HSP90 inhibitors: current development and potential in cancer therapy.
about
Review: The HSP90 molecular chaperone-an enigmatic ATPaseMutant p53: One, No One, and One Hundred ThousandHeat shock protein 90 targeting therapy: state of the art and future perspectiveThe G protein α chaperone Ric-8 as a potential therapeutic targetProposal of Dual Inhibitor Targeting ATPase Domains of Topoisomerase II and Heat Shock Protein 90Small Molecule Inhibitors to Disrupt Protein-protein Interactions of Heat Shock Protein 90 Chaperone MachineryEntamoeba Encystation: New Targets to Prevent the Transmission of AmebiasisGambogic acid identifies an isoform-specific druggable pocket in the middle domain of Hsp90βTargeting highly expressed extracellular HSP90 in breast cancer stem cells inhibits tumor growth in vitro and in vivo.Small molecule inhibitor screening identifified HSP90 inhibitor 17-AAG as potential therapeutic agent for gallbladder cancer.The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative DiseasesEffect of a heat shock protein 90-specific inhibitor on the proliferation and apoptosis induced by VEGF-C in cervical cancer cellsInduced protein degradation: an emerging drug discovery paradigm.Inactivation of multiple bacterial histidine kinases by targeting the ATP-binding domain.Synthesis, stereochemical analysis, and derivatization of myricanol provide new probes that promote autophagic tau clearance.FS-93, an Hsp90 inhibitor, induces G2/M arrest and apoptosis via the degradation of client proteins in oncogene addicted and derived resistant cancer cells.High-throughput screening system for inhibitors of human Heat Shock Factor 2.Everolimus downregulates estrogen receptor and induces autophagy in aromatase inhibitor-resistant breast cancer cells.Selection Transforms the Landscape of Genetic Variation Interacting with Hsp90.Dynamic proteomics reveals bimodal protein dynamics of cancer cells in response to HSP90 inhibitorThe HSP90 inhibitor 17-PAG effectively inhibits the proliferation and migration of androgen-independent prostate cancer cellsGeldanamycin induces apoptosis in human gastric carcinomas by affecting multiple oncogenic kinases that have synergic effects with TNF-related apoptosis-inducing ligand.Targeting heat-shock protein 90 with ganetespib for molecularly targeted therapy of gastric cancerNovel HSP90 inhibitors effectively target functions of thyroid cancer stem cell preventing migration and invasionHSP90 activity is required for MLKL oligomerisation and membrane translocation and the induction of necroptotic cell death.Molecular imaging of EGFR and CD44v6 for prediction and response monitoring of HSP90 inhibition in an in vivo squamous cell carcinoma modelRic-8A gene deletion or phorbol ester suppresses tumorigenesis in a mouse model of GNAQ(Q209L)-driven melanoma.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 vivoNon-benzoquinone geldanamycin analogs trigger various forms of death in human breast cancer cells.Reduced Contractility and Motility of Prostatic Cancer-Associated Fibroblasts after Inhibition of Heat Shock Protein 90Targeting Hsp90 with FS-108 circumvents gefitinib resistance in EGFR mutant non-small cell lung cancer cells.Prospective identification of resistance mechanisms to HSP90 inhibition in KRAS mutant cancer cells.Calpain Genetic Disruption and HSP90 Inhibition Combine To Attenuate Mammary Tumorigenesis.Chiral resolution and pharmacological characterization of the enantiomers of the Hsp90 inhibitor 2-amino-7-[4-fluoro-2-(3-pyridyl)phenyl]-4-methyl-7,8-dihydro-6H-quinazolin-5-one oxime.Alternative approaches to Hsp90 modulation for the treatment of cancer.Multidomain structure and correlated dynamics determined by self-consistent FRET networks.Mutational landscape of MCPyV-positive and MCPyV-negative Merkel cell carcinomas with implications for immunotherapy.Novobiocin Analogues That Inhibit the MAPK Pathway.Targeting protein quality control pathways in breast cancer.Novel C-Terminal Heat Shock Protein 90 Inhibitors (KU711 and Ku757) Are Effective in Targeting Head and Neck Squamous Cell Carcinoma Cancer Stem cells.
