Source:http://linkedlifedata.com/resource/pubmed/id/12766169
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions |
umls-concept:C0009325,
umls-concept:C0015576,
umls-concept:C0017262,
umls-concept:C0033382,
umls-concept:C0042567,
umls-concept:C0185117,
umls-concept:C0205250,
umls-concept:C0205314,
umls-concept:C0443211,
umls-concept:C0449774,
umls-concept:C0679622,
umls-concept:C0969669,
umls-concept:C1521970,
umls-concept:C1521991,
umls-concept:C1710548,
umls-concept:C2003941,
umls-concept:C2700116,
umls-concept:C2911684
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| pubmed:issue |
33
|
| pubmed:dateCreated |
2003-8-11
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| pubmed:databankReference | |
| pubmed:abstractText |
The type XXVII collagen gene codes for a novel vertebrate fibrillar collagen that is highly conserved in man, mouse, and fish (Fugu rubripes). The pro(alpha)1(XXVII) chain has a domain structure similar to that of the type B clade chains (alpha1(V), alpha3(V), alpha1(XI), and alpha2(XI)). However, compared with other vertebrate fibrillar collagens (types I, II, III, V, and XI), type XXVII collagen has unusual molecular features such as no minor helical domain, a major helical domain that is short and interrupted, and a short chain selection sequence within the NC1 domain. Pro(alpha)1(XXVII) mRNA is 9 kb and expressed by chondrocytes but also by a variety of epithelial cell layers in developing tissues including stomach, lung, gonad, skin, cochlear, and tooth. By Western blotting, type XXVII antisera recognized multiple bands of 240-110 kDa in tissue extracts and collagenous bands of 150-140 kDa in the conditioned medium of the differentiating chondrogenic ATDC5 cell line. Phylogenetic analyses revealed that type XXVII, together with the closely related type XXIV collagen gene, form a new, third clade (type C) within the vertebrate fibrillar collagen family. Furthermore, the exon structure of the type XXVII collagen gene is similar to, but distinct from, those of the genes coding for the type A or B clade pro(alpha) chains.
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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 |
Aug
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
15
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| pubmed:volume |
278
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
31067-77
|
| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:12766169-Amino Acid Sequence,
pubmed-meshheading:12766169-Animals,
pubmed-meshheading:12766169-Blotting, Western,
pubmed-meshheading:12766169-Conserved Sequence,
pubmed-meshheading:12766169-Evolution, Molecular,
pubmed-meshheading:12766169-Fibrillar Collagens,
pubmed-meshheading:12766169-Gene Expression Regulation, Developmental,
pubmed-meshheading:12766169-Humans,
pubmed-meshheading:12766169-Mice,
pubmed-meshheading:12766169-Molecular Sequence Data,
pubmed-meshheading:12766169-Phylogeny,
pubmed-meshheading:12766169-Protein Structure, Tertiary,
pubmed-meshheading:12766169-RNA, Messenger,
pubmed-meshheading:12766169-Sequence Analysis, DNA,
pubmed-meshheading:12766169-Takifugu,
pubmed-meshheading:12766169-Vertebrates
|
| pubmed:year |
2003
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| pubmed:articleTitle |
A novel and highly conserved collagen (pro(alpha)1(XXVII)) with a unique expression pattern and unusual molecular characteristics establishes a new clade within the vertebrate fibrillar collagen family.
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| pubmed:affiliation |
Wellcome Trust Centre for Cell-Matrix Research, School of Biological Sciences, University of Manchester, Manchester M13 9PT, United Kingdom. ray.boot-handford@man.ac.uk
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|