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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6033
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pubmed:dateCreated |
1985-10-22
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X02896,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X02897,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X02898,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X02899,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X02900
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pubmed:abstractText |
Genes encoding types I, II and III collagens (fibrillar collagens) contain many discrete-size exons, most of them 54 base pairs (bp) long, in addition to the 45-, 99-, 108- and 162-bp exons. It has been suggested that these collagen genes evolved from an ancestral coding unit of 54 bp. Type IV collagen is a specific component of basement membranes and contains two genetically distinct polypeptides, the alpha 1(IV) and alpha 2(IV) chains. It differs from the types I-III collagens in that it contains interruptions in the Gly-X-Y repeat sequence and does not form ordered fibrillar structures. We have isolated complementary DNA and genomic clones for the mouse alpha 2(IV) collagen chain and here characterize 64-, 123- and 182-bp exons in the Gly-X-Y coding domain of the gene. The data suggest that the alpha 2(IV) collagen gene may have evolved differently from those encoding the fibrillar collagens.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:issn |
0028-0836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
317
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
177-9
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading | |
pubmed:articleTitle |
Characterization of 64-, 123- and 182-base-pair exons in the mouse alpha 2(IV) collagen gene.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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