SUCLG1

SUCLG1

Succinate-CoA ligase, GDP-forming, alpha subunit, also known as SUCLG1, is a human gene.cite web | title = Entrez Gene: SUCLG1 succinate-CoA ligase, GDP-forming, alpha subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8802| accessdate = ]

PBB_Summary
section_title =
summary_text =

References

Further reading

PBB_Further_reading
citations =
*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=10.1016/0378-1119(94)90802-8
*cite journal | author=James M, Man NT, Edwards YH, Morris GE |title=The molecular basis for cross-reaction of an anti-dystrophin antibody with alpha-actinin. |journal=Biochim. Biophys. Acta |volume=1360 |issue= 2 |pages= 169–76 |year= 1997 |pmid= 9128182 |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=10.1016/S0378-1119(97)00411-3
*cite journal | author=Fraser ME, James MN, Bridger WA, Wolodko WT |title=Phosphorylated and dephosphorylated structures of pig heart, GTP-specific succinyl-CoA synthetase. |journal=J. Mol. Biol. |volume=299 |issue= 5 |pages= 1325–39 |year= 2000 |pmid= 10873456 |doi= 10.1006/jmbi.2000.3807
*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=Suzuki Y, Yamashita R, Shirota M, "et al." |title=Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions. |journal=Genome Res. |volume=14 |issue= 9 |pages= 1711–8 |year= 2004 |pmid= 15342556 |doi= 10.1101/gr.2435604
*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=Tsang HT, Connell JW, Brown SE, "et al." |title=A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex. |journal=Genomics |volume=88 |issue= 3 |pages= 333–46 |year= 2006 |pmid= 16730941 |doi= 10.1016/j.ygeno.2006.04.003
*cite journal | author=Ostergaard E, Christensen E, Kristensen E, "et al." |title=Deficiency of the alpha subunit of succinate-coenzyme A ligase causes fatal infantile lactic acidosis with mitochondrial DNA depletion. |journal=Am. J. Hum. Genet. |volume=81 |issue= 2 |pages= 383–7 |year= 2007 |pmid= 17668387 |doi= 10.1086/519222

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Нужна курсовая?

Look at other dictionaries:

  • Succinyl-CoA-Synthetasen — Succinyl CoA Ligase (GDP bildend) Modell des SCS Heterodimer (alpha blau, bet …   Deutsch Wikipedia

  • Succinil-CoA sintetasa — (GDP) subunidad α Otros nombres Succinato CoA ligasa (GDP) subunidad α HUGO 11449 Símbolo SUCLG1 …   Wikipedia Español

  • Succinyl-CoA-Synthetase — Succinat CoA Ligase (GDP bildend) Modell des SCS Heterodimer (alpha blau, beta gelb) vom Ha …   Deutsch Wikipedia

  • Succinyl coenzyme A synthetase — (succinate thiokinase) catalyzes the formation of succinate and coenzyme A, a 4 carbon metabolite, from succinyl CoA. ReactionSuccinyl CoA synthetase catalyzes a reversible step in the citric acid cycle, which involves the substrate level… …   Wikipedia

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”