Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane.
about
Diverse RNA-binding proteins interact with functionally related sets of RNAs, suggesting an extensive regulatory systemHuman autoantibodies against the 54 kDa protein of the signal recognition particle block function at multiple stagesGetting on target: the archaeal signal recognition particleX-ray structures of the signal recognition particle receptor reveal targeting cycle intermediatesSignal recognition particle components in the nucleolusMembrane integration of Sec61alpha: a core component of the endoplasmic reticulum translocation complexIntramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid dropletsThe 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 ribosome regulates the GTPase of the beta-subunit of the signal recognition particle receptorMembrane topogenesis of a type I signal-anchor protein, mouse synaptotagmin II, on the endoplasmic reticulumMechanism of association and reciprocal activation of two GTPasesTransforming growth factor beta-1 (TGFB1) and peak bone mass: association between intragenic polymorphisms and quantitative ultrasound of the heel.Therapeutic cancer vaccines: past, present, and futureThe Not4 RING E3 Ligase: A Relevant Player in Cotranslational Quality ControlFolding of hepatitis C virus E1 glycoprotein in a cell-free system.Structure of the phylogenetically most conserved domain of SRP RNA.Structure and assembly of the Alu domain of the mammalian signal recognition particleStructure of the GMPPNP-stabilized NG domain complex of the SRP GTPases Ffh and FtsYX-ray structure of the T. Aquaticus Ftsy:GDP complex suggests functional roles for the C-terminal helix of the SRP GTPasesCrystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communicationCryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptorA Structural Model of the Sgt2 Protein and Its Interactions with Chaperones and the Get4/Get5 ComplexThe SH3 domain of the Saccharomyces cerevisiae peroxisomal membrane protein Pex13p functions as a docking site for Pex5p, a mobile receptor for the import PTS1-containing proteins.Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo.Elongation arrest is a physiologically important function of signal recognition particle.Allele-specific suppression of a defective trans-Golgi network (TGN) localization signal in Kex2p identifies three genes involved in localization of TGN transmembrane proteins.An interaction between the SRP receptor and the translocon is critical during cotranslational protein translocation.The refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocationA functional GTPase domain, but not its transmembrane domain, is required for function of the SRP receptor beta-subunit.Sec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membrane.The Alu domain homolog of the yeast signal recognition particle consists of an Srp14p homodimer and a yeast-specific RNA structure.Membrane insertion, processing, and topology of cystic fibrosis transmembrane conductance regulator (CFTR) in microsomal membranesSelective inhibition of cotranslational translocation of vascular cell adhesion molecule 1Co-translational protein targeting by the signal recognition particleSRbeta coordinates signal sequence release from SRP with ribosome binding to the translocon.A complex of the signal sequence binding protein and the SRP RNA promotes translocation of nascent proteinsbam Lipoproteins Assemble BamA in vitro.Membrane topology and insertion of membrane proteins: search for topogenic signalsProteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins.Intracellular transport and secretion of salivary proteins.
P2860
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P2860
Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane.
@en
type
label
Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane.
@en
prefLabel
Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane.
@en
P1476
Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane.
@en
P2093
P304
P356
10.1146/ANNUREV.CB.10.110194.000511
P577
1994-01-01T00:00:00Z