A phase I study of the heat shock protein 90 inhibitor alvespimycin (17-DMAG) given intravenously to patients with advanced solid tumors
about
Targeting Cell Survival Proteins for Cancer Cell DeathHeat shock protein 90 targeting therapy: state of the art and future perspectiveHsp90: A New Player in DNA Repair?Maximizing the Therapeutic Potential of HSP90 InhibitorsAdvances in the clinical development of heat shock protein 90 (Hsp90) inhibitors in cancersTargeting the adaptive molecular landscape of castration-resistant prostate cancerHeat shock and other apoptosis-related proteins as therapeutic targets in prostate cancerCo-Crystalization and In Vitro Biological Characterization of 5-Aryl-4-(5-Substituted-2-4-Dihydroxyphenyl)-1,2,3-Thiadiazole Hsp90 InhibitorsC-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balancesRegulation and function of the human HSP90AA1 geneThe HSP90 inhibitor NVP-AUY922 radiosensitizes by abrogation of homologous recombination resulting in mitotic entry with unresolved DNA damage19-substituted benzoquinone ansamycin heat shock protein-90 inhibitors: biological activity and decreased off-target toxicity.Comprehensive analysis of published studies involving systemic treatment for chondrosarcoma of bone between 2000 and 2013.Getting folded: chaperone proteins in muscle development, maintenance and disease.Phase I dose-escalation study of the HSP90 inhibitor AUY922 in Japanese patients with advanced solid tumors.Heat shock protein 90 inhibitors in the treatment of cancer: current status and future directionsInhibition of heat shock protein 90 alleviates steatosis and macrophage activation in murine alcoholic liver injury.A physiologically based pharmacokinetic model of alvespimycin in mice and extrapolation to rats and humans.A first in human, safety, pharmacokinetics, and clinical activity phase I study of once weekly administration of the Hsp90 inhibitor ganetespib (STA-9090) in patients with solid malignancies.Hsp90 molecular chaperone inhibitors: are we there yet?Treatment of Bone TumorsHsp90 inhibitors and drug resistance in cancer: the potential benefits of combination therapies of Hsp90 inhibitors and other anti-cancer drugs17-ABAG, a novel geldanamycin derivative, inhibits LNCaP-cell proliferation through heat shock protein 90 inhibition.Inhibition of heat shock protein (molecular weight 90 kDa) attenuates proinflammatory cytokines and prevents lipopolysaccharide-induced liver injury in mice.HSP90 inhibitors decrease AID levels and activity in mice and in human cells.Population pharmacokinetic analysis of 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG) in adult patients with solid tumors.Combination therapy with HSP90 inhibitor 17-DMAG reconditions the tumor microenvironment to improve recruitment of therapeutic T cells.CPUY201112, a novel synthetic small-molecule compound and inhibitor of heat shock protein Hsp90, induces p53-mediated apoptosis in MCF-7 cells.Tumor-intrinsic and tumor-extrinsic factors impacting hsp90- targeted therapy.In vivo fluorescence lifetime imaging for monitoring the efficacy of the cancer treatment.Hypoxia attenuates Hsp90 inhibitor 17-DMAG-induced cyclin B1 accumulation in hepatocellular carcinoma cells.Molecular targets and mechanisms of radiosensitization using DNA damage response pathways.Potent antitrypanosomal activities of heat shock protein 90 inhibitors in vitro and in vivo.Clinical presentation, pathogenesis, diagnosis, and treatment of epidermolysis bullosa acquisitaDestabilization of the epidermal growth factor receptor (EGFR) by a peptide that inhibits EGFR binding to heat shock protein 90 and receptor dimerization.A purine scaffold HSP90 inhibitor BIIB021 has selective activity against KSHV-associated primary effusion lymphoma and blocks vFLIP K13-induced NF-κB.Heat shock protein 90 is critical for regulation of phenotype and functional activity of human T lymphocytes and NK cells.Reduced Contractility and Motility of Prostatic Cancer-Associated Fibroblasts after Inhibition of Heat Shock Protein 90Chemical signatures and new drug targets for gametocytocidal drug development.Hsp90 inhibition protects against inherited retinal degeneration.
