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

Tryptophanyl-tRNA synthetase

tryptophanyl-tRNA synthetase, tryptophan-tRNA-ligase
Top mentioned proteins: ACID, CAN, HAD, IFN-gamma, STEP
Papers using tryptophanyl-tRNA synthetase antibodies
A polycomb repression signature in metastatic prostate cancer predicts cancer outcome.
Randau Lennart, In PLoS ONE, 2006
... (mouse monoclonal-AR441, Lab Vision, Fremont, CA), GARS (glycyl-tRNA synthetase, rabbit polyclonal, Abcam, Cambridge, MA), WARS (tryptophanyl-tRNA synthetase, rabbit polyclonal, Abcam), KARS (lysyl-tRNA synthetase, rabbit ...
Papers on tryptophanyl-tRNA synthetase
Effect of Mini-Tyrosyl-tRNA Synthetase/Mini-Tryptophanyl-tRNA Synthetase on Angiogenesis in Rhesus Monkeys after Acute Myocardial Infarction.
Zhang et al., Chengdu, China. In Cardiovasc Ther, Feb 2016
AIMS: The purpose of this study was to clarify the effect of mini-tyrosyl-tRNA synthetase/mini-tryptophanyl-tRNA synthetase (mini-TyrRS/mini-TrpRS) in ischemic angiogenesis in rhesus monkeys with acute myocardial infarction (AMI).
Selective Inhibition of Bacterial Tryptophanyl-tRNA Synthetases by Indolmycin Is Mechanism-based.
Carter et al., Chapel Hill, United States. In J Biol Chem, Feb 2016
Indolmycin is a natural tryptophan analog that competes with tryptophan for binding to tryptophanyl-tRNA synthetase (TrpRS) enzymes.
Overexpressed tryptophanyl-tRNA synthetase, an angiostatic protein, enhances oral cancer cell invasiveness.
Yu et al., Taiwan. In Oncotarget, Oct 2015
Previously, we identified the angiostatic agent tryptophanyl-tRNA synthetase (TrpRS) as a dysregulated protein in OSCC based on a proteomics approach.
Resveratrol regulates naïve CD 8+ T-cell proliferation by upregulating IFN-γ-induced tryptophanyl-tRNA synthetase expression.
Park et al., Taejŏn, South Korea. In Bmb Rep, May 2015
We found that resveratrol enhances interferon (IFN)-γ-induced tryptophanyl-tRNA-synthetase (TTS) expression in bone marrow- derived dendritic cells (BMDCs).
In vitro reconstitution of indolmycin biosynthesis reveals the molecular basis of oxazolinone assembly.
Ryan et al., Vancouver, Canada. In Proc Natl Acad Sci U S A, Apr 2015
The bacterial tryptophanyl-tRNA synthetase inhibitor indolmycin features a unique oxazolinone heterocycle whose biogenetic origins have remained obscure for over 50 years.
The conceptus regulates tryptophanyl-tRNA synthetase and superoxide dismutase 2 in the sheep caruncular endometrium during early pregnancy.
Fowler et al., Jouy-le-Moutier, France. In Int J Biochem Cell Biol, Mar 2015
However, little is known about the regulation of endometrial tryptophanyl tRNA synthetase (WARS) and manganese superoxide dismutase (SOD2) protein expression by the implanting and post-implanting conceptus.
Exploring the substrate range of wild-type aminoacyl-tRNA synthetases.
Wang et al., New Haven, United States. In Chembiochem, 2014
Our results also show that E. coli tryptophanyl-tRNA synthetase (TrpRS) and tyrosyl-tRNA synthetase have overlapping substrate ranges.
A role for [Fe4S4] clusters in tRNA recognition--a theoretical study.
Stiebritz, Zürich, Switzerland. In Nucleic Acids Res, 2014
One fascinating example is a tryptophanyl-tRNA synthetase from the thermophilic bacterium Thermotoga maritima, TmTrpRS, that has recently been structurally characterized.
Listeria monocytogenes as novel carrier system for the development of live vaccines.
Stritzker et al., Würzburg, Germany. In Int J Med Microbiol, 2008
Based on the deletion of the chromosomal copy of the tryptophanyl-tRNA synthetase gene (trpS) and plasmid-based in trans complementation of the same, we were able to establish a balanced-lethal plasmid system in L. monocytogenes.
Relationship of two human tRNA synthetases used in cell signaling.
Ewalt et al., Los Angeles, United States. In Trends Biochem Sci, 2004
Human tyrosyl-tRNA synthetase (TyrRS) and tryptophanyl-tRNA synthetase (TrpRS) are closely related, dual function enzymes that act in protein biosynthesis and angiogenesis.
Interdomain interactions in oligomeric enzymes: creation of asymmetry in homo-oligomers and role in metabolite channeling between active centers of hetero-oligomers.
Nagradova, Moscow, Russia. In Febs Lett, 2001
In this review, the role of intrasubunit and intersubunit domain-domain interactions in the origins of pre-existent asymmetry of homo-oligomeric D-glyceraldehyde-3-phosphate dehydrogenase and tryptophanyl-tRNA synthetase is discussed on the basis of recent X-ray data and other available information about the properties of these and related enzymes.
Some novel transcription attenuation mechanisms used by bacteria.
Sarsero et al., Stanford, United States. In Biochimie, 1995
A temperature sensitive tryptophanyl-tRNA synthetase (trpS) mutant was previously observed to overexpress the trp operon and trpG, when grown at elevated temperatures in the presence of tryptophan.
Substrate selection by aminoacyl-tRNA synthetases.
Söll et al., New Haven, United States. In Nucleic Acids Symp Ser, 1994
The recent solving of the crystal structure of tryptophanyl-tRNA synthetase (TrpRS) has allowed comparable studies to be initiated in an aminoacyl-tRNA synthetase which, unlike GlnRS, does not require tRNA binding prior to amino acid activation.
Overcoming non-isomorphism by phase permutation and likelihood scoring: solution of the TrpRS crystal structure.
Carter et al., Chapel Hill, United States. In Acta Crystallogr A, 1994
In the crystal structure determination of the Bacillus stearothermophilus tryptophanyl-tRNA synthetase (TrpRS), however, the following had to be dealt with simultaneously: (1) a serious lack of isomorphism in the heavy-atom derivatives, resulting in large starting-phase errors; and (2) an initially poorly known molecular envelope.
Direct phase determination for the molecular envelope of tryptophanyl-tRNA synthetase from Bacillus stearothermophilus by X-ray contrast variation.
Bricogne et al., Chapel Hill, United States. In Acta Crystallogr A, 1990
Monoclinic crystals of Bacillus stearothermophilus tryptophanyl-tRNA synthetase grown in the presence of substrate tryptophan (space group P2(1)) display evidence of a low-resolution trigonal space group (P321).
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