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.
about
Mutations in the PTS1 receptor gene, PXR1, define complementation group 2 of the peroxisome biogenesis disordersA human Alu RNA-binding protein whose expression is associated with accumulation of small cytoplasmic Alu RNACarboxyl-terminal targeting and novel post-translational processing of JAW1, a lymphoid protein of the endoplasmic reticulumA protein of the endoplasmic reticulum involved early in polypeptide translocationGTP-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 receptorComparison of initiation of protein synthesis in procaryotes, eucaryotes, and organellesThe 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 probeTranslocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory proteinThe ribosome regulates the GTPase of the beta-subunit of the signal recognition particle receptorUse of endogenous signal sequences for transient production and efficient secretion by moss (Physcomitrella patens) cells.Protein translocation: what's the problem?Sec-secretion and sortase-mediated anchoring of proteins in Gram-positive bacteriaThe Sec-dependent pathwaySite-directed mutations in the Sindbis virus E2 glycoprotein identify palmitoylation sites and affect virus buddingProteolytic processing of the Sindbis virus membrane protein precursor PE2 is nonessential for growth in vertebrate cells but is required for efficient growth in invertebrate cellsInteraction of signal-recognition particle 54 GTPase domain and signal-recognition particle RNA in the free signal-recognition particleTranslational arrest by a prokaryotic signal recognition particle is mediated by RNA interactionsElongation arrest is a physiologically important function of signal recognition particle.Signal recognition particle receptor is important for cell growth and protein secretion in Saccharomyces cerevisiae.Plasmodium falciparum signal recognition particle components and anti-parasitic effect of ivermectin in blocking nucleo-cytoplasmic shuttling of SRP.The trypanosomatid signal recognition particle consists of two RNA molecules, a 7SL RNA homologue and a novel tRNA-like moleculeAlu sequences are processed 7SL RNA genesIsolation 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 membranesMolecular evolution of SRP cycle components: functional implicationsCompositional and structural features related to thermal stability in the archaea SRP19 and SRP54 signal recognition particle proteins.Isolation and nucleotide sequence of cDNA clone for bovine pancreatic anionic trypsinogen. Structural identity within the trypsin family.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.Surface proteins of gram-positive bacteria and mechanisms of their targeting to the cell wall envelope.Mechanisms of protein localization.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.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.The rat hepatocyte plasma membrane organic anion binding protein is immunologically related to the mitochondrial F1 adenosine triphosphatase beta-subunitMalaria circumsporozoite protein inhibits protein synthesis in mammalian cells.
P2860
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P2860
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.
description
1981 nî lūn-bûn
@nan
1981年の論文
@ja
1981年論文
@yue
1981年論文
@zh-hant
1981年論文
@zh-hk
1981年論文
@zh-mo
1981年論文
@zh-tw
1981年论文
@wuu
1981年论文
@zh
1981年论文
@zh-cn
name
Translocation of proteins acro ...... eased by microsomal membranes.
@ast
Translocation of proteins acro ...... eased by microsomal membranes.
@en
type
label
Translocation of proteins acro ...... eased by microsomal membranes.
@ast
Translocation of proteins acro ...... eased by microsomal membranes.
@en
prefLabel
Translocation of proteins acro ...... eased by microsomal membranes.
@ast
Translocation of proteins acro ...... eased by microsomal membranes.
@en
P2860
P356
P1476
Translocation of proteins acro ...... eased by microsomal membranes.
@en
P2093
P2860
P304
P356
10.1083/JCB.91.2.557
P407
P433
P577
1981-11-01T00:00:00Z