Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones
about
Combinatorial drug design targeting multiple cancer signaling networks controlled by mitochondrial Hsp90Heat shock transcription factor 1 as a therapeutic target in neurodegenerative diseasesAtomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinaseCdc37 has distinct roles in protein kinase quality control that protect nascent chains from degradation and promote posttranslational maturationSystematic Mutant Analyses Elucidate General and Client-Specific Aspects of Hsp90 FunctionHsp90-dependent assembly of the DBC2/RhoBTB2-Cullin3 E3-ligase complexThe HSP90 inhibitor NVP-AUY922 radiosensitizes by abrogation of homologous recombination resulting in mitotic entry with unresolved DNA damageRegulation of stress-inducible phosphoprotein 1 nuclear retention by protein inhibitor of activated STAT PIAS1.Celastrol inhibits Hsp90 chaperoning of steroid receptors by inducing fibrillization of the Co-chaperone p23Hsp90-Sgt1 and Skp1 target human Mis12 complexes to ensure efficient formation of kinetochore-microtubule binding sites.The BAG-1 isoform BAG-1M regulates keratin-associated Hsp70 chaperoning of aPKC in intestinal cells during activation of inflammatory signaling.Heat shock protein 90 inhibition depletes LATS1 and LATS2, two regulators of the mammalian hippo tumor suppressor pathway.Phase I and pharmacological study of cytarabine and tanespimycin in relapsed and refractory acute leukemia.An acetylation site in the middle domain of Hsp90 regulates chaperone function.Functioning of the Hsp90 machine in chaperoning checkpoint kinase I (Chk1) and the progesterone receptor (PR).Gedunin inactivates the co-chaperone p23 protein causing cancer cell death by apoptosis.Structural and functional basis of protein phosphatase 5 substrate specificity.90-kDa heat shock protein inhibition abrogates the topoisomerase I poison-induced G2/M checkpoint in p53-null tumor cells by depleting Chk1 and Wee1.New developments in Hsp90 inhibitors as anti-cancer therapeutics: mechanisms, clinical perspective and more potential.A small molecule cell-impermeant Hsp90 antagonist inhibits tumor cell motility and invasion.Designed Hsp90 heterodimers reveal an asymmetric ATPase-driven mechanism in vivo.HSP90 inhibition sensitizes head and neck cancer to platin-based chemoradiotherapy by modulation of the DNA damage response resulting in chromosomal fragmentation.Conformational dynamics of the molecular chaperone Hsp90Hsp90 and client protein maturation.Restricting direct interaction of CDC37 with HSP90 does not compromise chaperoning of client proteinsEffects of selective checkpoint kinase 1 inhibition on cytarabine cytotoxicity in acute myelogenous leukemia cells in vitro.Anti-tumor activity of the HSP90 inhibitor SNX-2112 in pediatric cancer cell lines.ATP binding to Hsp90 is sufficient for effective chaperoning of p53 protein.Ydj1 protects nascent protein kinases from degradation and controls the rate of their maturation.Hop cleavage and function in granzyme B-induced apoptosis.How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches.UNC45A localizes to centrosomes and regulates cancer cell proliferation through ChK1 activation.Rescue of atypical protein kinase C in epithelia by the cytoskeleton and Hsp70 family chaperones.Dimerization of Hsp90 is required for in vivo function. Design and analysis of monomers and dimers.Evidence for Hsp90 Co-chaperones in Regulating Hsp90 Function and Promoting Client Protein Folding.Hsp90α regulates ATM and NBN functions in sensing and repair of DNA double-strand breaks.Multiplexed Proteome Dynamics Profiling Reveals Mechanisms Controlling Protein Homeostasis.Hsp90 Is Essential for Chl1-Mediated Chromosome Segregation and Sister Chromatid Cohesion.Hsp90 charged-linker truncation reverses the functional consequences of weakened hydrophobic contacts in the N domain
