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Article

Schmid's metaphyseal chondrodysplasia mutations interfere with folding of the C-terminal domain of human collagen X expressed in Escherichia coli.

The Journal of biological chemistry - 2 Jul 1999

Dublet B, Vernet T, van der Rest M

Abstract excerpt

Human collagen X contains a highly conserved 161-amino acid C-terminal non-triple helical domain that is homologous to the C-terminal domain of collagen VIII and to the C1q module of the human C1 enzyme. We have expressed this domain (residues 545-680) in Escherichia coli as a glutathione S-transferase fusion protein. The purified fusion protein trimerizes spontaneously in vitro, and after thrombin cleavage, the...

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Identifiers

PMID: 10383388
DOI: 10.1074/jbc.274.27.18909

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Schmid's metaphyseal chondrodysplasia mutations interfere with folding of the C-terminal domain of human collagen X expressed in Escherichia coli.PMID 10383388Read ↗

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.Semantic proximity Read ↗

Aberrant signal peptide cleavage of collagen X in Schmid metaphyseal chondrodysplasia. Implications for the molecular basis of the disease.Semantic proximity Read ↗

Collagen X Chains Harboring Schmid Metaphyseal Chondrodysplasia NC1 Domain Mutations Are Selectively Retained and Degraded in Stably Transfected CellsSemantic proximity Read ↗

Amino acid substitutions of conserved residues in the carboxyl-terminal domain of the alpha 1(X) chain of type X collagen occur in two unrelated families with metaphyseal chondrodysplasia type Schmid.Semantic proximity Read ↗

Interaction of collagen alpha1(X) containing engineered NC1 mutations with normal alpha1(X) in vitro. Implications for the molecular basis of schmid metaphyseal chondrodysplasia.Semantic proximity Read ↗

Concentration of mutations causing Schmid metaphyseal chondrodysplasia in the C-terminal noncollagenous domain of type X collagen.Semantic proximity Read ↗

Mutations of COL10A1 in Schmid metaphyseal chondrodysplasia.Semantic proximity Read ↗

Mutations in three subdomains of the carboxy-terminal region of collagen type X account for most of the Schmid metaphyseal dysplasias.Semantic proximity Read ↗

Mutations in the N-terminal globular domain of the type X collagen gene (COL10A1) in patients with Schmid metaphyseal chondrodysplasia.Semantic proximity Read ↗

A nonsense mutation in the carboxyl-terminal domain of type X collagen causes haploinsufficiency in schmid metaphyseal chondrodysplasia.Semantic proximity Read ↗

A type X collagen mutation causes Schmid metaphyseal chondrodysplasia.Semantic proximity Read ↗

COL10A1 nonsense and frame-shift mutations have a gain-of-function effect on the growth plate in human and mouse metaphyseal chondrodysplasia type Schmid.Semantic proximity Read ↗

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