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The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.

The biochemical basis of the NADPH oxidase of phagocytes

Segal, Anthony W., Abo, Arie·1993·Trends in Biochemical Sciences
DOI 10.1016/0968-0004(93)90051-n
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Abstract

The NADPH oxidase is an electron transport chain found in lymphocytes and in the wall of the endocytic vacuole of 'professional' phagocytic cells. It is so called because NADPH is used as an electron donor to reduce oxygen to superoxide and hydrogen peroxide. The redox components are provided by a very unusual flavocytochrome b from the membrane, which is dependent upon cytosolic factors (including two specialized proteins, p47phox and p67phox) for activation. The small GTP-binding protein, p21rac, is also implicated in this system, possibly as the switch that triggers electron transport. This system provides a key to our understanding of the way in which these GTP-binding proteins function.

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Crossref · 10.1016/0968-0004(93)90051-n

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6 of 6 references verified0 citation errors · 0 not checkable

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Citations

Cites

Show all 6 references

Research works printed but not linked: 34

  1. Segal, 1989, J. Clin. Invest., 83, 1785, 10.1172/JCI114083 · DOI
  2. Cross, 1991, Biochim. Biophys. Acta, 1057, 281, 10.1016/S0005-2728(05)80140-9 · DOI
  3. Morel, 1991, Eur. J. Biochem., 201, 523, 10.1111/j.1432-1033.1991.tb16312.x · DOI
  4. Rossi, 1986, Biochim. Biophys. Acta, 853, 65, 10.1016/0304-4173(86)90005-4 · DOI
  5. Smith, 1991, Blood, 77, 673, 10.1182/blood.V77.4.673.673 · DOI
  6. Roos, 1983, J. Cell Biol., 97, 368, 10.1083/jcb.97.2.368 · DOI
  7. Segal, 1981, Nature, 290, 406, 10.1038/290406a0 · DOI
  8. Dorseuil, 1992, J. Biol. Chem., 267, 20540, 10.1016/S0021-9258(19)36716-X · DOI
  9. Garcia, 1992, Biochem. J., 286, 687, 10.1042/bj2860687 · DOI
  10. Segal, 1978, Nature, 276, 515, 10.1038/276515a0 · DOI
  11. Segal, 1987, Nature, 326, 88, 10.1038/326088a0 · DOI · Paper page
  12. Segal, 1983, New Engl. J. Med., 308, 245, 10.1056/NEJM198302033080503 · DOI
  13. Teahan, 1987, Nature, 327, 720, 10.1038/327720a0 · DOI
  14. Segal, 1992, Biochem. J., 284, 781, 10.1042/bj2840781 · DOI
  15. Abo, 1992, J. Biol. Chem., 267, 16767, 10.1016/S0021-9258(18)41846-7 · DOI
  16. Rotrosen, 1992, Science, 256, 1459, 10.1126/science.1318579 · DOI
  17. Hurst, 1991, J. Biol. Chem., 266, 1627, 10.1016/S0021-9258(18)52340-1 · DOI
  18. Dinauer, 1990, J. Clin. Invest., 86, 1729, 10.1172/JCI114898 · DOI
  19. Yamaguchi, 1989, J. Biol. Chem., 264, 112, 10.1016/S0021-9258(17)31230-9 · DOI
  20. Nugent, 1989, Biochem. J., 264, 921, 10.1042/bj2640921 · DOI
  21. Volpp, 1989, 86, 7195
  22. Pawson, 1992, Cell, 71, 359, 10.1016/0092-8674(92)90504-6 · DOI
  23. Bromberg, 1984, Cell Immunol., 88, 213, 10.1016/0008-8749(84)90066-2 · DOI
  24. Knoller, 1991, J. Biol. Chem., 266, 2795, 10.1016/S0021-9258(18)49917-6 · DOI
  25. Abo, 1991, J. Biol. Chem., 266, 23577, 10.1016/S0021-9258(18)54322-2 · DOI · Paper page
  26. Abo, 1991, Nature, 353, 668, 10.1038/353668a0 · DOI
  27. Didsbury, 1989, J. Biol. Chem., 264, 16378, 10.1016/S0021-9258(19)84716-6 · DOI · Paper page
  28. Fukumoto, 1990, Oncogene, 5, 1321
  29. Knaus, 1992, Science, 254, 1512, 10.1126/science.1660188 · DOI · Paper page
  30. Quinn, 1989, Nature, 342, 198, 10.1038/342198a0 · DOI
  31. Hart, 1992, Science, 258, 812, 10.1126/science.1439791 · DOI · Paper page
  32. Tamura, 1989, Arch. Biochem. Biophys., 275, 23, 10.1016/0003-9861(89)90345-7 · DOI
  33. Hori, 1991, Oncogene, 6, 515
  34. Boume, 1992, Nature, 358, 541, 10.1038/358541a0 · DOI

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Metadata

Authors
Segal, A. W., & Abo, A.
Venue
Trends in Biochemical Sciences
Publisher
Elsevier BV
Published
1993-02
Volume
18
Issue
2
Pages
43-47
ISSN
0968-0004
DOI
10.1016/0968-0004(93)90051-n
Cited by
459
References
6
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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CoChat. (2026). Citation check: The biochemical basis of the NADPH oxidase of phagocytes. https://app.cochat.ai/papers/10.1016/0968-0004(93)90051-n
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Segal, A. W., & Abo, A. (1993). The biochemical basis of the NADPH oxidase of phagocytes. Trends in Biochemical Sciences. https://doi.org/10.1016/0968-0004(93)90051-n