Familial Alzheimer's mutations within APPTM increase Aβ42 production by enhancing accessibility of ε-cleavage site

Nature Communications

Volumn 5, Issue , 2014, Pages

  Chen, Wen ^a   Gamache, Eric ^a   Rosenman, David J ^a   Xie, Jian ^a   Lopez, Maria M ^a   Li, Yue Ming ^b   Wang, Chunyu ^a  

^a Research Rensselaer Polytechnic Institute   (United States)

^b MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; GAMMA SECRETASE; AMYLOID BETA PROTEIN; DEUTERIUM; HYDROGEN; SECRETASE;

CHEMICAL BONDING; DEUTERIUM; DISEASE; GENE EXPRESSION; HYDROGEN; MENTAL HEALTH; MUTATION; PROTEIN;

ALZHEIMER DISEASE; ARTICLE; DEUTERIUM HYDROGEN EXCHANGE; DIMERIZATION; EPSILON CLEAVAGE SITE; FAMILIAL ALZHEIMERS DISEASE; FAMILIAL DISEASE; GENE MUTATION; HETERONUCLEAR SINGLE QUANTUM COHERENCE; HYDROGEN BOND; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CLEAVAGE; PROTEIN CONFORMATION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; CHEMISTRY; GENETICS; HUMAN; METABOLISM; MUTATION; PROTEIN TERTIARY STRUCTURE;

ALZHEIMER DISEASE; AMYLOID BETA-PEPTIDES; AMYLOID BETA-PROTEIN PRECURSOR; AMYLOID PRECURSOR PROTEIN SECRETASES; DEUTERIUM; HUMANS; HYDROGEN; MAGNETIC RESONANCE SPECTROSCOPY; MUTATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY;

EID: 84895768762     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms4037     Document Type: Article

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