P2860
Q26765447-4F6FA796-014A-4455-A828-9B2B02E82BE0Q26776302-36D601D5-512D-4B11-9D11-DA1C8989A813Q26778944-BDBD1835-B29C-4CDF-A309-C32B47EA9858Q26798318-8D64878F-82F8-48AD-BB83-62ABE9F5ACCCQ27022514-FF6DDE5A-D4BE-4067-A75B-73AB8465B0FAQ27022821-D91987D7-DA97-4203-8FF1-B387BE5849FAQ27026128-BF97C966-75E6-48A2-9C02-6581FB3E1E5BQ27673253-E1E4EFD5-976B-4500-B0EC-0D198A017E9BQ28271643-AA43ECB6-CA68-46D6-9288-6A57A86E97A6Q28646043-87F7FB1D-A450-48CF-89AC-598079760BDCQ28730558-AF1C02CB-D164-4C84-8622-2D6E15EDF1BEQ33584583-12249116-50B8-40A8-A62E-8EC12FFF4E19Q34038664-96719C99-BCA4-4328-ABCB-EFB9C58B2373Q34055646-C9B9AD30-60C3-4E1A-9215-DD186B82FE67Q34085148-E826E814-B026-43C0-92F6-482A1AA7F790Q34164027-C01C8A9C-2F60-4FD2-AE53-A63A5DA91812Q34216745-A98FDA2C-74EA-45CE-A42A-417D109F542BQ34570770-85029695-504C-4B64-8834-E12CA225CE91Q34636437-4951F6FF-DD8A-4FDB-9F37-BA6A1CDA758FQ35655105-BBF424E2-C836-4714-BAFD-8D3DF7323656Q35740708-9DDC760F-1B99-454C-9202-1BA630ADB42BQ35823157-A1C3B5E6-9947-4FD5-B653-97F28D0966E2Q35849973-CFEB6376-E41A-4EFD-B350-D1DC7DD362CAQ35930087-9B8334D4-FF88-4668-8256-E1B7FA01C75CQ35952172-54BE8262-8AB3-4B29-86A4-030C9AA3E027Q36060751-A081869B-5F2B-42B1-95E9-088B497E74D1Q36074307-0829C4FE-7865-41DA-8C09-404E621B1C90Q36442900-3742FD94-D4F2-44AB-9CF5-61FE80C8609FQ36465517-7F1B55BF-4969-4BDD-A6F9-D7DB85CF6BE6Q36647014-1A40222B-F412-46D6-A214-F84D238FA8C5Q36674083-51929DD4-8A84-416C-8D44-761379D60A2DQ36792626-E81DDE0A-F5F9-4933-B776-5A1A7A38B1A6Q36974927-7ABE566C-34DF-4BB2-BEA6-437261AF23B4Q37055162-04763923-EFCA-41CF-A890-FA1A12C05DB6Q37168481-603A0904-90CB-40C7-B581-0E8728DB46B4Q37245887-55694B53-0ADD-4BDE-B9DE-FB230D0E9FEFQ37286051-60BD4D49-B9EC-4C5E-9F2E-BF980AEA44E7Q37293806-408996F5-8582-41F1-801C-4B1D057175A8Q37489274-DBABED7C-61DF-47F4-A953-310C95D30C39Q37649115-1A18F21C-3A67-46B6-9729-97DCA38ADDBA
P2860
A phase I study of the heat shock protein 90 inhibitor alvespimycin (17-DMAG) given intravenously to patients with advanced solid tumors
description
2011 nî lūn-bûn
@nan
2011 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մարտին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
A phase I study of the heat sh ...... nts with advanced solid tumors
@ast
A phase I study of the heat sh ...... nts with advanced solid tumors
@en
A phase I study of the heat sh ...... nts with advanced solid tumors
@nl
type
label
A phase I study of the heat sh ...... nts with advanced solid tumors
@ast
A phase I study of the heat sh ...... nts with advanced solid tumors
@en
A phase I study of the heat sh ...... nts with advanced solid tumors
@nl
prefLabel
A phase I study of the heat sh ...... nts with advanced solid tumors
@ast
A phase I study of the heat sh ...... nts with advanced solid tumors
@en
A phase I study of the heat sh ...... nts with advanced solid tumors
@nl
P2093
P2860
P3181
P1476
A phase I study of the heat sh ...... nts with advanced solid tumors
@en
P2093
Anna Zetterlund
Anthea Hardcastle
Belle Roels
Florence Raynaud
Heidi Peachey
Hendrik-Tobias Arkenau
Ian Judson
Javier Moreno-Farre
Johan S de Bono
Martin M Eatock
P2860
P304
P3181
P356
10.1158/1078-0432.CCR-10-1927
P407
P50
P577
2011-03-15T00:00:00Z