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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 19kDa

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Top mentioned proteins: SRP54, SRP72, SRP14, CAN, ACID
Papers on SRP19
Circularization restores signal recognition particle RNA functionality in Thermoproteus.
Randau et al., Marburg an der Lahn, Germany. In Elife, 2014
Canonical SRP RNA genes have not been identified for some Thermoproteus species even though they contain SRP19 and SRP54 proteins.
SRP RNA remodeling by SRP68 explains its role in protein translocation.
Sinning et al., Heidelberg, Germany. In Science, 2014
We present the crystal structures of the RNA-binding domain of SRP68 (SRP68-RBD) alone and in complex with SRP RNA and SRP19.
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.
The association between DNA copy number aberrations at chromosome 5q22 and gastric cancer.
Wang et al., Kao-hsiung, Taiwan. In Plos One, 2013
We searched for a CNV and found a CNV (Variation 7468) containing part of the APC gene, the SRP19 gene and the REEP5 gene.
Mov10 and APOBEC3G localization to processing bodies is not required for virion incorporation and antiviral activity.
Pathak et al., In J Virol, 2013
In addition, overexpression of SRP19, which binds to 7SL RNA, depleted A3G from P bodies but did not affect its virion incorporation.
Compositional and structural features related to thermal stability in the archaea SRP19 and SRP54 signal recognition particle proteins.
Miralles, Paris, France. In J Mol Evol, 2011
In this study, we have used the archaea genome datasets to identify molecular trends related to thermal adaptation in the protein components (SRP19 and SRP54) of the signal recognition particle (SRP).
Structural insights into the assembly of the human and archaeal signal recognition particles.
Sinning et al., Heidelberg, Germany. In Acta Crystallogr D Biol Crystallogr, 2010
crystal structures of a crenarchaeal and the all-human SRP19-signal recognition particle RNA binary complexes presented here show that the asymmetric loop is bulged out in both binary complexes.
Variation in gene expression profiles of human monocytic U937 cells exposed to various fluxes of nitric oxide.
Drapier et al., Gif-sur-Yvette, France. In Free Radic Biol Med, 2010
cDNA microarray analysis and real-time quantitative PCR identified 45 NO-sensitive genes (>or=2-fold change), among which KLF2, KLF6, TSC22D3, DDIT4, MKP-5 (up-regulated), KIF23, histone H4, ARL6IP2, CLNS1A, SLC7A6, CDKN3, SRP19, and BCL11A (down-regulated) have not been reported before.
Archaea signal recognition particle shows the way.
Bhuiyan et al., Tyler, United States. In Archaea, 2009
Archaea SRP is composed of an SRP RNA molecule and two bound proteins named SRP19 and SRP54.
Characterization of RNA aptamers against SRP19 protein having sequences different from SRP RNA.
Sakamoto et al., Narashino, Japan. In Nucleic Acids Symp Ser (oxf), 2008
In this study, high affinity RNA molecules against SRP19 protein were selected by using a randomized library.
A threefold RNA-protein interface in the signal recognition particle gates native complex assembly.
Weeks et al., Chapel Hill, United States. In J Mol Biol, 2007
Data show that the presence of SRP54 during SRP19-RNA assembly dramatically alters the folding energy landscape to create a non-native folding pathway that leads to an aberrant SRP19-RNA conformation.
S-domain assembly of the signal recognition particle.
Hainzl et al., Umeå, Sweden. In Curr Opin Struct Biol, 2003
In higher eukaryotes, SRP biogenesis involves the sequential binding of SRP19 and SRP54 proteins to the S domain of 7S RNA.
Induced structural changes of 7SL RNA during the assembly of human signal recognition particle.
Nagai et al., Cambridge, United Kingdom. In Nat Struct Biol, 2002
crystal structure of a human SRP ternary complex consisting of SRP19, the M domain of SRP54 and the S domain of 7SL RNA
Structure of the SRP19 RNA complex and implications for signal recognition particle assembly.
Sauer-Eriksson et al., Umeå, Sweden. In Nature, 2002
Structure of the SRP19 RNA complex
Crystal structure of an early protein-RNA assembly complex of the signal recognition particle.
Cusack et al., Heidelberg, Germany. In Science, 2001
1.8 angstrom resolution crystal structure of human SRP19 in complex with its primary binding site on helix 6 of SRP RNA was determined
Identification of deletion mutations and three new genes at the familial polyposis locus.
Robertson et al., Salt Lake City, United States. In Cell, 1991
One of the new genes contained sequence identical to SRP19, the gene coding for the 19 kd component of the ribosomal signal recognition particle.
Identification and characterization of the familial adenomatous polyposis coli gene.
Robertson et al., Salt Lake City, United States. In Cell, 1991
DNA from 61 unrelated patients with adenomatous polyposis coli (APC) was examined for mutations in three genes (DP1, SRP19, and DP2.5) located within a 100 kb region deleted in two of the patients.
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