A possible effector role for the pleckstrin homology (PH) domain of dynamin

Proceedings of the National Academy of Sciences of the United States of America

Volumn 106, Issue 32, 2009, Pages 13359-13364

  Bethoney, Kelley A ^a   King, Megan C ^a,c   Hinshaw, Jenny E ^b   Ostap, E Michael ^a   Lemmon, Mark A ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^c YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Actin; Endocytosis; GTPase; Phosphoinositide; Vesicle

Indexed keywords

CLATHRIN; DYNAMIN; GUANOSINE TRIPHOSPHATASE; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PLECKSTRIN;

ACTIN POLYMERIZATION; ARTICLE; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; ELECTRON MICROSCOPY; ENDOCYTOSIS; EPIFLUORESCENCE MICROSCOPY; FLUORESCENCE; GEOMETRY; HUMAN; HUMAN CELL; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN LOCALIZATION; SEQUENCE HOMOLOGY;

DYNAMINS; ENDOCYTOSIS; HELA CELLS; HUMANS; MICROSCOPY, FLUORESCENCE; MODELS, MOLECULAR; MUTATION; PHOSPHATIDYLINOSITOL 4,5-DIPHOSPHATE; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; SEQUENCE HOMOLOGY, AMINO ACID; SUBCELLULAR FRACTIONS;

ANIMALIA;

EID: 69449101828     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0906945106     Document Type: Article

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