Center of Excellence of the European Union
 
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Selected publications

Articles

1.   Gál P, Dobó J, Beinrohr L, Pál G and Závodszky P (2013) [22990693]
  Inhibition of the serine proteases of the complement system.
  Adv Exp Med Biol 734, 23-40
2.   Gál P, Dobó J, Beinrohr L, Pál G and Závodszky P (2013) [23402017]
  Inhibition of the serine proteases of the complement system.
  Adv Exp Med Biol 735, 23-40
3.   Megyeri M, Harmat V, Major B, Végh Á, Balczer J, Héja D, Szilágyi K, Datz D, Pál G, Závodszky P, Gál P and Dobó J (2013) [23386610]
  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.
  J Biol Chem 288, 8922-34
4.   Paréj K, Dobó J, Závodszky P and Gál P (2013) [23399388]
  The control of the complement lectin pathway activation revisited: Both C1-inhibitor and antithrombin are likely physiological inhibitors, while α(2)-macroglobulin is not.
  Mol Immunol 54, 415-422
5.   Hess K, Ajjan R, Phoenix F, Dobó J, Gál P and Schroeder V (2012) [22536427]
  Effects of MASP-1 of the Complement System on Activation of Coagulation Factors and Plasma Clot Formation.
  PLoS ONE 7, e35690
6.   Thiel S, Jensen L, Degn SE, Nielsen HJ, Gál P, Dobó J and Jensenius JC (2012) [22670777]
  Mannan-binding lectin (MBL)-associated serine protease-1 (MASP-1), a serine protease associated with humoral pattern-recognition molecules: normal and acute-phase levels in serum and stoichiometry of lectin pathway components.
  Clin Exp Immunol 169, 38-48
7.   Héja D, Harmat V, Fodor K, Wilmanns M, Dobó J, Kékesi KA, Závodszky P, Gál P and Pál G (2012) [22511776]
  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.
  J Biol Chem 287, 20290-300
8.   Héja D, Kocsis A, Dobó J, Szilágyi K, Szász R, Závodszky P, Pál G and Gál P (2012) [22691502]
  Revised mechanism of complement lectin-pathway activation revealing the role of serine protease MASP-1 as the exclusive activator of MASP-2.
  P Natl Acad Sci Usa 109, 10498-503
9.   Kidmose RT, Laursen NS, Dobó J, Kjaer TR, Sirotkina S, Yatime L, Sottrup-Jensen L, Thiel S, Gál P and Andersen GR (2012) [22949645]
  Structural basis for activation of the complement system by component C4 cleavage.
  P Natl Acad Sci Usa 109, 15425-30
10.   Vonderviszt F, Sajó R, Dobó J and Závodszky P (2012) [22160896]
  The Use of a Flagellar Export Signal for the Secretion of Recombinant Proteins in Salmonella.
  Methods Mol Biol 824, 131-143
11.   Dobó J, Major B, Kékesi KA, Szabó I, Megyeri M, Hajela K, Juhász G, Závodszky P and Gál P (2011) [21625439]
  Cleavage of Kininogen and Subsequent Bradykinin Release by the Complement Component: Mannose-Binding Lectin-Associated Serine Protease (MASP)-1.
  PLoS ONE 6, e20036
12.   Dobó J, Varga J, Sajó R, Végh BM, Gál P, Závodszky P and Vonderviszt F (2010) [20008166]
  Application of a short, disordered N-terminal flagellin segment, a fully functional flagellar type III export signal, to expression of secreted proteins.
  Appl Environ Microb 76, 891-9
13.   Degn SE, Jensen L, Gál P, Dobó J, Holmvad SH, Jensenius JC and Thiel S (2010) [20673767]
  Biological variations of MASP-3 and MAp44, two splice products of the MASP1 gene involved in regulation of the complement system.
  J Immunol Methods 361, 37-50
14.   Kocsis A, Kékesi KA, Szász R, Végh BM, Balczer J, Dobó J, Závodszky P, Gál P and Pál G (2010) [20817870]
  Selective Inhibition of the Lectin Pathway of Complement with Phage Display Selected Peptides against Mannose-Binding Lectin-Associated Serine Protease (MASP)-1 and -2: Significant Contribution of MASP-1 to Lectin Pathway Activation.
