Two pathways through Cdc42 couple the N-formyl receptor to actin nucleation in permeabilized human neutrophils

Journal of Cell Biology

Volumn 150, Issue 4, 2000, Pages 785-796

  Glogauer, M ^a   Hartwig, J ^a   Stossel, T ^a  

^a BRIGHAM AND WOMEN S HOSPITAL   (United States)

Author keywords

Actin assembly; Arp2 3; FMLP; Rac; Signal transduction pathways

Indexed keywords

ACTIN; FORMYLMETHIONYLLEUCYLPHENYLALANINE; GUANOSINE TRIPHOSPHATASE; PHOSPHATIDYLINOSITIDE; PROTEIN CDC42; RAC PROTEIN; RECEPTOR;

ACTIN FILAMENT; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; HUMAN; HUMAN CELL; MEMBRANE PERMEABILITY; NEUTROPHIL; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN EXPRESSION; RECEPTOR OCCUPANCY; SIGNAL TRANSDUCTION;

ACTINS; ADULT; CDC42 GTP-BINDING PROTEIN; CELL MEMBRANE; CELL MEMBRANE PERMEABILITY; CELL SIZE; GLUCOSIDES; GUANOSINE TRIPHOSPHATE; HUMANS; KINETICS; N-FORMYLMETHIONINE LEUCYL-PHENYLALANINE; NERVE TISSUE PROTEINS; NEUTROPHILS; PEPTIDE FRAGMENTS; RECEPTORS, FORMYL PEPTIDE; RECEPTORS, IMMUNOLOGIC; RECEPTORS, PEPTIDE; SIGNAL TRANSDUCTION; WISKOTT-ALDRICH SYNDROME; WISKOTT-ALDRICH SYNDROME PROTEIN, NEURONAL;

EID: 0034698929     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.150.4.785     Document Type: Article

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