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Signal recognition particle receptor

SR alpha, DP alpha
The gene encodes a subunit of the endoplasmic reticulum signal recognition particle receptor that, in conjunction with the signal recognition particle, is involved in the targeting and translocation of signal sequence tagged secretory and membrane proteins across the endoplasmic reticulum. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Apr 2010] (from NCBI)
Top mentioned proteins: CAN, ACID, HAD, SRP54, MHC
Papers on SR alpha
Adenoviral targeting of gene expression to tumors.
Gerard et al., Dallas, United States. In Cancer Gene Ther, 2010
Constitutively active viral promoters (RSV, SRalpha) varied widely in their tumor selectivity, but hypoxia-responsive promoters (carbonic anhydrase 9, PAI-1, SOD2 and several chimeric constructs) showed the most tumor-selective expression.
Analysis of meniscal degeneration and meniscal gene expression.
Gruber et al., Charlotte, United States. In Bmc Musculoskelet Disord, 2009
Many of the genes classified in the biological processes of immune response, inflammatory response, biomineral formation and cell proliferation, including major histocompatibility complex, class II, DP alpha 1 (HLA-DPA1), integrin, beta 2 (ITGB2), ectonucleotide pyrophosphatase/phosphodiesterase 1 (ENPP1), ankylosis, progressive homolog (ANKH) and fibroblast growth factor 7 (FGF7), were expressed at significantly higher levels in OA meniscal cells compared to normal meniscal cells.
How transcription proceeds in a large artificial heterochromatin in human cells.
Shimizu et al., Hiroshima, Japan. In Nucleic Acids Res, 2009
We found that transcription of genes downstream to no-inducible SRalpha promoter was restricted to a few specific points inside the large HSR domain.
Predominant membrane localization is an essential feature of the bacterial signal recognition particle receptor.
Koch et al., Freiburg, Germany. In Bmc Biol, 2008
The SRbeta subunit is an integral membrane protein, which tethers the SRP-interacting SRalpha subunit permanently to the endoplasmic reticulum membrane.
Construction and preliminary investigation of a plasmid containing a novel immunotoxin DT390-IL-18 gene for the prevention of murine experimental autoimmune encephalomyelitis.
Zhang et al., Chengdu, China. In Dna Cell Biol, 2008
The novel eukaryotic plasmid DT390-IL-18-SRalpha, encoding recombinant immunotoxin DT390-IL-18, was constructed.
A cleavable N-terminal membrane anchor is involved in membrane binding of the Escherichia coli SRP receptor.
Koch et al., Freiburg, Germany. In J Mol Biol, 2008
Different from eukaryotes, the bacterial signal recognition particle (SRP) receptor lacks a membrane-tethering SRP receptor (SR) beta subunit and is composed of only the SR alpha homologue FtsY.
Expression of pIX gene induced by transgene promoter: possible cause of host immune response in first-generation adenoviral vectors.
Saito et al., Ōsaka, Japan. In Hum Gene Ther, 2007
Whereas CAG and SRalpha promoters activated the pIX promoter considerably through their enhancer effects, the EF1alpha promoter hardly did.
Differential effects of Mxi1-SRalpha and Mxi1-SRbeta in Myc antagonism.
Schreiber-Agus et al., United States. In Febs J, 2007
Two Mxi1 protein isoforms, Mxi1-SRalpha and Mxi1-SRbeta, have been described as sharing many biological properties.
[Therapeutic effect of a new recombinant immunotoxin mMIP-1alpha-DT390 on experimental autoimmune encephalomyelitis].
Zhang et al., Chengdu, China. In Nan Fang Yi Ke Da Xue Xue Bao, 2007
METHODS: EAE was induced in the low-sensitive strain C57BL/6 mice with intraperitoneal injection of myelin basic protein (MBP) to simulate the human disease multiple sclerosis, followed by intramuscular injection of cationic liposome carrying the plasmid DNA SRalpha-mMIP-1alpha-DT390 in the leg muscle to elicit resistance to EAE development.
Structural basis for the function of the beta subunit of the eukaryotic signal recognition particle receptor.
Blobel et al., New York City, United States. In Cell, 2003
This targeting step is regulated by three G proteins, SRP54, SR alpha, and SR beta, which act in concert.
Role of Sec61alpha in the regulated transfer of the ribosome-nascent chain complex from the signal recognition particle to the translocation channel.
Gilmore et al., Worcester, United States. In Cell, 2000
Ribosome-stripped microsomes were digested with proteases to sever cytoplasmic domains of SRalpha, SRbeta, TRAM, and the Sec61 complex.
Empty site forms of the SRP54 and SR alpha GTPases mediate targeting of ribosome-nascent chain complexes to the endoplasmic reticulum.
Gilmore et al., Worcester, United States. In Cell, 1997
The SRP54 and SR alpha subunits of the signal recognition particle (SRP) and the SRP receptor (SR) undergo a tightly coupled GTPase cycle that mediates the signal sequence-dependent attachment of ribosomes to the Sec61 complex.
Interaction of E. coli Ffh/4.5S ribonucleoprotein and FtsY mimics that of mammalian signal recognition particle and its receptor.
Walter et al., San Francisco, United States. In Nature, 1994
During targeting, the 54K SRP subunit (M(r) 54,000; SRP54), a GTP-binding protein, binds to signal sequences and then interacts with the alpha-subunit of the SRP receptor (SR alpha), another GTP-binding protein.
GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation.
Walter et al., San Francisco, United States. In Nature, 1993
This complex is directed to the endoplasmic reticulum membrane as a result of its interaction with the SRP receptor, a membrane protein composed of two subunits, SR alpha and SR beta, each of which also contains a GTP-binding domain.
A GTPase cycle in initiation of protein translocation across the endoplasmic reticulum membrane.
Walter et al., San Francisco, United States. In Ciba Found Symp, 1992
Targeting is mediated by the binding of SRP to the SRP receptor, a membrane protein comprising two different subunits, SR alpha and SR beta.
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