  J Immunol 185, 4169-78
15.   Gál P, Dobó J, Závodszky P and Sim RB (2009) [19477526]
  Early complement proteases: C1r, C1s and MASPs. A structural insight into activation and functions.
  Mol Immunol 46, 2745-52
16.   Dobó J, Harmat V, Beinrohr L, Sebestyén E, Závodszky P and Gál P (2009) [19564340]
  MASP-1, a Promiscuous Complement Protease: Structure of Its Catalytic Region Reveals the Basis of Its Broad Specificity.
  J Immunol 183, 1207-1214
17.   Beinrohr L, Dobó J, Závodszky P and Gál P (2008) [18977695]
  C1, MBL-MASPs and C1-inhibitor: novel approaches for targeting complement-mediated inflammation.
  Trends Mol Med 14, 511-21
18.   Dobó J, Harmat V, Sebestyén E, Beinrohr L, Závodszky P and Gál P (2008) [18765903]
  Purification, crystallization and preliminary X-ray analysis of human mannose-binding lectin-associated serine protease-1 (MASP-1) catalytic region.
  Acta Crystallogr F 64, 781-4
19.   Beinrohr L, Harmat V, Dobó J, Lörincz Z, Gál P and Závodszky P (2007) [17488724]
  C1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational disease.
  J Biol Chem 282, 21100-9
20.   Dementiev A , Dobó J and Gettins PG (2006) [16321984]
  Active site distortion is sufficient for proteinase inhibition by serpins: structure of the covalent complex of alpha1-proteinase inhibitor with porcine pancreatic elastase
  J Biol Chem 281, 3452-7
21.   Dobó J , Swanson R , Salvesen GS , Olson ST and Gettins PG (2006) [17052983]
  Cytokine response modifier a inhibition of initiator caspases results in covalent complex formation and dissociation of the caspase tetramer
  J Biol Chem 281, 38781-90
22.   Végh BM, Gál P, Dobó J, Závodszky P and Vonderviszt F (2006) [16674914]
  Localization of the flagellum-specific secretion signal in Salmonella flagellin.
  Biochem Bioph Res Co 345, 93-8
23.   Dobó J and Gettins PG (2004) [14593107]
  alpha1-Proteinase inhibitor forms initial non-covalent and final covalent complexes with elastase analogously to other serpin-proteinase pairs, suggesting a common mechanism of inhibition
  J Biol Chem 279, 9264-9
24.   Lacroix M, Ebel C, Kardos J, Dobó J, Gál P, Závodszky P, Arlaud GJ and Thielens NM (2001) [11445589]
  Assembly and enzymatic properties of the catalytic domain of human complement protease C1r.
  J Biol Chem 276, 36233-40
25.   Németh A, Svingor A, Pócsik M, Dobó J, Magyar C, Szilágyi A, Gál P and Závodszky P (2000) [10683439]
  Mirror image mutations reveal the significance of an intersubunit ion cluster in the stability of 3-isopropylmalate dehydrogenase.
  FEBS Lett 468, 48-52
26.   Lörincz Z, Gál P, Dobó J, Cseh S, Szilágyi K, Ambrus G and Závodszky P (2000) [10925288]
  The cleavage of two C1s subunits by a single active C1r reveals substantial flexibility of the C1s-C1r-C1r-C1s tetramer in the C1 complex.
  J Immunol 165, 2048-51
27.   Wong NK , Kojima M , Dobó J , Ambrus G and Sim RB (1999) [10698339]
  Activities of the MBL-associated serine proteases (MASPs) and their regulation by natural inhibitors
  Mol Immunol 36, 853-61
28.   Dobó J, Gál P, Szilágyi K, Cseh S, Lörincz Z, Schumaker VN and Závodszky P (1999) [9916740]
  One active C1r subunit is sufficient for the activity of the complement C1 complex: stabilization of C1r in the zymogen form by point mutations.
  J Immunol 162, 1108-12
29.   Cseh S, Gál P, Sárvári M, Dobó J, Lőrincz Z, Schumaker VN and Závodszky P (1996) [8676886]
  Functional effects of domain deletions in a multidomain serine protease, C1r.
  Mol Immunol 33, 351-9