Atomic force microscopy reveals drebrin induced remodeling of F-actin with subnanometer resolution

Nano Letters

Volumn 11, Issue 2, 2011, Pages 825-827

  Sharma, Shivani ^a   Grintsevich, Elena E ^a   Phillips, Martin L ^a   Reisler, Emil ^a   Gimzewski, James K ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b NATIONAL INSTITUTE FOR MATERIALS SCIENCE   (Japan)

Author keywords

AFM; drebrin; F actin remodeling; nanofilament mechanics; neuron cytoskeleton

Indexed keywords

ACTIN-BINDING PROTEINS; AFM; CYTOSKELETONS; DREBRIN; F-ACTIN; F-ACTIN REMODELING; HELICAL TWIST; HIGH RESOLUTION; MOLECULAR LEVELS; NANO SCALE; NANOFILAMENT MECHANICS; PERSISTENCE LENGTH; STRUCTURE ASSEMBLY; SUBNANOMETER RESOLUTION;

ATOMIC FORCE MICROSCOPY; BIOMECHANICS; FLUORINE; MECHANICAL PROPERTIES; PRESSURE EFFECTS;

PROTEINS;

ACTIN; DREBRINS; NEUROPEPTIDE;

ARTICLE; ATOMIC FORCE MICROSCOPY; BINDING SITE; CHEMISTRY; METHODOLOGY; PROTEIN BINDING; PROTEIN CONFORMATION; ULTRASTRUCTURE;

ACTINS; BINDING SITES; MICROSCOPY, ATOMIC FORCE; NEUROPEPTIDES; PROTEIN BINDING; PROTEIN CONFORMATION;

EID: 79851502285     PISSN: 15306984     EISSN: 15306992     Source Type: Journal    
DOI: 10.1021/nl104159v     Document Type: Article

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