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.   Csuka D, Munthe-Fog L, Skjoedt MO, Kocsis A, Zotter Z, Gál P, Varga L, Farkas H, Füst G and Garred P (2013) [23318225]
  The role of ficolins and MASPs in hereditary angioedema due to C1-inhibitor deficiency.
  Mol Immunol 54, 271-277
6.   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
7.   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
8.   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
9.   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
10.   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
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.   Kocsis J, Mészáros T, Madaras B, Tóth EK, Kamondi S, Gál P, Varga L, Prohászka Z and Füst G (2011) [20730518]
  High levels of acute phase proteins and soluble 70 kDa heat shock proteins are independent and additive risk factors for mortality in colorectal cancer.
  Cell Stress Chaperon 16, 49-55
13.   Beinrohr L, Murray-Rust TA, Dyksterhuis L, Závodszky P, Gál P, Pike RN and Wijeyewickrema LC (2011) [21683249]
  Serpins and the complement system.
  Method Enzymol 499, 55-75
14.   Gulla KC, Gupta K, Krarup A, Gal P, Schwaeble WJ, Sim RB, OConnor CD and Hajela K (2010) [20002787]
  Activation of mannan-binding lectin-associated serine proteases leads to generation of a fibrin clot.
  Immunology 129, 482-95
15.   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
16.   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
17.   Major B, Kardos J, Kékesi KA, Lorincz Z, Závodszky P and Gál P (2010) [20178990]
  Calcium-dependent conformational flexibility of a CUB domain controls activation of the complement serine protease C1r.
  J Biol Chem 285, 11863-9
18.   Láng A, Major B, Szilágyi K, Gáspári Z, Gál P, Závodszky P and Perczel A (2010) [20970424]
  Interaction between separated consecutive complement control modules of human C1r: Implications for dimerization of the full-length protease.
  FEBS Lett 584, 4565-4569
19.   Láng A, Szilágyi K, Major B, Gál P, Závodszky P and Perczel A (2010) [20796027]
  Intermodule cooperativity in the structure and dynamics of consecutive complement control modules in human C1r: structural biology.
  FEBS J 277, 3986-98
20.   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
21.   Than NG, Romero R, Goodman M, Weckle A, Xing J, Dong Z, Xu Y, Tarquini F, Szilagyi A, Gal P, Hou Z, Tarca AL, Kim CJ, Kim JS, Haidarian S, Uddin M, Bohn H, Benirschke K, Santolaya-Forgas J, Grossman LI, Erez O, Hassan SS, Zavodszky P, Papp Z and Wildman DE (2009) [19497882]
  A primate subfamily of galectins expressed at the maternal-fetal interface that promote immune cell death.
  P Natl Acad Sci Usa 106, 9731-6
22.   Megyeri M, Makó V, Beinrohr L, Doleschall Z, Prohászka Z, Cervenak L, Závodszky P and Gál P (2009) [19667088]
  Complement protease MASP-1 activates human endothelial cells: PAR4 activation is a link between complement and endothelial function.
  J Immunol 183, 3409-16
23.   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
24.   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
25.   Hajdú I, Bőthe C, Szilágyi A, Kardos J, Gál P and Závodszky P (2008) [18449535]
  Adjustment of conformational flexibility of glyceraldehyde-3-phosphate dehydrogenase as a means of thermal adaptation and allosteric regulation.
  Eur Biophys J Biophy 37, 1139-44
26.   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
27.   Varga L, Széplaki G, Laki J, Kocsis A, Kristóf K, Gál P, Bajtay Z, Wieslander J, Daha MR, Garred P, Madsen HO, Füst G and Farkas H (2008) [18460017]
  Depressed activation of the lectin pathway of complement in hereditary angioedema.
  Clin Exp Immunol 153, 68-74
28.   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
29.   Kardos J, Harmat V, Palló A, Barabás O, Szilágyi K, Gráf L, Náray-Szabó G, Goto Y, Závodszky P and Gál P (2008) [17996945]
  Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: structure of the active catalytic region of C1r.
  Mol Immunol 45, 1752-60
30.   Krarup A, Gulla KC, Gál P, Hajela K and Sim RB (2008) [18456010]
  The action of MBL-associated serine protease 1 (MASP1) on factor XIII and fibrinogen.
  Bba-proteins Proteom 1784, 1294-300
31.   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
32.   Széplaki G, Varga L, Laki J, Dósa E, Rugonfalvi-Kiss S, Madsen HO, Prohászka Z, Kocsis A, Gál P, Szabó A, Acsády G, Karádi I, Selmeci L, Garred P, Füst G and Entz L (2007) [17916775]
  Low c1-inhibitor levels predict early restenosis after eversion carotid endarterectomy.
  Arterioscl Throm Vas 27, 2756-62
33.   Gál P, Barna L, Kocsis A and Závodszky P (2007) [17544812]
  Serine proteases of the classical and lectin pathways: similarities and differences.
  Immunobiology 212, 267-77
34.   Krarup A, Wallis R, Presanis JS, Gál P and Sim RB (2007) [17637839]
  Simultaneous activation of complement and coagulation by MBL-associated serine protease 2.
