Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor
about
Classification of intrinsically disordered regions and proteinsMembrane topology of the 12- and the 25-kDa subunits of the mammalian signal peptidase complexA protein of the endoplasmic reticulum involved early in polypeptide translocationPurification of microsomal signal peptidase as a complexFf coliphages: structural and functional relationshipsThe signal recognition particle (SRP) RNA links conformational changes in the SRP to protein targetingThe beta subunit of the signal recognition particle receptor is a transmembrane GTPase that anchors the alpha subunit, a peripheral membrane GTPase, to the endoplasmic reticulum membraneThe signal recognition particle receptor is a complex that contains two distinct polypeptide chainsSegregation 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 particleSubcellular distribution of signal recognition particle and 7SL-RNA determined with polypeptide-specific antibodies and complementary DNA probeThe ribosome regulates the GTPase of the beta-subunit of the signal recognition particle receptorMechanism of association and reciprocal activation of two GTPasesCrystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communicationInteraction of signal-recognition particle 54 GTPase domain and signal-recognition particle RNA in the free signal-recognition particleStructural basis of signal sequence surveillance and selection by the SRP–FtsY complexSignal recognition particle receptor is important for cell growth and protein secretion in Saccharomyces cerevisiae.Genes required for completion of import of proteins into the endoplasmic reticulum in yeast.A functional GTPase domain, but not its transmembrane domain, is required for function of the SRP receptor beta-subunit.Sls1p stimulates Sec63p-mediated activation of Kar2p in a conformation-dependent manner in the yeast endoplasmic reticulum.Co-translational protein targeting by the signal recognition particleSRbeta coordinates signal sequence release from SRP with ribosome binding to the translocon.Targeting of NH2-terminal-processed microsomal protein to mitochondria: a novel pathway for the biogenesis of hepatic mitochondrial P450MT2Isolation 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 membranesCompositional and structural features related to thermal stability in the archaea SRP19 and SRP54 signal recognition particle proteins.Homodimerization of the G protein SRbeta in the nucleotide-free state involves proline cis/trans isomerization in the switch II region.The 68 kDa protein of signal recognition particle contains a glycine-rich region also found in certain RNA-binding proteins.Use of synthetic signal sequences to explore the protein export machinery.'RNA walk' a novel approach to study RNA-RNA interactions between a small RNA and its target.Mechanisms of protein localization.The structure of multiple polypeptide domains determines the signal recognition particle targeting requirement of Escherichia coli inner membrane proteins.Transient tether between the SRP RNA and SRP receptor ensures efficient cargo delivery during cotranslational protein targeting.The nascent-polypeptide-associated complex: having a "NAC" for fidelity in translocation.The intrinsic ability of ribosomes to bind to endoplasmic reticulum membranes is regulated by signal recognition particle and nascent-polypeptide-associated complex.Signal peptide cleavage is essential for surface expression of a regulatory T cell surface protein, leucine rich repeat containing 32 (LRRC32).The secD locus of E.coli codes for two membrane proteins required for protein export.Protein import into yeast mitochondria is inhibited by antibodies raised against 45-kd proteins of the outer membranePhysiological basis for conservation of the signal recognition particle targeting pathway in Escherichia coli.Metabolism of minor isoforms of prion proteins: Cytosolic prion protein and transmembrane prion proteinCo-translational targeting and translocation of the amino terminus of opsin across the endoplasmic membrane requires GTP but not ATP.
P2860
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P2860
Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor
description
1982 nî lūn-bûn
@nan
1982年の論文
@ja
1982年論文
@yue
1982年論文
@zh-hant
1982年論文
@zh-hk
1982年論文
@zh-mo
1982年論文
@zh-tw
1982年论文
@wuu
1982年论文
@zh
1982年论文
@zh-cn
name
Protein translocation across t ...... recognition particle receptor
@ast
Protein translocation across t ...... recognition particle receptor
@en
type
label
Protein translocation across t ...... recognition particle receptor
@ast
Protein translocation across t ...... recognition particle receptor
@en
prefLabel
Protein translocation across t ...... recognition particle receptor
@ast
Protein translocation across t ...... recognition particle receptor
@en
P2860
P356
P1476
Protein translocation across t ...... recognition particle receptor
@en
P2093
P2860
P304
P356
10.1083/JCB.95.2.470
P407
P433
P577
1982-11-01T00:00:00Z