Structural basis for the inhibition of HSP70 and DnaK chaperones by small-molecule targeting of a C-terminal allosteric pocket
about
Hsp70 May Be a Molecular Regulator of Schistosome Host InvasionSubstrate-binding domain conformational dynamics mediate Hsp70 allosteryClose and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiPA novel Hsp70 inhibitor prevents cell intoxication with the actin ADP-ribosylating Clostridium perfringens iota toxinA fragment-based approach applied to a highly flexible target: Insights and challenges towards the inhibition of HSP70 isoforms.An RNA aptamer specific to Hsp70-ATP conformation inhibits its ATPase activity independent of Hsp40.Mutations in the Yeast Hsp70, Ssa1, at P417 Alter ATP Cycling, Interdomain Coupling, and Specific Chaperone Functions.Nanomechanics of the substrate binding domain of Hsp70 determine its allosteric ATP-induced conformational change.HSP70 Inhibition Limits FAK-Dependent Invasion and Enhances the Response to Melanoma Treatment with BRAF Inhibitors.The Hsp70 interdomain linker is a dynamic switch that enables allosteric communication between two structured domains.Structural and Biological Interaction of hsc-70 Protein with Phosphatidylserine in Endosomal Microautophagy.Inhibition of stress-inducible HSP70 impairs mitochondrial proteostasis and function.Efficacy of the HSP70 inhibitor PET-16 in multiple myeloma.The remarkable multivalency of the Hsp70 chaperones.HSPA5 Gene encoding Hsp70 chaperone BiP in the endoplasmic reticulum.X-Linked Inhibitor of Apoptosis Protein (XIAP) is a Client of Heat Shock Protein 70 (Hsp70) and a Biomarker of its Inhibition.Chaperone substrate provides missing link for cancer drug discovery.
P2860
Q27303504-CD206868-8CC7-4EBF-8441-1E6CD9708448Q28262765-91AE1651-C463-4B9A-8BCB-36D52DEA4274Q28270851-27FA2024-7DED-467B-9495-551E04861B47Q30315590-2308F06A-DCEF-44C5-ABA9-F264DA7EDD1AQ30372203-B2EA44F8-E165-4250-AEB0-801BF722FE31Q35224117-2F62F63B-6A00-4C27-AE38-738D2631FDB5Q36058976-9E17DBE3-B866-4CFB-99D0-8BD188D35FACQ36378270-87FA47BA-3E73-4B95-884E-C69381A62947Q37082577-4149602B-DB94-42F5-A11F-908206ECCA97Q38654400-1CA7FB3D-2043-4E18-9389-7813E86E35F1Q38758528-7DA1F511-2BCE-4301-A0FD-BE63A55C310DQ38796931-33538A5C-BA1A-48E3-B24E-BB8318557FD8Q38852874-3842EBD1-4F5A-4DFE-96F3-FA0F3C35B3FBQ39144895-C5D25169-5DA2-428C-86B3-8D0B778166A8Q39175124-82BA83EE-0A96-4FDB-9481-0D9971063FB2Q47279123-1587BDB0-BCE9-40D5-957C-D4B76AE6FDE5Q49914023-F60A262B-DB33-4F65-B190-CD466F8C0E8A
P2860
Structural basis for the inhibition of HSP70 and DnaK chaperones by small-molecule targeting of a C-terminal allosteric pocket
description
2014 nî lūn-bûn
@nan
2014 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի նոյեմբերին 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
Structural basis for the inhib ...... a C-terminal allosteric pocket
@ast
Structural basis for the inhib ...... a C-terminal allosteric pocket
@en
Structural basis for the inhib ...... a C-terminal allosteric pocket
@nl
type
label
Structural basis for the inhib ...... a C-terminal allosteric pocket
@ast
Structural basis for the inhib ...... a C-terminal allosteric pocket
@en
Structural basis for the inhib ...... a C-terminal allosteric pocket
@nl
prefLabel
Structural basis for the inhib ...... a C-terminal allosteric pocket
@ast
Structural basis for the inhib ...... a C-terminal allosteric pocket
@en
Structural basis for the inhib ...... a C-terminal allosteric pocket
@nl
P2093
P2860
P3181
P356
P1433
P1476
Structural basis for the inhib ...... a C-terminal allosteric pocket
@en
P2093
Donna L George
Julia I-Ju Leu
Pingfeng Zhang
Ronen Marmorstein
P2860
P304
P3181
P356
10.1021/CB500236Y
P407
P577
2014-11-21T00:00:00Z