Structural analysis of the Sil1-Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factor
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The nucleotide exchange factors of Hsp70 molecular chaperonesProtein Folding and Mechanisms of ProteostasisBiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functionsA bacterial toxin and a nonenveloped virus hijack ER-to-cytosol membrane translocation pathways to cause diseaseRedox signaling via the molecular chaperone BiP protects cells against endoplasmic reticulum-derived oxidative stressFormation and Reversibility of BiP Protein Cysteine Oxidation Facilitate Cell Survival during and post Oxidative StressSil1, a nucleotide exchange factor for BiP, is not required for antibody assembly or secretionThe nucleotide exchange factors Grp170 and Sil1 induce cholera toxin release from BiP to enable retrotranslocation.C-terminal mutations destabilize SIL1/BAP and can cause Marinesco-Sjögren syndrome.Probing the ATP Site of GRP78 with Nucleotide Triphosphate Analogs.The Lhs1/GRP170 chaperones facilitate the endoplasmic reticulum-associated degradation of the epithelial sodium channelAn unexpected role for the yeast nucleotide exchange factor Sil1 as a reductant acting on the molecular chaperone BiP.The many functions of the endoplasmic reticulum chaperones and folding enzymes.Cellular Signature of SIL1 Depletion: Disease Pathogenesis due to Alterations in Protein Composition Beyond the ER Machinery.A nucleotide exchange factor promotes endoplasmic reticulum-to-cytosol membrane penetration of the nonenveloped virus simian virus 40.A Conserved Cysteine within the ATPase Domain of the Endoplasmic Reticulum Chaperone BiP is Necessary for a Complete Complement of BiP Activities.Marinesco-Sjögren syndrome protein SIL1 regulates motor neuron subtype-selective ER stress in ALS.A Parallel Comparison of Antigen Candidates for Development of an Optimized Serological Diagnosis of Schistosomiasis Japonica in the PhilippinesMarinesco-Sjögren Syndrome in an Emirati Child with a Novel Mutation in SIL1 Affecting the 5' Untranslated Region.Disrupted hydrogen bond network and impaired ATPase activity in an Hsc70 cysteine mutant.How Are Proteins Reduced in the Endoplasmic Reticulum?Diminished Ost3-dependent N-glycosylation of the BiP nucleotide exchange factor Sil1 is an adaptive response to reductive ER stress.Bap (Sil1) regulates the molecular chaperone BiP by coupling release of nucleotide and substrate.Nucleotide exchange factors Fes1 and HspBP1 mimic substrate to release misfolded proteins from Hsp70.SIL1 Rescued Bip Elevation-Related Tau Hyperphosphorylation in ER Stress.Tracking Effects of SIL1 Increase: Taking a Closer Look Beyond the Consequences of Elevated Expression Level.The nucleotide exchange factor SIL1 is required for glucose-stimulated insulin secretion from mouse pancreatic beta cells in vivo
P2860
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P2860
Structural analysis of the Sil1-Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factor
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2011 nî lūn-bûn
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2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված
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2011年の論文
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2011年論文
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2011年論文
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2011年論文
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2011年論文
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2011年論文
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2011年论文
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Structural analysis of the Sil ...... s a nucleotide-exchange factor
@ast
Structural analysis of the Sil ...... s a nucleotide-exchange factor
@en
Structural analysis of the Sil ...... s a nucleotide-exchange factor
@nl
type
label
Structural analysis of the Sil ...... s a nucleotide-exchange factor
@ast
Structural analysis of the Sil ...... s a nucleotide-exchange factor
@en
Structural analysis of the Sil ...... s a nucleotide-exchange factor
@nl
prefLabel
Structural analysis of the Sil ...... s a nucleotide-exchange factor
@ast
Structural analysis of the Sil ...... s a nucleotide-exchange factor
@en
Structural analysis of the Sil ...... s a nucleotide-exchange factor
@nl
P2093
P2860
P3181
P356
P1433
P1476
Structural analysis of the Sil ...... s a nucleotide-exchange factor
@en
P2093
Bingdong Sha
Jingzhi Li
P2860
P304
P3181
P356
10.1042/BJ20110500
P407
P577
2011-09-15T00:00:00Z