Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-12-17
pubmed:abstractText
The partial amino acid sequence of the sulfolobal thermoprotein biochemically characterized as poly(ADP-ribose)polymerase-like enzyme overlaps those of DING proteins. This group of proteins, widely occurring in animals, plants and eubacteria, shows a characteristic and highly conserved N-terminus, DINGGGATL. The sequence of the N-terminal region and of the analyzed tryptic peptides of the sulfolobal thermozyme shows a high similarity with most of the DING proteins from databases. This is the first example of a DING protein from a sulfolobal source.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1431-6730
pubmed:author
pubmed:issnType
Print
pubmed:volume
390
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
27-30
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
The ADP-ribosylating thermozyme from Sulfolobus solfataricus is a DING protein.
pubmed:affiliation
Department of Life Sciences, Faculty of Sciences M.F.N., Second University of Naples, Via Vivadi 45, I-81100 Caserta, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't