Center of Excellence of the European Union
 
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Selected publications

Articles

1.   Závodszky P and Hajdú I (2013) [23348674]
  Evolution of the concept of conformational dynamics of enzyme functions over half of a century: A personal view.
  Biopolymers 99, 263-9
2.   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
3.   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
4.   Závodszky P (2013) [23738340]
  Péter Friedrich (1936-2013).
  FEBS Lett 587, 1269-70
5.   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
6.   Varga A, Gráczer E, Chaloin L, Liliom K, Závodszky P, Lionne C and Vas M (2013) [23201309]
  Selectivity of kinases on the activation of tenofovir, an anti-HIV agent.
  Eur J Pharm Sci 48, 307-15
7.   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
8.   Gráczer É, Lionne C, Závodszky P, Chaloin L and Vas M (2013) [23421786]
  Transient kinetic studies reveal isomerization steps along the kinetic pathway of Thermus thermophilus 3-isopropylmalate dehydrogenase.
  FEBS J 280, 1764-72
9.   Varga A, Palmai Z, Gugolya Z, Gráczer E, Vonderviszt F, Závodszky P, Balog E and Vas M (2012) [23231058]
  Importance of aspartate residues in balancing the flexibility and fine-tuning the catalysis of human 3-phosphoglycerate kinase.
  Biochemistry-us 51, 10197-207
10.   Szilágyi A, Zhang Y and Závodszky P (2012) [22079367]
  Intra-chain 3D segment swapping spawns the evolution of new multidomain protein architectures.
  J Mol Biol 415, 221-35
11.   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
12.   Györffy D, Závodszky P and Szilágyi A (2012) [23221093]
  Pull moves for rectangular lattice polymer models are not fully reversible.
  Ieee Acm T Comput Bi 9, 1847-9
13.   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
14.   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
15.   Gráczer É, Merli A, Singh RK, Karuppasamy M, Závodszky P, Weiss MS and Vas M (2011) [21387033]
  Atomic level description of the domain closure in a dimeric enzyme: thermus thermophilus 3-isopropylmalate dehydrogenase.
  Mol Biosyst 7, 1646-59
16.   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
17.   Gráczer E, Konarev PV, Szimler T, Bacsó A, Bodonyi A, Svergun DI, Závodszky P and Vas M (2011) [21939659]
  Essential role of the metal-ion in the IPM-assisted domain closure of 3-isopropylmalate dehydrogenase.
  FEBS Lett 585, 3297-302
18.   Varga A, Chaloin L, Sági G, Sendula R, Gráczer E, Liliom K, Závodszky P, Lionne C and Vas M (2011) [21505655]
  Nucleotide promiscuity of 3-phosphoglycerate kinase is in focus: implications for the design of better anti-HIV analogues.
  Mol Biosyst 7, 1863-73
19.   Than NG, Romero R, Meiri H, Erez O, Xu Y, Tarquini F, Barna L, Szilagyi A, Ackerman R, Sammar M, Fule T, Karaszi K, Kovalszky I, Dong Z, Kim CJ, Zavodszky P, Papp Z and Gonen R (2011) [21799738]
  PP13, Maternal ABO Blood Groups and the Risk Assessment of Pregnancy Complications.
  PLoS ONE 6, e21564
20.   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
21.   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
22.   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
23.   Merli A, Manikandan K, Gráczer E, Schuldt L, Singh RK, Závodszky P, Vas M and Weiss MS (2010) [20516614]
  Crystallization and preliminary X-ray diffraction analysis of various enzyme-substrate complexes of isopropylmalate dehydrogenase from Thermus thermophilus.
  Acta Crystallogr F 66, 738-43
24.   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
25.   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
26.   Agócs G, Solymosi K, Varga A, Módos K, Kellermayer M, Závodszky P, Fidy J and Osváth S (2010) [20132817]
  Recovery of functional enzyme from amyloid fibrils.
