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.
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Abnormal type I collagen post-translational modification and crosslinking in a cyclophilin B KO mouse model of recessive osteogenesis imperfectaLack of cyclophilin B in osteogenesis imperfecta with normal collagen foldingDevelopmental regulation of FKBP65. An ER-localized extracellular matrix binding-proteinStructurally abnormal type II collagen in a severe form of Kniest dysplasia caused by an exon 24 skipping mutationVascular Ehlers-Danlos syndrome mutations in type III collagen differently stall the triple helical folding.Recombinant collagen studies link the severe conformational changes induced by osteogenesis imperfecta mutations to the disruption of a set of interchain salt bridges.Perinatal lethal osteogenesis imperfecta.Unstable molecules form stable tissuesConsortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans.Abnormal mineral-matrix interactions are a significant contributor to fragility in oim/oim boneAn additional function of the rough endoplasmic reticulum protein complex prolyl 3-hydroxylase 1·cartilage-associated protein·cyclophilin B: the CXXXC motif reveals disulfide isomerase activity in vitro.Location of glycine mutations within a bacterial collagen protein affects degree of disruption of triple-helix folding and conformation.Mutations in PPIB (cyclophilin B) delay type I procollagen chain association and result in perinatal lethal to moderate osteogenesis imperfecta phenotypes.The rough endoplasmic reticulum-resident FK506-binding protein FKBP65 is a molecular chaperone that interacts with collagens.Destabilization of osteogenesis imperfecta collagen-like model peptides correlates with the identity of the residue replacing glycineThe [corrected] SEC23-SEC31 [corrected] interface plays critical role for export of procollagen from the endoplasmic reticulumSum frequency vibrational spectroscopy: the molecular origins of the optical second-order nonlinearity of collagenIdentification of tropoelastin as a ligand for the 65-kD FK506-binding protein, FKBP65, in the secretory pathway.Characterization of alpha1(IV) collagen mutations in Caenorhabditis elegans and the effects of alpha1 and alpha2(IV) mutations on type IV collagen distribution.Disentangling mechanisms involved in collagen pyridinoline cross-linking: The immunophilin FKBP65 is critical for dimerization of lysyl hydroxylase 2Mapping the Effect of Gly Mutations in Collagen on α2β1 Integrin Binding.Mutations in the alpha 2(IV) basement membrane collagen gene of Caenorhabditis elegans produce phenotypes of differing severities.Mechanisms for exporting large-sized cargoes from the endoplasmic reticulum.Molecular dynamics simulations of the full triple helical region of collagen type I provide an atomic scale view of the protein's regional heterogeneity.Osteogenesis imperfecta: from phenotype to genotype and back again.Hsp47 and cyclophilin B traverse the endoplasmic reticulum with procollagen into pre-Golgi intermediate vesicles. A role for Hsp47 and cyclophilin B in the export of procollagen from the endoplasmic reticulum.A substrate preference for the rough endoplasmic reticulum resident protein FKBP22 during collagen biosynthesis.Mutation in cyclophilin B that causes hyperelastosis cutis in American Quarter Horse does not affect peptidylprolyl cis-trans isomerase activity but shows altered cyclophilin B-protein interactions and affects collagen foldingChicken FK506-binding protein, FKBP65, a member of the FKBP family of peptidylprolyl cis-trans isomerases, is only partially inhibited by FK506.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.Free energy simulation to investigate the effect of amino acid sequence environment on the severity of osteogenesis imperfecta by glycine mutations in collagen.A concerted mechanism for the suppression of a folding defect through interactions with chaperones.Prediction of collagen stability from amino acid sequence.Stickler-like syndrome due to a dominant negative mutation in the COL2A1 gene.Structural heterogeneity of type I collagen triple helix and its role in osteogenesis imperfecta.A thermodynamic analysis of the contribution of hydroxyproline to the structural stability of the collagen triple helix.Effects of glycosylated (2S,4R)-hydroxyproline on the stability and assembly of collagen triple helices.Thermodynamic and kinetic consequences of substituting glycine at different positions in a Pro-Hyp-Gly repeat collagen model peptide.
P2860
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P2860
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.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh
1993年學術文章
@zh-hant
name
Thermal stability and folding ...... iple helix of type I collagen.
@en
type
label
Thermal stability and folding ...... iple helix of type I collagen.
@en
prefLabel
Thermal stability and folding ...... iple helix of type I collagen.
@en
P2093
P2860
P356
P1476
Thermal stability and folding ...... iple helix of type I collagen.
@en
P2093
P2860
P304
P356
10.1002/AJMG.1320450204
P577
1993-01-01T00:00:00Z