Short leucine-rich glycoproteins of the extracellular matrix display diverse patterns of complement interaction and activation. - Wikidata - awgldk - TriplyDB

Short leucine-rich glycoproteins of the extracellular matrix display diverse patterns of complement interaction and activation.

Short leucine-rich glycoproteins of the extracellular matrix display diverse patterns of complement interaction and activation.

http://www.wikidata.org/entity/Q37382867

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Annexin-II, DNA, and histones serve as factor H ligands on the surface of apoptotic cells Biological interplay between proteoglycans and their innate immune receptors in inflammation Pre-Osteoarthritis: Definition and Diagnosis of an Elusive Clinical Entity Factor H autoantibodies and deletion of Complement Factor H-Related protein-1 in rheumatic diseases in comparison to atypical hemolytic uremic syndrome Extracellular matrix molecules: potential targets in pharmacotherapy.Low-grade inflammation as a key mediator of the pathogenesis of osteoarthritis.Human pentraxin 3 binds to the complement regulator c4b-binding protein.Genes involved in systemic and arterial bed dependent atherosclerosis--Tampere Vascular study The different roles of aggrecan interaction domains Novel scabies mite serpins inhibit the three pathways of the human complement system.The C-type lectin of the aggrecan G3 domain activates complement.The lectin pathway of complement and rheumatic heart disease.NC4 Domain of cartilage-specific collagen IX inhibits complement directly due to attenuation of membrane attack formation and indirectly through binding and enhancing activity of complement inhibitors C4B-binding protein and factor H.Crystals, inflammation, and osteoarthritis.The role of complement in tumor growth Novel insights into the function and dynamics of extracellular matrix in liver fibrosis.PRELP protein inhibits the formation of the complement membrane attack complex.Small leucine-rich proteoglycans orchestrate receptor crosstalk during inflammation.The role of synovitis in osteoarthritis pathogenesis Regulation of complement by cartilage oligomeric matrix protein allows for a novel molecular diagnostic principle in rheumatoid arthritis Serum COMP-C3b complexes in rheumatic diseases and relation to anti-TNF-α treatment.The proteoglycan biglycan enhances antigen-specific T cell activation potentially via MyD88 and TRIF pathways and triggers autoimmune perimyocarditis The small leucine-rich repeat proteoglycans in tissue repair and atherosclerosis Inflammation in joint injury and post-traumatic osteoarthritis Extracellular matrix lumican promotes bacterial phagocytosis, and Lum-/- mice show increased Pseudomonas aeruginosa lung infection severity.Biglycan: a multivalent proteoglycan providing structure and signals Extracellular matrix remodeling: the common denominator in connective tissue diseases. Possibilities for evaluation and current understanding of the matrix as more than a passive architecture, but a key player in tissue failure.Role of inflammation in the pathogenesis of osteoarthritis: latest findings and interpretations The complement system is activated in synovial fluid from subjects with knee injury and from patients with osteoarthritis.Fell-Muir Lecture: Proteoglycans and more--from molecules to biology.Innate immunity and rheumatoid arthritis.Complement and non-complement activating functions of C1q: a prototypical innate immune molecule.Factor h: a complement regulator in health and disease, and a mediator of cellular interactions.The complement system as a potential therapeutic target in rheumatic disease.Recent advances in the understanding of molecular mechanisms of cartilage degeneration, synovitis and subchondral bone changes in osteoarthritis.Small leucine-rich repeat proteoglycans in corneal inflammation and wound healing.Complement in removal of the dead - balancing inflammation.Complement factor H in host defense and immune evasion.MicroRNA regulation of extracellular matrix components in the process of atherosclerotic plaque destabilization.Serglycin inhibits the classical and lectin pathways of complement via its glycosaminoglycan chains: implications for multiple myeloma.

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P2860

Short leucine-rich glycoproteins of the extracellular matrix display diverse patterns of complement interaction and activation.

http://www.wikidata.org/entity/Q37382867

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 29 October 2008

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Short leucine-rich glycoprotei ...... nt interaction and activation.

@en

Short leucine-rich glycoprotei ...... nt interaction and activation.

@nl

type

label

Short leucine-rich glycoprotei ...... nt interaction and activation.

@en

Short leucine-rich glycoprotei ...... nt interaction and activation.

@nl

prefLabel

Short leucine-rich glycoprotei ...... nt interaction and activation.

@en

Short leucine-rich glycoprotei ...... nt interaction and activation.

@nl

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J.MOLIMM.2008.09.018

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Molecular Immunology

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Short leucine-rich glycoprotei ...... nt interaction and activation.

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Andreas P Sjöberg

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

Dick Heinegård

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

Gavin A Manderson

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

Matthias Mörgelin

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

P2860

Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta

The human lumican gene. Organization, chromosomal location, and expression in articular cartilage

A common haplotype in the complement regulatory gene factor H (HF1/CFH) predisposes individuals to age-related macular degeneration

Synthesis of classical pathway complement components by chondrocytes

Complement factor H polymorphism in age-related macular degeneration

Fibronectin binds to the C1q component of complement

Bone matrix proteins: isolation and characterization of a novel cell-binding keratan sulfate proteoglycan (osteoadherin) from bovine bone

The proteoglycan decorin binds C1q and inhibits the activity of the C1 complex

Complement. First of two parts

Complement. Second of two parts

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830-839

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scholarly article

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10.1016/J.MOLIMM.2008.09.018

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5

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46

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2008-10-29T00:00:00Z

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23430538

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P698

18962898

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P921

extracellular matrix

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2760063

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