Westin, Maria A K <br/><br/>
The identification of a succinyl-CoA thioesterase suggests a novel pathway for succinate production in peroxisomes.  [electronic resource] 

 -  The Journal of biological chemistry  Nov 2005 
 - 38125-32 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0021-9258 
<br/><br/><label>Standard No.: </label>10.1074/jbc.M508479200  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Animals<br/>Blotting, Western<br/>Cloning, Molecular<br/>Dicarboxylic Acids--chemistry<br/>Electrophoresis, Polyacrylamide Gel<br/>Endoplasmic Reticulum--metabolism<br/>Fatty Acids--metabolism<br/>Fibroblasts--metabolism<br/>Gene Expression Regulation<br/>Green Fluorescent Proteins--metabolism<br/>Humans<br/>Hydrolysis<br/>Kidney--metabolism<br/>Kinetics<br/>Liver--metabolism<br/>Male<br/>Mice<br/>Mice, Transgenic<br/>Models, Biological<br/>PPAR alpha--metabolism<br/>Palmitoyl-CoA Hydrolase--chemistry<br/>Peroxisomes--metabolism<br/>Pyrimidines--pharmacology<br/>RNA, Messenger--metabolism<br/>Recombinant Proteins--chemistry<br/>Reverse Transcriptase Polymerase Chain Reaction<br/>Substrate Specificity<br/>Succinic Acid--chemistry<br/>Thiolester Hydrolases--chemistry<br/>Time Factors<br/>Tissue Distribution<br/>Up-Regulation