  FEBS Lett 584, 1139-42
27.   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
28.   Hajdú I, Szilágyi A, Kardos J and Závodszky P (2009) [19527660]
  A link between hinge-bending domain motions and the temperature dependence of catalysis in 3-isopropylmalate dehydrogenase.
  Biophys J 96, 5003-12
29.   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
30.   Fülöp K, Barna L, Symmons O, Závodszky P and Váradi A (2009) [19133228]
  Clustering of disease-causing mutations on the domain-domain interfaces of ABCC6.
  Biochem Bioph Res Co 379, 706-9
31.   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
32.   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
33.   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
34.   Gráczer É., Varga A., Melnik B., Semisotnov G., Závodszky P. and Vas M. (2009) [-100076773]
  Symmetrical refolding of protein domains and subunits: example of the dimeric two-domain 3-Isopropylmalate dehydrogenases.
  Biochemistry-us 48, 1123-1134
35.   Varga A, Szabó J, Flachner B, Gugolya Z, Vonderviszt F, Závodszky P and Vas M (2009) [19854185]
  Thermodynamic analysis of substrate induced domain closure of 3-phosphoglycerate kinase.
  FEBS Lett 583, 3660-4
36.   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
37.   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
38.   Szabó J, Varga A, Flachner B, Konarev PV, Svergun DI, Závodszky P and Vas M (2008) [18540639]
  Communication between the nucleotide site and the main molecular hinge of 3-phosphoglycerate kinase.
  Biochemistry-us 47, 6735-44
39.   Kamondi S, Szilágyi A, Barna L and Závodszky P (2008) [18667161]
  Engineering the thermostability of a TIM-barrel enzyme by rational family shuffling.
  Biochem Bioph Res Co 374, 725-30
40.   Vas M., Varga A., Szabó J., Gráczer É., Flachner B., Závodszky P., Konarev P.V. and Svergun D.I. (2008) [-100047371]
  Insight into the Mechanism of Domain Movement and Its Role in Functioning of 3-Phosphoglycerate Kinase
  Moscow University Chemistry Bulletin 63, 114-119
41.   Varga A, Szabó J, Flachner B, Roy B, Konarev P, Svergun D, Závodszky P, Périgaud C, Barman T, Lionne C and Vas M (2008) [18096512]
  Interaction of human 3-phosphoglycerate kinase with l-ADP, the mirror image of d-ADP.
  Biochem Bioph Res Co 366, 994-1000
42.   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
43.   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
44.   Szabó J, Varga A, Flachner B, Konarev PV, Svergun DI, Závodszky P and Vas M (2008) [18358841]
  Role of side-chains in the operation of the main molecular hinge of 3-phosphoglycerate kinase.
  FEBS Lett 582, 1335-40
45.   Szilágyi A, Györffy D and Závodszky P (2008) [18441033]
  The twilight zone between protein order and disorder.
  Biophys J 95, 1612-26
46.   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
47.   Gráczer É, Varga A, Hajdú I, Melnik B, Szilágyi A, Semisotnov G, Závodszky P and Vas M (2007) [17887729]
  Rates of unfolding, rather than refolding, determine thermal stabilities of thermophilic, mesophilic, and psychrotrophic 3-isopropylmalate dehydrogenases.
  Biochemistry-us 46, 11536-49
48.   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
49.   Osváth S, Jäckel M, Agócs G, Závodszky P, Köhler G and Fidy J (2006) [16353200]
  Domain interactions direct misfolding and amyloid formation of yeast phosphoglycerate kinase.
  Proteins 62, 909-17
50.   Gál P, Végh B, Závodszky P and Vonderviszt F (2006) [16900123]
  Export signals.
  Nat Biotechnol 24, 900-1
51.   Osváth S, Herényi L, Závodszky P, Fidy J and Köhler G (2006) [16807241]
  Hierarchic finite level energy landscape model: to describe the refolding kinetics of phosphoglycerate kinase.
