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Signal recognition particle receptor, B subunit

SRbeta, APMCF1
The protein encoded by this gene has similarity to mouse protein which is a subunit of the signal recognition particle receptor (SR). This subunit is a transmembrane GTPase belonging to the GTPase superfamily. It anchors alpha subunit, a peripheral membrane GTPase, to the ER membrane. SR is required for the cotranslational targeting of both secretory and membrane proteins to the ER membrane. [provided by RefSeq, Jul 2008] (from NCBI)
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Top mentioned proteins: SR alpha, CAN, SRP54, p16, V1a
Papers on SRbeta
Measurement of the internal bremsstrahlung spectrum of a (89)Sr beta emitter in the 1-100keV photon energy regime.
Dhaliwal et al., Sangrūr, India. In Appl Radiat Isot, Apr 2015
The internal bremsstrahlung (IB) spectrum of (89)Sr, which is a unique first forbidden beta emitter, is studied in the 1-100keV photon energy regime.
[Underlying examination in the imaging of 89Sr bremsstrahlung radiation].
Kubota et al., Japan. In Nihon Hoshasen Gijutsu Gakkai Zasshi, 2010
We examined the optimal energy window and collimator when imaging with a gamma camera using bremsstrahlung radiation produced from (89)Sr beta rays.
Dose-effect relationships for recurrence of keloid and pterygium after surgery and radiotherapy.
Jürgenliemk-Schulz et al., Utrecht, Netherlands. In Int J Radiat Oncol Biol Phys, 2009
For pterygium recurrence after bare sclera surgery and (90)Sr beta-irradiation, a BED of about 30 Gy seems to be sufficient also to reduce the recurrence rate to less than 10%.
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.
Subcellular localization of APMCF1 and its biological significance of expression pattern in normal and malignant human tissues.
Yan et al., China. In J Exp Clin Cancer Res, 2008
BACKGROUND: APMCF1 is a novel human gene first cloned from apoptotic MCF-7 cells.
Direct imaging of radionuclide-produced electrons and positrons with an ultrathin phosphor.
Barrett et al., Tucson, United States. In J Nucl Med, 2008
The spatial resolution and sensitivity of the system were measured with a 3.7-kBq (90)Y/(90)Sr beta-source and a 70-microm resin bead labeled with (99m)Tc.
An interaction between the SRP receptor and the translocon is critical during cotranslational protein translocation.
Gilmore et al., Worcester, United States. In J Cell Biol, 2008
Surprisingly, the slow growth and cotranslational translocation defects caused by deletion of the transmembrane (TM) span of yeast SRbeta (SRbeta-DeltaTM) are exaggerated when the SSH1 gene is disrupted.
Pirh2 interacts with and ubiquitylates signal recognition particle receptor beta subunit.
Kitagawa et al., Hamamatsu, Japan. In Biomed Res, 2008
In this study, we identified signal recognition particle receptor beta subunit (SRbeta), an integral membrane protein of the endoplasmic reticulum (ER), as a novel Pirh2-interacting protein by yeast two-hybrid screening.
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.
Homologs of eukaryotic Ras superfamily proteins in prokaryotes and their novel phylogenetic correlation with their eukaryotic analogs.
Tian et al., Kunming, China. In Gene, 2007
Our phylogenetic analysis indicated eukaryotic Rab, Ran, Ras, and Rho families have the closest phylogenetic correlation with the 13 unambiguous prokaryotic homologs, whereas the other three eukaryotic protein families (SRbeta, Sar1, and Arf) branch separately from them, but have a relatively close relationship with the methanogenic archaebacterial homologs and MglA.
Introduction of G1 phase arrest in Human Hepatocellular carcinoma cells (HHCC) by APMCF1 gene transfection through the down-regulation of TIMP3 and up-regulation of the CDK inhibitors p21.
Wang et al., Xi'an, China. In Mol Biol Rep, 2006
APMCF1 participates at least partially in cell cycle regulation through regulating genes such as p21 and TIMP3.
Homodimerization of the G protein SRbeta in the nucleotide-free state involves proline cis/trans isomerization in the switch II region.
Blobel et al., Cambridge, United States. In Proc Natl Acad Sci U S A, 2006
Results describe the 2.2-A crystal structure of the nucleotide-free signal-recognition particle receptor beta domain.
Isolation of a novel member of small G protein superfamily and its expression in colon cancer.
Wang et al., Xi'an, China. In World J Gastroenterol, 2003
APMCF1 may be the gene coding human signal recognition particle receptor beta and belongs to the small-G protein superfamily. Its strong expression pattern in colon cancer suggests it may play a role in colon cancer 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.
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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