Folding of peptide models of collagen and misfolding in disease.
about
Proteomics approaches for the studies of bone metabolismSoft-tissue characters in higher primate phylogeneticsHow reliable are human phylogenetic hypotheses?Dynamic Water-Mediated Hydrogen Bonding in a Collagen Model Peptide.Conformational features of a natural break in the type IV collagen Gly-X-Y repeat.Collagen triple-helix formation in all-trans chains proceeds by a nucleation/growth mechanism with a purely entropic barrier.Fluorescence determination of tryptophan side-chain accessibility and dynamics in triple-helical collagen-like peptides.Location of glycine mutations within a bacterial collagen protein affects degree of disruption of triple-helix folding and conformation.A cellular model for the investigation of Fuchs' endothelial corneal dystrophy.Chiral imaging of collagen by second-harmonic generation circular dichroism.Designed coiled coils promote folding of a recombinant bacterial collagenOsteogenesis imperfecta model peptides: incorporation of residues replacing Gly within a triple helix achieved by renucleation and local flexibilityDestabilization of osteogenesis imperfecta collagen-like model peptides correlates with the identity of the residue replacing glycineThe role of collagen in thrombosis and hemostasis.NMR studies demonstrate a unique AAB composition and chain register for a heterotrimeric type IV collagen model peptide containing a natural interruption site.Folding and misfolding of the collagen triple helix: Markov analysis of molecular dynamics simulations.The physics of the interactions governing folding and association of proteins.Aggregation of granulocyte-colony stimulating factor in vitro involves a conformationally altered monomeric state.The interdigitated beta-helix domain of the P22 tailspike protein acts as a molecular clamp in trimer stabilizationActivin A suppresses osteoblast mineralization capacity by altering extracellular matrix (ECM) composition and impairing matrix vesicle (MV) production.NMR conformational and dynamic consequences of a gly to ser substitution in an osteogenesis imperfecta collagen model peptide.Synthesis and biological applications of collagen-model triple-helical peptides.The effect of purity upon the triple-helical stability of collagenous peptides.Matrix metalloproteinase collagenolysis in health and disease.Sequence dependence of kinetics and morphology of collagen model peptide self-assembly into higher order structures.Comparison of liquid chromatography-isotope ratio mass spectrometry (LC/IRMS) and gas chromatography-combustion-isotope ratio mass spectrometry (GC/C/IRMS) for the determination of collagen amino acid δ13C values for palaeodietary and palaeoecologicProtein misfolding diseases: prospects of pharmacological treatment.A comprehensive in silico analysis of non-synonymous and regulatory SNPs of human MBL2 gene.CD and NMR investigation of collagen peptides mimicking a pathological Gly-Ser mutation and a natural interruption in a similar highly charged sequence context.On-the-resin N-terminal modification of long synthetic peptides.Equilibrium thermal transitions of collagen model peptides.Analysis of the kinetics of folding of proteins and peptides using circular dichroism.Structural biology: Modelling collagen diseases.NMR monitoring of chain-specific stability in heterotrimeric collagen peptides.FTIR studies of collagen model peptides: complementary experimental and simulation approaches to conformation and unfolding.Free energy simulation to investigate the effect of amino acid sequence environment on the severity of osteogenesis imperfecta by glycine mutations in collagen.A peptide from the adenovirus fiber shaft forms amyloid-type fibrils.Localization of the serine protease-binding sites in the collagen-like domain of mannose-binding protein: indirect effects of naturally occurring mutations on protease binding and activation.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.Biomechanical comparison of xenogeneic bone material treated with different methods.
P2860
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P2860
Folding of peptide models of collagen and misfolding in disease.
description
1999 nî lūn-bûn
@nan
1999 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
name
Folding of peptide models of collagen and misfolding in disease.
@ast
Folding of peptide models of collagen and misfolding in disease.
@en
Folding of peptide models of collagen and misfolding in disease.
@nl
type
label
Folding of peptide models of collagen and misfolding in disease.
@ast
Folding of peptide models of collagen and misfolding in disease.
@en
Folding of peptide models of collagen and misfolding in disease.
@nl
prefLabel
Folding of peptide models of collagen and misfolding in disease.
@ast
Folding of peptide models of collagen and misfolding in disease.
@en
Folding of peptide models of collagen and misfolding in disease.
@nl
P1476
Folding of peptide models of collagen and misfolding in disease.
@en
P2093
P304
P356
10.1016/S0959-440X(99)80016-5
P577
1999-02-01T00:00:00Z