  J Biol Chem 281, 24375-80
52.   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
53.   Varga A, Flachner B, Konarev P, Gráczer É, Szabó J, Svergun D, Závodszky P and Vas M (2006) [16647059]
  Substrate-induced double sided H-bond network as a means of domain closure in 3-phosphoglycerate kinase.
  FEBS Lett 580, 2698-706
54.   Szenczi Á, Kardos J, Medgyesi GA and Závodszky P (2006) [16168667]
  The effect of solvent environment on the conformation and stability of human polyclonal IgG in solution.
  Biologicals 34, 5-14
55.   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
56.   Osváth S, Köhler G, Závodszky P and Fidy J (2005) [15883189]
  Asymmetric effect of domain interactions on the kinetics of folding in yeast phosphoglycerate kinase.
  Protein Sci 14, 1609-16
57.   Bellyei S, Szigeti A, Boronkai A, Szabo Z, Bene J, Janaky T, Barna L, Sipos K, Minik O, Kravjak A, Ohmacht R, Melegh B, Zavodszky P, Than GN, Sumegi B, Bohn H and Than NG (2005) [15664409]
  Cloning, sequencing, structural and molecular biological characterization of placental protein 20 (PP20)/human thiamin pyrophosphokinase (hTPK).
  Placenta 26, 34-46
58.   Debreczeni JÉ, Farkas L, Harmat V, Hetényi C, Hajdú I, Závodszky P, Kohama K and Nyitray L (2005) [16227209]
  Structural evidence for non-canonical binding of Ca2+ to a canonical EF-hand of a conventional myosin.
  J Biol Chem 280, 41458-64
59.   Kardos J, Okuno D, Kawai T, Hagihara Y, Yumoto N, Kitagawa T, Závodszky P, Naiki H and Goto Y (2005) [16185940]
  Structural studies reveal that the diverse morphology of beta(2)-microglobulin aggregates is a reflection of different molecular architectures.
  Biochim Biophys Acta 1753, 108-20
60.   Flachner B, Varga A, Szabó J, Barna L, Hajdú I, Gyimesi G, Závodszky P and Vas M (2005) [16363799]
  Substrate-assisted movement of the catalytic Lys 215 during domain closure: site-directed mutagenesis studies of human 3-phosphoglycerate kinase.
  Biochemistry-us 44, 16853-65
61.   Diószeghy Z, Závodszky P, Namba K and Vonderviszt F (2004) [15196929]
  Stabilization of flagellar filaments by HAP2 capping.
  FEBS Lett 568, 105-9
62.   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
63.   Barna L, Bellyei S, Szigeti A, Boronkai Á, Szabó Z, Ohmacht R, Janáky T, Than NG, Szilágyi A, Závodszky P and Sümegi B (2003) [-100002802]
  Humán placenta protein: szerkezettől a funkcióig.
  Biokémia 27, 88-96
64.   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
65.   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
66.   Varga L, Szilágyi K, Lőrincz Z, Berrens L, Thiel S, Závodszky P, Daha MR, Thielens NM, Arlaud GJ, Nagy K, Späth P and Füst G (2003) [12686499]
  Studies on the mechanisms of allergen-induced activation of the classical and lectin pathways of complement.
  Mol Immunol 39, 839-46
67.   Gál P, Ambrus G and Závodszky P (2002) [12396001]
  C1s, the protease messenger of C1. Structure, function and physiological significance.
  Immunobiology 205, 383-94
68.   Szilágyi A, Kovács KL, Rákhely G and Závodszky P (2002) [12032599]
  Homology modeling reveals the structural background of the striking difference in thermal stability between two related [NiFe]hydrogenases.
  J Mol Model 8, 58-64
69.   Kalabay L, Jakab L, Prohászka Z, Füst G, Benkö Z, Telegdy L, Lőrincz Z, Závodszky P, Arnaud P and Fekete B (2002) [11943951]
  Human fetuin/alpha2HS-glycoprotein level as a novel indicator of liver cell function and short-term mortality in patients with liver cirrhosis and liver cancer.
