Structural evolution and membrane interactions of Alzheimer's amyloid-βeta peptide oligomers: New knowledge from single-molecule fluorescence studies

Protein Science

Volumn 23, Issue 7, 2014, Pages 869-883

  Johnson, Robin D ^a,b   Steel, Duncan G ^a   Gafni, Ari ^a,b  

^a UNIVERSITY OF MICHIGAN   (United States)

^b UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

Alzheimer's disease; Amyloid eta peptide; Fluorescence; Oligomers; Peptide membrane interaction; Single molecule microscopy

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; OLIGOMER; AMYLOID BETA-PROTEIN (1-42); PEPTIDE FRAGMENT;

ALZHEIMER DISEASE; ARTIFICIAL MEMBRANE; BINDING AFFINITY; BINDING SITE; BLEACHING; CELL MEMBRANE; DISSOCIATION CONSTANT; FLUORESCENCE MICROSCOPY; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMAN; LIPID MEMBRANE; MEMBRANE BINDING; MOLECULAR EVOLUTION; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN BINDING; PROTEIN IMMOBILIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; REVIEW; SINGLE MOLECULE FLUORESCENCE MICROSCOPY; ANIMAL; CHEMISTRY; METABOLISM; PROCEDURES; PROTEIN MULTIMERIZATION;

AMYLOID BETA-PEPTIDES; ANIMALS; CELL MEMBRANE; HUMANS; MICROSCOPY, FLUORESCENCE; PEPTIDE FRAGMENTS; PROTEIN MULTIMERIZATION;

EID: 84904201655     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2479     Document Type: Review

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