The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Regulators of bacterial responses to nitric oxide
Abstract
Nitric oxide (NO) is an intermediate of the respiratory pathway known as denitrification, and is a by-product of anaerobic nitrite respiration in the enteric Bacteria. Pathogens are also exposed to NO inside host phagocytes, and possibly in other host niches as well. In recent years it has become apparent that there are multiple regulatory systems in prokaryotes that mediate responses to NO exposure. Owing to its reactivity, NO also has the potential to perturb the activities of other regulatory proteins, which are not necessarily directly involved in the response to NO. This review describes the current state of understanding of regulatory systems that respond to NO. An emerging trend is the predominance of iron proteins among the known physiological NO sensors.
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Cites
Andrews, S. C., Robinson, A. K., & Rodríguez-Quiñones, F. (2003) · FEMS Microbiology Reviews · doi:10.1016/s0168-6445(03)00055-x · Cited by 2,702 · cited 1×
“The Fur is a well-characterized transcriptional regulator that typically functions as an iron-dependent repressor to control the expression of genes involved in iron acquisition and utilization (Andrews et al., 2003).”
BackgroundAntimicrobial reactive oxygen and nitrogen species: concepts and controversies
Fang, F. C. (2004) · Nature Reviews Microbiology · doi:10.1038/nrmicro1004 · Cited by 1,676
Transcriptional Adaptation of Mycobacterium tuberculosis within Macrophages
Schnappinger, D., Ehrt, S., Voskuil, M. I., Liu, Y., Mangan, J. A., Monahan, I. M., Dolganov, G., Efron, B., Butcher, P. D., Nathan, C., et al. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20030846 · Cited by 1,420
Eriksson, S., Lucchini, S., Thompson, A., Rhen, M., & Hinton, J. C. D. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03313.x · Cited by 846
The PerR transcription factor senses H2O2 by metal-catalysed histidine oxidation
Lee, J.-W., & Helmann, J. D. (2006) · Nature · doi:10.1038/nature04537 · Cited by 547
Constantinidou, C., Hobman, J. L., Griffiths, L., Patel, M. D., Penn, C. W., Cole, J. A., & Overton, T. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512312200 · Cited by 280
Enzymes of the l-arginine to nitric oxide pathway
Stuehr, D. J. (2004) · The Journal of Nutrition · doi:10.1093/jn/134.10.2748s · Cited by 218
Cooper, C. E., Patel, R. P., Brookes, P. S., & Darley-Usmar, V. M. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02191-6 · Cited by 180
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Cited by
Barraud, N., Schleheck, D., Klebensberger, J., Webb, J. S., Hassett, D. J., Rice, S. A., & Kjelleberg, S. (2009) · Journal of Bacteriology · doi:10.1128/jb.00975-09 · Cited by 513
Nitrate and periplasmic nitrate reductases
Sparacino-Watkins, C., Stolz, J. F., & Basu, P. (2014) · Chem. Soc. Rev. · doi:10.1039/c3cs60249d · Cited by 426
Shatalin, K., Gusarov, I., Avetissova, E., Shatalina, Y., McQuade, L. E., Lippard, S. J., & Nudler, E. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0710950105 · Cited by 205
Nitric oxide regulation of bacterial biofilms
Arora, D. P., Hossain, S., Xu, Y., & Boon, E. M. (2015) · Biochemistry · doi:10.1021/bi501476n · Cited by 206
Bacterial nitric oxide synthases: what are they good for?
Sudhamsu, J., & Crane, B. R. (2009) · Trends in Microbiology · doi:10.1016/j.tim.2009.02.003 · Cited by 160
Metadata
- Authors
- Spiro, S.
- Venue
- FEMS Microbiology Reviews
- Publisher
- Oxford University Press (OUP)
- Published
- 2007-03
- Volume
- 31
- Issue
- 2
- Pages
- 193-211
- ISSN
- 0168-6445 (ISSN-L)
- 1574-6976
- OpenAlex
- W2065237831
- Cited by
- 207
- References
- 9
- FWCI
- 10.22
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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