Associated Papers
The p.W651fsX666 mutation on COL10A1 results in impaired trimerization of normal collagen X to induce Schmid type Metaphyseal chondrodysplasia.
Yang J et al.
Human Molecular Genetics, 2025
Collagen misfolding mutations: the contribution of the unfolded protein response to the molecular pathology.
Bateman JF et al.
Connective Tissue Research, 2022
A detailed understanding of the COL10A1 and SOX9 genes interaction based on potentially damaging mutations in gastric cancer using computational techniques.
Aktas SH et al.
Journal of Biomolecular Structure & Dynamics, 2022
Characterization of a novel COL10A1 variant associated with Schmid-type metaphyseal chondrodysplasia and a literature review.
Wu H et al.
Molecular Genetics & Genomic Medicine, 2021
Systematic analysis of the intersection of disease mutations with protein modifications.
Simpson CM et al.
Bmc Medical Genomics, 2019
Endoplasmic reticulum stress in chondrodysplasias caused by mutations in collagen types II and X.
Gawron K
Cell Stress & Chaperones, 2016
Mutations of COL10A1 in Schmid metaphyseal chondrodysplasia.
Bateman JF et al.
Human Mutation, 2005
Misfolding of collagen X chains harboring Schmid metaphyseal chondrodysplasia mutations results in aberrant disulfide bond formation, intracellular retention, and activation of the unfolded protein response.
Wilson R et al.
The Journal of Biological Chemistry, 2005
Identification of four novel COL10A1 missense mutations in schmid metaphyseal chondrodysplasia: further evidence that collagen X NC1 mutations impair trimer assembly.
Bateman JF et al.
Human Mutation, 2004
Collagen X chains harboring Schmid metaphyseal chondrodysplasia NC1 domain mutations are selectively retained and degraded in stably transfected cells.
Wilson R et al.
The Journal of Biological Chemistry, 2002
Insight into Schmid metaphyseal chondrodysplasia from the crystal structure of the collagen X NC1 domain trimer.
Bogin O et al.
Structure (london, England : 1993), 2002
Folding and assembly of type X collagen mutants that cause metaphyseal chondrodysplasia-type schmid. Evidence for co-assembly of the mutant and wild-type chains and binding to molecular chaperones.
McLaughlin SH et al.
The Journal of Biological Chemistry, 1999
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.
Marks DS et al.
The Journal of Biological Chemistry, 1999
Novel missense mutation resulting in the substitution of tyrosine by cysteine at codon 597 of the type X collagen gene associated with Schmid metaphyseal chondrodysplasia.
Sawai H et al.
Journal of Human Genetics, 1998
Site-directed mutagenesis of human type X collagen. Expression of alpha1(X) NC1, NC2, and helical mutations in vitro and in transfected cells.
Chan D et al.
The Journal of Biological Chemistry, 1996
Mutations within the gene encoding the alpha 1 (X) chain of type X collagen (COL10A1) cause metaphyseal chondrodysplasia type Schmid but not several other forms of metaphyseal chondrodysplasia.
Wallis GA et al.
Journal of Medical Genetics, 1996