Amyloid-β42 protofibrils are internalized by microglia more extensively than monomers

Brain Research

Volumn 1648, Issue , 2016, Pages 485-495

  Gouwens, Lisa K ^a   Makoni, Nyasha J ^a   Rogers, Victoria A ^a   Nichols, Michael R ^a  

^a UNIVERSITY OF MISSOURI ST LOUIS   (United States)

Author keywords

Aggregation; Amyloid beta protein; Inflammation; Internalization; Microglia; Protofibrils; Uptake

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; MONOMER; TUMOR NECROSIS FACTOR; AMYLOID BETA PROTEIN; AMYLOID BETA-PROTEIN (1-42); PEPTIDE FRAGMENT;

ALZHEIMER DISEASE; ANIMAL CELL; ARTICLE; BINDING AFFINITY; CELL INTERACTION; CELLULAR DISTRIBUTION; COMPARATIVE STUDY; CONTROLLED STUDY; FLUORESCENCE; INFLAMMATION; INTERNALIZATION; MICROGLIA; NONHUMAN; PHOTON CORRELATION SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN SECRETION; PROTEIN STRUCTURE; PROTEIN TRANSPORT; SIZE EXCLUSION CHROMATOGRAPHY; STOICHIOMETRY; TRANSMISSION ELECTRON MICROSCOPY; ANIMAL; C57BL MOUSE; CELL CULTURE; CHEMISTRY; METABOLISM; MOUSE; ULTRASTRUCTURE;

AMYLOID BETA-PEPTIDES; ANIMALS; CELLS, CULTURED; MICE; MICE, INBRED C57BL; MICROGLIA; PEPTIDE FRAGMENTS; TUMOR NECROSIS FACTOR-ALPHA;

EID: 84983401985     PISSN: 00068993     EISSN: 18726240     Source Type: Journal    
DOI: 10.1016/j.brainres.2016.08.016     Document Type: Article

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