Results 231 to 240 of about 56,989 (293)

BRCA1 interacts with acetyl-CoA carboxylase through its tandem of BRCT domains

open access: bronze, 2002
Clémence Magnard   +6 more
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Regulation of acetyl-CoA carboxylase

Biochemical Society Transactions, 2006
Acetyl-CoA carboxylase (ACC) catalyses the formation of malonyl-CoA, an essential substrate for fatty acid synthesis in lipogenic tissues and a key regulatory molecule in muscle, brain and other tissues. ACC contributes importantly to the overall control of energy metabolism and has provided an important model to explore mechanisms of enzyme control ...
Weissy Michele Lee   +4 more
openaire   +4 more sources

Regulation of mammalian acetyl-CoA carboxylase

Biochemical Society Transactions, 2002
Acetyl-CoA carboxylase (ACC) plays a critical role in the regulation of fatty acid metabolism and its two isoforms, ACCα and ACCβ, appear to have distinct functions in the control of fatty acid synthesis and fatty acid oxidation, respectively. They are regulated by similar short-term mechanisms of allosteric activation by citrate, and reversible ...
M. Munday
openaire   +4 more sources

Inhibition of acetyl-CoA carboxylase suppresses fatty acid synthesis and tumor growth of non-small-cell lung cancer in preclinical models

open access: yesNature Medicine, 2016
Continuous de novo fatty acid synthesis is a common feature of cancer that is required to meet the biosynthetic demands of a growing tumor. This process is controlled by the rate-limiting enzyme acetyl-CoA carboxylase (ACC), an attractive but ...
Matthew J Kolar   +2 more
exaly   +2 more sources

Regulation and structure of the heteromeric acetyl-CoA carboxylase

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2016
The enzyme acetyl-CoA carboxylase (ACCase) catalyzes the committed step of the de novo fatty acid biosynthesis (FAS) pathway by converting acetyl-CoA to malonyl-CoA. Two forms of ACCase exist in nature, a homomeric and heteromic form. The heteromeric form of this enzyme requires four different subunits for activity: biotin carboxylase; biotin carboxyl ...
Jay J. Thelen, Matthew J. Salie
openaire   +3 more sources

Structural basis for regulation of human acetyl-CoA carboxylase

Nature, 2018
Moritz Hunkeler   +2 more
exaly   +2 more sources

Acetyl CoA carboxylase

Archives of Biochemistry and Biophysics, 1971
Abstract A biotin carboxyl carrier protein (BCCP) from Escherichia coli has been purified and crystallized. The purified protein was found to be homogeneous by polyacrylamide gel electrophoresis and sedimentation in a synthetic boundary cell. BCCP has a sedimentation coefficient of 1.04 S, a diffusion coefficient ( D 20,w ) of 10.4 × 10 −7 cm 2 ...
Alfred W. Alberts   +2 more
openaire   +2 more sources

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