Substrate specificities of recombinant mannan-binding lectin-associated serine proteases-1 and -2
about
Factors of the lectin pathway of complement activation and their clinical associations in neonatesMASP1 mutations in patients with facial, umbilical, coccygeal, and auditory findings of Carnevale, Malpuech, OSA, and Michels syndromesPaths reunited: Initiation of the classical and lectin pathways of complement activationMembrane attack by complement: the assembly and biology of terminal complement complexesCrystal structure of the CUB1-EGF-CUB2 region of mannose-binding protein associated serine protease-2The X-ray Crystal Structure of Mannose-binding Lectin-associated Serine Proteinase-3 Reveals the Structural Basis for Enzyme Inactivity Associated with the Carnevale, Mingarelli, Malpuech, and Michels (3MC) SyndromeThe Serine Protease Domain of MASP-3: Enzymatic Properties and Crystal Structure in Complex with EcotinMurine serine proteases MASP-1 and MASP-3, components of the lectin pathway activation complex of complement, are encoded by a single structural geneTwo mechanisms for mannose-binding protein modulation of the activity of its associated serine proteasesThe lectin-complement pathway--its role in innate immunity and evolutionThe lectin pathway of complement activation is a critical component of the innate immune response to pneumococcal infectionRevised mechanism of complement lectin-pathway activation revealing the role of serine protease MASP-1 as the exclusive activator of MASP-2Simultaneous 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.Targeting 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.The X-ray structure of human mannan-binding lectin-associated protein 19 (MAp19) and its interaction site with mannan-binding lectin and L-ficolin.Deficiency in mannose-binding lectin-associated serine protease-2 does not increase susceptibility to Trypanosoma cruzi infectionComplement activation and cardiac surgery: a novel target for improving outcomes.Complement activation, regulation, and molecular basis for complement-related diseasesInteractions between mannose-binding lectin and MASPs during complement activation by the lectin pathwayMolecular structure and expression of anthropic, ovine, and murine forms of complement receptor type 2.Mannan binding lectin-associated serine protease-2 (MASP-2) critically contributes to post-ischemic brain injury independent of MASP-1Possible disease-modifying factors: the mannan-binding lectin pathway and infections in hereditary angioedema of children and adults.Stringent regulation of complement lectin pathway C3/C5 convertase by C4b-binding protein (C4BP).The structure, genetic polymorphisms, expression and biological functions of complement receptor type 1 (CR1/CD35).The complement system in ischemia-reperfusion injuriesMannan-binding lectin activates C3 and the alternative complement pathway without involvement of C2.The emerging roles of mannose-binding lectin-associated serine proteases (MASPs) in the lectin pathway of complement and beyond.Low MBL-associated serine protease 2 (MASP-2) levels correlate with urogenital schistosomiasis in Nigerian children.Mechanisms of mannose-binding lectin-associated serine proteases-1/3 activation of the alternative pathway of complement.Polyphosphate is a novel cofactor for regulation of complement by a serpin, C1 inhibitor.Targeting mechanisms at sites of complement activation for imaging and therapy.Localization of the serine protease-binding sites in the collagen-like domain of mannose-binding protein: indirect effects of naturally occurring mutations on protease binding and activation.Functional characterization of complement proteases C1s/mannan-binding lectin-associated serine protease-2 (MASP-2) chimeras reveals the higher C4 recognition efficacy of the MASP-2 complement control protein modules.L-ficolin binding and lectin pathway activation by acetylated low-density lipoprotein.Investigations on the pattern recognition molecule M-ficolin: quantitative aspects of bacterial binding and leukocyte association.C1 inhibitor function using contact-phase proteases as target: evaluation of an innovative assay.Molecular interactions between MASP-2, C4, and C2 and their activation fragments leading to complement activation via the lectin pathway.
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P248
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P2860
Substrate specificities of recombinant mannan-binding lectin-associated serine proteases-1 and -2
description
2001 nî lūn-bûn
@nan
2001 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Substrate specificities of rec ...... ated serine proteases-1 and -2
@ast
Substrate specificities of rec ...... ated serine proteases-1 and -2
@en
Substrate specificities of rec ...... ated serine proteases-1 and -2
@en-gb
Substrate specificities of rec ...... ated serine proteases-1 and -2
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type
label
Substrate specificities of rec ...... ated serine proteases-1 and -2
@ast
Substrate specificities of rec ...... ated serine proteases-1 and -2
@en
Substrate specificities of rec ...... ated serine proteases-1 and -2
@en-gb
Substrate specificities of rec ...... ated serine proteases-1 and -2
@nl
prefLabel
Substrate specificities of rec ...... ated serine proteases-1 and -2
@ast
Substrate specificities of rec ...... ated serine proteases-1 and -2
@en
Substrate specificities of rec ...... ated serine proteases-1 and -2
@en-gb
Substrate specificities of rec ...... ated serine proteases-1 and -2
@nl
P2093
P2860
P921
P3181
P356
P1476
Substrate specificities of rec ...... ated serine proteases-1 and -2
@en
P2093
P2860
P304
40880-40887
P3181
P356
10.1074/JBC.M105934200
P407
P577
2001-08-29T00:00:00Z