Hsp90 Inhibition Depletes Chk1 and Sensitizes Tumor Cells to Replication Stress
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference73 articles.
1. Structure, function, and mechanism of the Hsp90 molecular chaperone
2. Hsp90 inhibitors as novel cancer chemotherapeutic agents
3. Regulation of Signaling Protein Function and Trafficking by the hsp90/hsp70-Based Chaperone Machinery
4. Identification and Structural Characterization of the ATP/ADP-Binding Site in the Hsp90 Molecular Chaperone
5. The Amino-terminal Domain of Heat Shock Protein 90 (hsp90) That Binds Geldanamycin Is an ATP/ADP Switch Domain That Regulates hsp90 Conformation
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1. SIRT1 and HSP90α feed-forward circuit safeguards chromosome segregation integrity in diffuse large B cell lymphomas;Cell Death & Disease;2023-10-11
2. Heat shock protein 90 inhibitor 17-AAG down-regulates thymidine phosphorylase expression and potentiates the cytotoxic effect of tamoxifen and erlotinib in human lung squamous carcinoma cells;Biochemical Pharmacology;2022-10
3. Molecular chaperones in DNA repair mechanisms: Role in genomic instability and proteostasis in cancer;Life Sciences;2022-10
4. Targeting HSP90 as a Novel Therapy for Cancer: Mechanistic Insights and Translational Relevance;Cells;2022-09-06
5. The HSP90 inhibitor KW-2478 depletes the malignancy of BCR/ABL and overcomes the imatinib-resistance caused by BCR/ABL amplification;Experimental Hematology & Oncology;2022-05-27
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