Linked Life Data

10368301

Source:http://linkedlifedata.com/resource/pubmed/id/10368301

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1999-5-6
pubmed:databankReference
pubmed:abstractText
Angiogenesis is involved in tumor growth, macular degeneration, retinopathy and other diseases. Vascular endothelial growth factor (VEGF) stimulates angiogenesis by binding to specific receptors (VEGFRs) on the surface of vascular endothelial cells. VEGFRs are receptor tyrosine kinases that, like the platelet-derived growth factor receptors (PDGFRs), contain a large insert within the kinase domain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0969-2126
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
319-30
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:10368301-Adenosine Triphosphate, pubmed-meshheading:10368301-Amino Acid Sequence, pubmed-meshheading:10368301-Binding Sites, pubmed-meshheading:10368301-Catalytic Domain, pubmed-meshheading:10368301-Crystallography, X-Ray, pubmed-meshheading:10368301-Growth Substances, pubmed-meshheading:10368301-Humans, pubmed-meshheading:10368301-Kinetics, pubmed-meshheading:10368301-Models, Molecular, pubmed-meshheading:10368301-Molecular Sequence Data, pubmed-meshheading:10368301-Multigene Family, pubmed-meshheading:10368301-Mutagenesis, Site-Directed, pubmed-meshheading:10368301-Neovascularization, Physiologic, pubmed-meshheading:10368301-Peptide Fragments, pubmed-meshheading:10368301-Protein Conformation, pubmed-meshheading:10368301-Protein Folding, pubmed-meshheading:10368301-Protein Structure, Secondary, pubmed-meshheading:10368301-Protein-Tyrosine Kinases, pubmed-meshheading:10368301-Receptor Protein-Tyrosine Kinases, pubmed-meshheading:10368301-Receptors, Growth Factor, pubmed-meshheading:10368301-Receptors, Vascular Endothelial Growth Factor, pubmed-meshheading:10368301-Recombinant Fusion Proteins, pubmed-meshheading:10368301-Sequence Alignment, pubmed-meshheading:10368301-Sequence Homology, Amino Acid, pubmed-meshheading:10368301-Structure-Activity Relationship, pubmed-meshheading:10368301-Substrate Specificity
pubmed:year
1999
pubmed:articleTitle
Crystal structure of the kinase domain of human vascular endothelial growth factor receptor 2: a key enzyme in angiogenesis.
pubmed:affiliation
Agouron Pharmaceuticals, 3565 General Atomics Court, San Diego, CA 92121, USA. mctigue@agouron.com
pubmed:publicationType
Journal Article, Comparative Study