Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-3-15
pubmed:abstractText
Members of the Rho family of small GTP-binding proteins, such as Rho, Rac and Cdc42, have a role in a wide range of cell responses. These proteins function as molecular switches by virtue of a conformational change between the GTP-bound (active) and GDP-bound (inactive) forms. In addition, most members of the Rho and Rac subfamilies cycle between the cytosol and membrane. The cytosolic guanine nucleotide dissociation inhibitors, RhoGDIs, regulate both the GDP/GTP exchange cycle and the membrane association/dissociation cycle.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0969-2126
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
47-55
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10673424-Amino Acid Sequence, pubmed-meshheading:10673424-Animals, pubmed-meshheading:10673424-Binding Sites, pubmed-meshheading:10673424-Guanine Nucleotide Dissociation Inhibitors, pubmed-meshheading:10673424-Humans, pubmed-meshheading:10673424-Magnetic Resonance Spectroscopy, pubmed-meshheading:10673424-Models, Molecular, pubmed-meshheading:10673424-Molecular Sequence Data, pubmed-meshheading:10673424-Mutagenesis, Site-Directed, pubmed-meshheading:10673424-Protein Binding, pubmed-meshheading:10673424-Protein Conformation, pubmed-meshheading:10673424-Protein Folding, pubmed-meshheading:10673424-Protein Structure, Tertiary, pubmed-meshheading:10673424-Recombinant Proteins, pubmed-meshheading:10673424-Sequence Homology, Amino Acid, pubmed-meshheading:10673424-Thermodynamics, pubmed-meshheading:10673424-rac1 GTP-Binding Protein
pubmed:year
2000
pubmed:articleTitle
Mapping the binding site for the GTP-binding protein Rac-1 on its inhibitor RhoGDI-1.
pubmed:affiliation
Department of Biochemistry and Biological NMR Centre, University of Leicester, Leicester, LE1 7RH, UK. yun@le.ac.uk
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't