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Threonyl-tRNA synthetase

Tars, Threonine-tRNA Ligase
Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. Threonyl-tRNA synthetase belongs to the class-II aminoacyl-tRNA synthetase family [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, Interleukin-2, HAD, STEP, vascular endothelial growth factor
Papers on Tars
Aminoacyl-tRNA synthetase dependent angiogenesis revealed by a bioengineered macrolide inhibitor.
Francklyn et al., Cambridge, United Kingdom. In Sci Rep, 2014
These include angiogenesis, and human threonyl-tRNA synthetase (TARS) represents a potent pro-angiogenic AARS.
Threonyl-tRNA synthetase overexpression correlates with angiogenic markers and progression of human ovarian cancer.
Lounsbury et al., Burlington, United States. In Bmc Cancer, 2013
Our research has revealed that threonyl-tRNA synthetase (TARS) has an extracellular angiogenic activity separate from its function in protein synthesis.
Secreted Threonyl-tRNA synthetase stimulates endothelial cell migration and angiogenesis.
Lounsbury et al., Burlington, United States. In Sci Rep, 2012
Threonyl-tRNA synthetase (TARS) is an autoantigen in the autoimmune disorder myositis, and borrelidin, a potent inhibitor of TARS, inhibits angiogenesis.
Integrative genomics analysis of chromosome 5p gain in cervical cancer reveals target over-expressed genes, including Drosha.
Murty et al., New York City, United States. In Mol Cancer, 2007
Other 5p genes identified as targets of CNI play a role in DNA repair and cell cycle regulation (BASP1, TARS, PAIP1, BRD9, RAD1, SKP2, and POLS), signal transduction (OSMR), and mitochondrial oxidative phosphorylation (NNT, SDHA, and NDUFS6), suggesting that disruption of pathways involving these genes may contribute to CC progression.
Global gene expression profiling of ischemic preconditioning in the rat retina.
Bergen et al., Amsterdam, Netherlands. In Mol Vis, 2006
The group of altered genes contained a significant overrepresentation of genes involved in aminoacyl-tRNA synthetase activity (Iars, Lars, Cars, Yars, Gars, Tars), amino acid transport (Slc3a2, Slc6a6, Slc7a1, Slc38a2), regulation of transcription (including Egr1, Egr4, Nr4a1, Nr4a3, c-fos), and cell death (including Anxa1, Trib3).
In vivo retrovirus-mediated herpes simplex virus thymidine kinase gene therapy approach for adult T cell leukemia in a rat model.
Tomonaga et al., Nagasaki, Japan. In Jpn J Cancer Res, 1997
Following infection of the HTLV-I-transformed and tax-expressing rat T cell line TARS-1 with this retrovirus (LNLTK virus), high levels of HSV TK expression were observed and resulted in increased susceptibility to ganciclovir (GCV).
Producing positive, negative, and no cooperativity by mutations at a single residue located at the subunit interface in the aspartate receptor of Salmonella typhimurium.
Koshland et al., Berkeley, United States. In Biochemistry, 1996
Site-directed mutagenesis of the aspartate receptor of Salmonella typhimurium (Tars) at serine 68, a residue located within the aspartate binding pocket and at the subunit interface, identified this residue as an allosteric switch in this receptor.
Studies of the structural organization of a bacterial chemoreceptor by electron microscopy.
Hazelbauer et al., Pullman, United States. In J Struct Biol, 1994
Given the dimensions of the periplasmic domain of the closely related receptor Tars, determined by X-ray crystallography, and a minimum bilayer thickness of 3 nm, the cytoplasmic domain would be approximately 5.0 by 4.4 nm.
Phenotypic progression of a rat lymphoid cell line immortalized by human T-lymphotropic virus type I to induce lymphoma/leukemia-like disease in rats.
Mori et al., Kōchi, Japan. In J Virol, 1992
Rat lymphoid cells, TARS-1, immortalized by coculture with adult T-cell leukemia cells, were intraperitoneally injected into 65 newborn, inbred WKAH/Hkm rats.
Priming for in vitro and in vivo anti-human T lymphotropic virus type 1 cellular immunity by virus-related protein reconstituted into liposome.
Nakayama et al., Nagasaki, Japan. In J Immunol, 1991
In vitro sensitization with a HTLV-1-positive cell line, TARS-1, of spleen cells obtained from these animals generated killer cells specific for syngeneic HTLV-1-positive cells.
Rat cytotoxic T lymphocytes against human T-lymphotropic virus type 1-infected cells recognize gag gene and env gene encoded antigens.
Shiku et al., Nagasaki, Japan. In J Immunol, 1990
T cell immune responses in syngeneic WKA/H rats were analyzed by using lymphoid cell lines, TARS-1, TART-1, and TARL-2, infected with human T-lymphotropic virus type 1 (HTLV-1).
[Rat lymphoid cell lines producing human T cell leukemia virus-I].
Tateno, In Hokkaido Igaku Zasshi, 1987
Cocultivation of spleen cells, lymph node cells, and thymocytes of female Wistar-King-Aptekman rats with short-term cultured male adult T cell leukemia (ATL) cells in the presence of 5-bromo-2'-deoxyuridine (BudR) resulted in the establishment of rat lymphoid cell lines, TARS-1, TARL-2, and TART-1.
Expression of the HT462 antigen on fresh leukemic T cells and on cells of HTLV-I infected lines.
Takatsuki et al., In Leuk Res, 1986
Three HTLV-I infected rat cell lines (TARS-1, TART-1, TARL-2) did not express the HT462 antigen, although cells of these lines expressed other HTLV-I related antigens.
TCGF(IL 2)-receptor inducing factor(s). II. Possible role of ATL-derived factor (ADF) on constitutive IL 2 receptor expression of HTLV-I(+) T cell lines.
Honjo et al., In J Immunol, 1985
ADF also enhanced IL 2-R expression of a rat T cell line transformed by HTLV-1(TARS-1), as demonstrated with anti-rat IL 2 receptor monoclonal antibodies (ART-18).
Rat lymphoid cell lines producing human T cell leukemia virus. II. Constitutive expression of rat interleukin 2 receptor.
Osawa et al., In J Exp Med, 1985
Three rat lymphoid cell lines (TARS-1, TARL-2, and TART-1) (12) transformed by human T cell leukemia/lymphoma virus I (HTLV-I) had rearrangement of the beta chain gene of the T cell antigen receptor, and had integrated proviral DNA from HTLV-I in their genomes.
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