Homologs of the yeast Sec complex subunits Sec62p and Sec63p are abundant proteins in dog pancreas microsomes.
about
The SANT2 domain of the murine tumor cell DnaJ-like protein 1 human homologue interacts with alpha1-antichymotrypsin and kinetically interferes with its serpin inhibitory activityDifferent effects of Sec61α, Sec62 and Sec63 depletion on transport of polypeptides into the endoplasmic reticulum of mammalian cellsRegulated release of ERdj3 from unfolded proteins by BiPAn interaction between human Sec63 and nucleoredoxin may provide the missing link between the SEC63 gene and polycystic liver diseaseERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substratesThe concept of translocational regulationA Cellular J-Domain Protein Modulates Polyprotein Processing and Cytopathogenicity of a PestivirusSec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo.A novel type of co-chaperone mediates transmembrane recruitment of DnaK-like chaperones to ribosomesBiP clustering facilitates protein folding in the endoplasmic reticulumEvolutionary gain of function for the ER membrane protein Sec62 from yeast to humansIdentification and characterization of a novel endoplasmic reticulum (ER) DnaJ homologue, which stimulates ATPase activity of BiP in vitro and is induced by ER stress.Membrane protein insertion at the endoplasmic reticulum.Characterization of pancreatic ERj3p, a homolog of yeast DnaJ-like protein Scj1p.Topogenesis of membrane proteins: determinants and dynamics.Survey of the year 2000 commercial optical biosensor literature.Role of human sec63 in modulating the steady-state levels of multi-spanning membrane proteins.Targeting cell migration and the endoplasmic reticulum stress response with calmodulin antagonists: a clinically tested small molecule phenocopy of SEC62 gene silencing in human tumor cells.Sec63 and Xbp1 regulate IRE1α activity and polycystic disease severity.Cytosolic and ER J-domains of mammalian and parasitic origin can functionally interact with DnaK.Efficient secretion of small proteins in mammalian cells relies on Sec62-dependent posttranslational translocationVersatility of the endoplasmic reticulum protein folding factory.The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulumA new role for BiP: closing the aqueous translocon pore during protein integration into the ER membraneMammalian SRP receptor switches the Sec61 translocase from Sec62 to SRP-dependent translocationBiP mutants that are unable to interact with endoplasmic reticulum DnaJ proteins provide insights into interdomain interactions in BiP.Mutation of sec63 in zebrafish causes defects in myelinated axons and liver pathologyProtein translocation across the rough endoplasmic reticulum.Sec62 protein mediates membrane insertion and orientation of moderately hydrophobic signal anchor proteins in the endoplasmic reticulum (ER)How antibodies foldAll roads lead to Rome (but some may be harder to travel): SRP-independent translocation into the endoplasmic reticulum.The Sec translocon mediated protein transport in prokaryotes and eukaryotes.Membrane protein synthesis in cell-free systems: from bio-mimetic systems to bio-membranes.Protein transport into the human ER and related diseases, Sec61-channelopathies.The Brl domain in Sec63p is required for assembly of functional endoplasmic reticulum translocons.Sec62p, a component of the endoplasmic reticulum protein translocation machinery, contains multiple binding sites for the Sec-complexSec62 protein level is crucial for the ER stress tolerance of prostate cancer.Silencing of the SEC62 gene inhibits migratory and invasive potential of various tumor cells.Contribution of the HEDJ/ERdj3 cysteine-rich domain to substrate interactions.Co-chaperone Specificity in Gating of the Polypeptide Conducting Channel in the Membrane of the Human Endoplasmic Reticulum.
P2860
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P2860
Homologs of the yeast Sec complex subunits Sec62p and Sec63p are abundant proteins in dog pancreas microsomes.
description
2000 nî lūn-bûn
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2000 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունիսին 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
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2000年论文
@wuu
name
Homologs of the yeast Sec comp ...... ns in dog pancreas microsomes.
@ast
Homologs of the yeast Sec comp ...... ns in dog pancreas microsomes.
@en
type
label
Homologs of the yeast Sec comp ...... ns in dog pancreas microsomes.
@ast
Homologs of the yeast Sec comp ...... ns in dog pancreas microsomes.
@en
prefLabel
Homologs of the yeast Sec comp ...... ns in dog pancreas microsomes.
@ast
Homologs of the yeast Sec comp ...... ns in dog pancreas microsomes.
@en
P2093
P2860
P356
P1476
Homologs of the yeast Sec comp ...... ns in dog pancreas microsomes.
@en
P2093
Nastainczyk W
Skowronek MH
Tyedmers J
Zimmermann R
P2860
P304
P356
10.1073/PNAS.97.13.7214
P407
P577
2000-06-01T00:00:00Z