Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5618
pubmed:dateCreated
2003-4-18
pubmed:abstractText
The sequencing of complete genomes provides a list that includes the proteins responsible for cellular regulation. However, this does not immediately reveal what these proteins do, nor how they are assembled into the molecular machines and functional networks that control cellular behavior. The regulation of many different cellular processes requires the use of protein interaction domains to direct the association of polypeptides with one another and with phospholipids, small molecules, or nucleic acids. The modular nature of these domains, and the flexibility of their binding properties, have likely facilitated the evolution of cellular pathways. Conversely, aberrant interactions can induce abnormal cellular behavior and disease. The fundamental properties of protein interaction domains are discussed in this review and in detailed reviews on individual domains at Science's STKE at http://www.sciencemag.org/cgi/content/full/300/5618/445/DC1.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1095-9203
pubmed:author
pubmed:issnType
Electronic
pubmed:day
18
pubmed:volume
300
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
445-52
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:12702867-Amino Acid Motifs, pubmed-meshheading:12702867-Animals, pubmed-meshheading:12702867-Binding Sites, pubmed-meshheading:12702867-Catalytic Domain, pubmed-meshheading:12702867-Cell Physiological Phenomena, pubmed-meshheading:12702867-Cell Polarity, pubmed-meshheading:12702867-Enzymes, pubmed-meshheading:12702867-Evolution, Molecular, pubmed-meshheading:12702867-Kinetics, pubmed-meshheading:12702867-Protein Binding, pubmed-meshheading:12702867-Protein Processing, Post-Translational, pubmed-meshheading:12702867-Protein Structure, Secondary, pubmed-meshheading:12702867-Protein Structure, Tertiary, pubmed-meshheading:12702867-Protein Transport, pubmed-meshheading:12702867-Proteins, pubmed-meshheading:12702867-Proteomics, pubmed-meshheading:12702867-Receptors, Cell Surface, pubmed-meshheading:12702867-Repetitive Sequences, Amino Acid, pubmed-meshheading:12702867-Signal Transduction
pubmed:year
2003
pubmed:articleTitle
Assembly of cell regulatory systems through protein interaction domains.
pubmed:affiliation
Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Avenue, Toronto, Ontario M5G 1X5, Canada. pawson@mshri.on.ca
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't