Formation of a functional ribosome-membrane junction during translocation requires the participation of a GTP-binding protein.
about
Cloning and sequence analysis of human pituitary cDNA encoding the novel polypeptide 7B2Characterization of kinectin, a kinesin-binding protein: primary sequence and N-terminal topogenic signal analysisProtein translocation across the ER requires a functional GTP binding site in the alpha subunit of the signal recognition particle receptorThe 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 NS2 protein of hepatitis C virus is a transmembrane polypeptideBiosynthesis and biochemical properties of the hepatitis C virus core proteinA functional GTPase domain, but not its transmembrane domain, is required for function of the SRP receptor beta-subunit.SRbeta coordinates signal sequence release from SRP with ribosome binding to the translocon.Signal peptide-binding drug as a selective inhibitor of co-translational protein translocationA complex of the signal sequence binding protein and the SRP RNA promotes translocation of nascent proteinsMolecular evolution of SRP cycle components: functional implicationsRegulation of the ribosome-membrane junction at early stages of presecretory protein translocation in the mammalian endoplasmic reticulum.Residues 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.Co-translational targeting and translocation of the amino terminus of opsin across the endoplasmic membrane requires GTP but not ATP.HIV-1 Gag co-opts a cellular complex containing DDX6, a helicase that facilitates capsid assemblyIn vitro attachment of glycosyl-inositolphospholipid anchor structures to mouse Thy-1 antigen and human decay-accelerating factorSignal recognition particle (SRP), a ubiquitous initiator of protein translocation.Signal sequence recognition and targeting of ribosomes to the endoplasmic reticulum by the signal recognition particle do not require GTP.Intracellular traffic of newly synthesized proteins. Current understanding and future prospectsA yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum.Translocation of proteins across and integration of membrane proteins into the rough endoplasmic reticulum.Functional analysis of the ffh-trmD region of the Escherichia coli chromosome by using reverse genetics.A two-step recognition of signal sequences determines the translocation efficiency of proteins.Direct simulation of early-stage Sec-facilitated protein translocationFull-length prepro-alpha-factor can be translocated across the mammalian microsomal membrane only if translation has not terminated.Prepro-carboxypeptidase Y and a truncated form of pre-invertase, but not full-length pre-invertase, can be posttranslationally translocated across microsomal vesicle membranes from Saccharomyces cerevisiae.Integration of membrane proteins into the endoplasmic reticulum requires GTPAccess of proteinase K to partially translocated nascent polypeptides in intact and detergent-solubilized membranes.A novel GTP-binding protein, Sar1p, is involved in transport from the endoplasmic reticulum to the Golgi apparatus.Discrete nascent chain lengths are required for the insertion of presecretory proteins into microsomal membranesStage- and ribosome-specific alterations in nascent chain-Sec61p interactions accompany translocation across the ER membraneFunctional characterization of the 180-kD ribosome receptor in vivo.Identification of a novel stage of ribosome/nascent chain association with the endoplasmic reticulum membrane.GTP hydrolysis by complexes of the signal recognition particle and the signal recognition particle receptor.The N-terminal region of the 37-kDa translocated fragment of Pseudomonas exotoxin A aborts translocation by promoting its own export after microsomal membrane insertion.A nascent membrane protein is located adjacent to ER membrane proteins throughout its integration and translation.ER translocation intermediates are adjacent to a nonglycosylated 34-kD integral membrane protein.Protein translocation across the rough endoplasmic reticulum.Aberrant membrane insertion of a cytoplasmic tail deletion mutant of the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus.SRP keeps polypeptides translocation-competent by slowing translation to match limiting ER-targeting sites
P2860
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P2860
Formation of a functional ribosome-membrane junction during translocation requires the participation of a GTP-binding protein.
description
1986 nî lūn-bûn
@nan
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
1986年论文
@zh
1986年论文
@zh-cn
name
Formation of a functional ribo ...... tion of a GTP-binding protein.
@ast
Formation of a functional ribo ...... tion of a GTP-binding protein.
@en
type
label
Formation of a functional ribo ...... tion of a GTP-binding protein.
@ast
Formation of a functional ribo ...... tion of a GTP-binding protein.
@en
prefLabel
Formation of a functional ribo ...... tion of a GTP-binding protein.
@ast
Formation of a functional ribo ...... tion of a GTP-binding protein.
@en
P2860
P356
P1476
Formation of a functional ribo ...... tion of a GTP-binding protein.
@en
P2093
P2860
P304
P356
10.1083/JCB.103.6.2253
P407
P433
P577
1986-12-01T00:00:00Z