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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

SRA stem-loop interacting RNA binding protein

Steroid receptor RNA activator (SRA, or SRA1; MIM 603819) is a complex RNA molecule containing multiple stable stem-loop structures that functions in coactivation of nuclear receptors. SLIRP interacts with stem-loop structure-7 of SRA (STR7) and modulates nuclear receptor transactivation (Hatchell et al., 2006 [PubMed 16762838]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: HAD, CAN, SRA, OUT, POLYMERASE
Papers on SLIRP
Asymmetric margin setting at the cranial and caudal sides in respiratory gated and non-gated stereotactic body radiotherapy for lung cancer.
Teshima et al., Ōsaka, Japan. In Br J Radiol, Jan 2016
During the 100% duty cycle (DC100), 50% duty cycle (DC50), and 30% duty cycle (DC30), both centered on the 50 phase, the coordinates of the TCs were compared at the most cranial, and caudal positions on both 4DCT and EPID cine.
SLIRP Regulates the Rate of Mitochondrial Protein Synthesis and Protects LRPPRC from Degradation.
Larsson et al., Köln, Germany. In Plos Genet, Aug 2015
We have studied the in vivo role of SLIRP in regulation of mitochondrial DNA (mtDNA) gene expression and show here that it stabilizes its interacting partner protein LRPPRC by protecting it from degradation.
In Silico and in Vitro Study of Binding Affinity of Tripeptides to Amyloid β Fibrils: Implications for Alzheimer's Disease.
Li et al., Warsaw, Poland. In J Phys Chem B, May 2015
In vitro experiments showed that tight-binding tripeptides have significant depolymerizing activities and their DC50 values determined from dose-response curves were in micromolar range.
Tissue-specific responses to the LRPPRC founder mutation in French Canadian Leigh Syndrome.
LSFC Consortium et al., Montréal, Canada. In Hum Mol Genet, Feb 2015
LRPPRC forms a ribonucleoprotein complex with SLIRP, another RNA-binding protein, and this stabilizes polyadenylated mitochondrial mRNAs.
A human mitochondrial poly(A) polymerase mutation reveals the complexities of post-transcriptional mitochondrial gene expression.
Lightowlers et al., New York City, United States. In Hum Mol Genet, 2015
The addition of LRPPRC/SLIRP, a mitochondrial RNA-binding complex, enhanced activity of the wild-type mtPAP resulting in increased overall tail length.
Specific maltose derivatives modulate the swarming motility of nonswarming mutant and inhibit bacterial adhesion and biofilm formation by Pseudomonas aeruginosa.
Luk et al., Syracuse, United States. In Chembiochem, 2014
Although these molecules are not microbicidal, active maltose derivatives with bulky hydrocarbon groups inhibited bacterial adhesion, and exhibited biofilm inhibition and dispersion (IC50 ~20 μM and DC50 ~30 μM, respectively).
A conformationally flexible dinuclear Pt(II) complex with differential behavior of its two states toward quadruplex DNA.
Lippert et al., Dortmund, Germany. In Chemistry, 2013
Thus, the U isomer binds significantly more strongly to quadruplex DNA (DC50 =0.38 μM) than the Z isomer (DC50 =8.50 μM).
Amyloid aggregation of lysozyme: the synergy study of red wine polyphenols.
Nagy et al., Košice, Slovakia. In Proteins, 2013
The anti-amyloid activities of tested polyphenols were evaluated by the median depolymerization concentrations DC50 and median inhibition concentrations IC50 .
[Screening and identification of HLA-A0201 restricted cytotoxic T lymphocyte epitopes from hepatitis B virus E antigen in vitro].
Huang et al., Wenzhou, China. In Zhonghua Gan Zang Bing Za Zhi, 2013
The affinities of each were tested in vitro with T2 cells, which lack the transporter-associated with antigen transport (TAP) protein but express low levels of the MHC class I surface molecule, and measured by the T2 binding assay and DC50 assay.
Loss of the nuclear receptor corepressor SLIRP compromises male fertility.
Leedman et al., Perth, Australia. In Plos One, 2012
SRA stem Loop Interacting RNA-binding Protein (SLIRP) is a Steroid receptor RNA Activator (SRA) RNA-binding protein that is a potent repressor of NR activity.
Analysis of 953 human proteins from a mitochondrial HEK293 fraction by complexome profiling.
Nijtmans et al., Nijmegen, Netherlands. In Plos One, 2012
Our data also highlighted a putative ribonucleotide complex that potentially contains MRPL10, MRPL12 and MRPL53 together with LRPPRC and SLIRP.
Transcription-dependent nuclear localization of DAZAP1 requires an N-terminal signal.
Yen et al., Taipei, Taiwan. In Biochem Biophys Res Commun, 2012
In addition, using a yeast two-hybrid system, we have identified SLIRP as a N42-binding protein which may regulate DAZAP1 subcellular localization.
LRPPRC/SLIRP suppresses PNPase-mediated mRNA decay and promotes polyadenylation in human mitochondria.
Suzuki et al., Tokyo, Japan. In Nucleic Acids Res, 2012
The LRPPRC/SLIRP complex suppressed 3' exonucleolytic mRNA degradation mediated by PNPase and SUV3.
LRPPRC and SLIRP interact in a ribonucleoprotein complex that regulates posttranscriptional gene expression in mitochondria.
LSFC Consortium et al., Montréal, Canada. In Mol Biol Cell, 2010
LRPPRC exists in a high-molecular-weight complex, and it coimmunoprecipitates with SLIRP, a stem-loop RNA-binding protein.
A computational screen for regulators of oxidative phosphorylation implicates SLIRP in mitochondrial RNA homeostasis.
Mootha et al., Boston, United States. In Plos Genet, 2009
SLIRP plays an essential role in maintaining mitochondrial-localized mRNA transcripts that encode OxPhos protein subunits.
SRA and its binding partners: an expanding role for RNA-binding coregulators in nuclear receptor-mediated gene regulation.
Leedman et al., Perth, Australia. In Crit Rev Biochem Mol Biol, 2009
The subsequent identification of molecules capable of binding SRA, including SHARP, p68, and more recently SLIRP, which also function as coregulators, has further broadened our understanding of NR-dependent gene regulation.
The RNA coregulator SRA, its binding proteins and nuclear receptor signaling activity.
Leedman et al., Australia. In Iubmb Life, 2008
The subsequent identification of SRA-binding coregulator proteins, including p68, SHARP and more recently SLIRP, has provided important insight into SRA's mechanism of action and potentially offers new opportunities to target NR signaling pathways for therapeutic gain.
Gene control by large noncoding RNAs.
Nudler et al., New York City, United States. In Sci Stke, 2006
Recent reports identify a functional lncRNA, Evf-2, that operates during development to control the expression of specific homeodomain proteins, and they provide important insights into the mechanism of cooperation between a newly discovered nuclear receptor co-repressor protein (SLIRP) and steroid receptor activator RNA.
SLIRP, a small SRA binding protein, is a nuclear receptor corepressor.
Leedman et al., Australia. In Mol Cell, 2006
Our data demonstrate that SLIRP modulates NR transactivation, suggest it may regulate mitochondrial function, and provide mechanistic insight into interactions between SRA, SLIRP, SRC-1, and NCoR.
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