Signal sequences specify the targeting route to the endoplasmic reticulum membrane
about
LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulumMembrane integration of Sec61alpha: a core component of the endoplasmic reticulum translocation complexSignal recognition particle mediates post-translational targeting in eukaryotesThe similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevanceThe Sec-dependent pathwayStructure of Monomeric Yeast and Mammalian Sec61 Complexes Interacting with the Translating RibosomeSec61p is part of the endoplasmic reticulum-associated degradation machinerySec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo.ERAD and protein import defects in a sec61 mutant lacking ER-lumenal loop 7.Elongation arrest is a physiologically important function of signal recognition particle.Coordination of N-glycosylation and protein translocation across the endoplasmic reticulum membrane by Sss1 protein.Biogenesis of the signal recognition particle (SRP) involves import of SRP proteins into the nucleolus, assembly with the SRP-RNA, and Xpo1p-mediated export.An interaction between the SRP receptor and the translocon is critical during cotranslational protein translocation.A functional GTPase domain, but not its transmembrane domain, is required for function of the SRP receptor beta-subunit.The membrane stress response buffers lethal effects of lipid disequilibrium by reprogramming the protein homeostasis network.Cer1p functions as a molecular chaperone in the endoplasmic reticulum of Saccharomyces cerevisiae.The oligosaccharyltransferase complex from Saccharomyces cerevisiae. Isolation of the OST6 gene, its synthetic interaction with OST3, and analysis of the native complex.Regulation of ribosome biogenesis by the rapamycin-sensitive TOR-signaling pathway in Saccharomyces cerevisiae.The GPI transamidase complex of Saccharomyces cerevisiae contains Gaa1p, Gpi8p, and Gpi16p.Sec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membrane.The Alu domain homolog of the yeast signal recognition particle consists of an Srp14p homodimer and a yeast-specific RNA structure.Quality control of nonstop membrane proteins at the ER membrane and in the cytosol.Peroxisomal membrane proteins insert into the endoplasmic reticulum.Recognition of a subset of signal sequences by Ssh1p, a Sec61p-related protein in the membrane of endoplasmic reticulum of yeast Saccharomyces cerevisiae.Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding.The alpha and beta subunit of the nascent polypeptide-associated complex have distinct functionsHeterologous expression of a serine carboxypeptidase-like acyltransferase and characterization of the kinetic mechanism.Two alternative binding mechanisms connect the protein translocation Sec71-Sec72 complex with heat shock proteins.An improved reversibly dimerizing mutant of the FK506-binding protein FKBPThe SND proteins constitute an alternative targeting route to the endoplasmic reticulum.Protein targeting to the bacterial cytoplasmic membrane.The efficiency of protein compartmentalization into the secretory pathway.The structure of multiple polypeptide domains determines the signal recognition particle targeting requirement of Escherichia coli inner membrane proteins.Protein unfolding by mitochondria. The Hsp70 import motorEvasion of endoplasmic reticulum surveillance makes Wsc1p an obligate substrate of Golgi quality controlStudies of yeast oligosaccharyl transferase subunits using the split-ubiquitin system: topological features and in vivo interactions.The hydrophobic core of the Sec61 translocon defines the hydrophobicity threshold for membrane integration.N-terminal acetylation inhibits protein targeting to the endoplasmic reticulumTowards a functional understanding of protein N-terminal acetylationDefining the specificity of cotranslationally acting chaperones by systematic analysis of mRNAs associated with ribosome-nascent chain complexes.
P2860
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P2860
Signal sequences specify the targeting route to the endoplasmic reticulum membrane
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Signal sequences specify the targeting route to the endoplasmic reticulum membrane
@ast
Signal sequences specify the targeting route to the endoplasmic reticulum membrane
@en
type
label
Signal sequences specify the targeting route to the endoplasmic reticulum membrane
@ast
Signal sequences specify the targeting route to the endoplasmic reticulum membrane
@en
prefLabel
Signal sequences specify the targeting route to the endoplasmic reticulum membrane
@ast
Signal sequences specify the targeting route to the endoplasmic reticulum membrane
@en
P2093
P2860
P921
P356
P1476
Signal sequences specify the targeting route to the endoplasmic reticulum membrane
@en
P2093
P2860
P304
P356
10.1083/JCB.134.2.269
P407
P577
1996-07-01T00:00:00Z