RARS (gene)

Arginyl-tRNA synthetase, also known as RARS, is a human gene.cite web | title = Entrez Gene: RARS arginyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5917| accessdate = ]

PBB_Summary
section_title =
summary_text = 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. Arginyl-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family.cite web | title = Entrez Gene: RARS arginyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5917| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=McCune SA, Yu PL, Nance WE |title=A genetic study of erythrocyte arginine-tRNA synthetase activity in man. |journal=Acta geneticae medicae et gemellologiae |volume=26 |issue= 1 |pages= 21–7 |year= 1977 |pmid= 562050 |doi=
*cite journal | author=Norcum MT |title=Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts and detergents. |journal=J. Biol. Chem. |volume=266 |issue= 23 |pages= 15398–405 |year= 1991 |pmid= 1651330 |doi=
*cite journal | author=Wang HY, Pan F |title=Kinetic mechanism of arginyl-tRNA synthetase from human placenta. |journal=Int. J. Biochem. |volume=16 |issue= 12 |pages= 1379–85 |year= 1985 |pmid= 6530022 |doi=
*cite journal | author=Girjes AA, Hobson K, Chen P, Lavin MF |title=Cloning and characterization of cDNA encoding a human arginyl-tRNA synthetase. |journal=Gene |volume=164 |issue= 2 |pages= 347–50 |year= 1995 |pmid= 7590355 |doi=
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Rho SB, Lee JS, Jeong EJ, "et al." |title=A multifunctional repeated motif is present in human bifunctional tRNA synthetase. |journal=J. Biol. Chem. |volume=273 |issue= 18 |pages= 11267–73 |year= 1998 |pmid= 9556618 |doi=
*cite journal | author=Quevillon S, Robinson JC, Berthonneau E, "et al." |title=Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein. |journal=J. Mol. Biol. |volume=285 |issue= 1 |pages= 183–95 |year= 1999 |pmid= 9878398 |doi= 10.1006/jmbi.1998.2316
*cite journal | author=Park SG, Jung KH, Lee JS, "et al." |title=Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase. |journal=J. Biol. Chem. |volume=274 |issue= 24 |pages= 16673–6 |year= 1999 |pmid= 10358004 |doi=
*cite journal | author=Kim T, Park SG, Kim JE, "et al." |title=Catalytic peptide of human glutaminyl-tRNA synthetase is essential for its assembly to the aminoacyl-tRNA synthetase complex. |journal=J. Biol. Chem. |volume=275 |issue= 28 |pages= 21768–72 |year= 2000 |pmid= 10801842 |doi= 10.1074/jbc.M002404200
*cite journal | author=Kang J, Kim T, Ko YG, "et al." |title=Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases. |journal=J. Biol. Chem. |volume=275 |issue= 41 |pages= 31682–8 |year= 2000 |pmid= 10913161 |doi= 10.1074/jbc.M909965199
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Gevaert K, Goethals M, Martens L, "et al." |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566–9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Ling C, Yao YN, Zheng YG, "et al." |title=The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex. |journal=J. Biol. Chem. |volume=280 |issue= 41 |pages= 34755–63 |year= 2005 |pmid= 16055448 |doi= 10.1074/jbc.M413511200
*cite journal | author=Kimura K, Wakamatsu A, Suzuki Y, "et al." |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406
*cite journal | author=Ewing RM, Chu P, Elisma F, "et al." |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue= |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134
*cite journal | author=Bottoni A, Vignali C, Piccin D, "et al." |title=Proteasomes and RARS modulate AIMP1/EMAP II secretion in human cancer cell lines. |journal=J. Cell. Physiol. |volume=212 |issue= 2 |pages= 293–7 |year= 2007 |pmid= 17443684 |doi= 10.1002/jcp.21083

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