Structural heterogeneity of type I collagen triple helix and its role in osteogenesis imperfecta. - Wikidata - wikimedia - TriplyDB

Structural heterogeneity of type I collagen triple helix and its role in osteogenesis imperfecta.

Structural heterogeneity of type I collagen triple helix and its role in osteogenesis imperfecta.

http://www.wikidata.org/entity/Q46855555

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Abnormal type I collagen post-translational modification and crosslinking in a cyclophilin B KO mouse model of recessive osteogenesis imperfecta Candidate cell and matrix interaction domains on the collagen fibril, the predominant protein of vertebrates Matrix metalloproteinase interactions with collagen and elastin Genetic Defects in TAPT1 Disrupt Ciliogenesis and Cause a Complex Lethal Osteochondrodysplasia Understanding of the viscoelastic response of the human corneal stroma induced by riboflavin/UV-a cross-linking at the nano level.Recombinant collagen studies link the severe conformational changes induced by osteogenesis imperfecta mutations to the disruption of a set of interchain salt bridges.Actinidain-hydrolyzed type I collagen reveals a crucial amino acid sequence in fibril formation.Direct visualization of protease action on collagen triple helical structure.Carcinomas contain a matrix metalloproteinase-resistant isoform of type I collagen exerting selective support to invasion Molecular mechanism of type I collagen homotrimer resistance to mammalian collagenases.Location of glycine mutations within a bacterial collagen protein affects degree of disruption of triple-helix folding and conformation.Chaperoning osteogenesis: new protein-folding disease paradigms.Effects of ultraviolet-A and riboflavin on the interaction of collagen and proteoglycans during corneal cross-linking.COL1 C-propeptide cleavage site mutations cause high bone mass osteogenesis imperfecta.Osteogenesis imperfecta model peptides: incorporation of residues replacing Gly within a triple helix achieved by renucleation and local flexibility Variation in the helical structure of native collagen.Effects of gamma irradiation on collagen damage and remodeling.Structural and mechanical differences between collagen homo- and heterotrimers: relevance for the molecular origin of brittle bone disease.Osteogenesis imperfecta missense mutations in collagen: structural consequences of a glycine to alanine replacement at a highly charged site.Absence of FKBP10 in recessive type XI osteogenesis imperfecta leads to diminished collagen cross-linking and reduced collagen deposition in extracellular matrix.Collagen degradation by tumor-associated trypsins.Local amino acid sequence patterns dominate the heterogeneous phenotype for the collagen connective tissue disease Osteogenesis Imperfecta resulting from Gly mutations Absence of the ER Cation Channel TMEM38B/TRIC-B Disrupts Intracellular Calcium Homeostasis and Dysregulates Collagen Synthesis in Recessive Osteogenesis Imperfecta.Kuskokwim syndrome, a recessive congenital contracture disorder, extends the phenotype of FKBP10 mutations.NMR conformational and dynamic consequences of a gly to ser substitution in an osteogenesis imperfecta collagen model peptide.Osteogenesis imperfecta: recent findings shed new light on this once well-understood condition.Aortic dissection in osteogenesis imperfecta: case report and review of the literature.Mapping and Exploring the Collagen-I Proteostasis Network.The chaperone activity of 4PBA ameliorates the skeletal phenotype of Chihuahua, a zebrafish model for dominant osteogenesis imperfecta.Osteogenesis imperfecta presenting as aneurysmal subarachnoid haemorrhage in a 53-year-old man.Dominant-negative effects of COL7A1 mutations can be rescued by controlled overexpression of normal collagen VII.A validated software application to measure fiber organization in soft tissue.Molecular dynamics simulations of the full triple helical region of collagen type I provide an atomic scale view of the protein's regional heterogeneity.Osteoblast Malfunction Caused by Cell Stress Response to Procollagen Misfolding in α2(I)-G610C Mouse Model of Osteogenesis Imperfecta.Structural biology: Modelling collagen diseases.Sequence environment of mutation affects stability and folding in collagen model peptides of osteogenesis imperfecta.NMR monitoring of chain-specific stability in heterotrimeric collagen peptides.P4HA1 mutations cause a unique congenital disorder of connective tissue involving tendon, bone, muscle and the eye.4-PBA ameliorates cellular homeostasis in fibroblasts from osteogenesis imperfecta patients by enhancing autophagy and stimulating protein secretion.Consequences of Glycine Mutations in the Fibronectin-binding Sequence of Collagen.

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P2860

Structural heterogeneity of type I collagen triple helix and its role in osteogenesis imperfecta.

http://www.wikidata.org/entity/Q46855555

description

2007 nî lūn-bûn

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2007年の論文

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2007年学术文章

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Structural heterogeneity of ty ...... le in osteogenesis imperfecta.

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Structural heterogeneity of ty ...... le in osteogenesis imperfecta.

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Structural heterogeneity of ty ...... le in osteogenesis imperfecta.

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Structural heterogeneity of ty ...... le in osteogenesis imperfecta.

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Structural heterogeneity of ty ...... le in osteogenesis imperfecta.

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Structural heterogeneity of ty ...... le in osteogenesis imperfecta.

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Journal of Biological Chemistry

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Structural heterogeneity of ty ...... ole in osteogenesis imperfecta

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P2093

Angela M DeRidder

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Daniel J McBride

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Edward L Mertz

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Elena Makareeva

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Joan C Marini

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Mary B Sutter

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Natalia V Kuznetsova

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Wayne A Cabral

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P2860

Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta

Microfibrillar structure of type I collagen in situ

Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution

Osteogenesis imperfecta: prospects for molecular therapeutics

The zipper-like folding of collagen triple helices and the effects of mutations that disrupt the zipper

New analysis of the phylogenetic change of collagen thermostability

Use of the Cre/lox recombination system to develop a non-lethal knock-in murine model for osteogenesis imperfecta with an alpha1(I) G349C substitution. Variability in phenotype in BrtlIV mice

Selective retention and degradation of molecules with a single mutant alpha1(I) chain in the Brtl IV mouse model of OI

Hydrogen exchange and structural dynamics of proteins and nucleic acids

Differential expression of both extracellular and intracellular proteins is involved in the lethal or nonlethal phenotypic variation of BrtlIV, a murine model for osteogenesis imperfecta.

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4787-4798

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10.1074/JBC.M705773200

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8

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283

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Aileen M Barnes

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2007-12-11T00:00:00Z

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18073209

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P921

osteogenesis imperfecta