecular chaperone HSP90 (Sidera and Patsavoudi 2014; Whitesell et al. 2012; Xiao et al. 2006).”
Background
HSP90: A Key Player in Metal-Induced Carcinogenesis?
Abreu, P. L., Ferreira, L. M. R., Cunha‐Oliveira, T., Alpoim, M. C., & Urbano, A. M. (2019) · Heat shock proteins · doi:10.1007/978-3-030-23158-3_11 · Cited by 4
Small Molecule Screening Identifies HSP90 as a Modifier of RNA Foci in Myotonic Dystrophy Type 1
Johnson, S. J., Johnson, H. L., Powell, R. T., STEPHAN, C. C., Stossi, F., & Cooper, T. A. (2024) · Molecular and Cellular Biology · doi:10.1080/10985549.2024.2408025 · Cited by 2
HSP90/PUS7/THUMPD1 promotes metastasis and cisplatin resistance in gastric cancer cells
Ye, Z., He, J., Zuo, R., et al. (2025) · Scientific Reports · doi:10.1038/s41598-025-20167-7 · Cited by 2
The evolution of heat shock protein 90 C-terminal inhibitors: From novobiocin to potential clinical candidates
Jiang, X., & Blagg, B. S. J. (2026) · Cell Stress and Chaperones · doi:10.1016/j.cstres.2026.100165 · Cited by 3
“…signal transduction proteins (eg., Bcr-Abl, Alk, Braf, and Akt), transcription factors (eg., androgen receptors and HIF1α), cell cycle regulatory proteins (eg., Cdk4, Rb, and cyclin D), and antiapoptotic proteins (eg., Bcl2 and survivin), 39 many of which are associated with the ten hallmarks.”
HSP90 inhibitor CH5164840 induces micronuclei in TK6 cells via an aneugenic mechanism
Matsuzaki, K., Harada, A., Tanaka, K., Takeiri, A., & Mishima, M. (2014) · Mutation Research/Genetic Toxicology and Environmental Mutagenesis · doi:10.1016/j.mrgentox.2014.08.002 · Cited by 2
Role of Heat Shock Protein 90 in Regulating Downstream Signal Transduction Cascades
Lei, W., Duron, D. I., Stine, C., & Streicher, J. M. (2019) · Heat shock proteins · doi:10.1007/978-3-030-03952-3_9 · 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
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
The Candida albicans Hsp90 Chaperone Network Is Environmentally Flexible and Evolutionarily Divergent
Diezmann, S., & Cowen, L. E. (2014) · Springer eBooks · doi:10.1007/978-1-4939-1130-1_8 · Cited by 1
“The intricate liaison between Hsp90 and cancer proteins is being exploited for the development of anticancer therapeutics, and there are currently 13 Hsp90 inhibitors in clinical trials for the treatment of diverse cancers [15].”
Background
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
Targeting Hsp-90 Related Disease Entities for Therapeutic Development
Westlake, T. J., Sun, M., Rosenblum, B. C., Zhuang, Z., & Rosenblum, J. S. (2019) · Heat shock proteins · doi:10.1007/978-3-030-23158-3_10 · Cited by 1
Screening Technique for Heat Shock Protein 90 Inhibitors from Natural Products
Hu, Y., Zhang, X. J., Yang, X. T., Tang, Y. Y., Hu, L. Y., & Zhu, D. (2019) · Heat shock proteins · doi:10.1007/978-3-030-23158-3_19 · Cited by 1
Potential of HSP90 Inhibitors to Treat Neurofibromatosis-Related Tumors
Vitte, J., & Giovannini, M. (2015) · Heat shock proteins · doi:10.1007/978-3-319-17211-8_13
Allosteric Modulators of Heat Shock Protein 90 (HSP90)
Koay, Y. C., & McAlpine, S. R. (2016) · Royal Society of Chemistry eBooks · doi:10.1039/9781782629276-00404
Heat Shock Protein 90 c-Terminal Inhibitors in Cancer Treatment
Tutar, Y. (2015) · International Journal of Pharmaceutical Sciences and Developmental Research · doi:10.17352/ijpsdr.000001
“Hsp90 is essential for cancer cell survival and tumor progression pathways, therefore; Hsp90 inhibition has been remarkable anti-cancer drug target in oncology [2-4].”
Background

Authors: Sidera, K., & Patsavoudi, E.
Affiliations: Pasteur Hellenic Institute (GR)
Venue: Recent Patents on Anti-Cancer Drug Discovery
Publisher: Bentham Science Publishers Ltd.
Published: 2013-12-13
Volume: 9
Issue: 1
Pages: 1-20
ISSN: 1574-8928 (ISSN-L)
DOI: 10.2174/15748928113089990031
OpenAlex: W4245469960
Cited by: 222
References: 0
Citations by year: 2026: 3 · 2025: 7 · 2024: 8 · 2023: 17 · 2022: 14 · 2021: 28 · 2020: 21 · 2019: 31 · 2018: 18 · 2017: 19 · 2016: 28 · 2015: 19 · 2014: 8 · 2013: 1
FWCI: 8.35
Type: journal article
Language: en
Open access: closed
Locations: Recent Patents on Anti-Cancer Drug Discovery (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
Keywords: Hsp90 inhibitors, HSP90, molecular chaperones, cancer therapeutics, 17-AAG, drug discovery, clinical trials, patents, transformed phenotype, signal transduction, cell surface

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HSP90 Inhibitors: Current Development and Potential in Cancer Therapy

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