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A functional GTPase domain, but not its transmembrane domain, is required for function of the SRP receptor beta-subunit
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scholarly article
1 reference
stated in
PubMed
PubMed ID
9679135
retrieved
1 December 2016
title
A functional GTPase domain, but not its transmembrane domain, is required for function of the SRP receptor beta-subunit
(English)
1 reference
stated in
PubMed
PubMed ID
9679135
retrieved
1 December 2016
main subject
transmembrane protein
0 references
Signal recognition particle receptor subunit alpha YDR292C
1 reference
stated in
GOA release 2020-03-11
Signal recognition particle receptor subunit beta YKL154W
1 reference
stated in
GOA release 2020-03-11
author name string
S C Ogg
series ordinal
1
0 references
W P Barz
series ordinal
2
0 references
P Walter
series ordinal
3
0 references
language of work or name
English
0 references
publication date
27 July 1998
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published in
Journal of Cell Biology
1 reference
stated in
PubMed
PubMed ID
9679135
retrieved
1 December 2016
volume
142
0 references
page(s)
341-54
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issue
2
0 references
cites work
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GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation
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Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression
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The 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 membrane
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Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle
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The signal recognition particle receptor is a complex that contains two distinct polypeptide chains
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KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene
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The signal recognition particle in S. cerevisiae
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Signal recognition particle receptor is important for cell growth and protein secretion in Saccharomyces cerevisiae
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New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
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A Saccharomyces cerevisiae genomic plasmid bank based on a centromere-containing shuttle vector
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Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum
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Signal recognition particle contains a 7S RNA essential for protein translocation across the endoplasmic reticulum
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The signal recognition particle receptor mediates the GTP-dependent displacement of SRP from the signal sequence of the nascent polypeptide
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Targeting pathways to the endoplasmic reticulum membrane
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Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes
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Signal sequences specify the targeting route to the endoplasmic reticulum membrane
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29 September 2017
Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
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29 September 2017
Histidine-118 of elongation factor Tu: its role in aminoacyl-tRNA binding and regulation of the GTPase activity
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29 September 2017
Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane
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29 September 2017
Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor
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29 September 2017
A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum
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29 September 2017
Formation of a functional ribosome-membrane junction during translocation requires the participation of a GTP-binding protein
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PubMed Central
reference URL
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29 September 2017
Photocrosslinking of the signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle
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29 September 2017
A new RAS mutation that suppresses the CDC25 gene requirement for growth of Saccharomyces cerevisiae
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29 September 2017
Structural and functional dissection of Sec62p, a membrane-bound component of the yeast endoplasmic reticulum protein import machinery
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29 September 2017
The methionine-rich domain of the 54 kd protein subunit of the signal recognition particle contains an RNA binding site and can be crosslinked to a signal sequence
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29 September 2017
FtsY, the prokaryotic signal recognition particle receptor homologue, is essential for biogenesis of membrane proteins.
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2 June 2018
Characterization of molecules involved in protein translocation using a specific antibody
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2 June 2018
Topology of signal recognition particle receptor in endoplasmic reticulum membrane.
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2 June 2018
Each of the activities of signal recognition particle (SRP) is contained within a distinct domain: analysis of biochemical mutants of SRP.
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PubMed Central
reference URL
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2 June 2018
Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases
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Crossref
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21 January 2018
Oligomeric Rings of the Sec61p Complex Induced by Ligands Required for Protein Translocation
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Crossref
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21 January 2018
The signal sequence of nascent preprolactin interacts with the 54K polypeptide of the signal recognition particle
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1083%2FJCB.142.2.341
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21 January 2018
49 Rapid DNA isolations for enzymatic and hybridization analysis
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Crossref
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21 January 2018
Empty site forms of the SRP54 and SR alpha GTPases mediate targeting of ribosome-nascent chain complexes to the endoplasmic reticulum
1 reference
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Crossref
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21 January 2018
A structural and functional analysis of the docking protein. Characterization of active domains by proteolysis and specific antibodies
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9679135
retrieved
12 December 2020
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inferred from PubMed ID database lookup
Identifiers
DOI
10.1083/JCB.142.2.341
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PMCID
2133050
0 references
PubMed ID
9679135
1 reference
stated in
PubMed
PubMed ID
9679135
retrieved
1 December 2016
ResearchGate publication ID
13606231
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