Structurally abnormal type II collagen in a severe form of Kniest dysplasia caused by an exon 24 skipping mutation - Wikidata - awgldk - TriplyDB

Structurally abnormal type II collagen in a severe form of Kniest dysplasia caused by an exon 24 skipping mutation

Structurally abnormal type II collagen in a severe form of Kniest dysplasia caused by an exon 24 skipping mutation

http://www.wikidata.org/entity/Q28262263

about

Report of five novel and one recurrent COL2A1 mutations with analysis of genotype-phenotype correlation in patients with a lethal type II collagen disorder Maturation of collagen Ketoimine cross-links by an alternative mechanism to pyridinoline formation in cartilage.New molecular mechanism for Ullrich congenital muscular dystrophy: a heterozygous in-frame deletion in the COL6A1 gene causes a severe phenotype.Infrared assessment of bone quality: a review New insights into the assembly of extracellular microfibrils from the analysis of the fibrillin 1 mutation in the tight skin mouse.Ophthalmic and molecular genetic findings in Kniest dysplasia.Procollagen with skipping of alpha 1(I) exon 41 has lower binding affinity for alpha 1(I) C-telopeptide, impaired in vitro fibrillogenesis, and altered fibril morphology.Mutation Update for COL2A1 Gene Variants Associated with Type II Collagenopathies.Tracheomalacia in a neonate with kniest dysplasia: histopathologic and ultrastructural features.Mutation-based growth charts for SEDC and other COL2A1 related dysplasias.Impact of Arginine to Cysteine Mutations in Collagen II on Protein Secretion and Cell Survival.A study of the clinical and radiological features in a cohort of 93 patients with aCOL2A1mutation causing spondyloepiphyseal dysplasia congenita or a related phenotype Deletions and duplications of Gly-Xaa-Yaa triplet repeats in the triple helical domains of type I collagen chains disrupt helix formation and result in several types of osteogenesis imperfecta

P2860

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P2860

Structurally abnormal type II collagen in a severe form of Kniest dysplasia caused by an exon 24 skipping mutation

http://www.wikidata.org/entity/Q28262263

description

1998 nî lūn-bûn

@nan

1998 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

1998 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

1998年の論文

@ja

1998年論文

@yue

1998年論文

@zh-hant

1998年論文

@zh-hk

1998年論文

@zh-mo

1998年論文

@zh-tw

1998年论文

@wuu

name

Structurally abnormal type II ...... y an exon 24 skipping mutation

@ast

Structurally abnormal type II ...... y an exon 24 skipping mutation

@en

Structurally abnormal type II ...... y an exon 24 skipping mutation

@nl

type

label

Structurally abnormal type II ...... y an exon 24 skipping mutation

@ast

Structurally abnormal type II ...... y an exon 24 skipping mutation

@en

Structurally abnormal type II ...... y an exon 24 skipping mutation

@nl

prefLabel

Structurally abnormal type II ...... y an exon 24 skipping mutation

@ast

Structurally abnormal type II ...... y an exon 24 skipping mutation

@en

Structurally abnormal type II ...... y an exon 24 skipping mutation

@nl

P1433

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P2860

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P1433

Journal of Biological Chemistry

P1476

Structurally abnormal type II ...... y an exon 24 skipping mutation

@en

P2093

D H Cohn

http://www.w3.org/2001/XMLSchema#string

D J Wilkin

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D L Rimoin

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D R Eyre

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H J Kim

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M A Weis

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R S Lachman

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W R Wilcox

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P2860

Collagen type IX from human cartilage: a structural profile of intermolecular cross-linking sites

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

The deletion of six amino acids at the C-terminus of the alpha 1 (II) chain causes overmodification of type II and type XI collagen: further evidence for the association between small deletions in COL2A1 and Kniest dysplasia

Genetic variation at five trimeric and tetrameric tandem repeat loci in four human population groups.

Kniest dysplasia is characterized by an apparent abnormal processing of the C-propeptide of type II cartilage collagen resulting in imperfect fibril assembly

Thermal stability and folding of the collagen triple helix and the effects of mutations in osteogenesis imperfecta on the triple helix of type I collagen.

Assembly in vitro of thin and thick fibrils of collagen II from recombinant procollagen II. The monomers in the tips of thick fibrils have the opposite orientation from monomers in the growing tips of collagen I fibrils.

Identification of the molecular defect in a family with spondyloepiphyseal dysplasia.

The distribution of different molecular species of collagen in fibrous, elastic and hyaline cartilages of the pig.

A single amino acid substitution (G103D) in the type II collagen triple helix produces Kniest dysplasia.

P304

4761-8

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scholarly article

P356

10.1074/JBC.273.8.4761

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P407

P433

8

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P478

273

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P577

1998-02-20T00:00:00Z

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P5875

13761428

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P698

9468540

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