  Eur J Gastroen Hepat 14, 389-94
70.   Németh A, Kamondi S, Szilágyi A, Magyar C, Kovári Z and Závodszky P (2002) [12034443]
  Increasing the thermal stability of cellulase C using rules learned from thermophilic proteins: a pilot study.
  Biophys Chem 96, 229-41
71.   Svingor Á, Kardos J, Hajdú I, Németh A and Závodszky P (2001) [11369782]
  A better enzyme to cope with cold. Comparative flexibility studies on psychrotrophic, mesophilic, and thermophilic IPMDHs.
  J Biol Chem 276, 28121-5
72.   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
73.   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
74.   Hajós JP, Pijnenburg J, Usmany M, Zuidema D, Závodszky P and Vlak JM (2000) [10664413]
  High frequency recombination between homologous baculoviruses in cell culture.
  Arch Virol 145, 159-64
75.   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
76.   Galántai R, Bárdos-Nagy I, Módos K, Kardos J, Závodszky P and Fidy J (2000) [10620347]
  Serum albumin-lipid membrane interaction influencing the uptake of porphyrins.
  Arch Biochem Biophys 373, 261-70
77.   Szilágyi A and Závodszky P (2000) [10801491]
  Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey.
  Structure 8, 493-504
78.   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
79.   Hajós JP, Vermunt AM, Zuidema D, Kulcsár P, Varjas L, de Kort CA, Závodszky P and Vlak JM (1999) [10620049]
  Dissecting insect development: baculovirus-mediated gene silencing in insects.
  Insect Mol Biol 8, 539-44
80.   Kardos J, Bódi A, Závodszky P, Venekei I and Gráf L (1999) [10493792]
  Disulfide-linked propeptides stabilize the structure of zymogen and mature pancreatic serine proteases.
  Biochemistry-us 38, 12248-57
81.   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
82.   Závodszky P, Kardos J, Svingor Á and Petsko GA (1998) [9636162]
  Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins.
  P Natl Acad Sci Usa 95, 7406-11
83.   Lőrincz Z, Kalabay L, Cseh S, Závodszky P, Arnaud P and Jakab L (1998) [9873947]
  Isolation of human alpha 2HS-glycoprotein synthesized by Sf9 cells.
  Acta Microbiol Imm H 45, 419-24
84.   Hajós JP, Zuidema D, Kulcsár P, Heldens JG, Závodszky P and Vlak JM (1998) [9856092]
  Recombination of baculovirus DNA following lipofection of insect larvae.
  Arch Virol 143, 2045-50
85.   Gál P and Závodszky P (1998) [9777415]
  Structure and function of the serine-protease subcomponents of C1: protein engineering studies.
  Immunobiology 199, 317-26
86.   Sárvári M, Závodszky P, Molnár K, Lőw P and Sass M (1997) [9129671]
  Baculovirus-mediated trans-epithelial transport of proteins in infected caterpillars.
  J Gen Virol 78, 953-63
87.   Kaslik G, Kardos J, Szabó E, Szilágyi L, Závodszky P, Westler WM, Markley JL and Gráf L (1997) [9154928]
  Effects of serpin binding on the target proteinase: global stabilization, localized increased structural flexibility, and conserved hydrogen bonding at the active site.
  Biochemistry-us 36, 5455-64
88.   Wallon G, Lovett ST, Magyar C, Svingor A, Szilagyi A, Závodszky P, Ringe D and Petsko GA (1997) [9278279]
  Sequence and homology model of 3-isopropylmalate dehydrogenase from the psychrotrophic bacterium Vibrio sp. I5 suggest reasons for thermal instability.
  Protein Eng 10, 665-72
89.   Tseng Y, Zavodszky P and Schumaker VN (1997) [8993014]
  The human complement C1 complex has a picomolar dissociation constant at room temperature.
  J Immunol 158, 937-44
90.   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
91.   Zavodszky P and Cseh S (1996) [-100002658]
  Production of multidomain complement glycoproteins in insect cells.
