LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum
about
Intracellular catalysis of disulfide bond formation by the human sulfhydryl oxidase, QSOX1ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substratesHsp70 chaperones: cellular functions and molecular mechanismThe nucleotide exchange factors of Hsp70 molecular chaperonesBiP 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 TherapeuticsStructural analysis of the Sil1-Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factorSec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo.Saccharomyces cerevisiae Rot1p is an ER-localized membrane protein that may function with BiP/Kar2p in protein folding.Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1pNucleotide binding by Lhs1p is essential for its nucleotide exchange activity and for function in vivo.Yeast GTB1 encodes a subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum.A novel role for Gtb1p in glucose trimming of N-linked glycans.HspBP1, an Hsp70 cochaperone, has two structural domains and is capable of altering the conformation of the Hsp70 ATPase domainHspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factorProtein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiPThe gene disrupted in Marinesco-Sjögren syndrome encodes SIL1, an HSPA5 cochaperoneThe HSP70 chaperone machinery: J proteins as drivers of functional specificityThe challenge of improved secretory production of active pharmaceutical ingredients in Saccharomyces cerevisiae: a case study on human insulin analogs.Reduced translocation of nascent prion protein during ER stress contributes to neurodegeneration.Hsp110 is required for spindle length control.The BiP molecular chaperone plays multiple roles during the biogenesis of torsinA, an AAA+ ATPase associated with the neurological disease early-onset torsion dystonia.N-terminal acetylation inhibits protein targeting to the endoplasmic reticulumPhenotypic switching in Candida glabrata accompanied by changes in expression of genes with deduced functions in copper detoxification and stressImpact of the lectin chaperone calnexin on the stress response, virulence and proteolytic secretome of the fungal pathogen Aspergillus fumigatus.Role of the unfolded protein response in regulating the mucin-dependent filamentous-growth mitogen-activated protein kinase pathway.A review of the mammalian unfolded protein response.The unfolded protein response supports cellular robustness as a broad-spectrum compensatory pathway.All in the family: atypical Hsp70 chaperones are conserved modulators of Hsp70 activity.Rkr1/Ltn1 Ubiquitin Ligase-mediated Degradation of Translationally Stalled Endoplasmic Reticulum Proteins.Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase.The impact of the unfolded protein response on human diseaseFeature Identification of Compensatory Gene Pairs without Sequence Homology in Yeast.Versatility of the endoplasmic reticulum protein folding factory.Flo11p-independent control of "mat" formation by hsp70 molecular chaperones and nucleotide exchange factors in yeastThe endoplasmic reticulum-associated degradation pathways of budding yeast.Cellular response to unfolded proteins in the endoplasmic reticulum of plants.The Lhs1/GRP170 chaperones facilitate the endoplasmic reticulum-associated degradation of the epithelial sodium channel
P2860
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P2860
LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum
description
2000 nî lūn-bûn
@nan
2000 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
LHS1 and SIL1 provide a lumena ...... into the endoplasmic reticulum
@ast
LHS1 and SIL1 provide a lumena ...... into the endoplasmic reticulum
@en
LHS1 and SIL1 provide a lumena ...... into the endoplasmic reticulum
@en-gb
LHS1 and SIL1 provide a lumena ...... into the endoplasmic reticulum
@nl
type
label
LHS1 and SIL1 provide a lumena ...... into the endoplasmic reticulum
@ast
LHS1 and SIL1 provide a lumena ...... into the endoplasmic reticulum
@en
LHS1 and SIL1 provide a lumena ...... into the endoplasmic reticulum
@en-gb
LHS1 and SIL1 provide a lumena ...... into the endoplasmic reticulum
@nl
prefLabel
LHS1 and SIL1 provide a lumena ...... into the endoplasmic reticulum
@ast
LHS1 and SIL1 provide a lumena ...... into the endoplasmic reticulum
@en
LHS1 and SIL1 provide a lumena ...... into the endoplasmic reticulum
@en-gb
LHS1 and SIL1 provide a lumena ...... into the endoplasmic reticulum
@nl
P2860
P921
P356
P1433
P1476
LHS1 and SIL1 provide a lumena ...... into the endoplasmic reticulum
@en
P2093
C J Stirling
P2860
P304
P356
10.1093/EMBOJ/19.23.6440
P407
P577
2000-12-01T00:00:00Z