Structural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D
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Crystal structure of the catalytic domain of human complement c1s: a serine protease with a handleStructures of C3b in complex with factors B and D give insight into complement convertase formationStructural basis for complement factor I control and its disease-associated sequence polymorphismsNew structural motifs on the chymotrypsin fold and their potential roles in complement factor BThe crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex.The 2.2-A crystal structure of human pro-granzyme K reveals a rigid zymogen with unusual featuresCrystal structure of the serine protease domain of prophenoloxidase activating factor-ICrystallographic and Kinetic Evidence of Allostery in a Trypsin-like ProteaseCrystal Structures of Prethrombin-2 Reveal Alternative Conformations under Identical Solution Conditions and the Mechanism of Zymogen ActivationExposure of R169 controls protein C activation and autoactivationThe linker connecting the two kringles plays a key role in prothrombin activationA serpin-induced extensive proteolytic susceptibility of urokinase-type plasminogen activator implicates distortion of the proteinase substrate-binding pocket and oxyanion hole in the serpin inhibitory mechanism.Inhibition of complement as a therapeutic approach in inflammatory central nervous system (CNS) diseaseAllostery in trypsin-like proteases suggests new therapeutic strategies.Complement factor D in age-related macular degenerationManduca sexta hemolymph proteinase 21 activates prophenoloxidase-activating proteinase 3 in an insect innate immune response proteinase cascade.Conformational selection in trypsin-like proteases.A Pulmonary Perspective on GASPIDs: Granule-Associated Serine Peptidases of Immune Defense.C3 dysregulation due to factor H deficiency is mannan-binding lectin-associated serine proteases (MASP)-1 and MASP-3 independent in vivo.Residue Asp-189 controls both substrate binding and the monovalent cation specificity of thrombin.Buried Hydrogen Bond Interactions Contribute to the High Potency of Complement Factor D Inhibitors.Analysis of Factor D Isoforms in Malpuech-Michels-Mingarelli-Carnevale Patients Highlights the Role of MASP-3 as a Maturase in the Alternative Pathway of Complement.The properdin pathway: an "alternative activation pathway" or a "critical amplification loop" for C3 and C5 activation?
P2860
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P2860
Structural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D
description
1999 nî lūn-bûn
@nan
1999 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Structural basis of profactor ...... protease, complement factor D
@ast
Structural basis of profactor ...... protease, complement factor D
@en
Structural basis of profactor ...... protease, complement factor D
@nl
type
label
Structural basis of profactor ...... protease, complement factor D
@ast
Structural basis of profactor ...... protease, complement factor D
@en
Structural basis of profactor ...... protease, complement factor D
@nl
prefLabel
Structural basis of profactor ...... protease, complement factor D
@ast
Structural basis of profactor ...... protease, complement factor D
@en
Structural basis of profactor ...... protease, complement factor D
@nl
P2093
P2860
P356
P1433
P1476
Structural basis of profactor ...... protease, complement factor D
@en
P2093
P2860
P304
P356
10.1093/EMBOJ/18.4.804
P407
P577
1999-02-15T00:00:00Z