Identification and characterization of a membrane component essential for the translocation of nascent proteins across the membrane of the endoplasmic reticulum.
about
Protein translocation across the ER requires a functional GTP binding site in the alpha subunit of the signal recognition particle receptorSegregation of the polypeptide translocation apparatus to regions of the endoplasmic reticulum containing ribophorins and ribosomes. II. Rat liver microsomal subfractions contain equimolar amounts of ribophorins and ribosomesProtein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particleThe ribosome regulates the GTPase of the beta-subunit of the signal recognition particle receptorCrystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communicationIsolation and characterization of cDNA clones for rat ribophorin I: complete coding sequence and in vitro synthesis and insertion of the encoded product into endoplasmic reticulum membranesMultiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeastMechanisms of protein localization.YidC, a newly defined evolutionarily conserved protein, mediates membrane protein assembly in bacteria.Folding and misfolding of the prion protein in the secretory pathway.Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes.Mechanisms for the incorporation of proteins in membranes and organelles.Molecular components of the signal sequence that function in the initiation of protein exportProtein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptorCharacterization of secretory protein translocation: ribosome-membrane interaction in endoplasmic reticulumAntiribophorin antibodies inhibit the targeting to the ER membrane of ribosomes containing nascent secretory polypeptides.Alkaline phosphatase secretion-negative mutant of Bacillus licheniformis 749/CFunctional substitution of the signal recognition particle 54-kDa subunit by its Escherichia coli homolog.Divergent regulation of protein synthesis in the cytosol and endoplasmic reticulum compartments of mammalian cells.Peroxin-dependent targeting of a lipid-droplet-destined membrane protein to ER subdomainsDistinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins.Prion disease: a tale of folds and strains.Localization of mRNAs to the endoplasmic reticulum.Protein transport into the human ER and related diseases, Sec61-channelopathies.The α-helical structure of prodomains promotes translocation of intrinsically disordered neuropeptide hormones into the endoplasmic reticulum.A novel translational control mechanism involving RNA structures within coding sequences.The organization of the 7SL RNA in the signal recognition particle.A membrane component of the endoplasmic reticulum that may be essential for protein translocation.A microsomal ATP-binding protein involved in efficient protein transport into the mammalian endoplasmic reticulum.Determinants of membrane-targeting and transmembrane translocation during bacterial protein export.A membrane component essential for vectorial translocation of nascent proteins across the endoplasmic reticulum: requirements for its extraction and reassociation with the membraneProtein translocation across wheat germ microsomal membranes requires an SRP-like componentCharacterization of molecules involved in protein translocation using a specific antibody.Signal recognition particle-dependent membrane insertion of mouse invariant chain: a membrane-spanning protein with a cytoplasmically exposed amino terminusAlteration of the cytoplasmic domain of the membrane-spanning glycoprotein p62 of Semliki Forest virus does not affect its polar distribution in established lines of Madin-Darby canine kidney cellsChloroplast FtsY, chloroplast signal recognition particle, and GTP are required to reconstitute the soluble phase of light-harvesting chlorophyll protein transport into thylakoid membranes.The signal sequence receptor, unlike the signal recognition particle receptor, is not essential for protein translocation.Direct evidence for a coupling between synthesis and export of PhoS in E. coli.The carboxyl terminus of the membrane-binding domain of cytochrome b5 spans the bilayer of the endoplasmic reticulum.Isolating SRP.
P2860
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P2860
Identification and characterization of a membrane component essential for the translocation of nascent proteins across the membrane of the endoplasmic reticulum.
description
1980 nî lūn-bûn
@nan
1980年の論文
@ja
1980年論文
@yue
1980年論文
@zh-hant
1980年論文
@zh-hk
1980年論文
@zh-mo
1980年論文
@zh-tw
1980年论文
@wuu
1980年论文
@zh
1980年论文
@zh-cn
name
Identification and characteriz ...... of the endoplasmic reticulum.
@en
type
label
Identification and characteriz ...... of the endoplasmic reticulum.
@en
prefLabel
Identification and characteriz ...... of the endoplasmic reticulum.
@en
P2860
P356
P1476
Identification and characteriz ...... of the endoplasmic reticulum.
@en
P2093
Dobberstein B
P2860
P304
P356
10.1083/JCB.87.2.503
P407
P433
P577
1980-11-01T00:00:00Z