P2860
Q26753822-31E4C474-28E7-44FE-92B6-A8BBFD88B82DQ26770576-BB5736CB-B9E8-42BF-839B-4D76A9D3E288Q26776302-913525F7-0D79-49D1-A085-F5C4F05DD75AQ26824363-9982C5F4-088E-4874-A660-4FD123E547A0Q26997981-7A32B7CE-B321-4776-A1D8-87A0CBCAD4B9Q27022376-9AE32061-0C17-4117-B1D5-C3885D889859Q28069614-AB38132D-978F-49AF-9E07-56909A476CD3Q28829208-8474634A-443F-476A-955F-64FE3C652723Q30805174-C480C4A3-5D3E-4A36-9D08-FFBB2E1375CCQ33688577-E5FDEEC9-966E-45F8-81C1-9A09BD1F14C3Q33692255-EE9B1755-686D-4B40-902B-6FDE26BB5132Q34292365-E36625AE-8C2A-4A0E-BAE5-D81B971D0EB8Q34545841-516EF197-73A3-4707-A18F-F085A82F5960Q34992446-DDEAEE9C-ED98-4618-B1C6-E857F310E088Q35542753-92E9A069-C477-4A61-A2E9-CFA21DFA4D15Q35745004-014A627C-CFC8-4B2A-8D18-5B8081F82FF1Q35930818-C797BB90-F4AC-4EDC-81A1-D366352614D6Q36078905-9A5D8594-7CC8-42DB-A100-48BF8B0254EBQ36170641-669EAC38-C61C-48E2-B9BB-665CFAB23FA0Q36300140-D8708C9F-781C-4F68-8C77-DB5346D9E95BQ36309425-40015E89-AE84-4D1C-BD35-005E9282C8E9Q36334890-FBAE9BA9-CE1C-4B05-A274-1317422C1AAAQ36347106-9A119A1A-DBB0-4F3D-B028-47952D6842DCQ36451879-DB4E9BA9-6C84-425D-97BF-118295BC1F5AQ36751725-C1F320B2-5FA7-4467-AE92-7A69081AC1E6Q36762341-30D42A29-0A57-4BD9-9783-817547FE387DQ37096232-0829E12C-FA3C-47DD-95BA-1D804BD71954Q37142416-8D3CA9DF-7CEC-41B9-899A-EC7C8233C536Q37278393-D8076CB9-A4C5-4628-8375-AFE9C76C628EQ37293806-A786730E-E0B4-4B97-A031-2BC71F4A9E25Q37603214-8524A791-EDB8-438A-AAA7-A6C4E6E8172EQ37702589-65D2CF0C-0BA0-406A-A283-6EEEF3451F15Q38769105-9FE97E18-2558-4E5A-87C6-6A3CAA99C3AEQ39002157-E5B0FC86-33F4-4147-95F8-E04EB5C7E09EQ39103704-EA6D20C2-C924-4B62-86BD-C5B30BA37BDFQ39130356-BA9F5AD5-12DD-497F-AB99-141EF6704736Q39926027-630119ED-9700-49A3-AC9C-E1FB3284B81CQ42245370-E4373200-DB58-4F67-B396-1488F41B5235Q46087491-11D35A14-77F9-4128-BBBD-376CC675620AQ46420352-943FDAD0-43C6-48FB-A7BE-5A39822225CF
P2860
HSP90 inhibitors: current development and potential in cancer therapy.
description
2014 nî lūn-bûn
@nan
2014 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
HSP90 inhibitors: current development and potential in cancer therapy.
@ast
HSP90 inhibitors: current development and potential in cancer therapy.
@en
HSP90 inhibitors: current development and potential in cancer therapy.
@nl
type
label
HSP90 inhibitors: current development and potential in cancer therapy.
@ast
HSP90 inhibitors: current development and potential in cancer therapy.
@en
HSP90 inhibitors: current development and potential in cancer therapy.
@nl
prefLabel
HSP90 inhibitors: current development and potential in cancer therapy.
@ast
HSP90 inhibitors: current development and potential in cancer therapy.
@en
HSP90 inhibitors: current development and potential in cancer therapy.
@nl
P1476
HSP90 inhibitors: current development and potential in cancer therapy.
@en
P2093
Evangelia Patsavoudi
Katerina Sidera
P356
10.2174/157488980901140428100532
P577
2014-01-01T00:00:00Z