Zobrazeno 1 - 10
of 143
pro vyhledávání: '"J McFie"'
The monoacylglycerol acyltransferase pathway contributes to triacylglycerol synthesis in HepG2 cells
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-14 (2022)
Abstract The monoacylglycerol acyltransferase (MGAT) pathway has a well-established role in the small intestine where it facilitates the absorption of dietary fat. In enterocytes, MGAT participates in the resynthesis of triacylglycerol using substrat
Externí odkaz:
https://doaj.org/article/87fe8281c5de4bb18df92615d1f0d8bc
Publikováno v:
PLoS ONE, Vol 14, Iss 1, p e0210396 (2019)
Triacylglycerol synthesis is catalyzed by acyl CoA:diacylglycerol acyltransferase-2 (DGAT2). DGAT2 is an integral membrane protein that is localized to the endoplasmic reticulum and interacts with lipid droplets. Using BioId, a method to detect proxi
Externí odkaz:
https://doaj.org/article/b2acf3ebbbb84957951342e75ee9586c
Autor:
Christopher J. Hlynialuk, Binbing Ling, Zakery N. Baker, Paul A. Cobine, Lisa D. Yu, Aren Boulet, Timothy Wai, Amzad Hossain, Amr M. El Zawily, Pamela J. McFie, Scot J. Stone, Francisca Diaz, Carlos T. Moraes, Deepa Viswanathan, Michael J. Petris, Scot C. Leary
Publikováno v:
Cell Reports, Vol 10, Iss 6, Pp 933-943 (2015)
Human SCO1 fulfills essential roles in cytochrome c oxidase (COX) assembly and the regulation of copper (Cu) homeostasis, yet it remains unclear why pathogenic mutations in this gene cause such clinically heterogeneous forms of disease. Here, we esta
Externí odkaz:
https://doaj.org/article/0340b7e99d004b629b58872104cbc6a2
Autor:
Pamela J. McFie, Scot J. Stone
Publikováno v:
Journal of Lipid Research, Vol 52, Iss 9, Pp 1760-1764 (2011)
Triacylglycerols (TG) are the major storage form of energy in eukaryotic organisms and are synthesized primarily by acyl CoA:1,2-diacylglycerol acyltransferase (DGAT) enzymes. In vitro DGAT activity has previously been quantified by measuring the inc
Externí odkaz:
https://doaj.org/article/368b7becdd8545f3b42d0987d06500c5
Publikováno v:
Biochimica et biophysica acta. Molecular and cell biology of lipids. 1866(9)
In eukaryotic organisms, two unrelated acyl-CoA:diacylglycerol acyltransferase (DGAT) enzymes, DGAT1 and DGAT2, catalyze the final step of the triacylglycerol biosynthetic pathway. Both enzymes are highly expressed in lipogenic tissues, such as adipo
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1863:1068-1081
Diacylglycerol acyltranferase-2 (DGAT2) is a resident protein of the endoplasmic reticulum that catalyzes the synthesis of triacylglycerol. When lipid droplet formation is stimulated by incubating cells with fatty acids, DGAT2 becomes concentrated ar
Autor:
Kinoti Julie Nkirote, J. McFie
Publikováno v:
Journal of Accounting. 1:1-17
Purpose: The focus of the study was on the possibility of adopting Basel II accord by Kenya commercial banks. Methodology: The study adopted a descriptive survey design. A population of 45 commercial banks was identified from the central bank of Keny
Autor:
Huyen Vu, Pamela J. McFie, Sabrina Izzard, Luc G. Berthiaume, Erwan Beauchamp, Youzhi Jin, S. Stone
Publikováno v:
Biochimica et Biophysica Acta Molecular and Cell Biology of Lipids
Biochimica et Biophysica Acta Molecular and Cell Biology of Lipids, Elsevier, 2016, 1861 (9, Part A), pp.1192-1204
Biochimica et Biophysica Acta Molecular and Cell Biology of Lipids, Elsevier, 2016, 1861 (9, Part A), pp.1192-1204
International audience; Acyl CoA:2-monoacylglycerol acyltransferase (MGAT)-2 has an important role in dietary fat absorption in the intestine. MGAT2 resides in the endoplasmic reticulum and catalyzes the synthesis of diacylglycerol which is then util
Publikováno v:
Biochemical and Biophysical Research Communications. 475:264-270
Background MGAT3 catalyzes the synthesis of 1,2-diacylglycerol from 2-monoacylglycerol in an acyl CoA-dependent reaction. Although initially identified as an MGAT enzyme, MGAT3 is more closely related to DGAT2 than to MGAT1 and MGAT2. Furthermore, MG
Autor:
Scot C. Leary, Francisca Diaz, Michael J. Petris, Chris Hlynialuk, Timothy Wai, Amr M. El Zawily, Paul A. Cobine, S. Stone, Amzad Hossain, Pamela J. McFie, Lisa D. Yu, Deepa Viswanathan, Aren Boulet, Binbing Ling, Carlos T. Moraes, Zakery N. Baker
Publikováno v:
Cell Reports
Cell Reports, Elsevier Inc, 2015, 10 (6), pp.933-943. ⟨10.1016/j.celrep.2015.01.019⟩
Cell Reports, Vol 10, Iss 6, Pp 933-943 (2015)
Cell Reports, Elsevier Inc, 2015, 10 (6), pp.933-943. ⟨10.1016/j.celrep.2015.01.019⟩
Cell Reports, Vol 10, Iss 6, Pp 933-943 (2015)
Summary Human SCO1 fulfills essential roles in cytochrome c oxidase (COX) assembly and the regulation of copper (Cu) homeostasis, yet it remains unclear why pathogenic mutations in this gene cause such clinically heterogeneous forms of disease. Here,