Linked Life Data

11733036

Source:http://linkedlifedata.com/resource/pubmed/id/11733036

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2001-12-4
pubmed:abstractText
ERA (Escherichia coli Ras-like protein) is an E. coli GTP binding protein that is essential for proliferation. A DNA database search suggests that homologous sequences with ERA exist in various organisms including human, mouse, Drosophila, Caenorhabditis elegans and Antirrhinum majus. However, the physiological function of eukaryotic ERA-like proteins is not known.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1356-9597
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
987-1001
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11733036-Amino Acid Sequence, pubmed-meshheading:11733036-Animals, pubmed-meshheading:11733036-Apoptosis, pubmed-meshheading:11733036-Base Sequence, pubmed-meshheading:11733036-Blotting, Northern, pubmed-meshheading:11733036-DNA Primers, pubmed-meshheading:11733036-Escherichia coli, pubmed-meshheading:11733036-Escherichia coli Proteins, pubmed-meshheading:11733036-Fluorescent Antibody Technique, pubmed-meshheading:11733036-GTP-Binding Proteins, pubmed-meshheading:11733036-HeLa Cells, pubmed-meshheading:11733036-Humans, pubmed-meshheading:11733036-In Situ Nick-End Labeling, pubmed-meshheading:11733036-Molecular Sequence Data, pubmed-meshheading:11733036-Mutation, pubmed-meshheading:11733036-Protein Processing, Post-Translational, pubmed-meshheading:11733036-Proto-Oncogene Proteins c-bcl-2, pubmed-meshheading:11733036-RNA-Binding Proteins, pubmed-meshheading:11733036-Recombinant Proteins, pubmed-meshheading:11733036-Sequence Homology, Amino Acid, pubmed-meshheading:11733036-bcl-X Protein
pubmed:year
2001
pubmed:articleTitle
Mammalian homologue of E. coli Ras-like GTPase (ERA) is a possible apoptosis regulator with RNA binding activity.
pubmed:affiliation
Department of Applied Chemistry, Faculty of Science and Technology, Keio University, Hiyoshi, Kohoku-ku, Yokohama 223-8522, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't