Neutrophil β 2 integrin inhibition by enhanced interactions of vasodilator-stimulated phosphoprotein with S-nitrosylated actin

Journal of Biological Chemistry

Volumn 286, Issue 37, 2011, Pages 32854-32865

  Thom, Stephen R ^a,b   Bhopale, Veena M ^a   Yang, Ming ^a   Bogush, Marina ^a   Huang, Shaohui ^a   Milovanova, Tatyana N ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b HOSPITAL OF THE UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN FILAMENT; ACTIN POLYMERIZATION; CELL CONCENTRATIONS; CHEMICAL INHIBITORS; CLOSE PROXIMITY; CYTOSKELETAL NETWORK; F-ACTIN; HIGH AFFINITY; HYPEROXIA; INTEGRINS; PROTEIN KINASE; RAC ACTIVATION; REACTIVE SPECIES; S-NITROSYLATION; VASODILATOR-STIMULATED PHOSPHOPROTEINS;

AMINO ACIDS; ENZYMES; LAKES; PHOSPHORYLATION; POLYMERIZATION; POLYMERS; RNA;

PROTEINS;

8 BROMO CYCLIC GMP; ACTIN; BETA2 INTEGRIN; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC GMP DEPENDENT PROTEIN KINASE; FORMYLMETHIONYLLEUCYLPHENYLALANINE; RAC1 PROTEIN; RAC2 PROTEIN; VASODILATOR STIMULATED PHOSPHOPROTEIN; 8-BROMOCYCLIC GMP; ACTIN BINDING PROTEIN; CD18 ANTIGEN; CELL ADHESION MOLECULE; CYCLIC GMP; DRUG DERIVATIVE; PHOSPHOPROTEIN; PROTEIN KINASE; SMALL INTERFERING RNA; VASODILATOR-STIMULATED PHOSPHOPROTEIN;

ACTIN POLYMERIZATION; ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; BINDING AFFINITY; CONCENTRATION RESPONSE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME INHIBITION; HYPEROXIA; MOUSE; NEUTROPHIL; NITROSYLATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN LOCALIZATION; ACTIN FILAMENT; ANIMAL; DRUG EFFECT; GENETICS; METABOLISM; MOUSE MUTANT;

ACTIN CYTOSKELETON; ACTINS; ANIMALS; ANTIGENS, CD18; CELL ADHESION MOLECULES; CYCLIC GMP; ENZYME ACTIVATION; MICE; MICE, KNOCKOUT; MICROFILAMENT PROTEINS; N-FORMYLMETHIONINE LEUCYL-PHENYLALANINE; NEUTROPHILS; PHOSPHOPROTEINS; PROTEIN BINDING; PROTEIN KINASES; RNA, SMALL INTERFERING;

EID: 80052772424     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.255778     Document Type: Article

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