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Journal of the American Chemical Society

Volumn 133, Issue 31, 2011, Pages 12001-12008

Single molecule tracking analysis reveals that the surface mobility of amyloid oligomers is driven by their conformational structure

(2) Calamai, Martino a Pavone, Francesco S a

a UNIVERSITY OF FLORENCE (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL STRUCTURES; DYNAMIC BEHAVIORS; HETEROGENEOUS DYNAMICS; LIVING CELL; MEMBRANE MOBILITY; QUATERNARY STRUCTURE; SINGLE PARTICLE TRACKING; SINGLE-MOLECULE TRACKING; STRUCTURAL POLYMORPHISMS; STRUCTURAL TYPE; SUPRAMOLECULAR ASSEMBLIES; SURFACE MOBILITY; TOXIC EFFECT;

ANTIBODIES; CELL MEMBRANES; CONFORMATIONS; GLYCOPROTEINS;

OLIGOMERS;

AMYLOID BETA OLIGOMER; OLIGOMER; UNCLASSIFIED DRUG;

ARTICLE; CELL MEMBRANE; CHEMICAL ANALYSIS; CHEMICAL STRUCTURE; CONFORMATIONAL TRANSITION; HUMAN; HUMAN CELL; NEUROBLASTOMA CELL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; SURFACE PROPERTY;

AMYLOID BETA-PEPTIDES; HUMANS; PARTICLE SIZE; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; SURFACE PROPERTIES; TISSUE DISTRIBUTION; TUMOR CELLS, CULTURED;

EID: 79961165345 PISSN: 00027863 EISSN: 15205126 Source Type: Journal
DOI: 10.1021/ja200951f Document Type: Article

Times cited : (31)

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