Linked Life Data

16202152

Source:http://linkedlifedata.com/resource/pubmed/id/16202152

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2005-10-27
pubmed:abstractText
ADP-ribosylation is an enzyme-catalyzed posttranslational protein modification in which mono(ADP-ribosyl)transferases (mARTs) and poly(ADP-ribosyl)transferases (pARTs) transfer the ADP-ribose moiety from NAD onto specific amino acid side chains and/or ADP-ribose units on target proteins.
pubmed:commentsCorrections
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pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1471-2164
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
139
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:16202152-Humans, pubmed-meshheading:16202152-Animals, pubmed-meshheading:16202152-Mice, pubmed-meshheading:16202152-Rats, pubmed-meshheading:16202152-Species Specificity, pubmed-meshheading:16202152-Ribose, pubmed-meshheading:16202152-Models, Molecular, pubmed-meshheading:16202152-Protein Conformation, pubmed-meshheading:16202152-Amino Acid Sequence, pubmed-meshheading:16202152-Tissue Distribution, pubmed-meshheading:16202152-Models, Genetic, pubmed-meshheading:16202152-Molecular Sequence Data, pubmed-meshheading:16202152-Adenosine Diphosphate, pubmed-meshheading:16202152-Phylogeny, pubmed-meshheading:16202152-Protein Structure, Tertiary, pubmed-meshheading:16202152-Sequence Homology, Amino Acid, pubmed-meshheading:16202152-Catalytic Domain, pubmed-meshheading:16202152-Poly(ADP-ribose) Polymerases, pubmed-meshheading:16202152-Introns, pubmed-meshheading:16202152-Ubiquitin, pubmed-meshheading:16202152-Computational Biology, pubmed-meshheading:16202152-Databases, Genetic
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