BRICHOS domains efficiently delay fibrillation of amyloid β-peptide

Journal of Biological Chemistry

Volumn 287, Issue 37, 2012, Pages 31608-31617

  Willander, Hanna ^a,b   Presto, Jenny ^a,b   Askarieh, Glareh ^a   Biverstål, Henrik ^b   Frohm, Birgitta ^c   Knight, Stefan D ^a   Johansson, Jan ^a,b   Linse, Sara ^c  

^a SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES   (Sweden)

^b KAROLINSKA INSTITUTE   (Sweden)

^c LUND UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATION PROCESS; ALZHEIMER; AMYLOID DISEASE; AMYLOID FIBRIL; CONCENTRATION-DEPENDENT; FIBRIL FORMATION; INHIBITORY MECHANISM; KINETIC EXPERIMENT; LAG PHASE; LAG-TIME; LUNG FIBROSIS; MAIN EFFECT; MEMBRANE PROTEINS; MOLECULAR EVENTS; PRION DISEASE; PROLIFERATIVE DISEASE; PROTEIN MISFOLDING; SHEET STRUCTURE; STOICHIOMETRIC RATIO; SURFACTANT PROTEINS;

AGGLOMERATION; AMINO ACIDS; BIOLOGICAL MEMBRANES; ELECTRON MICROSCOPY; NEURODEGENERATIVE DISEASES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OLIGOMERS; PEPTIDES; SURFACE ACTIVE AGENTS;

GLYCOPROTEINS;

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; HYDROGEN; HYDROXYL GROUP; MONOMER; PROTEIN; PROTEIN BRI2; RECOMBINANT PROTEIN; SURFACTANT PROTEIN C; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; BRICHOS DOMAIN; CIRCULAR DICHROISM; CONCENTRATION (PARAMETERS); ELECTRON MICROSCOPY; GEL PERMEATION CHROMATOGRAPHY; HYDROGEN BOND; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN MODIFICATION; PROTEIN STRUCTURE; QUANTITATIVE ANALYSIS; REPRODUCIBILITY; STOICHIOMETRY;

AMYLOID; AMYLOID BETA-PEPTIDES; CIRCULAR DICHROISM; HUMANS; MODELS, MOLECULAR; NEURODEGENERATIVE DISEASES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, TERTIARY; PULMONARY FIBROSIS;

EID: 84866070823     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.393157     Document Type: Article

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