Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Subrahmanyam S. Chirala"'
Autor:
Jianqiang Mao, Salih J. Wakil, Parichher Kordari, Subrahmanyam S. Chirala, Huiguang Li, Tattym Shaikenov, Francesco J. DeMayo, Zi-Wei Gu, Lutfi Abu-Elheiga, William C. Heird
Publikováno v:
Proceedings of the National Academy of Sciences. 103:8552-8557
In animals, liver and white adipose are the main sites for the de novo fatty acid synthesis. Deletion of fatty acid synthase or acetyl-CoA carboxylase (ACC) 1 in mice resulted in embryonic lethality, indicating that the de novo fatty acid synthesis i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59ffc67e0e9f7cc98ef4276197bec426
https://doi.org/10.1073/pnas.0603115103
https://doi.org/10.1073/pnas.0603115103
Autor:
Salih J. Wakil, Zei-Wei Gu, Lutfi Abu-Elheiga, Won Keun Oh, Subrahmanyam S. Chirala, Parichher Kordari, Tattym Shaikenov
Publikováno v:
Proceedings of the National Academy of Sciences. 102:1384-1389
Acc2 -/- mutant mice, when fed a high-fat/high-carbohydrate (HF/HC) diet, were protected against diet-induced obesity and diabetes. To investigate the role of acetyl-CoA carboxylase 2 (ACC2) in the regulation of energy metabolism in adipose tissues,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d09da3d98920fd914230a852bdedef5
https://doi.org/10.1073/pnas.0409451102
https://doi.org/10.1073/pnas.0409451102
Publikováno v:
Proceedings of the National Academy of Sciences. 101:15567-15572
Human fatty acid synthase is a large homodimeric multifunctional enzyme that synthesizes palmitic acid. The unique carboxyl terminal thioesterase domain of fatty acid synthase hydrolyzes the growing fatty acid chain and plays a critical role in regul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d94fa253a19f475069a4bf8de7ef6b66
https://doi.org/10.1073/pnas.0406901101
https://doi.org/10.1073/pnas.0406901101
Publikováno v:
Proceedings of the National Academy of Sciences. 100:7515-7520
Acetyl-CoA carboxylase 1 (ACC1) catalyzes the formation of malonyl-CoA, the C 2 donor for de novo synthesis of long-chain fatty acids. We have identified 64 exons, including 7 alternatively spliced minor exons (1A, 1B, 1C, 3, 5A′, 5A, and 5B) in hu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cdbf2a6fca826f9e7984fabb6aaac95c
https://doi.org/10.1073/pnas.1332670100
https://doi.org/10.1073/pnas.1332670100
Autor:
Milton J. Finegold, Subrahmanyam S. Chirala, Martin M. Matzuk, Jianqiang Mao, Kathleen A. Mahon, Lutfi Abu-Elheiga, Hua Chang, Salih J. Wakil
Publikováno v:
Proceedings of the National Academy of Sciences. 100:6358-6363
In animals, including humans, the source of long-chain saturated fatty acids is de novo synthesis, which is mediated by fatty acid synthase (FAS), ingested food, or both. To understand the importance of de novo fatty acid synthesis, we generated FAS
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77efa4e899de14e813e7eb4ff0abdcd7
https://doi.org/10.1073/pnas.0931394100
https://doi.org/10.1073/pnas.0931394100
Publikováno v:
Proceedings of the National Academy of Sciences. 97:3948-3953
To understand cholesterol-mediated regulation of human fatty acid synthase promoter I, we tested various 5′-deletion constructs of promoter I-luciferase reporter gene constructs in HepG2 cells. The reporter gene constructs that contained only the S
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d578d7eea837fa85e320420c13dece7
https://doi.org/10.1073/pnas.040574197
https://doi.org/10.1073/pnas.040574197
Publikováno v:
Proceedings of the National Academy of Sciences. 95:12260-12265
To investigate the regulation of the human fatty acid synthase gene by the thyroid hormone triiodothyronine, various constructs of the human fatty acid synthase promoter and the luciferase reporter gene were transfected in combination with plasmids e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1c07cb628f13b48f0eee94ca13cf0da
https://doi.org/10.1073/pnas.95.21.12260
https://doi.org/10.1073/pnas.95.21.12260
Publikováno v:
Journal of Biological Chemistry. 271:13584-13592
We have isolated and sequenced a genomic clone coding for the first three exons and the 5'-flanking region of the human fatty-acid synthase gene. The translation initiation site, ATG, is located in exon II. Primer extension and S1 nuclease analyses s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::715d455320a1ea5ac5e945b99405a300
https://doi.org/10.1074/jbc.271.23.13584
https://doi.org/10.1074/jbc.271.23.13584
Autor:
Matthew H. Hsu, Lutfi Abu-Elheiga, Walid Al-Feel, Wei Yong Huang, Salih J. Wakil, Ming Hong Tai, Subrahmanyam S. Chirala, Arumugam Jayakumar
Publikováno v:
Proceedings of the National Academy of Sciences. 92:8695-8699
Fatty acid synthase (FAS; EC 2.3.1.85) was purified to near homogeneity from a human hepatoma cell line, HepG2. The HepG2 FAS has a specific activity of 600 nmol of NADPH oxidized per min per mg, which is about half that of chicken liver FAS. All the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e97d1e86dec331652039647da08833d7
https://doi.org/10.1073/pnas.92.19.8695
https://doi.org/10.1073/pnas.92.19.8695
Autor:
Antonio Baldini, Lutfi Abu-Elheiga, Salih J. Wakil, Subrahmanyam S. Chirala, Arumugam Jayakumar
Publikováno v:
Proceedings of the National Academy of Sciences. 92:4011-4015
We have cloned and sequenced the cDNA coding for human HepG2 acetyl-CoA carboxylase (ACC; EC 6.4.1.2). The sequence has an open reading frame of 7038 bp that encode 2346 amino acids (M(r), 264,737). The C-terminal 2.6-kb sequence is very different fr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2ce97d9238244916886b891a2e20eeb
https://doi.org/10.1073/pnas.92.9.4011
https://doi.org/10.1073/pnas.92.9.4011