prof. RNDr. Erik Sedlák, DrSc.

Current positions:

Head of Center for Interdisciplinary Biosciences
President of Slovak Biophysical Society
Member of the Comitee of Slovak Society for Biochemistry and Molecular Biology

Education:

1988 – 93: MSc. in Biophysics – P.J. Safarik University in Kosice
1993 – 97: Ph.D. study in Biochemistry – P.J. Safarik University in Kosice
2006 – Habilitation to Associate Professor in Chemistry – P.J. Safarik University in Kosice

Research interests:

Protein evolution of proteins/enzymes
Thermodynamics and kinetics stability of proteins, including immunoglobulins and membrane proteins such as GPCRs
Hofmeister effect on properties of proteins and enzymes
Conformational properties of proteins in regards with their function, e.g. cytochrome c, LOV domain, albumin

1988 – 93 MSc. in Biophysics – P.J. Šafárik University in Košice (UPJS)
1993 – 97 Ph.D. study in Biochemistry – UPJS
2006 Habilitation to Associate Professor in Chemistry – UPJS
2020 DrSc. in Biophysics – committee of Prof. Pavol Miškovský, DrSc.

Languages:

English, Slovak

Professional positions:

1996-1998 Research Associate in Biochemistry, UPJS
1999-2001 Research Scientist & Faculty Member in Biochemistry, UPJS
2002-2007 Research Scientist & Faculty Member in Biochemistry, UPJS
2003-2007 Head of Department of Biochemistry, UPJS
2007-2013 Several continual foreign stays
2010-2011 Associate Editor for Biochemistry in Chemical papers (Bratislava)
2011-2013 Editor in Chemical papers (Bratislava)
2013-presence Senior Research Associate at Center for Interdisciplinary Biosciences, UPJS
Associate Professor at Department of Biochemistry, UPJS
2018-presence Head of Center for Interdisciplinary Biosciences, Technology and Innovation Park, UPJS

Postdoctoral research training:

1994 (1 month), 1995 (3 months), 1997 (1 month), 2000 (2 months), 2002 (1 month) 2004 (1 month), 2005 (1 month) Laboratorium für Biochemie, Universität Bayreuth, Germany, with Prof. Dr. Mathias Sprinzl, Dr.h.c.
1998-1999 (21 months) Postdoctoral Research Associate in Biochemistry, The University of Texas Health Science Center, San Antonio, with Prof. Neal C. Robinson.

Project: “Functional Association of Cardiolipin with Cytochrome c Oxidase and bc1.”

2001-2002 (12 months) Postdoctoral Senior Research Associate in Biochemistry, The University of Texas Health Science Center, San Antonio, with Prof. Neal C. Robinson.
2003 (3 months) Project: “Function of Cardiolipin in Cytochrome c Oxidase and bc1.”
2007-2008 (18 months) Postdoctoral Senior Research Associate in Biochemistry, The Rice University, Houston, USA, with Assoc. Prof. Dr. Pernilla Wittung-Stafshede.

Project: “Folding mechanisms of copper transport proteins.”

2008-2009 (12 months) Postdoctoral Senior Research Associate in Biochemistry, The University of Texas Health Science Center, San Antonio, with Prof. Neal C. Robinson.

Project: “The functional and structural role of phospholipids bound to mitochondrial complexes.”

2009-2013 (46 months) Postdoctoral Associate in Biochemistry, The University of Zürich, Zürich, Switzerland with Prof. Dr. Andreas Plückthun.

Projekt: “ Conversion of integral membrane receptors into soluble forms ” (Marie-Curie Intra-European Fellowship)

2014 (4 months) Visiting Researcher in laboratory of Prof. Dr. Andeas Plückthun, Department of Biochemistry, The University of Zürich, Zürich, Switzerland
2016 (2 months) Visiting Researcher in laboratory of Prof. Dr. Andeas Plückthun, Department of Biochemistry, The University of Zürich, Zürich, Switzerland

Technical Expertise:

(i) Ribosome and Yeast displays – directed evolution methods for peptides/proteins.
(ii) Spectral techniques – absorbance spectroscopy, fluorescence and circular dichroism.
(iii) Differential scanning calorimetry – determination of thermodynamic parameters from microcalorimetric measurements of reversible and irreversible transitions; isothermal titration calorimetry.
(iv) Chromatography and analytical techniques (HPLC, FPLC), ELISA, Western blotting, SDS PAGE, with experience in analysis of experiments on analytical ultracentrifugation (from Center for Analytical Ultracentrifugation of Macromolecular Assemblies (CAUMA) in San Antonio).
(v) Protein purification (from heart tissue – cytochrome c oxidase, from bacteria – translation, elongation factors, heterologously expressed proteins).
(vi) Basic molecular biology, biochemical and biophysical methods.

