Triple helical collagen-like peptides: engineering and applications in matrix biology. - Test2 - elhamkhani - TriplyDB

Triple helical collagen-like peptides: engineering and applications in matrix biology.

Triple helical collagen-like peptides: engineering and applications in matrix biology.

http://www.wikidata.org/entity/Q36251441

about

Production of self-assembling biomaterials for tissue engineering Temperature-dependent higher order structures of the (Pro-Pro-Gly)₁₀-modified dendrimer.Spatio-temporal modification of collagen scaffolds mediated by triple helical propensity.Biological matrices and bionanotechnology.Synthesis and biological applications of collagen-model triple-helical peptides.Design of stimuli-responsive dendrimers.Determining the Substrate Specificity of Matrix Metalloproteases using Fluorogenic Peptide Substrates.The synthesis and coupling of photoreactive collagen-based peptides to restore integrin reactivity to an inert substrate, chemically-crosslinked collagen The Yersinia adhesin YadA binds to a collagenous triple-helical conformation but without sequence specificity.Stabilization of collagen-model, triple-helical peptides for in vitro and in vivo applications.Structural heterogeneity of type I collagen triple helix and its role in osteogenesis imperfecta.Thermodynamic and kinetic consequences of substituting glycine at different positions in a Pro-Hyp-Gly repeat collagen model peptide.Design of Stimuli-Responsive Dendrimers for Biomedical Purposes

P2860

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P2860

Triple helical collagen-like peptides: engineering and applications in matrix biology.

http://www.wikidata.org/entity/Q36251441

description

2005 nî lūn-bûn

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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2005年论文

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2005年论文

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name

Triple helical collagen-like peptides: engineering and applications in matrix biology.

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Triple helical collagen-like peptides: engineering and applications in matrix biology.

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Triple helical collagen-like peptides: engineering and applications in matrix biology.

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Triple helical collagen-like peptides: engineering and applications in matrix biology.

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Triple helical collagen-like peptides: engineering and applications in matrix biology.

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Triple helical collagen-like peptides: engineering and applications in matrix biology.

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P1433

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03008200591008518

P1433

Connective Tissue Research

P1476

Triple helical collagen-like peptides: engineering and applications in matrix biology.

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P2093

Takaki Koide

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P2860

Structural basis of collagen recognition by integrin alpha2beta1

Hydrolysis of triple-helical collagen peptide models by matrix metalloproteinases

Sweet is stable: glycosylation stabilizes collagen.

Synthesis of heterotrimeric collagen peptides containing the alpha1beta1 integrin recognition site of collagen type IV.

Xaa-Arg-Gly triplets in the collagen triple helix are dominant binding sites for the molecular chaperone HSP47.

Role of carbohydrate in stabilizing the triple-helix in a model for a deep-sea hydrothermal vent worm collagen.

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.

Multiple binding sites in collagen type I for the integrins alpha1beta1 and alpha2beta1.

Hydroxylation-induced stabilization of the collagen triple helix. Acetyl-(glycyl-4(R)-hydroxyprolyl-4(R)-hydroxyprolyl)(10)-NH(2) forms a highly stable triple helix.

Amino acid propensities for the collagen triple-helix.

P304

131-141

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scholarly article

P356

10.1080/03008200591008518

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P433

3

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P478

46

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P577

2005-01-01T00:00:00Z

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P698

16147856

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