Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle
about
p180 promotes the ribosome-independent localization of a subset of mRNA to the endoplasmic reticulumClassification of intrinsically disordered regions and proteinsMammalian Sec61 is associated with Sec62 and Sec63GTP-binding membrane protein of Escherichia coli with sequence homology to initiation factor 2 and elongation factors Tu and GFf coliphages: structural and functional relationshipsProtein translocation across the ER requires a functional GTP binding site in the alpha subunit of the signal recognition particle receptorThe 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 membraneSubcellular distribution of signal recognition particle and 7SL-RNA determined with polypeptide-specific antibodies and complementary DNA probeMechanism of association and reciprocal activation of two GTPasesThe endoplasmic reticulum: structure, function and response to cellular signalingBiosynthesis and biochemical properties of the hepatitis C virus core proteinInteraction of signal-recognition particle 54 GTPase domain and signal-recognition particle RNA in the free signal-recognition particleSignal recognition particle receptor is important for cell growth and protein secretion in Saccharomyces cerevisiae.A functional GTPase domain, but not its transmembrane domain, is required for function of the SRP receptor beta-subunit.Identification of Pex13p a peroxisomal membrane receptor for the PTS1 recognition factorSls1p stimulates Sec63p-mediated activation of Kar2p in a conformation-dependent manner in the yeast endoplasmic reticulum.Membrane insertion, processing, and topology of cystic fibrosis transmembrane conductance regulator (CFTR) in microsomal membranesCo-translational protein targeting by the signal recognition particleThe PERK eukaryotic initiation factor 2 alpha kinase is required for the development of the skeletal system, postnatal growth, and the function and viability of the pancreasMolecular evolution of SRP cycle components: functional implicationsMultiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeastResidues in SRP9/14 essential for elongation arrest activity of the signal recognition particle define a positively charged functional domain on one side of the protein.Transient tether between the SRP RNA and SRP receptor ensures efficient cargo delivery during cotranslational protein targeting.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).Co-translational targeting and translocation of the amino terminus of opsin across the endoplasmic membrane requires GTP but not ATP.Multifunctional roles for the protein translocation machinery in RNA anchoring to the endoplasmic reticulum.Signal recognition particle (SRP), a ubiquitous initiator of protein translocation.Structure of 4.5S RNA in the signal recognition particle of Escherichia coli as studied by enzymatic and chemical probing.Signal sequence recognition and targeting of ribosomes to the endoplasmic reticulum by the signal recognition particle do not require GTP.mRNA translation is compartmentalized to the endoplasmic reticulum following physiological inhibition of cap-dependent translation.Intracellular traffic of newly synthesized proteins. Current understanding and future prospectsGenetic and biochemical analysis of the fission yeast ribonucleoprotein particle containing a homolog of Srp54p.YidC, a newly defined evolutionarily conserved protein, mediates membrane protein assembly in bacteria.Protein targeting and degradation are coupled for elimination of mislocalized proteins.Translocation of proteins across and integration of membrane proteins into the rough endoplasmic reticulum.The cytoplasmic domain of rhesus cytomegalovirus Rh178 interrupts translation of major histocompatibility class I leader peptide-containing proteins prior to translocation.Location of signal sequences for membrane insertion of the Na+,K+-ATPase alpha subunit.Efficient Secretion of Recombinant Proteins from Rice Suspension-Cultured Cells Modulated by the Choice of Signal Peptide
P2860
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P2860
Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle
description
1982 nî lūn-bûn
@nan
1982 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1982 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
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
name
Protein translocation across t ...... he signal recognition particle
@ast
Protein translocation across t ...... he signal recognition particle
@en
Protein translocation across t ...... he signal recognition particle
@nl
type
label
Protein translocation across t ...... he signal recognition particle
@ast
Protein translocation across t ...... he signal recognition particle
@en
Protein translocation across t ...... he signal recognition particle
@nl
prefLabel
Protein translocation across t ...... he signal recognition particle
@ast
Protein translocation across t ...... he signal recognition particle
@en
Protein translocation across t ...... he signal recognition particle
@nl
P2860
P3181
P356
P1476
Protein translocation across t ...... he signal recognition particle
@en
P2093
P2860
P3181
P356
10.1083/JCB.95.2.463
P407
P433
P577
1982-11-01T00:00:00Z