Linked Life Data

9856335

Source:http://linkedlifedata.com/resource/pubmed/id/9856335

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1999-3-4
pubmed:abstractText
Ubiquitin (Ub) is a highly conserved small protein present universally in eukaryotic cells, which is covalently attached to substrate proteins by a cascade system, consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. The modification of cellular proteins with Ub targets them for degradation by a large multisubunit protease, called the 26S proteasome. The unexpected existence of many genes encoding E2 and E3 reveals that a number of distinct Ub-ligating pathways operate for selective proteolysis in cells, implying its involvement in divergent biologically important processes. Currently, it becomes clear that a set of novel molecules with a structural similarity to Ub, called Ub-like proteins (Ubls), is present in various eukaryotic cells. They are divided into two subclasses: type-1 Ubls with small sizes, such as SUMO1 and NEDD8, that are ligated to target proteins in a fashion similar, but not identical, to the ubiquitination pathway, and another type-2 Ubls that contain Ub-like structure in a variety of different classes of large proteins having apparently distinct functions, such as Rad23, Elongin B, and Parkin. Ub and type-1 Ubls are central players consisting of a new type of post-translational protein-modifying system, although the significance of type-2 Ubl remains obscure.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1016-8478
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
503-12
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
The ligation systems for ubiquitin and ubiquitin-like proteins.
pubmed:affiliation
The Tokyo Metropolitan Institute of Medical Science, and CREST, Japan, Science and Technology Corporation. tanakak@rinshoken.or.jp
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't