about
Quantitative analysis of HSP90-client interactions reveals principles of substrate recognitionTel2 structure and function in the Hsp90-dependent maturation of mTOR and ATR complexesApigenin inhibits proliferation and induces apoptosis in human multiple myeloma cells through targeting the trinity of CK2, Cdc37 and Hsp90Heat shock proteins at the crossroads between cancer and Alzheimer's diseaseThe human Cdc37.Hsp90 complex studied by heteronuclear NMR spectroscopyHeat shock proteins and heat shock factor 1 in carcinogenesis and tumor development: an updateCanonical and kinase activity-independent mechanisms for extracellular signal-regulated kinase 5 (ERK5) nuclear translocation require dissociation of Hsp90 from the ERK5-Cdc37 complexOverexpression of C-MYC oncogene in prostate cancer predicts biochemical recurrence.FW-04-806 inhibits proliferation and induces apoptosis in human breast cancer cells by binding to N-terminus of Hsp90 and disrupting Hsp90-Cdc37 complex formation.Hsp90/Cdc37 chaperone/co-chaperone complex, a novel junction anticancer target elucidated by the mode of action of herbal drug Withaferin ACell surface Cdc37 participates in extracellular HSP90 mediated cancer cell invasionIdentification of regulators of the innate immune response to cytosolic DNA and retroviral infection by an integrative approach.Heat shock proteins in breast cancer progression--a suitable case for treatment?Heat shock proteins and cancer vaccines: developments in the past decade and chaperoning in the decade to comeThe oncogenic role of the cochaperone Sgt1Identification of a DYRK1A Inhibitor that Induces Degradation of the Target Kinase using Co-chaperone CDC37 fused with Luciferase nanoKAZ.Molecular chaperones in mammary cancer growth and breast tumor therapyCombined HSP90 and kinase inhibitor therapy: Insights from The Cancer Genome Atlas.Systematic identification of the HSP90 candidate regulated proteome.Anti-cancer activity of withaferin A in B-cell lymphoma.Heat Shock Proteins Promote Cancer: It's a Protection RacketSilencing the cochaperone CDC37 destabilizes kinase clients and sensitizes cancer cells to HSP90 inhibitorsThe chaperones Hsp90 and Cdc37 mediate the maturation and stabilization of protein kinase C through a conserved PXXP motif in the C-terminal tail.New developments in Hsp90 inhibitors as anti-cancer therapeutics: mechanisms, clinical perspective and more potential.Hsp90, an unlikely ally in the war on cancer.The shock of aging: molecular chaperones and the heat shock response in longevity and aging--a mini-review.Targeting Hsp90 with FS-108 circumvents gefitinib resistance in EGFR mutant non-small cell lung cancer cells.Alternate strategies of Hsp90 modulation for the treatment of cancer and other diseases.Molecular cochaperones: tumor growth and cancer treatment.The Mysterious Ways of ErbB2/HER2 TraffickingRole and Regulation of Myeloid Zinc Finger Protein 1 in Cancer.Restricting direct interaction of CDC37 with HSP90 does not compromise chaperoning of client proteinsCancer and necroptosis: friend or foe?The eNOS signalosome and its link to endothelial dysfunction.Novel celastrol derivatives inhibit the growth of hepatocellular carcinoma patient-derived xenografts.Optimisation of Downscaled Tandem Affinity Purifications to Identify Core Protein Complexes.Disruption of Heat Shock Protein 90 (Hsp90)-Protein Kinase Cδ (PKCδ) Interaction by (-)-Maackiain Suppresses Histamine H1 Receptor Gene Transcription in HeLa Cells.In vivo identification of regulators of cell invasion across basement membranes.Suppressing the CDC37 cochaperone in hepatocellular carcinoma cells inhibits cell cycle progression and cell growth.Tumor heterogeneity, clonal evolution, and therapy resistance: an opportunity for multitargeting therapy.
