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Human Interaction Network Ontology
Last uploaded:
June 27, 2014
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Preferred Name | Collagen type VII dimerization | |
Synonyms |
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Definitions |
has a Stoichiometric coefficient of 2 Collagen VII triple-helices form an anti-parallel dimer, associating through disulfide bonds formed in a 60-nm overlap (NC2 domain) of the amino terminal triple helical ends. A portion of this region is proteolytically removed (Morris et al. 1986, Chen et al. 2001) prior to aggregation of dimers into anchoring fibrils (Lundstrum et al. 1986). Edited: Jupe, S, 2012-11-12 Authored: Jupe, S, 2012-04-30 Reviewed: Raleigh, Stewart, 2012-10-08 Reviewed: Ricard-Blum, Sylvie, 2012-11-19 Reviewed: Kalamajski, Sebastian, 2012-10-08 |
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ID |
http://purl.obolibrary.org/obo/HINO_0022361 |
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comment |
has a Stoichiometric coefficient of 2 Collagen VII triple-helices form an anti-parallel dimer, associating through disulfide bonds formed in a 60-nm overlap (NC2 domain) of the amino terminal triple helical ends. A portion of this region is proteolytically removed (Morris et al. 1986, Chen et al. 2001) prior to aggregation of dimers into anchoring fibrils (Lundstrum et al. 1986). Edited: Jupe, S, 2012-11-12 Authored: Jupe, S, 2012-04-30 Reviewed: Raleigh, Stewart, 2012-10-08 Reviewed: Ricard-Blum, Sylvie, 2012-11-19 Reviewed: Kalamajski, Sebastian, 2012-10-08
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definition source |
Pubmed11986329 Reactome, http://www.reactome.org Pubmed11274208 Pubmed3013874 Pubmed3082888
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label |
Collagen type VII dimerization
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prefixIRI |
HINO:0022361
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prefLabel |
Collagen type VII dimerization
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seeAlso |
Reactome Database ID Release 432214324 ReactomeREACT_150302
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subClassOf |
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