The collαgen III fibril has a "flexi-rod" structure of flexible sequences interspersed with rigid bioactive domains including two with hemostatic roles.

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Revealing Accessibility of Cryptic Protein Binding Sites within the Functional Collagen Fibril.Transcriptome analysis of skin fibroblasts with dominant negative COL3A1 mutations provides molecular insights into the etiopathology of vascular Ehlers-Danlos syndrome.

P2860

Q47112384-BCCCB7EE-0F87-4B26-8F80-A38BFA9E3784 Q48217824-01C66254-D968-405D-B649-4EEF4E7558E1

P2860

The collαgen III fibril has a "flexi-rod" structure of flexible sequences interspersed with rigid bioactive domains including two with hemostatic roles.

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http://www.wikidata.org/entity/Q41006430

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2017 nî lūn-bûn

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2017年の論文

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2017年論文

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2017年論文

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2017年論文

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2017年論文

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2017年論文

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2017年论文

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2017年论文

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2017年论文

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The collαgen III fibril has a ...... ing two with hemostatic roles.

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The collαgen III fibril has a ...... ing two with hemostatic roles.

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The collαgen III fibril has a ...... ing two with hemostatic roles.

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P1476

The collαgen III fibril has a ...... ing two with hemostatic roles.

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P2093

Anton V Persikov

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Hayat Dagher

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J Des Parkin

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James D San Antonio

http://www.w3.org/2001/XMLSchema#string

Shane T Jensen

http://www.w3.org/2001/XMLSchema#string

Xavier Jeunemaitre

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P2860

Crystallographic insight into collagen recognition by discoidin domain receptor 2

Aegyptin displays high-affinity for the von Willebrand factor binding site (RGQOGVMGF) in collagen and inhibits carotid thrombus formation in vivo

Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin

A single high-affinity binding site for von Willebrand factor in collagen III, identified using synthetic triple-helical peptides

Type I, II, III, IV, V, and VI collagens serve as extracellular ligands for the isoforms of platelet-derived growth factor (AA, BB, and AB)

Collagens are functional, high affinity ligands for the inhibitory immune receptor LAIR-1

Characterization of binding properties of the myelin-associated glycoprotein to extracellular matrix constituents

Molecular basis for the action of the collagen-specific chaperone Hsp47/SERPINH1 and its structure-specific client recognition

Candidate cell and matrix interaction domains on the collagen fibril, the predominant protein of vertebrates

Crystal structure of human type III collagen Gly991-Gly1032 cystine knot-containing peptide shows both 7/2 and 10/3 triple helical symmetries

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e0175582

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scholarly article

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10.1371/JOURNAL.PONE.0175582

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English

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P478

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Judy Savige

Raymond Dalgleish

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2017-07-13T00:00:00Z

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28704418

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P932

5509119

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The collαgen III fibril has a "flexi-rod" structure of flexible sequences interspersed with rigid bioactive domains including two with hemostatic roles.

about

P2860

P2860

The collαgen III fibril has a "flexi-rod" structure of flexible sequences interspersed with rigid bioactive domains including two with hemostatic roles.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932