Nucleotide binding by Lhs1p is essential for its nucleotide exchange activity and for function in vivo.
about
Unfolding the Role of Large Heat Shock Proteins: New Insights and Therapeutic ImplicationsBiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functionsHigh molecular weight stress proteins: Identification, cloning and utilisation in cancer immunotherapyThe Endoplasmic Reticulum Chaperone GRP170: From Immunobiology to Cancer TherapeuticsA Non-enveloped Virus Hijacks Host Disaggregation Machinery to Translocate across the Endoplasmic Reticulum MembraneRole of the unfolded protein response in regulating the mucin-dependent filamentous-growth mitogen-activated protein kinase pathway.Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.The Grp170 nucleotide exchange factor executes a key role during ERAD of cellular misfolded clients.The Lhs1/GRP170 chaperones facilitate the endoplasmic reticulum-associated degradation of the epithelial sodium channelThe large Hsp70 Grp170 binds to unfolded protein substrates in vivo with a regulation distinct from conventional Hsp70s.An unexpected role for the yeast nucleotide exchange factor Sil1 as a reductant acting on the molecular chaperone BiP.The secretory pathway: exploring yeast diversity.Interactions between intersubunit transmembrane domains regulate the chaperone-dependent degradation of an oligomeric membrane protein.The endoplasmic reticulum Grp170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110.A nucleotide exchange factor promotes endoplasmic reticulum-to-cytosol membrane penetration of the nonenveloped virus simian virus 40.Spatial localisation of chaperone distribution in the endoplasmic reticulum of yeast.Signalling mucin Msb2 Regulates adaptation to thermal stress in Candida albicans.Interactions between Kar2p and its nucleotide exchange factors Sil1p and Lhs1p are mechanistically distinct.Diminished Ost3-dependent N-glycosylation of the BiP nucleotide exchange factor Sil1 is an adaptive response to reductive ER stress.
P2860
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P2860
Nucleotide binding by Lhs1p is essential for its nucleotide exchange activity and for function in vivo.
description
2009 nî lūn-bûn
@nan
2009 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Nucleotide binding by Lhs1p is ...... vity and for function in vivo.
@ast
Nucleotide binding by Lhs1p is ...... vity and for function in vivo.
@en
Nucleotide binding by Lhs1p is ...... vity and for function in vivo.
@nl
type
label
Nucleotide binding by Lhs1p is ...... vity and for function in vivo.
@ast
Nucleotide binding by Lhs1p is ...... vity and for function in vivo.
@en
Nucleotide binding by Lhs1p is ...... vity and for function in vivo.
@nl
prefLabel
Nucleotide binding by Lhs1p is ...... vity and for function in vivo.
@ast
Nucleotide binding by Lhs1p is ...... vity and for function in vivo.
@en
Nucleotide binding by Lhs1p is ...... vity and for function in vivo.
@nl
P2093
P2860
P3181
P356
P1476
Nucleotide binding by Lhs1p is ...... vity and for function in vivo.
@en
P2093
Colin J Stirling
Daniel Humphries
Gregor J Steel
Jeanine de Keyzer
Sarah J Hale
P2860
P304
P3181
P356
10.1074/JBC.M109.055160
P407
P577
2009-11-13T00:00:00Z