Control of heterotypic fibril formation by collagen V is determined by chain stoichiometry. - Wikidata - awgldk - TriplyDB

Control of heterotypic fibril formation by collagen V is determined by chain stoichiometry.

Control of heterotypic fibril formation by collagen V is determined by chain stoichiometry.

http://www.wikidata.org/entity/Q33952845

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The signal peptide of Staphylococcus aureus panton valentine leukocidin LukS component mediates increased adhesion to heparan sulfates Development of a functional skin matrix requires deposition of collagen V heterotrimers Col V siRNA engineered tenocytes for tendon tissue engineering The collagen V homotrimer [alpha1(V)](3) production is unexpectedly favored over the heterotrimer [alpha1(V)](2)alpha2(V) in recombinant expression systems.Characterization of the matrilin coiled-coil domains reveals seven novel isoforms.Biosynthetic processing of the Pro-alpha1(V)Pro-alpha2(V)Pro-alpha3(V) procollagen heterotrimer.Interleukin-17-dependent autoimmunity to collagen type V in atherosclerosis Profile of collagen gene expression in the glenohumeral capsule of patients with traumatic anterior instability of the shoulder Minor fibrillar collagens, variable regions alternative splicing, intrinsic disorder, and tyrosine sulfation Comprehensive mass spectrometric mapping of the hydroxylated amino acid residues of the α1(V) collagen chain.Mucosal Administration of Collagen V Ameliorates the Atherosclerotic Plaque Burden by Inducing Interleukin 35-dependent Tolerance.Bronchiolitis obliterans syndrome: the Achilles' heel of lung transplantation.Humoral immunity and the development of obliterative bronchiolitis after lung transplantation: is there a link?Type V Collagen in Health, Disease, and Fibrosis.Tendon's ultrastructure.Enzymatic cleavage specificity of the proalpha1(V) chain processing analysed by site-directed mutagenesis.Identification of binding partners interacting with the α1-N-propeptide of type V collagen.Scleroderma-like remodeling induced by type V collagen.Structural requirements for heparin/heparan sulfate binding to type V collagen.A comprehensive study of the spatial and temporal expression of the col5a1 gene in mouse embryos: a clue for understanding collagen V function in developing connective tissues.Collagen types I, III, and V constitute the thick collagen fibrils of the mouse decidua.

P2860

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P2860

Control of heterotypic fibril formation by collagen V is determined by chain stoichiometry.

http://www.wikidata.org/entity/Q33952845

description

2001 nî lūn-bûn

@nan

2001 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2001 թվականի հունիսին հրատարակված գիտական հոդված

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2001年の論文

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2001年論文

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2001年論文

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2001年論文

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2001年論文

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2001年論文

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2001年论文

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name

Control of heterotypic fibril ...... rmined by chain stoichiometry.

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Control of heterotypic fibril ...... rmined by chain stoichiometry.

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type

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Control of heterotypic fibril ...... rmined by chain stoichiometry.

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Control of heterotypic fibril ...... rmined by chain stoichiometry.

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prefLabel

Control of heterotypic fibril ...... rmined by chain stoichiometry.

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Control of heterotypic fibril ...... rmined by chain stoichiometry.

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P1433

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P1433

Journal of Biological Chemistry

P1476

Control of heterotypic fibril ...... rmined by chain stoichiometry.

@en

P2093

Bernocco S

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

Chanut-Delalande H

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Fichard A

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Garrone R

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Hulmes DJ

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Ruggiero F

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P2860

The pro-alpha3(V) collagen chain. Complete primary structure, expression domains in adult and developing tissues, and comparison to the structures and expression domains of the other types V and XI procollagen chains

Mutations of the alpha2(V) chain of type V collagen impair matrix assembly and produce ehlers-danlos syndrome type I

Schwann cells synthesize type V collagen that contains a novel alpha 4 chain. Molecular cloning, biochemical characterization, and high affinity heparin binding of alpha 4(V) collagen

Targeted mutation in the col5a2 gene reveals a regulatory role for type V collagen during matrix assembly

Compound heterozygosity for a disease-causing G1489E [corrected] and disease-modifying G530S substitution in COL5A1 of a patient with the classical type of Ehlers-Danlos syndrome: an explanation of intrafamilial variability?

Diversity in the processing events at the N-terminus of type-V collagen.

Another look at collagen V and XI molecules.

Null alleles of the COL5A1 gene of type V collagen are a cause of the classical forms of Ehlers-Danlos syndrome (types I and II).

Collagen type I and type V are present in the same fibril in the avian corneal stroma.

Cartilage contains mixed fibrils of collagen types II, IX, and XI.

P304

24352-24359

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P31

scholarly article

P356

10.1074/JBC.M101182200

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P407

P433

26

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P478

276

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P577

2001-06-01T00:00:00Z

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P698

11423559

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P921