  Cytotechnology 20, 279-288
92.   Magyar C, Szilágyi A and Závodszky P (1996) [8875643]
  Relationship between thermal stability and 3-D structure in a homology model of 3-isopropylmalate dehydrogenase from Escherichia coli.
  Protein Eng 9, 663-70
93.   Zavodszky P and Cseh S (1996) [-100002659]
  The first component of complement: Protein engineering to reveal the structure and the mechanism of activation of C1.
  Turk J Immunol 2, 11-24
94.   Szilágyi A and Závodszky P (1995) [8637847]
  Structural basis for the extreme thermostability of D-glyceraldehyde-3-phosphate dehydrogenase from Thermotoga maritima: analysis based on homology modelling.
  Protein Eng 8, 779-89
95.   Vonderviszt F, Závodszky P, Ishimura M, Uedaira H and Namba K (1995) [7658470]
  Structural organization and assembly of flagellar hook protein from Salmonella typhimurium.
  J Mol Biol 251, 520-32
96.   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
97.   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
98.   Závodszky P, Gál P, Cseh S and Schumaker VN (1993) [8172556]
  Protein engineering studies on C1r and C1s.
  Behring Inst Mitt. 93, 103-14
99.   Monkovic DD, VanDusen WJ, Petroski CJ, Garsky VM, Sardana MK, Zavodszky P, Stern AM and Friedman PA (1992) [1449478]
  Invertebrate aspartyl/asparaginyl beta-hydroxylase: potential modification of endogenous epidermal growth factor-like modules.
  Biochem Bioph Res Co 189, 233-41
100.   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
101.   Tseng Y, Poon PH, Zavodszky P and Schumaker VN (1991) [1890306]
  Spontaneous activation of serum C1 in vitro. Role of C1 inhibitor.
  J Immunol 147, 1884-90
102.   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
103.   Wrba A, Schweiger A, Schultes V, Jaenicke R and Závodszky P (1990) [2271518]
  Extremely thermostable D-glyceraldehyde-3-phosphate dehydrogenase from the eubacterium Thermotoga maritima.
  Biochemistry-us 29, 7584-92
104.   Jaenicke R and Závodszky P (1990) [2200715]
  Proteins under extreme physical conditions.
  FEBS Lett 268, 344-9
105.   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
106.   Schumaker VN, Tseng Y, Poon PH, Bianchino AC and Zavodszky P (1989) [2803179]
  Spontaneous activation of reconstituted and serum C1 and the role of C1-inhibitor.
  Behring Inst Mitt. notSet, 102-10
107.   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
108.   Schumaker VN, Zavodszky P and Poon PH (1987) [3036181]
  Activation of the first component of complement.
  Annu Rev Immunol 5, 21-42
109.   Kilár F and Závodszky P (1987) [3816786]
  Non-covalent interactions between Fab and Fc regions in immunoglobulin G molecules. Hydrogen-deuterium exchange studies.
  Eur J Biochem 162, 57-61
110.   Vonderviszt F, Török J, Lakatos S, Kilár F and Závodszky P (1987) [3498482]
  Quantitative analysis of the interaction between immune complex and C1q complement subcomponent. The role of interdomain interactions in rabbit IgG in binding of C1q to immune precipitates.
  Biochem J 243, 449-55
111.   Kilár F, Simon I, Lakatos S, Vonderviszt F, Medgyesi GA and Závodszky P (1985) [3971974]
  Conformation of human IgG subclasses in solution. Small-angle X-ray scattering and hydrodynamic studies.
  Eur J Biochem 147, 17-25
112.   Závodszky P (1981) [7019028]
  Conformational flexibility of antibody molecules.
  Haematologia (Budap) 14, 79-83
113.   Zav\'yalov VP, Abramov VM, Ivannikov AI, Loseva OI, Dudich IV, Dudich EI, Tischenko VM, Khechinashvili NN, Franĕk F, Medgyesi G, Závodszky P and Jaton JC (1981) [7019029]
  Correspondence between structure and function of immunoglobulin G subclasses.
