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Volumn 82, Issue 8, 2000, Pages 727-732

C-terminal region of the cytosolic subunit p47(phox) is a primary target of conformational change during the activation of leukocyte NADPH oxidase

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME B558; PROTEIN KINASE C; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; TRYPTOPHAN;

EID: 0033818989     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(00)01153-6     Document Type: Article
Times cited : (6)

References (34)
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    • Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion
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  • 30
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    • Activation of the leukocyte NADPH oxidase subunit p47(phox) by protein kinase C. A phosphorylation-dependent change in the conformation of the C-terminal end of p47(phox)
    • (1997) Biochemistry , vol.36 , pp. 7474-7480
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  • 34
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    • Anionic amphiphile-independent activation of the phagocyte NADPH oxidase in a cell-free system by p47(phox) and p67(phox), both in C terminally truncated forms. Implication for regulatory Src homology 3 domain-mediated interactions
    • (1998) J. Biol. Chem. , vol.273 , pp. 4232-4236
    • Hata, K.1    Ito, T.2    Takeshige, K.3    Sumimoto, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.