rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
1
|
pubmed:dateCreated |
1992-12-30
|
pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D10715,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D12944,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D12945,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D12946,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D12947,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D12948,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D12949,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D12950,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D12951,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X58826,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X67120
|
pubmed:abstractText |
Using a subtraction cloning approach we had previously isolated a series of murine cDNA clones representing the genes predominantly expressed in the embryonic brain and down-regulated during development. We now report that one of these cDNA clones encodes a novel type of GTP-binding protein. The predicted protein of 40.5 kD, named DRG, contains five structural motifs characteristic of the GTP-binding proteins. Consistently, bacterially expressed and cellular DRG proteins are capable of binding GTP in vitro. Sequences closely related to the DRG protein are found in other species including Drosophila and Halobacterium. Based on these observations, we propose that DRG represents an evolutionarily conserved novel class of GTP-binding protein which may play an important role in cell physiology.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Nov
|
pubmed:issn |
0006-291X
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
30
|
pubmed:volume |
189
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
363-70
|
pubmed:dateRevised |
2010-11-18
|
pubmed:meshHeading |
pubmed-meshheading:1449490-Aging,
pubmed-meshheading:1449490-Amino Acid Sequence,
pubmed-meshheading:1449490-Animals,
pubmed-meshheading:1449490-Base Sequence,
pubmed-meshheading:1449490-Brain,
pubmed-meshheading:1449490-Carrier Proteins,
pubmed-meshheading:1449490-Clone Cells,
pubmed-meshheading:1449490-Embryo, Mammalian,
pubmed-meshheading:1449490-GTP-Binding Proteins,
pubmed-meshheading:1449490-Gene Expression Regulation,
pubmed-meshheading:1449490-Gene Library,
pubmed-meshheading:1449490-Glutathione Transferase,
pubmed-meshheading:1449490-Maltose,
pubmed-meshheading:1449490-Maltose-Binding Proteins,
pubmed-meshheading:1449490-Mice,
pubmed-meshheading:1449490-Molecular Sequence Data,
pubmed-meshheading:1449490-Molecular Weight,
pubmed-meshheading:1449490-Neurons,
pubmed-meshheading:1449490-Open Reading Frames,
pubmed-meshheading:1449490-RNA, Messenger,
pubmed-meshheading:1449490-Recombinant Fusion Proteins,
pubmed-meshheading:1449490-Sequence Homology, Amino Acid
|
pubmed:year |
1992
|
pubmed:articleTitle |
DRG: a novel developmentally regulated GTP-binding protein.
|
pubmed:affiliation |
Laboratory of Molecular Oncology, RIKEN, Tsukuba Life Science Center, Ibaraki, Japan.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|