The DOI matches its Crossref record; 58 of the 58 references it cites were found in a registry or an index.
Novel Human Homologues of p47 and p67 Participate in Activation of Superoxide-producing NADPH Oxidases
Open accessAbstract
The catalytic core of a superoxide-producing NADPH oxidase (Nox) in phagocytes is gp91phox/Nox2, a membrane-integrated protein that forms a heterodimer with p22phox to constitute flavocytochrome b558. The cytochrome becomes activated by interacting with the adaptor proteins p47phox and p67phox as well as the small GTPase Rac. Here we describe the cloning of human cDNAs for novel proteins homologous to p47phox and p67phox, designated p41nox and p51nox, respectively; the former is encoded by NOXO1 (Nox organizer 1), and the latter is encoded by NOXA1 (Nox activator 1). The novel homologue p41nox interacts with p22phox via the two tandem SH3 domains, as does p47phox. The protein p51nox as well as p67phox can form a complex with p47phox and with p41nox via the C-terminal SH3 domain and binds to GTP-bound Rac via the N-terminal domain containing four tetratricopeptide repeat motifs. These bindings seem to play important roles, since p47phox and p67phox activate the phagocyte oxidase via the same interactions. Indeed, p41nox and p51nox are capable of replacing the corresponding classical homologue in activation of gp91phox. Nox1, a homologue of gp91phox, also can be activated in cells, when it is coexpressed with p41nox and p51nox, with p41nox and p67phox, or with p47phox and p51nox; in the former two cases, Nox1 is partially activated without any stimulants added, suggesting that p41nox is normally in an active state. Thus, the novel homologues p41nox and p51nox likely function together or in combination with a classical one, thereby activating the two Nox family oxidases.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“This loop in NOX4 seems to provide steric hindrance to slow down superoxide release, forcing two superoxide molecules to react with each other in a reaction that appears to be catalyzed, in part, by a histidine residue (925).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [925]
In the citing paper
“The mechanism of NOX4 is still controversial, but elegant work by Takac et al. indicates that the E-loop (sequence between helices V and VI) of NOX4 shows notable differences with the other NOX isoforms (925).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [925]
Citations
Cites
BABIOR, B. M. (1999) · Blood · doi:10.1182/blood.v93.5.1464 · Cited by 2,147
pEF-BOS, a powerful mammalian expression vector
Mizushima, S., & Nagata, S. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.17.5322 · Cited by 1,594
Cell transformation by the superoxide-generating oxidase Mox1
Suh, Y.-A., Arnold, R. S., Lassegue, B., Shi, J., Xu, X., Sorescu, D., Chung, A. B., Griendling, K. K., & Lambeth, J. D. (1999) · Nature · doi:10.1038/43459 · Cited by 1,480
Identification of Renox, an NAD(P)H oxidase in kidney
Geiszt, M., Kopp, J. B., Várnai, P., & Leto, T. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.130135897 · Cited by 840
Lassègue, B., Sorescu, D., Szöcs, K., Yin, Q., Akers, M., Zhang, Y., Grant, S. L., Lambeth, J. D., & Griendling, K. K. (2001) · Circulation Research · doi:10.1161/hh0901.090299 · Cited by 839
Homologs of gp91 phox : cloning and tissue expression of Nox3, Nox4, and Nox5
Cheng, G., Cao, Z., Xu, X., Meir, E. G. V., & Lambeth, J. D. (2001) · Gene · doi:10.1016/s0378-1119(01)00449-8 · Cited by 820
A Ca2+-activated NADPH Oxidase in Testis, Spleen, and Lymph Nodes
Bánfi, B., Molnár, G., Maturana, A., Steger, K., Hegedûs, B., Demaurex, N., & Krause, K.-H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103034200 · Cited by 622
Assembly of the phagocyte NADPH oxidase: molecular interaction of oxidase proteins
DeLeo, F. R., & Quinn, M. T. (1996) · Journal of Leukocyte Biology · doi:10.1002/jlb.60.6.677 · Cited by 526
A Novel Superoxide-producing NAD(P)H Oxidase in Kidney
Shiose, A., Kuroda, J., Tsuruya, K., Hirai, M., Hirakata, H., Naito, S., Hattori, M., Sakaki, Y., & Sumimoto, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007597200 · Cited by 517
Self-citationTwo Novel Proteins Activate Superoxide Generation by the NADPH Oxidase NOX1
Bánfi, B., Clark, R. A., Steger, K., & Krause, K.-H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200613200 · Cited by 491
Flagged first, then by citations
Cited by
Sorted by citations
The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989
Reactive Oxygen Species in Inflammation and Tissue Injury
Mittal, M., Siddiqui, M. R., Tran, K., Reddy, S. P., & Malik, A. B. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.5149 · Cited by 4,897
NOX enzymes and the biology of reactive oxygen
Lambeth, J. D. (2004) · Nature Reviews Immunology · doi:10.1038/nri1312 · Cited by 3,125
RHO GTPASES: Biochemistry and Biology
Jaffe, A. B., & Hall, A. (2005) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.21.020604.150721 · Cited by 3,009
Role of Oxidative Modifications in Atherosclerosis
Stocker, R., & Keaney, J. F. (2004) · Physiological Reviews · doi:10.1152/physrev.00047.2003 · Cited by 2,646
Metadata
- Authors
- Takeya, R., Ueno, N., Kami, K., Taura, M., Kohjima, M., Izaki, T., Nunoi, H., & Sumimoto, H.
- Affiliations
- Kyushu University (JP)
- University of Miyazaki (JP)
- Corresponding author
- Sumimoto, Hideki
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-07
- Volume
- 278
- Issue
- 27
- Pages
- 25234-25246
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC4358237
- OpenAlex
- W2003241255
- Cited by
- 380
- References
- 58
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 3 · 2023: 10 · 2022: 5 · 2021: 8 · 2020: 9 · 2019: 11 · 2018: 7 · 2017: 14 · 2016: 9 · 2015: 9 · 2014: 13 · 2013: 20 · 2012: 15
- FWCI
- 12.69
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Keywords
- NADPH oxidase, p47phox, p67phox, NOXO1, NOXA1, gp91phox, p22phox, flavocytochrome b558, Rac GTPase, SH3 domain, NOX1, superoxide production, phagocytes, oxidase activation, adaptor proteins
- MeSH terms
- Amino Acid Sequence, Cloning, Molecular, Enzyme Activation, Humans, Molecular Sequence Data, Phosphoproteins, Genome, Human, Sequence Alignment, Sequence Homology, DNA, Complementary, NADPH Oxidases, Adaptor Proteins, Vesicular Transport, Adaptor Proteins, Signal Transducing
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
