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

Signal recognition particle 14kDa

SRP14, Srp14p
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Top mentioned proteins: SRP54, SRP19, SRP72, CAN, ACID
Papers on SRP14
Latent Pathways Identification by Microarray Expression Profiles in Thyroid-Associated Ophthalmopathy Patients.
Liu et al., Shanghai, China. In Endocr Pathol, Sep 2015
Several upregulated DEGs encoding signal recognition particle (e.g., SRP14, SRP54, and SRP9) were found to be enriched in protein export pathway.
Engineering protein folding and translocation improves heterologous protein secretion in Saccharomyces cerevisiae.
Hou et al., Jinan, China. In Biotechnol Bioeng, Sep 2015
The over-expression of co-translational translocation components Srp14p and Srp54p enhanced the secretion of three heterologous proteins (β-glucosidase, endoglucanase, and α-amylase), but over-expressing the cytosolic chaperone Ssa1p (involved in post-translational translocation) only enhanced the secretion of β-glucosidase.
CHO cell engineering to prevent polypeptide aggregation and improve therapeutic protein secretion.
Mermod et al., Genève, Switzerland. In Metab Eng, 2014
We further show that proper processing and secretion were restored by over-expressing human signal receptor protein SRP14 and other components of the secretion pathway.
Plasmodium falciparum signal recognition particle components and anti-parasitic effect of ivermectin in blocking nucleo-cytoplasmic shuttling of SRP.
Tuteja et al., New Delhi, India. In Cell Death Dis, 2013
Here we report that Plasmodium falciparum SRP is composed of six polypeptides; SRP9, SRP14, SRP19, SRP54, SRP68 and SRP72 and a 303nt long SRP RNA.
Establishing reference genes for use in real-time quantitative PCR analysis of early equine embryos.
Stout et al., Utrecht, Netherlands. In Reprod Fertil Dev, 2010
SRP14, RPL4 and PGK1 were identified by geNorm analysis as stably expressed reference genes suitable for data normalisation.
Residues in SRP9/14 essential for elongation arrest activity of the signal recognition particle define a positively charged functional domain on one side of the protein.
Strub et al., Genève, Switzerland. In Rna, 2010
mutational study on SRP9/14 that identified and characterized regions and single residues essential for elongation arrest activity
Structure of SRP14 from the Schizosaccharomyces pombe signal recognition particle.
Cusack et al., Orsay, France. In Acta Crystallogr D Biol Crystallogr, 2009
Many of the protein-RNA contacts centred on the conserved U-turn motif are likely to be conserved in fission yeast.The combination of SAD and RIP phases yielded an interpretable electron-density map.
SRP keeps polypeptides translocation-competent by slowing translation to match limiting ER-targeting sites.
Strub et al., Genève, Switzerland. In Cell, 2008
SRP14 mutant proteins with absence of a peptide elongation delay caused inefficient targeting of preproteins leading to defects in secretion, depletion of proteins in the endogenous membranes, and reduced cell growth.
A new mechanism of 6-((2-(dimethylamino)ethyl)amino)-3-hydroxy-7H-indeno(2,1-c)quinolin-7-one dihydrochloride (TAS-103) action discovered by target screening with drug-immobilized affinity beads.
Handa et al., Yokohama, Japan. In Mol Pharmacol, 2008
The results revealed that TAS-103 disrupts SRP complex formation and reduces the amount of SRP14 and SRP19.
Genomic selection of reference genes for real-time PCR in human myocardium.
Cameron et al., Christchurch, New Zealand. In Bmc Med Genomics, 2007
RESULTS: Signal recognition particle 14 kDa (SRP14), tumor protein, translationally-controlled 1 (TPT1) and eukaryotic elongation factor 1A1 (EEF1A1) were ranked the most stable genes.
Characterization of APOBEC3G binding to 7SL RNA.
Trono et al., Lausanne, Switzerland. In Retrovirology, 2007
However, we also demonstrate that APOBEC3F and APOBEC3G are normally recruited into and inhibit the infectivity of DeltaVif HIV1 virions when 7SLRNA is prevented from accessing particles by RNA interference against SRP14 or by over expression of SRP19, both components of the signal recognition particle.
Unraveling the components of protein translocation pathway in human malaria parasite Plasmodium falciparum.
Tuteja, New Delhi, India. In Arch Biochem Biophys, 2007
SRP contains SRP RNA and other polypeptides such as SRP9, SRP14, SRP19 and SRP54.
The tmRDB and SRPDB resources.
Zwieb et al., Århus, Denmark. In Nucleic Acids Res, 2006
Also shown are alignments of the tmRNA-associated proteins SmpB, ribosomal protein S1, alanyl-tRNA synthetase and Elongation Factor Tu, as well as the SRP proteins SRP9, SRP14, SRP19, SRP21, SRP54 (Ffh), SRP68, SRP72, cpSRP43, Flhf, SRP receptor (alpha) and SRP receptor (beta).
Advances in the structure and functions of signal recognition particle in protein targeting.
Singh et al., Chandīgarh, India. In J Biol Regul Homeost Agents, 2003
SRP14 and SRP9 help in the elongation arrest by interacting with signal peptide.
Structure and assembly of the Alu domain of the mammalian signal recognition particle.
Cusack et al., Grenoble, France. In Nature, 2000
The Alu domain of the mammalian signal recognition particle (SRP) comprises the heterodimer of proteins SRP9 and SRP14 bound to the 5' and 3' terminal sequences of SRP RNA.
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