The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Biological significance of nitric oxide-mediated protein modifications
Abstract
Nitric oxide (NO), despite an apparently simple diatomic structure, has a wide variety of functions in both physiology and pathology and within every major organ system. It has become an increasingly important scientific challenge to decipher how this wide range of activity is achieved. To this end a number of investigators have begun to explore how NO-mediated posttranslational modifications of proteins may represent mechanisms of cellular signaling. These modifications include: 1) binding to metal centers; 2) nitrosylation of thiol and amine groups; 3) nitration of tyrosine, tryptophan, amine, carboxylic acid, and phenylalanine groups; and 4) oxidation of thiols (both cysteine and methionine residues) and tyrosine. However, two particular modifications have recently received much attention, nitrosylation of thiols to produce S-nitrosothiol and nitration of tyrosine residues to produce nitrotyrosine. It is the purpose of this review to examine the possibility that these modifications may play a role in NO-mediated signaling.
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Cites
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“When NO binds to the ferrous state of the heme group [oxidation of the heme iron to the ferric state results in enzyme inactivation and heme loss (39)], it severs the bond between the heme iron and the histidine residue via an axial dislocation of the iron.”
BackgroundStamler (2001) · doi:10.1016/s0092-8674(01)00495-0 · Cited by 1,261
Nitric oxide circulates in mammalian plasma primarily as an S-nitroso adduct of serum albumin.
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A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans
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Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide.
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Self-citationProteomic method identifies proteins nitrated in vivo during inflammatory challenge
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Eosinophil peroxidase nitrates protein tyrosyl residues
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Cited by
Nitric Oxide and Peroxynitrite in Health and Disease
Pacher, P., Beckman, J. S., & Liaudet, L. (2007) · Physiological Reviews · doi:10.1152/physrev.00029.2006 · Cited by 6,390
Strategies to increase nitric oxide signalling in cardiovascular disease
Lundberg, J. O., Gladwin, M. T., & Weitzberg, E. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4623 · Cited by 576
Nitration of Tyrosine 10 Critically Enhances Amyloid β Aggregation and Plaque Formation
Kummer, M. P., Hermes, M., Delekarte, A., Hammerschmidt, T., Kumar, S., Terwel, D., Walter, J., Pape, H.-C., König, S., Roeber, S., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.07.001 · Cited by 336
Macrophages and Inflammatory Mediators in Chemical Toxicity: A Battle of Forces
Laskin, D. L. (2009) · Chemical Research in Toxicology · doi:10.1021/tx900086v · Cited by 287
S-Nitrosothiols: cellular formation and transport
Zhang, Y., & Hogg, N. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.12.016 · Cited by 257
Metadata
- Authors
- Gow, A. J., Farkouh, C. R., Munson, D. A., Posencheg, M. A., & Ischiropoulos, H.
- Venue
- American Journal of Physiology-Lung Cellular and Molecular Physiology
- Publisher
- American Physiological Society
- Published
- 2004-08
- Volume
- 287
- Issue
- 2
- Pages
- L262-L268
- ISSN
- 1040-0605 (ISSN-L)
- 1522-1504
- OpenAlex
- W2131474149
- Cited by
- 385
- References
- 10
- FWCI
- 17.86
- Type
- journal article
- Language
- en
- Open access
- closed
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