Two mechanisms for mannose-binding protein modulation of the activity of its associated serine proteases
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Activation of mannan-binding lectin-associated serine proteases leads to generation of a fibrin clotA novel mannose-binding lectin/ficolin-associated protein is highly expressed in heart and skeletal muscle tissues and inhibits complement activationPaths reunited: Initiation of the classical and lectin pathways of complement activationQuantitative 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 PathwayMonospecific Inhibitors Show That Both Mannan-binding Lectin-associated Serine Protease-1 (MASP-1) and -2 Are Essential for Lectin Pathway Activation and Reveal Structural Plasticity of MASP-2Engineering novel complement activity into a pulmonary surfactant proteinComplement: a key system for immune surveillance and homeostasisRevised mechanism of complement lectin-pathway activation revealing the role of serine protease MASP-1 as the exclusive activator of MASP-2Discrete MBL-MASP complexes show wide inter-individual variability in concentration: data from UK vs Armenian populations.Simultaneous activation of complement and coagulation by MBL-associated serine protease 2Essential role of mannose-binding lectin-associated serine protease-1 in activation of the complement factor DMannan-binding lectin in cardiovascular disease.Scabies mite inactive serine proteases are potent inhibitors of the human complement lectin pathwayAnalogous interactions in initiating complexes of the classical and lectin pathways of complementTargeting of mannan-binding lectin-associated serine protease-2 confers protection from myocardial and gastrointestinal ischemia/reperfusion injury.Complement activation by ligand-driven juxtaposition of discrete pattern recognition complexes.Complementing the inflammasome.Human mannose-binding lectin inhibitor prevents myocardial injury and arterial thrombogenesis in a novel animal modelHuman L-ficolin (ficolin-2) and its clinical significance.Complement activation, regulation, and molecular basis for complement-related diseasesEndogenous and natural complement inhibitor attenuates myocardial injury and arterial thrombogenesis.Interactions between mannose-binding lectin and MASPs during complement activation by the lectin pathwayPossible disease-modifying factors: the mannan-binding lectin pathway and infections in hereditary angioedema of children and adults.CsMAP34, a teleost MAP with dual role: A promoter of MASP-assisted complement activation and a regulator of immune cell activity.Structural and functional overview of the lectin complement pathway: its molecular basis and physiological implication.Parasitic scabies mites and associated bacteria joining forces against host complement defence.Carbohydrate recognition and complement activation by rat ficolin-B.The emerging roles of mannose-binding lectin-associated serine proteases (MASPs) in the lectin pathway of complement and beyond.Dangerous liaisons: complement, coagulation, and kallikrein/kinin cross-talk act as a linchpin in the events leading to thromboinflammation.The complement factor H-related proteins.Localization and characterization of the mannose-binding lectin (MBL)-associated-serine protease-2 binding site in rat ficolin-A: equivalent binding sites within the collagenous domains of MBLs and ficolinsHeterocomplexes of mannose-binding lectin and the pentraxins PTX3 or serum amyloid P component trigger cross-activation of the complement system.Cardioprotection by an anti-MASP-2 antibody in a murine model of myocardial infarction.Molecular interactions between MASP-2, C4, and C2 and their activation fragments leading to complement activation via the lectin pathway.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.
P2860
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P2860
Two mechanisms for mannose-binding protein modulation of the activity of its associated serine proteases
description
2004 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունիսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2004
@ast
im Juni 2004 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2004/06/18)
@sk
vědecký článek publikovaný v roce 2004
@cs
wetenschappelijk artikel (gepubliceerd op 2004/06/18)
@nl
наукова стаття, опублікована в червні 2004
@uk
name
Two mechanisms for mannose-bin ...... ts associated serine proteases
@ast
Two mechanisms for mannose-bin ...... ts associated serine proteases
@en
Two mechanisms for mannose-bin ...... ts associated serine proteases
@nl
type
label
Two mechanisms for mannose-bin ...... ts associated serine proteases
@ast
Two mechanisms for mannose-bin ...... ts associated serine proteases
@en
Two mechanisms for mannose-bin ...... ts associated serine proteases
@nl
prefLabel
Two mechanisms for mannose-bin ...... ts associated serine proteases
@ast
Two mechanisms for mannose-bin ...... ts associated serine proteases
@en
Two mechanisms for mannose-bin ...... ts associated serine proteases
@nl
P2860
P356
P1476
Two mechanisms for mannose-bin ...... ts associated serine proteases
@en
P2093
Ce-Belle Chen
Russell Wallis
P2860
P304
26058–26065
P356
10.1074/JBC.M401318200
P407
P577
2004-06-18T00:00:00Z