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Details on Person Metaphyseal chondrodysplasia type Schmid mutations are predicted to occur in two distinct three-dimensional clusters within type X collagen NC1 domains that retain the ability to trimerize

Class:IdLiteratureReference:9017618
_displayNameMetaphyseal chondrodysplasia type Schmid mutations are predicted to occur in two distinct three-dimensional clusters within type X collagen NC1 domains that retain the ability to trimerize
_timestamp2017-08-23 11:54:29
author[Person:9017606] Marks, D S
[Person:9017627] Gregory, C A
[Person:9017598] Wallis, G A
[Person:8948285] Brass, A
[Person:9017601] Kadler, K E
[Person:9017613] Boot-Handford, R P
created[InstanceEdit:9017635] Varusai, Thawfeek, 2017-08-23
journalJ. Biol. Chem.
modified[InstanceEdit:9017680] Varusai, Thawfeek, 2017-08-23
pages3632-41
pubMedIdentifier9920912
titleMetaphyseal chondrodysplasia type Schmid mutations are predicted to occur in two distinct three-dimensional clusters within type X collagen NC1 domains that retain the ability to trimerize
volume274
year1999
(literatureReference)[Pathway:9014523] Assembly of abnormal collagen fibrils and other multimeric structures [Homo sapiens]
[Reaction:9017602] Defective procollagen type X [Homo sapiens]
[Reaction:9017620] Formation of defective COL10A1 collagen networks [Homo sapiens]
[Reaction:9017623] Defective procollagen type X bind to form an abnormal procollagen triple helix [Homo sapiens]
[BlackBoxEvent:9017640] Secretion of abnormal COL10A1 collagens [Homo sapiens]
[Reaction:9017722] Defective type X collagen associates with collagen type II fibrils [Homo sapiens]
[Pathway:9018067] Abnormal non-integrin membrane-ECM interactions [Homo sapiens]
[Reaction:9018101] DDR2 binds COL10A1-defective collagen type I, II, III, V, X fibrils [Homo sapiens]
[Pathway:9018204] Abnormal degradation of the extracellular matrix [Homo sapiens]
[Pathway:9018210] Abnormal collagen degradation [Homo sapiens]
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No pathways have been reviewed or authored by Metaphyseal chondrodysplasia type Schmid mutations are predicted to occur in two distinct three-dimensional clusters within type X collagen NC1 domains that retain the ability to trimerize (9017618)