Phosphorylation-independent Association of CXCR2 with the Protein Phosphatase 2A Core Enzyme

Journal of Biological Chemistry

Volumn 276, Issue 20, 2001, Pages 16960-16968

  Fan, Guo Huang ^b   Yang, Wei ^b   Sai, Jiqing ^b   Richmond, Ann ^a,b  

^a DEPARTMENT OF VETERANS AFFAIRS   (United States)

^b VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL CULTURE; ENZYME KINETICS; MONOMERS; MUTAGENESIS;

BIORECEPTORS; DEPHOSPHORYLATION;

BIOCHEMISTRY;

BETA 2 ADRENERGIC RECEPTOR; CALCIUM; CHEMOKINE; CHEMOKINE RECEPTOR; CHEMOKINE RECEPTOR CXCR2; COMPLEMENTARY DNA; DYNAMIN; G PROTEIN COUPLED RECEPTOR; GLUTATHIONE TRANSFERASE; OKADAIC ACID; PHOSPHOPROTEIN PHOSPHATASE 2A; HYBRID PROTEIN; PHOSPHOPROTEIN PHOSPHATASE; RECOMBINANT PROTEIN;

ARTICLE; CALCIUM MOBILIZATION; CHEMOTAXIS; DEPHOSPHORYLATION; EMBRYO; ENZYME PHOSPHORYLATION; FLUOROMETRY; GENE OVEREXPRESSION; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; INTERNALIZATION; KIDNEY CELL; PLASMID; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; WESTERN BLOTTING; YEAST; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BINDING SITE; CELL LINE; CHEMISTRY; DRUG EFFECT; ENDOCYTOSIS; GENE DELETION; GENETIC TRANSFECTION; GENETICS; GROWTH, DEVELOPMENT AND AGING; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; MUTAGENESIS; NEUTROPHIL; NUCLEOTIDE SEQUENCE; PHOSPHORYLATION; SACCHAROMYCES CEREVISIAE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BINDING SITES; CELL LINE; CLONING, MOLECULAR; CONSERVED SEQUENCE; ENDOCYTOSIS; HUMANS; MOLECULAR SEQUENCE DATA; MUTAGENESIS; MUTAGENESIS, SITE-DIRECTED; NEUTROPHILS; OKADAIC ACID; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHORYLATION; RECEPTORS, INTERLEUKIN-8B; RECOMBINANT FUSION PROTEINS; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SEQUENCE ALIGNMENT; SEQUENCE DELETION; SEQUENCE HOMOLOGY, AMINO ACID; TRANSFECTION;

EID: 0035907361     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M009292200     Document Type: Article

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