  Haematologia (Budap) 14, 85-94
114.   Závodszky P, Jaton JC, Venyaminov SY and Medgyesi GA (1981) [7266478]
  Increase of conformational stability of homogeneous rabbit immunoglobulin G after hapten binding.
  Mol Immunol 18, 39-46
115.   Váli Z, Kilár F, Lakatos S, Venyaminov SA and Závodszky P (1980) [6775703]
  L-alanine dehydrogenase from Thermus thermophilus.
  Biochim Biophys Acta 615, 34-47
116.   Závodszky P (1980) [-100017568]
  The immonoglobulin molecule. Organisation of several functions in one macromolecule.
  23, 289-320
117.   Boyd J, Easterbrook-Smith SB, Závodszky P, Mountford-Wright C and Dwek RA (1979) [528014]
  Mobility and symmetry in the Fc and pFc\\\' fragments as probed by 1H NMR.
  Mol Immunol 16, 851-8
118.   Závodszky P and MOSHKOV KA (1979) [-100017292]
  MOLECULAR-ORGANIZATION OF HUMAN CERULOPLASMIN AS REVEALED BY LIMITED PROTEOLYSIS AND ELECTRON-MICROSCOPY
  Bioorganicheskaya Khimiya 5, 395-407
119.   Moshkov KA, Lakatos S, Hajdu J, Závodszky P and Neifakh SA (1979) [436837]
  Proteolysis of human ceruloplasmin. Some peptide bonds are particularly susceptible to proteolytic attack.
  Eur J Biochem 94, 127-34
120.   Zavodszky P, Easterbrook-Smith SB and Dwek RA (1979) [118917]
  The isolation of a globular fragment of rabbit immunoglobulin G probably corresponding to the intact C gamma 2 homology region.
  Mol Immunol 16, 899-905
121.   Lakatos S, Halász G and Závodszky P (1978) [744388]
  Conformational stability of lactate dehydrogenase from Bacillus thermus-aquaticus [proceedings]
  Biochem Soc T 6, 1195-7
122.   Easterbrook-Smith SB, Závodszky P, Willan KJ, Gettins P and Dwek RA (1978) [744370]
  Structural basis of recognition in the immune response.
  Biochem Soc T 6, 1126-31
123.   Závodszky P, Johansen JT and Hvidt A (1976) [-100017451]
  HYDROGEN-EXCHANGE STUDY OF CONFORMATIONAL STABILITY OF HUMAN CARBONIC ANHYDRASE-B AND ITS METALLOCOMPLEXES
  Acta Biochim Biophys Acad Sci Hung 11, 219-220
124.   Lakatos S and Závodszky P (1976) [177307]
  The effect of substrates on the association equilibrium of mammalian D-glyceraldehyde 3-phosphate dehydrogenase.
  FEBS Lett 63, 145-8
125.   Venyaminov SY, Rajnavölgyi É, Medgyesi GA, Gergely J and Závodszky P (1976) [9279]
  The role of interchain disulphide bridges in the conformational stability of human immunoglobulin G1 subclass. Hydrogen-deuterium exchange studies.
  Eur J Biochem 67, 81-6
126.   Závodszky P, Johansen JT and Hvidt A (1975) [240709]
  Hydrogen-exchange study of the conformational stability of human carbonic-anhydrase B and its metallocomplexes.
  Eur J Biochem 56, 67-72
127.   Moshkov K A, Lakatos S and Závodszky P (1975) [-100017567]
  STUDIES ON QUATERNARY STRUCTURE OF HUMAN CERULOPLASMIN BY SEDIMENTATION EQUILIBRIUM METHOD
  Ann Biol Clin-paris 33, 202-203
128.   Závodszky P (1974) [-100017565]
  Hungarian scientific instruments in biochemical research
  30, 1-11
129.   Gráf L, Szalontai B, Barát E, Závodszky P, Borvendég J, Hermann I and Cseh G (1974) [4451026]
  Studies on the multiplicity of polypeptide hormones. I. Isolation of human pituitary growth hormone and characterization of the aggregates.
