Dimerization of the transmembrane domain of amyloid precursor protein is determined by residues around the γ-secretase cleavage sites

Journal of Biological Chemistry

Volumn 292, Issue 38, 2017, Pages 15826-15837

  Yan, Yan ^a,b,c   Xu, Ting Hai ^a,b,c   Harikumar, Kaleeckal G ^d   Miller, Laurence J ^d   Melcher, Karsten ^c   Xu, H Eric ^a,c  

^a SHANGHAI INSTITUTE OF MATERIA MEDICA   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

^c VAN ANDEL RESEARCH INSTITUTE   (United States)

^d MAYO GRADUATE SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; AMINO ACIDS; ENERGY TRANSFER; GLYCOPROTEINS; PEPTIDES;

AMYLOID PRECURSOR PROTEINS; BIOLUMINESCENCE RESONANCE ENERGY TRANSFER; C-TERMINAL FRAGMENTS; CRITICAL DETERMINANT; PROTEIN INTERACTION; SECONDARY STRUCTURES; TRANS-MEMBRANE DOMAINS; TRANSMEMBRANE HELICES;

DIMERIZATION;

ALANINE; AMYLOID PRECURSOR PROTEIN; GAMMA SECRETASE; HYBRID PROTEIN; ISOLEUCINE; NOTCH RECEPTOR; OLIGOMER; PROLINE; VALINE; AMYLOID BETA-PROTEIN PRECURSOR C-TERMINAL FRAGMENT BETA, HUMAN; PEPTIDE FRAGMENT; SECRETASE;

AMINO TERMINAL SEQUENCE; ARTICLE; BIOLUMINESCENCE RESONANCE ENERGY TRANSFER; BIOTINYLATION; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DIMERIZATION; ENZYME SUBSTRATE; MUTANT; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN CLEAVAGE; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; SITE DIRECTED MUTAGENESIS; WILD TYPE; AMINO ACID SEQUENCE; BINDING SITE; CELL LINE; CELL MEMBRANE; CHEMISTRY; GENETICS; HUMAN; METABOLISM; MUTAGENESIS; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN MULTIMERIZATION;

AMINO ACID SEQUENCE; AMYLOID BETA-PROTEIN PRECURSOR; AMYLOID PRECURSOR PROTEIN SECRETASES; BINDING SITES; CELL LINE; CELL MEMBRANE; HUMANS; MUTAGENESIS; PEPTIDE FRAGMENTS; PROTEIN DOMAINS; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; PROTEOLYSIS;

EID: 85029752439     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M117.789669     Document Type: Article

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