Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains
about
Getting on target: the archaeal signal recognition particleCloning and sequence analyses of cDNAs for interferon- and virus-induced human Mx proteins reveal that they contain putative guanine nucleotide-binding sites: functional study of the corresponding gene promoterA threefold RNA-protein interface in the signal recognition particle gates native complex assemblyAn analysis of vertebrate mRNA sequences: intimations of translational controlProtein translocation across the ER requires a functional GTP binding site in the alpha subunit of the signal recognition particle receptorResistance to influenza virus and vesicular stomatitis virus conferred by expression of human MxA proteinThe 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 receptorSec-secretion and sortase-mediated anchoring of proteins in Gram-positive bacteriaStructure of the GMPPNP-stabilized NG domain complex of the SRP GTPases Ffh and FtsYHeterodimeric GTPase Core of the SRP Targeting ComplexInteraction 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.Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression.SRbeta coordinates signal sequence release from SRP with ribosome binding to the translocon.Assembly of the human signal recognition particle (SRP): overlap of regions required for binding of protein SRP54 and assembly controlA complex of the signal sequence binding protein and the SRP RNA promotes translocation of nascent proteinsMolecular evolution of SRP cycle components: functional implicationsThe complete general secretory pathway in gram-negative bacteriaMembrane topology and insertion of membrane proteins: search for topogenic signalsFunctional characterization of recombinant chloroplast signal recognition particle.The 68 kDa protein of signal recognition particle contains a glycine-rich region also found in certain RNA-binding proteins.Membrane protein biogenesis in Ffh- or FtsY-depleted Escherichia coli.Protein targeting to the bacterial cytoplasmic membrane.Surface proteins of gram-positive bacteria and mechanisms of their targeting to the cell wall envelope.The structure of multiple polypeptide domains determines the signal recognition particle targeting requirement of Escherichia coli inner membrane proteins.ftsE(Ts) affects translocation of K+-pump proteins into the cytoplasmic membrane of Escherichia coli.The nascent-polypeptide-associated complex: having a "NAC" for fidelity in translocation.Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins.Oligomeric complexes involved in translocation of proteins across the membrane of the endoplasmic reticulum.The secD locus of E.coli codes for two membrane proteins required for protein export.Neisseria gonorrhoeae PilA is an FtsY homologEscherichia coli translocase: the unravelling of a molecular machine.Physiological basis for conservation of the signal recognition particle targeting pathway in Escherichia coli.A fast and efficient procedure to produce scFvs specific for large macromolecular complexes.New prospects in studying the bacterial signal recognition particle pathway.Glycoprotein folding in the endoplasmic reticulum.Genetic screen yields mutations in genes encoding all known components of the Escherichia coli signal recognition particle pathway.Signal recognition particle (SRP), a ubiquitous initiator of protein translocation.
P2860
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P2860
Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains
description
1989 nî lūn-bûn
@nan
1989 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Homology of 54K protein of sig ...... h putative GTP-binding domains
@ast
Homology of 54K protein of sig ...... h putative GTP-binding domains
@en
Homology of 54K protein of sig ...... h putative GTP-binding domains
@nl
type
label
Homology of 54K protein of sig ...... h putative GTP-binding domains
@ast
Homology of 54K protein of sig ...... h putative GTP-binding domains
@en
Homology of 54K protein of sig ...... h putative GTP-binding domains
@nl
prefLabel
Homology of 54K protein of sig ...... h putative GTP-binding domains
@ast
Homology of 54K protein of sig ...... h putative GTP-binding domains
@en
Homology of 54K protein of sig ...... h putative GTP-binding domains
@nl
P2093
P356
P1433
P1476
Homology of 54K protein of sig ...... h putative GTP-binding domains
@en
P2093
B Dobberstein
P2888
P304
P356
10.1038/340478A0
P407
P577
1989-08-10T00:00:00Z
P5875
P6179
1043109897