Proteins sharing PNPLA domain, a new family of enzymes regulating lipid metabolism

• Published in: M.S. Médecine sciences Vol. 26; no. 2; p. 177
• Main Authors: Baulande, Sylvain, Langlois, Clotilde
• Format: Journal Article
• Language: French
• Published: France 01.02.2010
• Subjects: Amino Acid Sequence; Animals; Arabidopsis Proteins - chemistry; Arabidopsis Proteins - physiology; Caenorhabditis elegans Proteins - chemistry; Caenorhabditis elegans Proteins - physiology; Carboxylic Ester Hydrolases - chemistry; Carboxylic Ester Hydrolases - classification; Carboxylic Ester Hydrolases - genetics; Carboxylic Ester Hydrolases - physiology; Catalytic Domain - genetics; Conserved Sequence; Drosophila Proteins - chemistry; Drosophila Proteins - physiology; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - physiology; Humans; Lipase - chemistry; Lipase - physiology; Lipid Metabolism - genetics; Lipid Metabolism - physiology; Lipolysis - genetics; Mammals - metabolism; Mice; Molecular Sequence Data; Multigene Family; Phospholipases A2, Calcium-Independent - chemistry; Phospholipases A2, Calcium-Independent - physiology; Phylogeny; Plant Proteins - chemistry; Plant Proteins - physiology; Saccharomyces cerevisiae Proteins - chemistry; Saccharomyces cerevisiae Proteins - physiology; Sequence Alignment; Sequence Homology, Amino Acid; Species Specificity

Genome sequencing technologies led to tremendous breakthrough in biology uncovering numerous genes unknown so far and thus opening the field of deep investigations to understand their associated biological functions. As a matter of fact, functional genomics have been progressively replacing sequence...