Linked Life Data

18000527

Source:http://linkedlifedata.com/resource/pubmed/id/18000527

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2007-11-26
pubmed:abstractText
A decade has passed since SUMO (small ubiquitin-related modifier) was discovered to be a reversible post-translational protein modifier. During this time many enzymes that participate in regulated SUMO-conjugation and -deconjugation pathways have been identified and characterized. In parallel, the search for SUMO substrates has produced a long list of targets, which appear to be involved in most cellular functions. Sumoylation is a highly dynamic process and its outcomes are extremely diverse, ranging from changes in localization to altered activity and, in some cases, stability of the modified protein. At first glance, these effects have nothing in common; however, it seems that they all result from changes in the molecular interactions of the sumoylated proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1471-0080
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
947-56
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Concepts in sumoylation: a decade on.
pubmed:affiliation
Department of Biochemie I, Faculty of Medicine, University of Goettingen, Humboldt Allee 23, 37073 Goettingen, Germany.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't