Linked Life Data

15691593

Source:http://linkedlifedata.com/resource/pubmed/id/15691593

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2005-2-4
pubmed:abstractText
Specific post-translational modifications resulting from the reaction of nitric oxide or nitric oxide-derived reactive nitrogen species with selective proteins may explain the pleiotropic effects of this molecule in biological systems. Three specific reactions, binding to metal centers, nitrosation of nucleophilic centers and nitration of aromatic residues constitute a major component of the biological reactivity of nitric oxide. We postulate that the chemical reactivity of nitric oxide within biological systems allows this simple diatomic molecule to operate as an integrator of physiological homeostasis and potentially under not completely understood circumstances as a mediator of pathological phenotypes. This chapter reviews the chemistry, putative biological functions and significance of the principal nitric oxide-mediated proteins modifications.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0300-483X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
208
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
299-303
pubmed:dateRevised
2005-11-16
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Pathophysiological functions of nitric oxide-mediated protein modifications.
pubmed:affiliation
Stokes Research Institute, Children's Hospital of Philadelphia, University of Pennsylvania, Abramson Research Center, Rm. 416, 34th Street, Civic Center Building, Philadelphia, PA 19104, USA. ischirop@mail.med.upenn.edu
pubmed:publicationType
Journal Article, Review