A conserved region between the TPR and activation domains of p67 phox participates in activation of the phagocyte NADPH oxidase

Journal of Biological Chemistry

Volumn 285, Issue 41, 2010, Pages 31435-31445

  Maehara, Yuichi ^a,b   Miyano, Kei ^a,b   Yuzawa, Satoru ^a,b   Akimoto, Risa ^a,b   Takeya, Ryu ^a,b   Sumimoto, Hideki ^a,b  

^a KYUSHU UNIVERSITY   (Japan)

^b KYUSHU UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN-ANTIBODY REACTIONS; MOLECULAR OXYGEN; PROTEINS;

ACTIVATION DOMAIN; ALANINE SUBSTITUTION; BINDING ACTIVITIES; BINDING DOMAIN; CATALYTIC CORE; CELL STIMULATION; CONSERVED REGIONS; CYTOSOLIC PROTEINS; ELECTRON TRANSPORTING; OXIDASE ACTIVATION; PHAGOCYTE NADPH OXIDASE; RESTING CELLS; SUPEROXIDE PRODUCTION; SUPEROXIDES;

AMINO ACIDS;

ENZYME; OXIDOREDUCTASE; PROTEIN NOX3; PROTEIN P67PHOX; RAC PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 1; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 2; SUPEROXIDE; UNCLASSIFIED DRUG; CYBB PROTEIN, HUMAN; MEMBRANE PROTEIN; NEUTROPHIL CYTOSOL FACTOR 67K; NEUTROPHIL CYTOSOLIC FACTOR 1; NOX1 PROTEIN, HUMAN; NOX3 PROTEIN, HUMAN; PHOSPHOPROTEIN;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME ACTIVATION; GENETIC CONSERVATION; HUMAN; HUMAN CELL; MUTATION; NONHUMAN; PHAGOCYTE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; ANIMAL; CHO CELL LINE; CRICETULUS; ENZYMOLOGY; GENETICS; HAMSTER; METABOLISM; MISSENSE MUTATION; PHYSIOLOGY; PROTEIN MOTIF; PROTEIN TERTIARY STRUCTURE;

AMINO ACID MOTIFS; AMINO ACID SUBSTITUTION; ANIMALS; CHO CELLS; CRICETINAE; CRICETULUS; ENZYME ACTIVATION; HUMANS; MEMBRANE GLYCOPROTEINS; MEMBRANE PROTEINS; MUTATION, MISSENSE; NADPH OXIDASE; PHAGOCYTES; PHOSPHOPROTEINS; PROTEIN STRUCTURE, TERTIARY; RAC GTP-BINDING PROTEINS; SUPEROXIDES;

EID: 77957768024     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.161166     Document Type: Article

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