about
Collagen structure and stabilityCrystal structure of the collagen triple helix model [(Pro-Pro-Gly)(10)](3)Stabilization of the collagen triple helix by O-methylation of hydroxyproline residuesEffect of cysteine 85 on biochemical properties and biological function of human surfactant protein A variantsCollagen VI related muscle disordersA mouse model for dominant collagen VI disorders: heterozygous deletion of Col6a3 Exon 16Peptide tessellation yields micrometre-scale collagen triple helicesRational design of fiber forming supramolecular structuresA 'Collagen Hug' model for Staphylococcus aureus CNA binding to collagenSynthesis of heterotrimeric collagen peptides containing the alpha1beta1 integrin recognition site of collagen type IV.The peptides acetyl-(Gly-3(S)Hyp-4(R)Hyp)10-NH2 and acetyl-(Gly-Pro-3(S)Hyp)10-NH2 do not form a collagen triple helix.4R- and 4S-iodophenyl hydroxyproline, 4R-pentynoyl hydroxyproline, and S-propargyl-4-thiolphenylalanine: conformationally biased and tunable amino acids for bioorthogonal reactions.Expanding the family of collagen proteins: recombinant bacterial collagens of varying composition form triple-helices of similar stability.A novel COL1A1 mutation in infantile cortical hyperostosis (Caffey disease) expands the spectrum of collagen-related disorders.De novo self-assembling collagen heterotrimers using explicit positive and negative design.How sequence defines structure: a crystallographic map of DNA structure and conformation.The contribution of interchain salt bridges to triple-helical stability in collagen.Unstable molecules form stable tissuesA study of degradation of historic parchment using small-angle X-ray scattering, synchrotron-IR and multivariate data analysis.Tunable control of polyproline helix (PPII) structure via aromatic electronic effects: an electronic switch of polyproline helix.Laser tissue welding analyzed using fluorescence, Stokes shift spectroscopy, and Huang-Rhys parameter.The aberrance of the 4S diastereomer of 4-hydroxyproline.Fluorescence determination of tryptophan side-chain accessibility and dynamics in triple-helical collagen-like peptides.Triple helical structure and stabilization of collagen-like molecules with 4(R)-hydroxyproline in the Xaa position.Development of a Förster resonance energy transfer assay for monitoring bacterial collagenase triple-helical peptidase activity.Matrix metalloproteinase inhibition by heterotrimeric triple-helical Peptide transition state analoguesEngineering D-Amino Acid Containing Collagen Like Peptide at the Cleavage Site of Clostridium histolyticum Collagenase for Its Inhibition.Synthetic heterotrimeric collagen peptides as mimics of cell adhesion sites of the basement membrane.Intra-articular injection of a nutritive mixture solution protects articular cartilage from osteoarthritic progression induced by anterior cruciate ligament transection in mature rabbits: a randomized controlled trialThermoresponsive self-assembly of nanostructures from a collagen-like peptide-containing diblock copolymer.A Single Stereodynamic Center Modulates the Rate of Self-Assembly in a Biomolecular System.Triple helical collagen-like peptides: engineering and applications in matrix biology.Prospects and limitations of the rational engineering of fibrillar collagensTriple-helical transition state analogues: a new class of selective matrix metalloproteinase inhibitors.Hydroxyproline-free single composition ABC collagen heterotrimerCollagen-like peptides and peptide-polymer conjugates in the design of assembled materials.The role of cross-chain ionic interactions for the stability of collagen model peptides.R992C (p.R1192C) Substitution in collagen II alters the structure of mutant molecules and induces the unfolded protein response.Synthesis and biological applications of collagen-model triple-helical peptides.Design of nanostructures based on aromatic peptide amphiphiles.
P2860
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P2860
description
2000 nî lūn-bûn
@nan
2000 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Amino acid propensities for the collagen triple-helix.
@ast
Amino acid propensities for the collagen triple-helix.
@en
type
label
Amino acid propensities for the collagen triple-helix.
@ast
Amino acid propensities for the collagen triple-helix.
@en
prefLabel
Amino acid propensities for the collagen triple-helix.
@ast
Amino acid propensities for the collagen triple-helix.
@en
P2093
P356
P1433
P1476
Amino acid propensities for the collagen triple-helix.
@en
P2093
Kirkpatrick A
Persikov AV
Ramshaw JA
P304
14960-14967
P356
10.1021/BI001560D
P407
P577
2000-12-01T00:00:00Z