Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2003-1-15
pubmed:abstractText
Disabled-1 (Dab1) is an intracellular adaptor protein that regulates migrations of various classes of neurons during mammalian brain development. Dab1 function depends on its tyrosine phosphorylation, which is stimulated by Reelin, an extracellular signaling molecule. Reelin increases the stoichiometry of Dab1 phosphorylation and downregulates Dab1 protein levels. Reelin binds to various cell surface receptors, including two members of the low-density lipoprotein receptor family that also bind to Dab1. Mutations in Dab1, its phosphorylation sites, Reelin, or the Reelin receptors cause a common phenotype. However, the molecular mechanism whereby Reelin regulates Dab1 tyrosine phosphorylation is poorly understood.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules, Neuronal, http://linkedlifedata.com/resource/pubmed/chemical/Dab1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Extracellular Matrix Proteins, http://linkedlifedata.com/resource/pubmed/chemical/FYN protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Fyn protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-abl, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-fyn, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-yes, http://linkedlifedata.com/resource/pubmed/chemical/Seminal Plasma Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine, http://linkedlifedata.com/resource/pubmed/chemical/YES1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/reelin protein, http://linkedlifedata.com/resource/pubmed/chemical/src-Family Kinases
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0960-9822
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9-17
pubmed:dateRevised
2010-3-23
pubmed:meshHeading
pubmed-meshheading:12526739-Animals, pubmed-meshheading:12526739-Brain, pubmed-meshheading:12526739-Cell Adhesion Molecules, Neuronal, pubmed-meshheading:12526739-Cells, Cultured, pubmed-meshheading:12526739-Enzyme Inhibitors, pubmed-meshheading:12526739-Extracellular Matrix Proteins, pubmed-meshheading:12526739-Gene Expression Regulation, Developmental, pubmed-meshheading:12526739-Humans, pubmed-meshheading:12526739-Mice, pubmed-meshheading:12526739-Mice, Mutant Strains, pubmed-meshheading:12526739-Nerve Tissue Proteins, pubmed-meshheading:12526739-Neurons, pubmed-meshheading:12526739-Phosphoproteins, pubmed-meshheading:12526739-Phosphorylation, pubmed-meshheading:12526739-Protein-Tyrosine Kinases, pubmed-meshheading:12526739-Proto-Oncogene Proteins, pubmed-meshheading:12526739-Proto-Oncogene Proteins c-abl, pubmed-meshheading:12526739-Proto-Oncogene Proteins c-fyn, pubmed-meshheading:12526739-Proto-Oncogene Proteins c-yes, pubmed-meshheading:12526739-Seminal Plasma Proteins, pubmed-meshheading:12526739-Serine Endopeptidases, pubmed-meshheading:12526739-Signal Transduction, pubmed-meshheading:12526739-Tyrosine, pubmed-meshheading:12526739-src-Family Kinases
pubmed:year
2003
pubmed:articleTitle
Fyn tyrosine kinase is a critical regulator of disabled-1 during brain development.
pubmed:affiliation
Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, 98109, Seattle, WA, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't