HspBP1, an Hsp70 cochaperone, has two structural domains and is capable of altering the conformation of the Hsp70 ATPase domain
about
Prion-impairing mutations in Hsp70 chaperone Ssa1: effects on ATPase and chaperone activities.Role of Hsp70 ATPase domain intrinsic dynamics and sequence evolution in enabling its functional interactions with NEFs.Measurement and interpretation of 15N-1H residual dipolar couplings in larger proteins.HSP70 binding protein 1 (HspBP1) suppresses HIV-1 replication by inhibiting NF-κB mediated activation of viral gene expression.Heat shock protein 70-binding protein 1 is highly expressed in high-grade gliomas, interacts with multiple heat shock protein 70 family members, and specifically binds brain tumor cell surfacesMultiple hsp70 isoforms in the eukaryotic cytosol: mere redundancy or functional specificity?HspBP1 levels are elevated in breast tumor tissue and inversely related to tumor aggressiveness.Hsp70 protein complexes as drug targets.Modulation of the chaperone DnaK allosterism by the nucleotide exchange factor GrpE.Extracellular HspBP1 and Hsp72 synergistically activate epidermal growth factor receptor.Human serum contains detectable levels of the Hsp70 cochaperone HspBP1 and antibodies bound to HspBP1.The heat shock-binding protein (HspBP1) protects cells against the cytotoxic action of the Tag7-Hsp70 complex.Interactions between Kar2p and its nucleotide exchange factors Sil1p and Lhs1p are mechanistically distinct.Anticancer drugs up-regulate HspBP1 and thereby antagonize the prosurvival function of Hsp70 in tumor cells.
P2860
Q27934126-217E3AB2-8562-4636-A237-68AEDD119BFAQ33700525-40A20474-8EFD-4FC5-B0C3-BEA0B0EA873BQ33715066-9C0536FB-D8DC-47E8-B999-5B07A64177B8Q36627905-05842042-ACF7-442D-9133-08B7A9AB1E0CQ36922469-636E1A89-D715-4C98-AA10-D771545F777CQ37200825-6B83706A-DACB-4002-AEB0-987F2D87DEF6Q37308819-91796365-3C54-46EC-ACDB-95E3840095CDQ38037745-D5F36F44-DDB9-4FF2-9CA9-CAAFCEC7135DQ39715289-79E6A6A3-3281-4984-A17A-29CA39CA0C20Q39921054-0E38C253-CA43-42F8-876E-420F93D67F74Q40309034-554F9D51-ADBC-453A-A83A-3D901098ECE3Q42224288-E5C409DC-884A-429A-A3AF-D389A68432FDQ42737400-DA8B8235-4D81-471E-A9FA-8F2C1ABF2E5CQ48077559-185F18A2-1621-4614-A737-424E7253473A
P2860
HspBP1, an Hsp70 cochaperone, has two structural domains and is capable of altering the conformation of the Hsp70 ATPase domain
description
2003 nî lūn-bûn
@nan
2003 թուականի Մայիսին հրատարակուած գիտական յօդուած
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2003 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
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name
HspBP1, an Hsp70 cochaperone, ...... ion of the Hsp70 ATPase domain
@ast
HspBP1, an Hsp70 cochaperone, ...... ion of the Hsp70 ATPase domain
@en
HspBP1, an Hsp70 cochaperone, ...... ion of the Hsp70 ATPase domain
@nl
type
label
HspBP1, an Hsp70 cochaperone, ...... ion of the Hsp70 ATPase domain
@ast
HspBP1, an Hsp70 cochaperone, ...... ion of the Hsp70 ATPase domain
@en
HspBP1, an Hsp70 cochaperone, ...... ion of the Hsp70 ATPase domain
@nl
prefLabel
HspBP1, an Hsp70 cochaperone, ...... ion of the Hsp70 ATPase domain
@ast
HspBP1, an Hsp70 cochaperone, ...... ion of the Hsp70 ATPase domain
@en
HspBP1, an Hsp70 cochaperone, ...... ion of the Hsp70 ATPase domain
@nl
P2093
P2860
P356
P1476
HspBP1, an Hsp70 cochaperone, ...... ion of the Hsp70 ATPase domain
@en
P2093
Catherine A McLellan
Deborah A Raynes
Vince Guerriero
P2860
P304
P356
10.1074/JBC.M301109200
P407
P577
2003-05-23T00:00:00Z