  Acta Biochim Biophys Acad Sci Hung 9, 309-17
130.   Závodszky P (1974) [-100017566]
  Ultracentrifugal separation and analysis serum lipoproteins
  30, 23-27
131.   Lakatos S, Závodszky P and Elődi P (1972) [11946448]
  Dissociation of mammalian D-glyceraldehyde-3-phosphate dehydrogenase into monomers.
  FEBS Lett 20, 324-326
132.   Závodszky P, Biszku E, Abaturov LV and Szabolcsi G (1972) [5084287]
  Effect of thiol blocking and substrate binding on the conformation and conformational stability of rabbit muscle aldolase.
  Acta Biochim Biophys Acad Sci Hung 7, 1-10
133.   Závodszky P and Elödi P (1970) [5531276]
  Structural investigations on pancreatic alpha-amylase. II. Determination of the molecular weight by sedimentation and light scattering.
  Acta Biochim Biophys Acad Sci Hung 5, 225-9
134.   Abaturov L B, Závodszky P and Varsavszkij J M (1968) [-100017564]
  Hydrogen isotopic exchange between enz glyceraldehyde-3-phosphate dehydrogenase and heavy water pig muscle inst ir spectra.
  Mol Biol (Mosk) 2, 136-47
135.   Bolotina IA, Markovich DS, Volkenstein MV and Zavodszky P (1967) [4382210]
  Investigation of the conformation of D-glyceraldehyde-3-phosphate dehydrogenase.
  Biochim Biophys Acta 132, 260-70
136.   Bolotina IA, Markovich DS, Volkenstein MV and Zavodszky P (1967) [4382211]
  Investigation of the conformation of lactate dehydrogenase and of its catalytic activity.
  Biochim Biophys Acta 132, 271-81
137.   Závodszky P and Biszku E (1967) [-100017560]
  The hydrodynamic properties and the molecular weight of aldolase and aldolase-T
  Acta Biochim Biophys Acad Sci Hung 2, 109-112
138.   Bolotina IA, Volkenstein MV, Závodszky P and Markovich DS (1966) [10019857]
  Polarimetric investigation of conformational changes of d-glyceraldehyde-3-phosphate dehydrogenase.
  Biochemistry-moscow+ 31, 567
139.   Závodszky P, Abaturov L B and Varsavszkij J M (1966) [-100017294]
  Structure of glyceraldehyde-3-phosphate dehydrogenase and its alteration by coenzyme binding
  Acta Biochim Biophys Acad Sci Hung 1, 389-402
140.   Markovich DS, Závodszky P and Volkenshteĭn MV (1966) [4296593]
  [Conformational changes in lactic dehydrogenase under inhibition]
  Doklady Akademii Nauk Sssr 170, 204-5
141.   Markovich DS, Závodszky P and Vol\'kenshteĭn MV (1966) [6001322]
  [On the structure of D-glyceraldehyde-3-phosphate dehydrogenase]
  Biokhimiia 31, 873-7
142.   Bolotina IA, Volkenshteĭn MV, Závodszky P and Markovich DS (1966) [4299363]
  [Polarimetric studies of the conformational changes in D-glyceric aldehyde-3-phosphate dehydrogenase]
  Biokhimiia 31, 649-53
143.   Závodszky P (1965) [-100017293]
  Ultracentrifugal studies on dissociable protein systems
  1, 1-10

Books or book chapters

1.   Szilagyi A, Kardos J, Osvath Sz, Barna L and Zavodszky P (2007)
  Protein folding
  Handbook of Neurochemistry and Molecular Neurobiology 7, Chapter 10
2.   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
3.   Zavodszky P, Vonderviszt F, Lakatos S, Kilar F, Simon I, Torok J, Sziva D and Sarvari M (1986)
  Domain sructure and signal transduction within antibody molecules
  Multidomain proteins 157, 157-173