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Details on Person The complete primary structure of type XII collagen shows a chimeric molecule with reiterated fibronectin type III motifs, von Willebrand factor A motifs, a domain homologous to a noncollagenous region of type IX collagen, and short collagenous domains with an Arg-Gly-Asp site

Class:IdLiteratureReference:2168011
_displayNameThe complete primary structure of type XII collagen shows a chimeric molecule with reiterated fibronectin type III motifs, von Willebrand factor A motifs, a domain homologous to a noncollagenous region of type IX collagen, and short collagenous domains with an Arg-Gly-Asp site
_timestamp2012-03-23 16:23:45
author[Person:375937] Yamagata, M
[Person:266378] Yamada, Kenneth
[Person:2167969] Yamada, SS
[Person:114010] Shinomura, T
[Person:111776] Tanaka, Hiroshi
[Person:351134] Nishida, Y
[Person:1173236] Obara, M
[Person:1971438] Kimata, K
created[InstanceEdit:2168010] Jupe, S, 2012-03-23
journalJ Cell Biol
pages209-21
pubMedIdentifier1918137
titleThe complete primary structure of type XII collagen shows a chimeric molecule with reiterated fibronectin type III motifs, von Willebrand factor A motifs, a domain homologous to a noncollagenous region of type IX collagen, and short collagenous domains with an Arg-Gly-Asp site
volume115
year1991
(literatureReference)[Summation:2168049] Collagen type XII is a member of the fibril-associated colla...
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No pathways have been reviewed or authored by The complete primary structure of type XII collagen shows a chimeric molecule with reiterated fibronectin type III motifs, von Willebrand factor A motifs, a domain homologous to a noncollagenous region of type IX collagen, and short collagenous domains with an Arg-Gly-Asp site (2168011)