Linked Life Data

18596417

Source:http://linkedlifedata.com/resource/pubmed/id/18596417

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2008-9-22
pubmed:abstractText
Histidine triad (HIT) proteins represent a small family of nucleotide-binding and -hydrolyzing proteins, which attracted the attention of cancer biologists because their expression is lost in multiple human malignancies. To some of the family members including Fhit, Hint1 and Hint2, a tumor suppressive activity was assigned. Although highly similar in structure, their mode of action appears to be different as they are not able to compensate each other's function. Surprisingly, in any reported assay system the enzymatic activity of the histidine triad proteins was not required for their tumor suppressor function. Until recently, little was known about the molecular mechanisms mediating the tumor suppressor activities of histidine triad proteins. The identification of new interaction partners started to shed light on the signaling pathways modulated by the HIT proteins. Here, we summarize these findings with special emphasis on the histidine triad proteins Hint1 and Fhit and their repressive activity on the beta-catenin signaling function.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1551-4005
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1326-31
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Beta-catenin takes a HIT.
pubmed:affiliation
Department of Laboratory Medicine and Pathobiochemistry, Campus Benjamin Franklyn, Charité-Universitätsmedizin Berlin, Berlin, Germany. otmar.huber@charite.de
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't