Delayed triple helix formation of mutant collagen from patients with osteogenesis imperfecta.
about
Abnormal type I collagen post-translational modification and crosslinking in a cyclophilin B KO mouse model of recessive osteogenesis imperfectaProlyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfectaLack of cyclophilin B in osteogenesis imperfecta with normal collagen foldingGene targeting of mutant COL1A2 alleles in mesenchymal stem cells from individuals with osteogenesis imperfectaProlyl 3-hydroxylase 1 and CRTAP are mutually stabilizing in the endoplasmic reticulum collagen prolyl 3-hydroxylation complexDefective C-propeptides of the proalpha2(I) chain of type I procollagen impede molecular assembly and result in osteogenesis imperfectaExome sequencing identifies truncating mutations in human SERPINF1 in autosomal-recessive osteogenesis imperfectaCollagen structure and stabilityTwo forms of collagen XVII in keratinocytes. A full-length transmembrane protein and a soluble ectodomainVascular Ehlers-Danlos syndrome mutations in type III collagen differently stall the triple helical folding.Defective collagen crosslinking in bone, but not in ligament or cartilage, in Bruck syndrome: indications for a bone-specific telopeptide lysyl hydroxylase on chromosome 17.Some, but not all, glycine substitution mutations in COL7A1 result in intracellular accumulation of collagen VII, loss of anchoring fibrils, and skin blistering.Perinatal lethal osteogenesis imperfecta.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 dysplasiaCompound heterozygosity for a disease-causing G1489E [corrected] and disease-modifying G530S substitution in COL5A1 of a patient with the classical type of Ehlers-Danlos syndrome: an explanation of intrafamilial variability?Unstable molecules form stable tissuesAbnormal mineral-matrix interactions are a significant contributor to fragility in oim/oim boneLocation of glycine mutations within a bacterial collagen protein affects degree of disruption of triple-helix folding and conformation.Pulse-chase analysis of procollagen biosynthesis by azidohomoalanine labeling.A cellular model for the investigation of Fuchs' endothelial corneal dystrophy.Chaperoning osteogenesis: new protein-folding disease paradigms.Osteogenesis imperfecta model peptides: incorporation of residues replacing Gly within a triple helix achieved by renucleation and local flexibilityEngineering D-Amino Acid Containing Collagen Like Peptide at the Cleavage Site of Clostridium histolyticum Collagenase for Its Inhibition.Folding and misfolding of the collagen triple helix: Markov analysis of molecular dynamics simulations.Mapping the Effect of Gly Mutations in Collagen on α2β1 Integrin Binding.A Novel Mutation in a Japanese Family with X-linked Alport Syndrome.High- and low-dose OPG-Fc cause osteopetrosis-like changes in infant mice.New perspectives on osteogenesis imperfectaPharmacological and biological therapeutic strategies for osteogenesis imperfecta.Molecular Outcome, Prediction, and Clinical Consequences of Splice Variants in COL1A1, Which Encodes the proα1(I) Chains of Type I Procollagen.Confirmation of the pathogenicity of a mutation p.G337C in the COL1A2 gene associated with osteogenesis imperfecta.Sequence environment of mutation affects stability and folding in collagen model peptides of osteogenesis imperfecta.Defects of type I procollagen metabolism correlated with decrease of prolidase activity in a case of lethal osteogenesis imperfecta.Transformation of the mechanism of triple-helix peptide folding in the absence of a C-terminal nucleation domain and its implications for mutations in collagen disorders.Structural heterogeneity of type I collagen triple helix and its role in osteogenesis imperfecta.Disrupted collagen architecture in the crystal structure of a triple-helical peptide with a Gly-->Ala substitution.Consequences of Glycine Mutations in the Fibronectin-binding Sequence of Collagen.Collagen metabolism is a novel target of the neuropeptide alpha-melanocyte-stimulating hormone.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
Delayed triple helix formation of mutant collagen from patients with osteogenesis imperfecta.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年学术文章
@wuu
1994年学术文章
@zh-cn
1994年学术文章
@zh-hans
1994年学术文章
@zh-my
1994年学术文章
@zh-sg
1994年學術文章
@yue
1994年學術文章
@zh
1994年學術文章
@zh-hant
name
Delayed triple helix formation ...... with osteogenesis imperfecta.
@en
Delayed triple helix formation ...... with osteogenesis imperfecta.
@nl
type
label
Delayed triple helix formation ...... with osteogenesis imperfecta.
@en
Delayed triple helix formation ...... with osteogenesis imperfecta.
@nl
prefLabel
Delayed triple helix formation ...... with osteogenesis imperfecta.
@en
Delayed triple helix formation ...... with osteogenesis imperfecta.
@nl
P356
P1476
Delayed triple helix formation ...... with osteogenesis imperfecta.
@en
P2093
Bruckner P
Steinmann B
P304
P356
10.1006/JMBI.1994.1199
P407
P577
1994-02-01T00:00:00Z