scholarly article | Q13442814 |
P356 | DOI | 10.1042/BJ1750999 |
P953 | full work available at URL | https://europepmc.org/articles/PMC1186163 |
https://europepmc.org/articles/PMC1186163?pdf=render | ||
https://portlandpress.com/biochemj/article-pdf/175/3/999/620453/bj1750999.pdf | ||
https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/33667/?tool=EBI | ||
https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/33667/pdf/?tool=EBI | ||
P932 | PMC publication ID | 1186163 |
P698 | PubMed publication ID | 33667 |
P5875 | ResearchGate publication ID | 23099450 |
P2093 | author name string | D. P. Bloxham | |
R. A. Chalkley | |||
S. J. Coghlin | |||
W. Salam | |||
P2860 | cites work | The oxoacyl-coenzyme A thiolases of animal tissues | Q24531818 |
Selective inhibition of cholesterol synthesis by cell-free preparations of rat liver by using inhibitors of cytoplasmic acetoacetyl-coenzyme A thiolase | Q28323499 | ||
A kinetic and fluorimetric investigation of papain modified at tryptophan-69 and -177 by N-bromosuccinimide | Q28363413 | ||
The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis | Q29053311 | ||
On the Mechanism of Ketogenesis and Its Control. Purification, Kinetic Mechanism and Regulation of Different Forms of Mitochondrial Acetoacetyl-CoA Thiolases from Ox Liver | Q33964092 | ||
beta-Hydroxy-beta-methyl-glutaryl coenzyme A reductase, cleavage and condensing enzymes in relation to cholesterol formation in rat liver | Q34250090 | ||
Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase | Q34254828 | ||
Binding Energy, Specificity, and Enzymic Catalysis: The Circe Effect | Q39066223 | ||
Assay of the mycobactins by measurement of the growth of Mycobacterium johnei | Q39108455 | ||
Improved Alkylation of Acetoacetyl-Coenzyme A Thiolase by Extension of Chain Length in Chloromethyl Ketone Fatty Acids | Q39126547 | ||
Modification of pig heart lactate dehydrogenase with methyl methanethiosulphonate to produce an enzyme with altered catalytic activity | Q39143165 | ||
Regulation of lipogenesis in animal tissues. | Q39874939 | ||
Regulation of steroid biosynthesis | Q39901996 | ||
Simple alkanethiol groups for temporary blocking of sulfhydryl groups of enzymes | Q39920355 | ||
Intracellular localization of the 3-hydroxy-3-methylglutaryl coenzme A cycle enzymes in liver. Separate cytoplasmic and mitochondrial 3-hydroxy-3-methylglutaryl coenzyme A generating systems for cholesterogenesis and ketogenesis | Q39924567 | ||
Use of methanethiolation to investigate the catalytic role of sulphydryl groups in rabbit skeletal muscle pyruvate kinase | Q40169830 | ||
Substrate stereochemistry of the acetyl-CoA acetyltransferase reaction | Q40332338 | ||
The kinetic mechanism and properties of the cytoplasmic acetoacetyl-coenzyme A thiolase from rat liver | Q41998444 | ||
Synthesis of fatty acids in the perused mouse liver | Q42137477 | ||
Reversible blocking of amino groups with citraconic anhydride | Q42152949 | ||
Selective modification of rabbit muscle pyruvate kinase by 5-chloro-4-oxopentanoic acid | Q42537194 | ||
Kinetic and molecular properties of citraconyl-aldolase. The reversible denaturation and hybridization of the native and modified enzymes | Q42561990 | ||
The reaction of aldolase with 2-methylmaleic anhydride | Q42935293 | ||
Two forms of acetoacetyl coenzyme A thiolase in yeast. I. Separation and properties | Q44397373 | ||
Lipogenesis in hepatocytes of genetically obese rats | Q44769101 | ||
Structure of horse muscle phosphoglycerate kinase. Some results on the chain conformation, substrate binding and evolution of the molecule from a 3 angstrom Fourier map. | Q47854756 | ||
Lipogenesis in rat hepatocytes | Q68680838 | ||
The isolation of hormone-sensitive rat hepatocytes by a modified enzymatic technique | Q68796803 | ||
Fatty acid and 3- -hydroxysterol synthesis in the perfused rat liver. Including measurements on the production of lactate, pyruvate, -hydroxy-butyrate, and acetoacetate by the fed liver | Q69502528 | ||
Inactivation of pig heart thiolase by 3-butynoyl coenzyme A, 3-pentynoyl coenzyme A, and 4-bromocrotonyl coenzyme A | Q69575072 | ||
Beta-hydroxydecanoyl thioester dehydrase. Studies on molecular structure and active site | Q69890778 | ||
On the mode of interaction of -hydroxydecanoyl thioester dehydrase with allenic acid derivatives | Q70449049 | ||
The active site cysteines of thiolase | Q71585746 | ||
Mode of Inhibition of β-Hydroxydecanoyl Thioester Dehydrase by 3-Decynoyl-N-acetylcysteamine | Q71639464 | ||
Effect of (—)-Hydroxycitrate on Fatty Acid Synthesis by Rat Liver in Vivo | Q71755435 | ||
[Purification and crystallization of thiolase; study of its action mechanism] | Q72228523 | ||
DETERNATION OF CO-FACTOR DISSOCIATION CONSTANTS FROM THE KINETICS OF INHIBITION OF ENZYMES | Q76957912 | ||
Amino acid sequence around the reactive cysteine residues in thiolase | Q77913752 | ||
P433 | issue | 3 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | biochemistry | Q7094 |
cell biology | Q7141 | ||
fatty acid | Q61476 | ||
P1104 | number of pages | 13 | |
P304 | page(s) | 999-1011 | |
P577 | publication date | 1978-12-01 | |
P1433 | published in | Biochemical Journal | Q864221 |
P1476 | title | Synthesis of chloromethyl ketone derivatives of fatty acids. Their use as specific inhibitors of acetoacetyl-coenzyme A thiolase, cholesterol biosynthesis and fatty acid synthesis | |
P478 | volume | 175 |
Q71012254 | 47 Chloromethyl ketone derivatives of fatty acids |
Q42881906 | Chloroacetone as an active-site-directed inhibitor of the aliphatic amidase from Pseudomonas aeruginosa |
Q28360071 | Inhibition of hydroxymethylglutaryl-coenzyme A synthase by L-659,699 |
Q41850567 | Mechanism of action of β-oxoacyl-CoA thiolase from rat liver cytosol. Direct evidence for the order of addition of the two acetyl-CoA molecules during the formation of acetoacetyl-CoA |
Q68380132 | Selective reduction of fatty acid oxidation in colonocytes: correlation with ulcerative colitis |
Q54772028 | The use of suicide substrates to select mutants of Escherichia coli lacking enzymes of alcohol fermentation. |