- SARS (gene)
Seryl-tRNA synthetase, also known as SARS, is a human
gene .cite web | title = Entrez Gene: SARS seryl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6301| accessdate = ]PBB_Summary
section_title =
summary_text = This gene belongs to the class II amino-acyl tRNA family. The encoded enzyme catalyzes the transfer of L-serine to tRNA (Ser) and is related to bacterial and yeast counterparts.cite web | title = Entrez Gene: SARS seryl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6301| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Härtlein M, Cusack S |title=Structure, function and evolution of seryl-tRNA synthetases: implications for the evolution of aminoacyl-tRNA synthetases and the genetic code. |journal=J. Mol. Evol. |volume=40 |issue= 5 |pages= 519–30 |year= 1995 |pmid= 7540217 |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=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=Vincent C, Tarbouriech N, Härtlein M |title=Genomic organization, cDNA sequence, bacterial expression, and purification of human seryl-tRNA synthase. |journal=Eur. J. Biochem. |volume=250 |issue= 1 |pages= 77–84 |year= 1998 |pmid= 9431993 |doi=
*cite journal | author=Heckl M, Busch K, Gross HJ |title=Minimal tRNA(Ser) and tRNA(Sec) substrates for human seryl-tRNA synthetase: contribution of tRNA domains to serylation and tertiary structure. |journal=FEBS Lett. |volume=427 |issue= 3 |pages= 315–9 |year= 1998 |pmid= 9637248 |doi=
*cite journal | author=Shah ZH, Toompuu M, Hakkinen T, "et al." |title=Novel coding-region polymorphisms in mitochondrial seryl-tRNA synthetase (SARSM) and mitoribosomal protein S12 (RPMS12) genes in DFNA4 autosomal dominant deafness families. |journal=Hum. Mutat. |volume=17 |issue= 5 |pages= 433–4 |year= 2001 |pmid= 11317363 |doi= 10.1002/humu.1123
*cite journal | author=Shimada N, Suzuki T, Watanabe K |title=Dual mode recognition of two isoacceptor tRNAs by mammalian mitochondrial seryl-tRNA synthetase. |journal=J. Biol. Chem. |volume=276 |issue= 50 |pages= 46770–8 |year= 2002 |pmid= 11577083 |doi= 10.1074/jbc.M105150200
*cite journal | author=Rigler R, Cronvall E, Hirsch R, "et al." |title=Interactions of seryl-tRNA synthetase with serine and phenylalanine specific tRNA. |journal= |volume=11 |issue= 5 |pages= 320–323 |year= |pmid= 11945516 |doi=
*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=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*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=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/msb4100134PBB_Controls
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