P21-activated kinase 2 in neutrophils can be regulated by phosphorylation at multiple sites and by a variety of protein phosphatases

Journal of Immunology

Volumn 171, Issue 7, 2003, Pages 3785-3793

  Zhan, Qian ^a   Ge, Qingyuan ^b   Ohira, Taisuke ^a,c   Van Dyke, Thomas ^c   Badwey, John A ^a  

^a BRIGHAM AND WOMEN S HOSPITAL   (United States)

^b CELL SIGNALING TECHNOLOGY   (United States)

^c BOSTON UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMOATTRACTANT; FORMYLMETHIONYLLEUCYLPHENYLALANINE; GLUTATHIONE; GUANINE NUCLEOTIDE EXCHANGE FACTOR; P21 ACTIVATED KINASE 1; P21 ACTIVATED KINASE 2; P21 ACTIVATED KINASE 3; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE 2A; PHOSPHOPROTEIN PHOSPHATASE 2C; PHOSPHOTRANSFERASE; PROTEIN P21; PROTEIN P21 ACTIVATED KINASE 2; SERINE; THREONINE; UNCLASSIFIED DRUG;

ANTIBODY SPECIFICITY; ARTICLE; AUTOPHOSPHORYLATION; BINDING SITE; BIOCHEMISTRY; CONTROLLED STUDY; DEPHOSPHORYLATION; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME PHOSPHORYLATION; ENZYME REGULATION; ENZYME STRUCTURE; GUINEA PIG; HUMAN; HUMAN CELL; IN VITRO STUDY; NEUTROPHIL; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION;

EID: 0141920605     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.171.7.3785     Document Type: Article

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