Identification of a Domain of Lecithin–Cholesterol Acyltransferase That Is Involved in Interfacial Recognition
- 1 March 1997
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 232 (3), 783-787
- https://doi.org/10.1006/bbrc.1997.6375
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- Human Hepatic and Lipoprotein Lipase: The Loop Covering the Catalytic Site Mediates Lipase Substrate SpecificityPublished by Elsevier ,1995
- Substrate and positional specificities of human and mouse lecithin-cholesterol acyltransferases. Studies with wild type recombinant and chimeric enzymes expressed in vitroBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1994
- Lecithin:cholesterol acyltransferase: role of N-linked glycosylation in enzyme functionBiochemical Journal, 1993
- Lecithin-cholesterol acyltransferase: effects of mutagenesis at N-linked oligosaccharide attachment sites on acyl acceptor specificityBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1993
- Structure-function relationships in human lecithin:cholesterol acyltransferase. Site-directed mutagenesis at serine residues 181 and 216Biochemistry, 1991
- Lecithin-cholesterol acyltransferase in the metabolism of high-density lipoproteinsBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1991
- Effects of site-directed mutagenesis at residues cysteine-31 and cysteine-184 on lecithin-cholesterol acyltransferase activity.Proceedings of the National Academy of Sciences, 1991
- Structure of human pancreatic lipaseNature, 1990
- Site-directed mutagenesis by overlap extension using the polymerase chain reactionGene, 1989
- Human lecithin-cholesterol acyltransferase gene: complete gene sequence and sites of expressionNucleic Acids Research, 1986