P2860
Q24647585-DE934534-20FB-4573-892D-13AA8A7DAFC8Q27026884-6EF6C00F-C2F6-4009-850C-968D6D14EAD5Q27713462-CBF79FDC-72CF-497D-A86B-D5DA1A62EF98Q27938495-406E2206-3E05-4746-B082-BF623D301774Q27939655-775E69D2-25E1-4BA3-835B-2A27E71C8F40Q28540619-6926A4CD-829A-4962-A291-19082F7CDBDEQ28730558-401988D5-1BB1-4220-9D08-E91DAC36D37EQ30409858-5C78C0F3-1B2A-4EA9-B809-A3D9F3E57A0AQ33662410-980A83B5-CDA7-449C-86D6-5F151533ACB1Q33799179-0A5B8869-B51C-46AD-B102-D46A6CFEF4ACQ34043240-7DBE8190-F028-4C86-BCE0-E2D160F75093Q34268075-3CBAB925-831B-411B-8457-0117EF322C5EQ35528633-085B19BC-9D56-4E16-9F06-661C7AD4BDB0Q35729439-7B38CC1E-351E-47C4-BE87-2B747FCB8F12Q36259346-007AC8ED-07E4-4340-AFD2-C5144668A935Q36666275-4E4F4116-9F38-411E-A534-5D3139C4B9F4Q37181747-7212FD5A-35F9-4DBF-83AF-6774FAE72058Q37199458-128C4CF5-2542-40CF-8E1B-E9B2BA7E68AEQ37215989-5A345EAC-2C4D-4620-BEA2-49186AD984B9Q37369580-DE511A88-FFF6-4573-AFA8-15150F2DB3A1Q37582269-2B2179BB-2720-4780-BFD5-1B98B61C753BQ37615630-109C6790-BE5A-46E1-A5BD-77484C451BEFQ37854116-0314528D-F9BF-427E-983B-56A4ED910061Q37928519-76FF472B-829A-4448-A28A-36F4FD441459Q38725015-CCB75229-61CF-412D-8CF8-A4A37A5105EAQ39301264-3CB9D7AE-E590-4BB2-B77F-CDFC6CF779C5Q39499295-3D1F89B9-FBED-4002-AC7B-BA6D999DB5A8Q39670676-8629CBA0-3AE1-4DE2-82B9-E9B89B3CFDB6Q39768529-5250B512-C28E-4302-90BD-C06B0D4AC44BQ40226952-5BECC829-9D6E-46BE-A9E1-401D2041844CQ41596905-EDA26313-D6C9-4563-8C5D-510219A45DDEQ42116121-11130001-A4F2-436D-A876-4DCB7A0C5E63Q43102403-155FAE80-164F-4619-80E7-1C7FC7288AB9Q46972334-175CCDC9-ED79-4D8D-8CCE-75C29A838E99Q47362455-5F064E37-EE0B-4CC9-9DA7-A3A8874551D1Q50934451-DF801AA2-D290-424C-86B3-7D29432202C0Q52725933-81BEE58A-DAD4-436B-8D9D-603DC5FE704FQ55364966-D894DF35-D56F-4552-B57E-A8974E2E6F25Q58360990-F3494CC6-1BDD-49AF-94AC-4602C1BCD88B
P2860
Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones
description
2006 nî lūn-bûn
@nan
2006 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones
@ast
Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones
@en
Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones
@en-gb
Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones
@nl
type
label
Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones
@ast
Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones
@en
Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones
@en-gb
Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones
@nl
prefLabel
Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones
@ast
Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones
@en
Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones
@en-gb
Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones
@nl
P2093
P2860
P356
P1476
Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones
@en
P2093
Bridget Stensgard
David O Toft
Jill M Wagner
Larry M Karnitz
Sara J Felts
Sonnet J H Arlander
P2860
P304
P356
10.1074/JBC.M508687200
P407
P577
2006-02-03T00:00:00Z