Invited congress lectures:

7 lectures (international congresses) including 3 plenary lectures

Graduated PhD students (supervisor/co-supervisor 7(3)/2:

Kristína Mižáková „Use of the yeast display method for the expression and selection of new thrombolytics“ (in the process)
Monika Štulajterová „Purification and characterization of selected staphylokinase mutants“ (in the process)
Kristína Felčíková „Development of efficient genetically encoded photosensitizers“ (in the process)
2022 Veronika Dzurillová (thesis defense: UPJS) „Use of ribosome display in enzyme development“
2022 Veronika Talafová (thesis defense: UPJS) „Study of the biophysical properties of proteins derived from the fibrils of the European garden spider Araneus diadematus“
2022 Martin Berta (thesis defense: UPJS) „Study of the stability and solubility of selected G-protein coupled receptors“
2019 Martina Petrenčáková (as co-supervisor, thesis defense: UPJS) „Isolation and study of properties of the LOV2 domain from Avena sativa“
2019 Michal Nemergut (thesis defense: UPJS) „Study of biophysical properties of selected DARPins and antibodies“
2019 Eva Dušeková (thesis defense: UPJS) „The effect of Hofmeister salts on the properties of hydrolytic enzymes“
2014 Kamil Tóth (thesis defense: UPJS) „Characterization of binding interactions of NADH oxidase ligands from Thermus thermophilus in active sites and in external environmental modules“
2011 Nataša Tomášková (thesis defense: UPJS) „The effect of anions of the Hofmeister series on the properties of cytochrome c“
2006 Gabriel Žoldák (as co-supervisor, thesis defense: UPJS) „Conformational stability and its effect on the function of some multidomain thermophilic proteins from Thermus thermophilus“

Diploma students:

20 finished

Publications:

83 publications in international peer-reviewed journals (see WOS and Scopus databases), cited more than 1200 times, Hirsch index (Scopus) 25

Scientific projects (E.S. principal or co-principal investigator):

I. Science grant agency of the Ministry of education of the SR and of the Slovak Academy of Sciences (VEGA) (9)

2022-2025 VEGA 2/0034/22 (principal investigator)

Project: Study and modification of properties of spider protein overexpressed in Escherichia coli

2022-2024 VEGA 1/0074/22 (principal investigator)

Project: Modification of catalytic properties of haloalkane dehalogenases by protein evolution methods 2019-2021 VEGA 1/0175/19 (co-principal investigator)

Project: Aggregation of immunoglobulins and prediction of their colloidal stability by methods of advanced kinetic analyses

2017-2019 VEGA 2/0009/17 (20 990 €, co-principal investigator)

Project: Oxidative stress and phospholipid-protein interactions: functional and structural consequences

2016-2018 VEGA 1/0423/16 (39 478 €, principal investigator)

Project: Conversion of integral membrane receptor into water soluble form

2014-2016 VEGA 2/0062/14 (11 388 €, co-principal investigator)

Final evaluation: excellent results

Project: Functionality and Structural Integrity of Proteins in Bicelles – Implications for Mitochondrial and Amyloidogenic Proteins

2012-2014 VEGA 1/0521/12 (6 225 €, co-principal investigator)

Final evaluation: successful

Project: Modulation of protein dynamics and catalytical properties of enzymes by Hofmeister ions.

2007-2009 VEGA 1/4319/07 (18 787 €, co-principal investigator)

Final evaluation: successful

Project: Study of conformational, functional, and sequentional diversities of flavoproteins and chosen homodimeric oxidases.

2006-2008 VEGA 1/3252/06 (17 991 €, principal investigator)

Final evaluation: excellent results

Project: Stability and dynamics of chosen multidomain translational factors from thermophile bacteria Thermus thermophilus.

2004-2006 VEGA 1/1272/04 (18 190 €, co-principal investigator)

Final evaluation: successful

Project: Effect of polyanions on structure, stabilty, and solubility of proteins.

2003-2005 VEGA 1/0432/03 (22 737 €, principal investigator)

Final evaluation: successful

Project: Modulation of structural and functional properties of flavoproteinoxidases from thermophile Thermus thermophilus and mesophile Aspergillus niger by modification of solvent properties.

