Functional importance of covalent homodimer of reelin protein linked via its central region

Journal of Biological Chemistry

Volumn 286, Issue 40, 2011, Pages 35247-35256

  Yasui, Norihisa ^a,c   Kitago, Yu ^a   Beppu, Ayako ^a   Kohno, Takao ^b   Morishita, Shunsuke ^b   Gomi, Hiroki ^b   Nagae, Masamichi ^a,d   Hattori, Mitsuharu ^b   Takagi, Junichi ^a  

^a OSAKA UNIVERSITY   (Japan)

^b NAGOYA CITY UNIVERSITY   (Japan)

^c UNIVERSITY OF CHICAGO   (United States)

^d RIKEN   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

APOLIPOPROTEIN E; BINDING ASSAYS; BINDING CAPABILITY; BRAIN DEVELOPMENT; CHEMICAL NATURE; CULTURED NEURONS; CYSTEINE RESIDUES; HIGH MOLECULAR WEIGHT; HIGHER ORDER; HOMODIMERIZATION; HOMODIMERS; INTERCHAIN DISULFIDE BONDS; MULTIMERIZATION; MULTIMERS; N-TERMINALS; NON-COVALENT INTERACTION; OLIGOMERIC STATE; PRIMARY STRUCTURES; SIGNALING ACTIVITY; VERY LOW DENSITY LIPOPROTEIN RECEPTORS;

AMINO ACIDS; COVALENT BONDS; OLIGOMERIZATION; OLIGOMERS; SURFACE PLASMON RESONANCE;

PROTEINS;

APOLIPOPROTEIN E; APOLIPOPROTEIN E RECEPTOR 2; CYSTEINE; HOMODIMER; REELIN; UNCLASSIFIED DRUG; VERY LOW DENSITY LIPOPROTEIN RECEPTOR;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; DIMERIZATION; DISULFIDE BOND; IMMUNOBLOTTING; MOLECULAR WEIGHT; MOUSE; NERVE CELL; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN MULTIMERIZATION; PROTEIN PURIFICATION; SIGNAL TRANSDUCTION; SURFACE PLASMON RESONANCE;

AMINO ACID SEQUENCE; ANIMALS; BRAIN; CELL ADHESION MOLECULES, NEURONAL; CELL LINE; CHO CELLS; CRICETINAE; CRICETULUS; DIMERIZATION; DISULFIDES; EXTRACELLULAR MATRIX PROTEINS; HUMANS; MICE; MOLECULAR SEQUENCE DATA; NERVE TISSUE PROTEINS; NEURONS; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; SERINE ENDOPEPTIDASES; SIGNAL TRANSDUCTION;

EID: 80053422050     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.242719     Document Type: Article

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