Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6297
pubmed:dateCreated
1990-12-14
pubmed:abstractText
Proteins that bind and hydrolyse GTP are being discovered at a rapidly increasing rate. Each of these many GTPases acts as a molecular switch whose 'on' and 'off' states are triggered by binding and hydrolysis of GTP. Conserved structure and mechanism in myriad versions of the switch--in bacteria, yeast, flies and vertebrates--suggest that all derive from a single primordial protein, repeatedly modified in the course of evolution to perform a dazzling variety of functions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
348
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
125-32
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:2122258-Animals, pubmed-meshheading:2122258-Biological Transport, pubmed-meshheading:2122258-Cysteine, pubmed-meshheading:2122258-Endocytosis, pubmed-meshheading:2122258-Exocytosis, pubmed-meshheading:2122258-GTP Phosphohydrolase-Linked Elongation Factors, pubmed-meshheading:2122258-GTP-Binding Proteins, pubmed-meshheading:2122258-Guanosine Triphosphate, pubmed-meshheading:2122258-Humans, pubmed-meshheading:2122258-Neurofibromatosis 1, pubmed-meshheading:2122258-Peptide Elongation Factors, pubmed-meshheading:2122258-Peptide Initiation Factors, pubmed-meshheading:2122258-Pheromones, pubmed-meshheading:2122258-Protein Processing, Post-Translational, pubmed-meshheading:2122258-Proto-Oncogene Proteins p21(ras), pubmed-meshheading:2122258-Saccharomyces cerevisiae, pubmed-meshheading:2122258-Signal Transduction
pubmed:year
1990
pubmed:articleTitle
The GTPase superfamily: a conserved switch for diverse cell functions.
pubmed:affiliation
Department of Pharmacology, University of California, San Francisco 94143.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't