Role of conserved proline residues in human apolipoprotein A-IV structure and function

Journal of Biological Chemistry

Volumn 290, Issue 17, 2015, Pages 10689-10702

  Deng, Xiaodi ^a   Walker, Ryan G ^a   Morris, Jamie ^a   Davidson, W Sean ^a   Thompson, Thomas B ^a  

^a UNIVERSITY OF CINCINNATI COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ASSOCIATION REACTIONS; CROSSLINKING; DIMERS; EMULSIFICATION; LIPOPROTEINS; OLIGOMERS; PROTEINS; THERMODYNAMIC STABILITY; X RAY SCATTERING;

CARDIO-VASCULAR DISEASE; CHEMICAL CROSS-LINKING; CHOLESTEROL EFFLUX; HELICAL STRUCTURES; LIPOPROTEIN PARTICLES; SELF-ASSOCIATIONS; STRUCTURAL STABILIZATION; X RAY CRYSTAL STRUCTURES;

CRYSTAL STRUCTURE;

ALANINE; APOLIPOPROTEIN A4; PROLINE; APOLIPOPROTEIN A; APOLIPOPROTEIN A-IV; CHOLESTEROL; LIPOSOME; PROTEIN BINDING; RECOMBINANT PROTEIN;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CHOLESTEROL TRANSPORT; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIMERIZATION; HUMAN; MOLECULAR WEIGHT; MOUSE; MUTAGENESIS; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN CROSS LINKING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LIPID INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; RESIDUE ANALYSIS; SEQUENCE ALIGNMENT; STRUCTURE ANALYSIS; THERMOSTABILITY; X RAY CRYSTALLOGRAPHY; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; METABOLISM; NUCLEOTIDE SEQUENCE; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; SITE DIRECTED MUTAGENESIS; SMALL ANGLE SCATTERING; THERMODYNAMICS; X RAY DIFFRACTION;

ALANINE; AMINO ACID SUBSTITUTION; APOLIPOPROTEINS A; CHOLESTEROL; CONSERVED SEQUENCE; HUMANS; LIPOSOMES; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROLINE; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SCATTERING, SMALL ANGLE; THERMODYNAMICS; X-RAY DIFFRACTION;

EID: 84928393874     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.637058     Document Type: Article

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