Linked Life Data

14632312

Source:http://linkedlifedata.com/resource/pubmed/id/14632312

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-4
pubmed:dateCreated
2003-11-24
pubmed:abstractText
Neurotrophins are essential for the survival and differentiation of neurons in the central and peripheral nervous systems. The binding of neurotrophins to their Trk receptors induces autophosphorylation of tyrosine residues and activation of several signaling components. However, the downstream signaling cascades remain to be fully elucidated. Here we describe molecular cloning of human SH2-B alpha, PH and SH2-domain-containing adaptor protein, as a TrkB binding protein, and how SH2-B alpha associate with the cytoplasmic domain of TrkB at phosphorylated tyrosine residues in the kinase activation loop. There was no distinct inhibitory or inducing effect on kinase activity detected by either a full-length or an SH2 domain of SH2-B alpha in vitro, even though the regulation mechanism of the activation loop on tyrosine kinase activity has been described. In addition to SH2-B alpha, the expression of three SH2-B alternative splice variants, SH2-B beta, gamma and delta, was detected in human cell lines. These splicing variants have unique carboxyl-terminal amino acid sequences due to insertion sequences as well as reading frameshifts.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1078-0297
pubmed:author
pubmed:issnType
Print
pubmed:volume
111
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
27-39
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Association of SH2-B to phosphorylated tyrosine residues in the activation loop of TrkB.
pubmed:affiliation
Novartis Pharma K.K., Tsukuba Research Institute, Tsukuba, Ibaraki 300-2611, Japan. suzukike@kyorin-u.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't