Center of Excellence of the European Union
Home
Research
Services
Education
About us
Institute
Contacts
Public information
History
Conferences
Seminars
Recent publications
Directory
Location
Recent 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 A,
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 complement lectin pathway.
J Biol Chem
notSet
,
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