  PLoS ONE 2, e623
35.   Gál P, Végh B, Závodszky P and Vonderviszt F (2006) [16900123]
  Export signals.
  Nat Biotechnol 24, 900-1
36.   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
37.   Gál P, Harmat V, Kocsis A, Bián T, Barna L, Ambrus G, Végh B, Balczer J, Sim RB, Náray-Szabó G and Závodszky P (2005) [16040602]
  A true autoactivating enzyme. Structural insight into mannose-binding lectin-associated serine protease-2 activations.
  J Biol Chem 280, 33435-44
38.   Presanis JS, Hajela K, Ambrus G, Gál P and Sim RB (2004) [14725788]
  Differential substrate and inhibitor profiles for human MASP-1 and MASP-2.
  Mol Immunol 40, 921-9
39.   Harmat V, Gál P, Kardos J, Szilágyi K, Ambrus G, Végh B, Náray-Szabó G and Závodszky P (2004) [15364579]
  The structure of MBL-associated serine protease-2 reveals that identical substrate specificities of C1s and MASP-2 are realized through different sets of enzyme-substrate interactions.
  J Mol Biol 342, 1533-46
40.   Sárvári M, Vágó I, Wéber CS, Nagy J, Gál P, Mák M, Kósa JP, Závodszky P and Pázmány T (2003) [12667643]
  Inhibition of C1q-beta-amyloid binding protects hippocampal cells against complement mediated toxicity.
  J Neuroimmunol 137, 12-8
41.   Ambrus G, Gál P, Kojima M, Szilágyi K, Balczer J, Antal J, Gráf L, Laich A, Moffatt BE, Schwaeble W, Sim RB and Závodszky P (2003) [12538697]
  Natural substrates and inhibitors of mannan-binding lectin-associated serine protease-1 and -2: a study on recombinant catalytic fragments.
  J Immunol 170, 1374-82
42.   Gál P, Ambrus G and Závodszky P (2002) [12396001]
  C1s, the protease messenger of C1. Structure, function and physiological significance.
  Immunobiology 205, 383-94
43.   Hajela K, Kojima M, Ambrus G, Wong KH, Moffatt BE, Ferluga J, Hajela S, Gál P and Sim RB (2002) [12396008]
  The biological functions of MBL-associated serine proteases (MASPs).
  Immunobiology 205, 467-75
44.   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
45.   Gal P and Ambrus G (2001) [-100002667]
  Structure and function of complement activating enzyme complexes: C1 and Mbl-masps.
  Curr Protein Pept Sc 2, 43-59
46.   Kardos J, Gál P, Szilágyi L, Thielens NM, Szilágyi K, Lőrincz Z, Kulcsár P, Gráf L, Arlaud GJ and Závodszky P (2001) [11673533]
  The role of the individual domains in the structure and function of the catalytic region of a modular serine protease, C1r.
  J Immunol 167, 5202-8
47.   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
48.   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
49.   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
50.   Gál P and Závodszky P (1998) [9777415]
  Structure and function of the serine-protease subcomponents of C1: protein engineering studies.
  Immunobiology 199, 317-26
51.   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
52.   Gál P, Cseh S, Schumaker VN and Závodszky P (1994) [7866721]
  The structure and function of the first component of complement: genetic engineering approach (a review).
  Acta Microbiol Imm H 41, 361-80
53.   Kovács A, Gál P and Závodszky P (1993) [8278582]
  A simple method to assess in vivo repair of ultraviolet radiation-induced lesions of specific DNA sequences of restriction sites.
  Radiat Res 136, 397-403
54.   Závodszky P, Gál P, Cseh S and Schumaker VN (1993) [8172556]
  Protein engineering studies on C1r and C1s.
  Behring Inst Mitt. 93, 103-14
55.   Luo C, Thielens NM, Gagnon J, Gal P, Sarvari M, Tseng Y, Tosi M, Zavodszky P, Arlaud GJ and Schumaker VN (1992) [1533159]
  Recombinant human complement subcomponent C1s lacking beta-hydroxyasparagine, sialic acid, and one of its two carbohydrate chains still reassembles with C1q and C1r to form a functional C1 complex.
  Biochemistry-us 31, 4254-62
56.   Sárvári M, Csikós G, Sass M, Gál P, Schumaker VN and Závodszky P (1990) [2182025]
  Ecdysteroids increase the yield of recombinant protein produced in baculovirus insect cell expression system.
  Biochem Bioph Res Co 167, 1154-61
57.   Gál P, Sárvári M, Szilágyi K, Závodszky P and Schumaker VN (1989) [2557186]
  Expression of hemolytically active human complement component C1r proenzyme in insect cells using a baculovirus vector.
  notSet 6, 433-41
58.   Vonderviszt F, Lakatos S, Gál P, Sárvári M and Závodszky P (1987) [3675596]
  A molten globule-like unfolding intermediate of a four domain protein, the Fc fragment of the IgG molecule.
  Biochem Bioph Res Co 148, 92-8

Books or book chapters

1.   Gal P, Ambrus G, Lorincz Z and Zavodszky P (2004)
  The initiation complexes of the classical and lectin patways.
  The complement system. Novel roles in health and disease. , 19-43