Linked Life Data

20682783

Source:http://linkedlifedata.com/resource/pubmed/id/20682783

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
41
pubmed:dateCreated
2010-10-4
pubmed:abstractText
Post-translational modifications have major importance for the structure and function of a multiplicity of proteins. Phosphorylation is a widespread phenomenon among eukaryotic proteins. Whereas O-phosphorylation on the side chains of serine, threonine, and tyrosine in proteins is well known and has been studied extensively, to our knowledge the endogenous phosphorylation of hydroxyproline has not previously been reported. In the present work, we provide evidence for the first time that O-phosphohydroxyproline (Hyp(P)) is a proteinogenic amino acid. To detect Hyp(P) in proteins we generated a Hyp(P)-specific polyclonal antibody. We could identify Hyp(P) in various proteins by Western blot analysis, and we characterized the sequence position of Hyp(P) in the protein ?-crystallin A by electrospray ionization-tandem mass spectrometry. Our experiments clearly demonstrate hydroxylation and subsequent phosphorylation of a proline residue in ?-crystallin A in the eye as well as in heart tissue of rat.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1083-351X
pubmed:author
pubmed:issnType
Electronic
pubmed:day
8
pubmed:volume
285
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
31484-90
pubmed:dateRevised
2011-10-10
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Characterization of O-phosphohydroxyproline in rat {alpha}-crystallin A.
pubmed:affiliation
Biological Medical Research Center, Heinrich-Heine-University of Düsseldorf, Moorenstrasse 5, 40225 Düsseldorf, Germany.
pubmed:publicationType
Journal Article