Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2003-2-20
pubmed:abstractText
Growth factors and their receptor tyrosine kinases play pivotal roles in development, normal physiology, and pathology. Signal transduction is regulated primarily by receptor endocytosis and degradation in lysosomes ("receptor downregulation"). c-Cbl is an adaptor that modulates this process by recruiting binding partners, such as ubiquitin-conjugating enzymes. The role of another group of adaptors, Sprouty proteins, is less understood; although, studies in insects implicated the founder protein in the negative regulation of several receptor tyrosine kinases.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/CBL protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Epidermal Growth Factor, http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-cbl, http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Epidermal Growth Factor, http://linkedlifedata.com/resource/pubmed/chemical/Spry2 protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine, http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin, http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0960-9822
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
297-307
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:12593795-Animals, pubmed-meshheading:12593795-Cell Line, pubmed-meshheading:12593795-Cricetinae, pubmed-meshheading:12593795-Cysteine Endopeptidases, pubmed-meshheading:12593795-Epidermal Growth Factor, pubmed-meshheading:12593795-Feedback, pubmed-meshheading:12593795-Humans, pubmed-meshheading:12593795-Hydrolysis, pubmed-meshheading:12593795-Multienzyme Complexes, pubmed-meshheading:12593795-Nerve Tissue Proteins, pubmed-meshheading:12593795-Proteasome Endopeptidase Complex, pubmed-meshheading:12593795-Proto-Oncogene Proteins, pubmed-meshheading:12593795-Proto-Oncogene Proteins c-cbl, pubmed-meshheading:12593795-Receptor, Epidermal Growth Factor, pubmed-meshheading:12593795-Signal Transduction, pubmed-meshheading:12593795-Tyrosine, pubmed-meshheading:12593795-Ubiquitin, pubmed-meshheading:12593795-Ubiquitin-Protein Ligases
pubmed:year
2003
pubmed:articleTitle
Sprouty fine-tunes EGF signaling through interlinked positive and negative feedback loops.
pubmed:affiliation
Department of Biological Regulation, The Weizmann Institute of Science, Rehovot 76100, Israel.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't