Signal recognition particle mediates a transient elongation arrest of preprolactin in reticulocyte lysate.
about
A ribosome-associating factor chaperones tail-anchored membrane proteinsEpithelial V-like antigen (EVA), a novel member of the immunoglobulin superfamily, expressed in embryonic epithelia with a potential role as homotypic adhesion molecule in thymus histogenesisA human Alu RNA-binding protein whose expression is associated with accumulation of small cytoplasmic Alu RNAThe perinucleolar compartmentRibosome regulation by the nascent peptideDissecting eukaryotic translation and its control by ribosome density mapping.Translational 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.Saccharomyces SRP RNA secondary structures: a conserved S-domain and extended Alu-domain.A complex of the signal sequence binding protein and the SRP RNA promotes translocation of nascent proteinsMolecular evolution of SRP cycle components: functional implicationsStructures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interactionThe efficiency of protein compartmentalization into the secretory pathway.'RNA walk' a novel approach to study RNA-RNA interactions between a small RNA and its target.Proteomic analysis of etiolated juvenile tetraploid Robinia pseudoacacia branches during different cutting periods.The intrinsic ability of ribosomes to bind to endoplasmic reticulum membranes is regulated by signal recognition particle and nascent-polypeptide-associated complex.The perinucleolar compartment.New prospects in studying the bacterial signal recognition particle pathway.Global mapping of translation initiation sites in mammalian cells at single-nucleotide resolution.Topogenesis of membrane proteins: determinants and dynamics.The SRP9/14 subunit of the signal recognition particle (SRP) is present in more than 20-fold excess over SRP in primate cells and exists primarily free but also in complex with small cytoplasmic Alu RNAsThe 3' end formation in small RNAs.A truncation in the 14 kDa protein of the signal recognition particle leads to tertiary structure changes in the RNA and abolishes the elongation arrest activity of the particle.A highly efficient, cell-free translation/translocation system prepared from Xenopus eggsA conserved PUF-Ago-eEF1A complex attenuates translation elongation.Translation elongation regulates substrate selection by the signal recognition particle.A two-step recognition of signal sequences determines the translocation efficiency of proteins.Down-regulation of the trypanosomatid signal recognition particle affects the biogenesis of polytopic membrane proteins but not of signal peptide-containing proteins.Discrete nascent chain lengths are required for the insertion of presecretory proteins into microsomal membranesSubstrate-specific regulation of the ribosome- translocon junction by N-terminal signal sequencesA nascent membrane protein is located adjacent to ER membrane proteins throughout its integration and translation.A mutation in the signal recognition particle 7S RNA of the yeast Yarrowia lipolytica preferentially affects synthesis of the alkaline extracellular protease: in vivo evidence for translational arrestAssembly of the Alu domain of the signal recognition particle (SRP): dimerization of the two protein components is required for efficient binding to SRP RNA.SRP keeps polypeptides translocation-competent by slowing translation to match limiting ER-targeting sitesBinding sites of the 9- and 14-kilodalton heterodimeric protein subunit of the signal recognition particle (SRP) are contained exclusively in the Alu domain of SRP RNA and contain a sequence motif that is conserved in evolution.Assembly of the 68- and 72-kD proteins of signal recognition particle with 7S RNAIn vivo kinetics of protein targeting to the endoplasmic reticulum determined by site-specific phosphorylationElectrostatics in the ribosomal tunnel modulate chain elongation rates.The Srp54 GTPase is essential for protein export in the fission yeast Schizosaccharomyces pombe.
P2860
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P2860
Signal recognition particle mediates a transient elongation arrest of preprolactin in reticulocyte lysate.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年学术文章
@wuu
1989年学术文章
@zh-cn
1989年学术文章
@zh-hans
1989年学术文章
@zh-my
1989年学术文章
@zh-sg
1989年學術文章
@yue
1989年學術文章
@zh
1989年學術文章
@zh-hant
name
Signal recognition particle me ...... lactin in reticulocyte lysate.
@ast
Signal recognition particle me ...... lactin in reticulocyte lysate.
@en
type
label
Signal recognition particle me ...... lactin in reticulocyte lysate.
@ast
Signal recognition particle me ...... lactin in reticulocyte lysate.
@en
prefLabel
Signal recognition particle me ...... lactin in reticulocyte lysate.
@ast
Signal recognition particle me ...... lactin in reticulocyte lysate.
@en
P2860
P356
P1476
Signal recognition particle me ...... lactin in reticulocyte lysate.
@en
P2093
P2860
P304
P356
10.1083/JCB.109.6.2617
P407
P433
P577
1989-12-01T00:00:00Z