Bacterial and cell-free production of APP671-726 containing amyloid precursor protein transmembrane and metal-binding domains

Biochemistry (Moscow)

Volumn 78, Issue 11, 2013, Pages 1263-1271

  Bocharova, O V ^a   Urban, A S ^a   Nadezhdin, K D ^a   Bocharov, E V ^a   Arseniev, A S ^a  

^a SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

Author keywords

amyloid precursor protein; NMR spectroscopy; recombinant protein; transmembrane domain

Indexed keywords

BACTERIA (MICROORGANISMS);

AMYLOID PRECURSOR PROTEIN; PEPTIDE FRAGMENT; RECOMBINANT PROTEIN; SECRETASE;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; ARTICLE; BIOSYNTHESIS; CHEMISTRY; DIMERIZATION; ESCHERICHIA COLI; GENETICS; HUMAN; ISOLATION AND PURIFICATION; ISOTOPE LABELING; LIPID BILAYER; METABOLISM; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE; PATHOLOGY; PROTEIN TERTIARY STRUCTURE;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AMYLOID BETA-PROTEIN PRECURSOR; AMYLOID PRECURSOR PROTEIN SECRETASES; DIMERIZATION; ESCHERICHIA COLI; HUMANS; ISOTOPE LABELING; LIPID BILAYERS; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS;

EID: 84889011162     PISSN: 00062979     EISSN: 16083040     Source Type: Journal    
DOI: 10.1134/S0006297913110060     Document Type: Article

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