Results 141 to 150 of about 19,848 (176)

Exercise training decreases the concentration of malonyl-CoA and increases the expression and activity of malonyl-CoA decarboxylase in human muscle

American Journal of Physiology-Endocrinology and Metabolism, 2006
The study was designed to evaluate whether changes in malonyl-CoA and the enzymes that govern its concentration occur in human muscle as a result of physical training. Healthy, middle-aged subjects were studied before and after a 12-wk training program that significantly increased V̇o2 maxby 13% and decreased intra-abdominal fat by 17%.
Jeanette E, Kuhl, Neil B, Ruderman, Nicolas, Musi, Laurie J, Goodyear, Mary Elizabeth, Patti, Sarah, Crunkhorn, Deepti, Dronamraju, Anders, Thorell, Jonas, Nygren, Olle, Ljungkvist, Marie, Degerblad, Agneta, Stahle, Torkel B, Brismar, Kirstine L, Andersen, Asish K, Saha, Suad, Efendic, Peter N, Bavenholm   +16 more
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Design and Synthesis of Heterocyclic Malonyl‐CoA Decarboxylase Inhibitors.

ChemInform, 2006
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
Jie-Fei, Cheng, Mi, Chen, Bin, Liu, Zheng, Hou, Thomas, Arrhenius, Alex M, Nadzan   +5 more
openaire   +2 more sources

Nerve stimulation decreases malonyl-CoA in skeletal muscle

Journal of Applied Physiology, 1992
This study was designed to determine the effect of in situ electrical stimulation of the sciatic nerve on malonyl-CoA, an inhibitor of carnitine palmitoyl transferase, in the gastrocnemius/plantaris muscle group of rats. The left sciatic nerve was stimulated at a frequency of 5 Hz with 100-ms trains of impulses (50 Hz) for 1, 3, or 5 min.
C, Duan, W W, Winder
openaire   +2 more sources

Expression, purification, and characterization of human malonyl-CoA decarboxylase

Protein Expression and Purification, 2004
The recombinant human malonyl-CoA decarboxylase (hMCD) was overexpressed in Escherichia coli with and without the first 39 N-terminal amino acids via a cleavable MBP-fusion construct. Proteolytic digestion using genenase I to remove the MBP-fusion tag was optimized for both the full length and truncated hMCD.
Demin, Zhou, Phoebe, Yuen, Donald, Chu, Vicki, Thon, Steve, McConnell, Steven, Brown, Andria, Tsang, Michael, Pena, Anna, Russell, Jie-Fei, Cheng, Alex M, Nadzan, Miguel S, Barbosa, Jason R B, Dyck, Gary D, Lopaschuk, Guang, Yang   +14 more
openaire   +2 more sources

Malonyl CoA as a Metabolic Switch and a Regulator of Insulin Sensitivity

1998
Malonyl CoA is a regulator of carnitine palmitoyl transferase 1 (CPT1), the enzyme that controls the transfer of long chain fatty acyl CoA into mitochondria where it is oxidized. Recent studies indicate that in skeletal muscle the concentration of malonyl CoA is acutely (minutes) regulated by changes in its fuel supply and energy expenditure.
N B, Ruderman, A K, Saha, D, Vavvas, T, Kurowski, D R, Laybutt, C, Schmitz-Peiffer, T, Biden, E W, Kraegen   +7 more
openaire   +2 more sources

Brain abnormalities in a case of malonyl-CoA decarboxylase deficiency

Molecular Genetics and Metabolism, 2006
Malonyl-CoA decarboxylase (MCD) deficiency is an extremely rare inborn error of metabolism that presents with metabolic acidosis, hypoglycemia, and/or cardiomyopathy. Patients also show neurological signs and symptoms that have been infrequently reported.
de Wit, M. C. Y., de Coo, I. F. M., Verbeek, E., Schot, R., Schoonderwoerd, G. C., Duran, M., de Klerk, J. B. C., Huijmans, J. G. M., Lequin, M. H., Verheijen, F. W., Mancini, G. M. S.   +10 more
openaire   +3 more sources

Novel trifluoroacetophenone derivatives as malonyl-CoA decarboxylase inhibitors

Bioorganic & Medicinal Chemistry Letters, 2007
A series of trifluoroacetophenone derivatives were prepared and evaluated as malonyl-CoA decarboxylase (MCD) inhibitors. Some of the 'reverse amide' analogs were found to be potent inhibitors of MCD enzyme activity. The trifluoroacetyl group may interact with the MCD active site as the hydrate in a similar fashion to the hexafluoroisopropanol analogs ...
David M, Wallace, Masayuki, Haramura, Jie-Fei, Cheng, Thomas, Arrhenius, Alex M, Nadzan   +4 more
openaire   +2 more sources

Structural insight into bi‐functional malonyl‐CoA reductase

Environmental Microbiology, 2019
Summary The bi‐functional malonyl‐CoA reductase is a key enzyme of the 3‐hydroxypropionate bi‐cycle for bacterial CO 2 fixation, catalysing the reduction of malonyl‐CoA to malonate semialdehyde and further reduction to 3‐hydroxypropionate.
Hyeoncheol Francis Son, Sangwoo Kim, Hogyun Seo, Jiyeon Hong, Donghoon Lee, Kyeong Sik Jin, Sunghoon Park, Kyung‐Jin Kim   +7 more
openaire   +3 more sources

Malonyl-CoA Signaling, Lipid Partitioning, and Glucolipotoxicity

Diabetes, 2002
β-Cells possess inherent mechanisms to adapt to overnutrition and the prevailing concentrations of glucose, fatty acids, and other fuels to maintain glucose homeostasis. However, this is balanced by potentially harmful actions of the same nutrients. Both glucose and fatty acids may cause good/adaptive or evil/toxic actions on the β-cell, depending on ...
Marc Prentki, Erik Joly, Wissal El-Assaad, Raphaël Roduit   +3 more
openaire   +1 more source

Recent progress in metabolic engineering of Saccharomyces cerevisiae for the production of malonyl-CoA derivatives

Journal of Biotechnology, 2021
Yingli Liu, Yu Deng, Yunying Zhao
exaly