A highly conserved motif within the NH2-terminal coiled-coil domain of angiopoietin-like protein 4 confers its inhibitory effects on lipoprotein lipase by disrupting the enzyme dimerization

Journal of Biological Chemistry

Volumn 284, Issue 18, 2009, Pages 11942-11952

  Yau, Ming Hon ^a   Wang, Yu ^a   Lam, Karen S L ^a   Zhang, Jialiang ^a   Wu, Donghai ^b   Xu, Aimin ^a  

^a UNIVERSITY OF HONG KONG   (Hong Kong)

^b GUANGZHOU INSTITUTES OF BIOMEDICINE AND HEALTH   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ANGIOPOIETIN; COILED-COIL DOMAINS; CONSENSUS MOTIF; IN-VITRO; INHIBITORY EFFECT; LIPOPROTEIN LIPASE; MULTIPLE SEQUENCE ALIGNMENTS; MUTANT PROTEINS; PLASMA TRIGLYCERIDES; POLAR AMINO ACIDS; POLAR RESIDUES; STRUCTURAL BASIS; SYNTHETIC PEPTIDE; VERY LOW DENSITY LIPOPROTEINS;

AMINATION; AMINES; AMINO ACIDS; CHARGE COUPLED DEVICES; DIGITAL CAMERAS; DIMERIZATION; ENZYMES; OLIGOMERS; ORGANIC ACIDS; PLASMA DIAGNOSTICS;

ENZYME INHIBITION;

ALANINE; ANGIOPOIETIN; ANGIOPOIETIN LIKE PROTEIN 4; GLUTAMINE; HISTIDINE; LIPOPROTEIN LIPASE; SYNTHETIC PEPTIDE; TRIACYLGLYCEROL; UNCLASSIFIED DRUG; ANGPTL3 PROTEIN, HUMAN; ANGPTL3 PROTEIN, MOUSE; ANGPTL4 PROTEIN, HUMAN; ANGPTL4 PROTEIN, MOUSE; ENZYME INHIBITOR;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CONSENSUS SEQUENCE; CONTROLLED STUDY; DIMERIZATION; ENZYME ACTIVITY; ENZYME INHIBITION; GENE DISRUPTION; GENE SEQUENCE; GENETIC CONSERVATION; IN VITRO STUDY; MALE; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN MOTIF; SEQUENCE ALIGNMENT; TRIACYLGLYCEROL BLOOD LEVEL; ANIMAL; CELL STRAIN 3T3; DRUG ANTAGONISM; GENETICS; HUMAN; METABOLISM; METHODOLOGY; MUTATION; PEPTIDE MAPPING; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE;

MUS;

3T3-L1 CELLS; AMINO ACID MOTIFS; AMINO ACID SUBSTITUTION; ANGIOPOIETINS; ANIMALS; DIMERIZATION; ENZYME INHIBITORS; HUMANS; LIPOPROTEIN LIPASE; MICE; MUTATION; PEPTIDE MAPPING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT;

EID: 66449084528     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M809802200     Document Type: Article

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