Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1997-2-27
pubmed:abstractText
The tyrosine and dual-specificity phosphatases are involved in signaling, cell growth and differentiation, and the cell cycle. The enzymes share a common catalytic mechanism mediated by an active site cysteine, arginine and aspartic acid. Supplementary domains assist in targeting and substrate specificity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/CDC14 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/CDKN3 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase Inhibitor..., http://linkedlifedata.com/resource/pubmed/chemical/Dual-Specificity Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine, http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases..., http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine, http://linkedlifedata.com/resource/pubmed/chemical/cdc25 Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/dual specificity phosphatase 12, http://linkedlifedata.com/resource/pubmed/chemical/myotubularin
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0968-0004
pubmed:author
pubmed:issnType
Print
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
413-7
pubmed:dateRevised
2008-10-29
pubmed:meshHeading
pubmed-meshheading:8987394-Amino Acid Sequence, pubmed-meshheading:8987394-Animals, pubmed-meshheading:8987394-Binding Sites, pubmed-meshheading:8987394-Cell Cycle Proteins, pubmed-meshheading:8987394-Conserved Sequence, pubmed-meshheading:8987394-Cyanobacteria, pubmed-meshheading:8987394-Cyclin-Dependent Kinase Inhibitor Proteins, pubmed-meshheading:8987394-Dual-Specificity Phosphatases, pubmed-meshheading:8987394-Humans, pubmed-meshheading:8987394-Hydrolysis, pubmed-meshheading:8987394-Models, Molecular, pubmed-meshheading:8987394-Molecular Sequence Data, pubmed-meshheading:8987394-Molecular Weight, pubmed-meshheading:8987394-Phosphoprotein Phosphatases, pubmed-meshheading:8987394-Phosphorylation, pubmed-meshheading:8987394-Phosphotyrosine, pubmed-meshheading:8987394-Protein Conformation, pubmed-meshheading:8987394-Protein Tyrosine Phosphatases, pubmed-meshheading:8987394-Protein Tyrosine Phosphatases, Non-Receptor, pubmed-meshheading:8987394-Rhodobacter, pubmed-meshheading:8987394-Saccharomyces cerevisiae Proteins, pubmed-meshheading:8987394-Salmonella, pubmed-meshheading:8987394-Substrate Specificity, pubmed-meshheading:8987394-Tyrosine, pubmed-meshheading:8987394-cdc25 Phosphatases
pubmed:year
1996
pubmed:articleTitle
Structure and function of the protein tyrosine phosphatases.
pubmed:affiliation
Biophysics Research Division, University of Michigan, Ann Arbor 48109-1055, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't