|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0006556,
umls-concept:C0009015,
umls-concept:C0020792,
umls-concept:C0128818,
umls-concept:C0139903,
umls-concept:C0205250,
umls-concept:C1135183,
umls-concept:C1514562,
umls-concept:C1561491,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
|
|
pubmed:issue |
3
|
|
pubmed:dateCreated |
1994-2-3
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
The full length cDNA of porcine moesin and radixin have been cloned and sequenced. Comparison of the closely related sequences of human, murine and porcine moesin, ezrin and radixin with a protein from Echinococcus multilocularis, an evolutionarily quite distant human parasite, reveals several highly invariant domains in the aminoterminal and carboxyterminal regions. Most of these conserved domains are clustered around tyrosine residues that are putative phosphorylation sites for tyrosine phosphokinases.
|
|
pubmed:grant |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Blood Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ezrin,
http://linkedlifedata.com/resource/pubmed/chemical/moesin,
http://linkedlifedata.com/resource/pubmed/chemical/radixin
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Dec
|
|
pubmed:issn |
0006-3002
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
14
|
|
pubmed:volume |
1216
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
479-82
|
|
pubmed:dateRevised |
2007-11-14
|
|
pubmed:meshHeading |
pubmed-meshheading:8268231-Amino Acid Sequence,
pubmed-meshheading:8268231-Animals,
pubmed-meshheading:8268231-Base Sequence,
pubmed-meshheading:8268231-Blood Proteins,
pubmed-meshheading:8268231-Cloning, Molecular,
pubmed-meshheading:8268231-Conserved Sequence,
pubmed-meshheading:8268231-Cytoskeletal Proteins,
pubmed-meshheading:8268231-DNA, Complementary,
pubmed-meshheading:8268231-Echinococcus,
pubmed-meshheading:8268231-Humans,
pubmed-meshheading:8268231-Membrane Proteins,
pubmed-meshheading:8268231-Mice,
pubmed-meshheading:8268231-Microfilament Proteins,
pubmed-meshheading:8268231-Molecular Sequence Data,
pubmed-meshheading:8268231-Phosphoproteins,
pubmed-meshheading:8268231-Protein Biosynthesis,
pubmed-meshheading:8268231-Proteins,
pubmed-meshheading:8268231-Sequence Homology, Amino Acid,
pubmed-meshheading:8268231-Swine
|
|
pubmed:year |
1993
|
|
pubmed:articleTitle |
Cloning and sequencing of porcine moesin and radixin cDNA and identification of highly conserved domains.
|
|
pubmed:affiliation |
Department of Pathology, Stanford University School of Medicine, CA 94305-5324.
|
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
|