P2860
Q24297748-79E50543-A9E9-464F-BD8C-AA16C0445A3DQ24297874-6C67CDD5-3303-4C51-9059-1D3955EC7539Q24336102-15B4DB59-FF57-40B6-82C4-50D7EAC01F87Q26864311-54DA90CC-5ECB-470B-9BC8-D9E7146F594FQ27653114-A227C12D-B85D-4134-8BDC-D94705A2BE18Q28272905-3E240B1B-6D57-4ECA-B6FB-DB6B494493BDQ28854310-63601C0E-B859-4BCC-ADEE-8C0CFED9828AQ33685303-99B69E3C-CDD9-43E5-8288-37FED32BADC9Q33817522-F01447E1-7E55-41A3-8D66-FD676165D2EBQ33826976-6D1BDA92-584F-4B4F-BB8B-76303E4B4692Q34388870-67957B56-07B6-4AA6-A951-326FD79593CDQ34522027-97863D5C-BA8E-41B7-86BA-F7BFD342900EQ35070272-AD5F56ED-E709-41FF-97E9-84BE95D47781Q35624884-0954BD2B-4F46-42B7-8094-7A73AF8F2FF3Q35668922-AAD28449-9611-4F51-8393-C659CA3BB0C1Q35733743-2E2ADE50-8ACD-4429-B1CB-D1C1B0DE2655Q35843133-EE237A1F-9192-4539-A78D-BC7032FDA5ACQ35930811-8836FB8F-0663-433A-AADF-97A356788376Q36209058-72EBF73D-F134-4129-B7DA-441A2314451DQ36213500-59088597-00DF-457B-9C1D-E2C0E2A2520FQ37013952-FFEED325-457B-45C5-8E86-56B27A332F0EQ37083059-AD18CA35-4DC9-4EF1-907A-04BDD564700AQ37099170-68B96E40-3EBA-4ABD-80C5-A329AC4C2CDCQ37215989-7ABF809F-51BE-46AC-9A7A-71E54480D67CQ37274497-EE5939A3-35C6-483D-9BEC-A186146AAB32Q37527534-812F258E-C9FF-45A1-B47A-A98F681E89D2Q37603214-462CAFB6-E9EE-4418-99CD-DD881996AD5DQ37622446-5CC0C098-2357-4948-8E73-BB4D527C0D40Q38166376-219E8466-83A5-4EF2-ACA8-1B9EC25A3DECQ38237727-071D5F49-5810-41D2-BAE9-610BF3D435EFQ38436667-8CBF5288-A6B2-4CB3-BB8C-7E16C7B8EBBBQ38725015-1FC2FB4F-AA27-4989-9A3D-0DCB1AA66283Q38799139-F42F8902-B775-4AC6-88D9-1B42B3A8C1A0Q38835675-D4F4DB76-0E79-4DB7-894C-E890FF273AE9Q38972744-27DEA374-6A78-4530-B013-8B2816D06A98Q39357505-A3613D40-BADA-4F2C-8C5C-AEBCD8735CFCQ40517760-3E06919E-ADC0-4C20-B039-2019E31B4982Q41929985-FCCBFDB5-EFA3-43CE-881C-7B23FEE61121Q42202989-E71F6B59-BF91-4CB0-8529-4ED5A15F3C7FQ42722265-D39766A2-A453-4F1E-AB0B-6183D9201105
P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 30 May 2008
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Targeting the oncogene and kinome chaperone CDC37.
@en
Targeting the oncogene and kinome chaperone CDC37.
@nl
type
label
Targeting the oncogene and kinome chaperone CDC37.
@en
Targeting the oncogene and kinome chaperone CDC37.
@nl
prefLabel
Targeting the oncogene and kinome chaperone CDC37.
@en
Targeting the oncogene and kinome chaperone CDC37.
@nl
P2093
P2860
P356
P1476
Targeting the oncogene and kinome chaperone CDC37.
@en
P2093
Jinrong Cheng
Mary Ann Stevenson
Phillip J Gray
Stuart K Calderwood
Thomas Prince
P2860
P2888
P304
P356
10.1038/NRC2420
P407
P577
2008-05-30T00:00:00Z