Recombinant procollagen II: Deletion of D period segments identifies sequences that are required for helix stabilization and generates a temperature-sensitive N-proteinase cleavage site.
about
Matrix metalloproteinase interactions with collagen and elastinUbiquitous amyloidsCollagen XVII is destabilized by a glycine substitution mutation in the cell adhesion domain Col15Bacterial collagen-like proteins that form triple-helical structuresA role for prolyl 3-hydroxylase 2 in post-translational modification of fibril-forming collagensThe functions of the multiproduct and rapidly evolving dec-1 eggshell gene are conserved between evolutionarily distant species of DrosophilaType I collagen is thermally unstable at body temperatureDissecting a bacterial collagen domain from Streptococcus pyogenes: sequence and length-dependent variations in triple helix stability and folding.Structural and mechanical differences between collagen homo- and heterotrimers: relevance for the molecular origin of brittle bone disease.Prospects and limitations of the rational engineering of fibrillar collagensR992C (p.R1192C) Substitution in collagen II alters the structure of mutant molecules and induces the unfolded protein response.The role of collagen charge clusters in the modulation of matrix metalloproteinase activity.Procollagen with skipping of alpha 1(I) exon 41 has lower binding affinity for alpha 1(I) C-telopeptide, impaired in vitro fibrillogenesis, and altered fibril morphology.Bioengineered Collagens.Molecular dynamics simulations of the full triple helical region of collagen type I provide an atomic scale view of the protein's regional heterogeneity.Mapping critical sites in collagen II for rational design of gene-engineered proteins for cell-supporting materials.Structural heterogeneity of type I collagen triple helix and its role in osteogenesis imperfecta.Molecular mechanism of alpha 1(I)-osteogenesis imperfecta/Ehlers-Danlos syndrome: unfolding of an N-anchor domain at the N-terminal end of the type I collagen triple helix.Impact of Arginine to Cysteine Mutations in Collagen II on Protein Secretion and Cell Survival.Thermal (in)stability of type I collagen fibrils.Substrate conformation modulates aggrecanase (ADAMTS-4) affinity and sequence specificity. Suggestion of a common topological specificity for functionally diverse proteases.
P2860
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P2860
Recombinant procollagen II: Deletion of D period segments identifies sequences that are required for helix stabilization and generates a temperature-sensitive N-proteinase cleavage site.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh-hant
name
Recombinant procollagen II: De ...... ve N-proteinase cleavage site.
@en
Recombinant procollagen II: De ...... ve N-proteinase cleavage site.
@nl
type
label
Recombinant procollagen II: De ...... ve N-proteinase cleavage site.
@en
Recombinant procollagen II: De ...... ve N-proteinase cleavage site.
@nl
prefLabel
Recombinant procollagen II: De ...... ve N-proteinase cleavage site.
@en
Recombinant procollagen II: De ...... ve N-proteinase cleavage site.
@nl
P2093
P2860
P356
P1476
Recombinant procollagen II: De ...... ive N-proteinase cleavage site
@en
P2093
D J Prockop
D Mechling
H P Bächinger
W V Arnold
P2860
P304
31822-31828
P356
10.1074/JBC.273.48.31822
P407
P577
1998-11-01T00:00:00Z