307 results on '"Dobó, József"'
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2. Synergy of protease-binding sites within the ecotin homodimer is crucial for inhibition of MASP enzymes and for blocking lectin pathway activation
3. Activities of MASPs, The Complement Proteases Associated with Collectins and Ficolins
4. MASP-1 of the complement system alters fibrinolytic behaviour of blood clots
5. The Lectin Pathway of the Complement System—Activation, Regulation, Disease Connections and Interplay with Other (Proteolytic) Systems
6. SARS-CoV-2 Nucleocapsid Protein Is Not Responsible for Over-Activation of Complement Lectin Pathway.
7. MASP-1
8. Complement MASP-1 Modifies Endothelial Wound Healing.
9. Complement inhibition can decrease the haemostatic response in a microvascular bleeding model at multiple levels
10. 171 The dominant form of the C1 inhibitor R444C variant causing type II hereditary angioedema is its covalent adduct with serum albumin explaining elevated levels
11. 217 An ecotin ortholog turns out to be a potent classical pathway inhibitor and might provide information on the relative efficacy of C1r versus C1s inhibition
12. Complement MASP-1 enhances adhesion between endothelial cells and neutrophils by up-regulating E‐selectin expression
13. Human primary endothelial label-free biochip assay reveals unpredicted functions of plasma serine proteases
14. Cooperation of Complement MASP-1 with Other Proinflammatory Factors to Enhance the Activation of Endothelial Cells
15. Quantification of the zymogenicity and the substrate-induced activity enhancement of complement factor D
16. MASP-1 of the complement system promotes clotting via prothrombin activation
17. Inhibition of the Serine Proteases of the Complement System
18. Editorial: Complement: Latest developments regarding structure, mechanism, and connections to other proteolytic pathways
19. Correction: Synergy of protease-binding sites within the ecotin homodimer is crucial for inhibition of MASP enzymes and for blocking lectin pathway activation
20. Soluble components of the flagellar export apparatus, FliI, FliJ, and FliH, do not deliver flagellin, the major filament protein, from the cytosol to the export gate
21. Multiple roles of complement MASP-1 at the interface of innate immune response and coagulation
22. Serum MASP-1 in complex with MBL activates endothelial cells
23. Dissociation and re-association studies on the interaction domains of mannan-binding lectin (MBL)-associated serine proteases, MASP-1 and MASP-2, provide evidence for heterodimer formation
24. The control of the complement lectin pathway activation revisited: Both C1-inhibitor and antithrombin are likely physiological inhibitors, while α2-macroglobulin is not
25. 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
26. Structural basis for activation of the complement system by component C4 cleavage
27. Revised mechanism of complement lectin-pathway activation revealing the role of serine protease MASP-1 as the exclusive activator of MASP-2
28. Monospecific 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-2
29. Complement lectin pathway components MBL and MASP-1 promote haemostasis upon vessel injury in a microvascular bleeding model
30. Proprotein Convertases and the Complement System
31. Directed Evolution-Driven Increase of Structural Plasticity Is a Prerequisite for Binding the Complement Lectin Pathway Blocking MASP-Inhibitor Peptides
32. Complement lectin pathway components MBL and MASP-1 promote haemostasis upon vessel injury in a microvascular bleeding model
33. MASP-1
34. Biological variations of MASP-3 and MAp44, two splice products of the MASP1 gene involved in regulation of the complement system
35. Fasciola hepatica is refractory to complement killing by preventing attachment of mannose binding lectin (MBL) and inhibiting MBL-associated serine proteases (MASPs) with serpins
36. Early complement proteases: C1r, C1s and MASPs. A structural insight into activation and functions
37. C1, MBL–MASPs and C1-inhibitor: novel approaches for targeting complement-mediated inflammation
38. C1 Inhibitor Serpin Domain Structure Reveals the Likely Mechanism of Heparin Potentiation and Conformational Disease
39. C1 Inhibitor: Quantification and Purification
40. Proprotein Convertase Is the Highest-Level Activator of the Alternative Complement Pathway in the Blood
41. Inhibition of the Serine Proteases of the Complement System
42. The Use of a Flagellar Export Signal for the Secretion of Recombinant Proteins in Salmonella
43. Cytokine Response Modifier A Inhibition of Initiator Caspases Results in Covalent Complex Formation and Dissociation of the Caspase Tetramer
44. Active Site Distortion Is Sufficient for Proteinase Inhibition by Serpins: STRUCTURE OF THE COVALENT COMPLEX OF α1-PROTEINASE INHIBITOR WITH PORCINE PANCREATIC ELASTASE
45. Localization of the flagellum-specific secretion signal in Salmonella flagellin
46. ITIH4 acts as a protease inhibitor by a novel inhibitory mechanism
47. Patterns of C1-Inhibitor/Plasma Serine Protease Complexes in Healthy Humans and in Hereditary Angioedema Patients
48. Cleavage of kininogen and subsequent bradykinin release by MASP-1: OP81
49. Patterns of C1-Inhibitor/Plasma Serine Protease Complexes in Healthy Humans and in Hereditary Angioedema Patients
50. α1-Proteinase Inhibitor Forms Initial Non-covalent and Final Covalent Complexes with Elastase Analogously to Other Serpin-Proteinase Pairs, Suggesting a Common Mechanism of Inhibition
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