MASP-1 induces a unique cytokine pattern in endothelial cells: a novel link between complement system and neutrophil granulocytes. - Wikidata - wikimedia - TriplyDB

MASP-1 induces a unique cytokine pattern in endothelial cells: a novel link between complement system and neutrophil granulocytes.

MASP-1 induces a unique cytokine pattern in endothelial cells: a novel link between complement system and neutrophil granulocytes.

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Versatility of the complement system in neuroinflammation, neurodegeneration and brain homeostasis CsMAP34, a teleost MAP with dual role: A promoter of MASP-assisted complement activation and a regulator of immune cell activity.Reincarnation of ancient links between coagulation and complement.The emerging roles of mannose-binding lectin-associated serine proteases (MASPs) in the lectin pathway of complement and beyond.Plasma MASP-1 concentration and its relationship to recovery from coronary artery lesion in children with Kawasaki disease.Transcriptome analysis of inflammation-related gene expression in endothelial cells activated by complement MASP-1.Sparking Fire Under the Skin? Answers From the Association of Complement Genes With Pemphigus Foliaceus.AmpliSeq Screening of Genes Encoding the C-Type Lectin Receptors and Their Signaling Components Reveals a Common Variant in MASP1 Associated with Pulmonary Tuberculosis in an Indian Population.The Lectin Pathway of Complement in Myocardial Ischemia/Reperfusion Injury—Review of Its Significance and the Potential Impact of Therapeutic Interference by C1 Esterase Inhibitor.Be on Target: Strategies of Targeting Alternative and Lectin Pathway Components in Complement-Mediated Diseases

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MASP-1 induces a unique cytokine pattern in endothelial cells: a novel link between complement system and neutrophil granulocytes.

http://www.wikidata.org/entity/Q37529606

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 29 January 2014

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

MASP-1 induces a unique cytoki ...... m and neutrophil granulocytes.

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MASP-1 induces a unique cytoki ...... m and neutrophil granulocytes.

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MASP-1 induces a unique cytoki ...... m and neutrophil granulocytes.

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MASP-1 induces a unique cytoki ...... m and neutrophil granulocytes.

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MASP-1 induces a unique cytoki ...... m and neutrophil granulocytes.

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MASP-1 induces a unique cytoki ...... m and neutrophil granulocytes.

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JOURNAL.PONE.0087104

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MASP-1 induces a unique cytoki ...... em and neutrophil granulocytes

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Csaba I Tímár

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Erika Kajdácsi

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József Dobó

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Krisztina Futosi

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Márton Megyeri

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Péter Gál

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Péter K Jani

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Veronika Makó

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Zoltán Doleschall

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Natural substrates and inhibitors of mannan-binding lectin-associated serine protease-1 and -2: a study on recombinant catalytic fragments

Quantitative Characterization of the Activation Steps of Mannan-binding Lectin (MBL)-associated Serine Proteases (MASPs) Points to the Central Role of MASP-1 in the Initiation of the Complement Lectin Pathway

Complement protease MASP-1 activates human endothelial cells: PAR4 activation is a link between complement and endothelial function

Activation of the cAMP pathway synergistically increases IL-1-induced IL-6 gene expression in FRTL-5 thyroid cells: involvement of AP-1 transcription factors

Kinase pathways in chemoattractant-induced degranulation of neutrophils: the role of p38 mitogen-activated protein kinase activated by Src family kinases

Revised mechanism of complement lectin-pathway activation revealing the role of serine protease MASP-1 as the exclusive activator of MASP-2

Vascular endothelial growth factor expression of intercellular adhesion molecule 1 (ICAM-1), vascular cell adhesion molecule 1 (VCAM-1), and E-selectin through nuclear factor-kappa B activation in endothelial cells.

Cleavage of kininogen and subsequent bradykinin release by the complement component: mannose-binding lectin-associated serine protease (MASP)-1

Functional architecture of Weibel-Palade bodies.

A revised model for the secretion of tPA and cytokines from cultured endothelial cells.

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