Source:http://linkedlifedata.com/resource/pubmed/id/17485091
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
13
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pubmed:dateCreated |
2007-5-25
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pubmed:abstractText |
AlphaI domain integrins have been found in the ascidian Ciona intestinalis. We produced Ciona alpha1I domain as a recombinant protein. It did not recognize fibril-forming collagens or bind to GFOGER or other similar motifs in triple-helical peptides. No GFOGER motifs were found in Ciona collagens. As Ciona alpha1I bound to collagen IX, we propose that before the emergence of GFOGER-dependent collagen receptors in vertebrates, alphaI domain integrins might have been able to bind to collagen with alternative mechanisms.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
581
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2434-40
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pubmed:meshHeading |
pubmed-meshheading:17485091-Amino Acid Sequence,
pubmed-meshheading:17485091-Animals,
pubmed-meshheading:17485091-Ciona intestinalis,
pubmed-meshheading:17485091-Collagen,
pubmed-meshheading:17485091-Conserved Sequence,
pubmed-meshheading:17485091-Evolution, Molecular,
pubmed-meshheading:17485091-Humans,
pubmed-meshheading:17485091-Hydrogen Bonding,
pubmed-meshheading:17485091-Integrins,
pubmed-meshheading:17485091-Models, Molecular,
pubmed-meshheading:17485091-Molecular Sequence Data,
pubmed-meshheading:17485091-Oligopeptides,
pubmed-meshheading:17485091-Protein Conformation,
pubmed-meshheading:17485091-Sequence Alignment
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pubmed:year |
2007
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pubmed:articleTitle |
Analysis of an ascidian integrin provides new insight into early evolution of collagen recognition.
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pubmed:affiliation |
Department of Biochemistry and Food Chemistry, University of Turku, Turku FI-20014, Finland. miratu@utu.fi
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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