II. Slovak Research and Development Agency (APVV) (2)

2021-2025 APVV 20-0340 (215 000 €, principal investigator)
Project: Development of efficient genetically encoded photosensitizers
2016-2020 APVV 15-0069 (170 000 €, principal investigator)
Project: Conversion of integral membrane protein into water soluble form: the case of GPCR

Final evaluation: excellent results

III. Other grants:

2009-2011 Marie-Curie Intra-European Fellowship (~200 000 €, principal investigator)

2005 Deutsche Forschungsgemeinschaft in collaboration with Prof. Dr. Mathias Sprinzl, Dr.h.c., Universität Bayreuth, Germany (12 613 €, co-principal investigator)

2005 Development project awarded by Ministry of education of Slovak Republic (17 426 €, principal investigator)

List of Publications (first or corresponding author in 61):

(83) Hovanová V., Hovan A., Humenik M., Sedlák E. (2023) Only kosmotropic anions trigger fibrillization of the recombinant core spidroin eADF4(C16). Protein Sci. 32, e4832. IF₂₀₂₂ 8.0 Q1
(82) Hovanová V., Hovan A., Žoldák G., Sedlák E., *Humenik M. (2023) Global analysis of kinetics reveals the role of secondary nucleation in recombinant spider silk self-assembly. Protein Sci. 32, e4722. IF₂₀₂₂ 8.0 Q1
(81) Toul M., Slonková V., Mičan J., Urminsky A., Tomková M., Benešová I., Sedlák E., Bednář D., Damborský J., Hernychová L., Prokop Z. (2023) Analysis and Engineering of Glycosylation in Thrombolytics. Biotechnol. Adv. 66, 108174. IF₂₀₂₂ 16.0 Q1
(80) Džupponová V., Tomášková N., Antošová A., Sedlák E., Žoldák G. (2023) Salt-specific suppression of the cold denaturation of thermophilic multi-domain initiation factor 2. Int. J. Mol. Sci. 24, 6787. IF₂₀₂₂ 5.6 Q1
(79) Nemergut M., Sedláková D., Fabriciová G., Belej D., Jancura D., Sedlák E. (2023) Explanations of Inconsistency in Thermal Unfolding of Human Serum Albumin. Int. J. Biol. Macromol. 232, 123379. IF₂₀₂₂ 8.2 Q1
(78) Dušeková E., Garajová K., Yavaşer R., Tomková M., Sedláková D., Dzurillová V., Kulik N., Fadaei F., Shaposhnikova A., Minofar B., Sedlák E. (2022) Modulation of global stability, ligand binding, and catalytic properties of trypsin by anions. Biophys. Chem. 288, 106856. IF₂₀₂₁ 3.628 Q2
(77) Hovan A., Sedláková D., Berta M., Bánó G., Sedlák E. (2022) Singlet oxygen quenching as a probe of cytochrome c molten globule state formation. Phys. Chem. Chem. Phys. 24, 13317-13324. IF₂₀₂₁ 3.945 Q1
(76) Dušeková E., Berta M., Sedláková D., Řeha D., Dzurillová V., Shaposhnikova A., Fadaei F., Tomková M., Minofar B., Sedlák E. (2022) Specific effect of anions on properties of 3C protease. Biophys. Chem. 287, 106825. IF₂₀₂₁ 3.628 Q2
(75) Hovan A., Berta M., Sedláková D., Miškovský P., Bánó G., Sedlák E. (2021) Heme is responsible for enhanced singlet oxygen quenching in cytochrome c. Phys. Chem. Chem. Phys. 23, 15557-15563. IF₂₀₂₀ 3.676 Q1
(74) Nemergut M., Škrabana R., Berta M., Plückthun A., Sedlák E. (2021) Efficient purification of MBP fusion proteins on DARPin affinity matrix. Int. J. Biol. Macromol. 187, 105-112. IF₂₀₂₀ 6.953 Q1
(73) Tomášková N., Novák P, Kožár T., Petrenčáková M., Jancura D., Yassaghi G., Man P., Sedlák E. (2020) Early modification of cytochrome c by hydrogen peroxide triggers its fast degradation. Int. J. Biol. Macromol. 174, 413-423. IF₂₀₂₀ 6.953 Q1
(72) Sedlák E., Kožár T., Varhač R., Musatov A., Tomášková N. (2021) Anions specific effects on alkaline state of cytochrome c. Biochemistry (Moscow) 86(1), 59-73. IF₂₀₁₉ 2.487 Q2_(SJR)/Q4_(JCR)
(71) Sedlák E., Kožár T., Musatov A. (2020) (invited review) Interplay between aggregation state, subunits composition and tightly bound cardiolipin of bovine heart cytochrome c oxidase. Physiological relevance. Cells 9, 2588. IF₂₀₁₉ 4.366 Q2
(70) Garajová K., Sedláková D., Berta M., Gažová Z., Sedlák E. (2020) Destabilization effect of imidazolium ionic liquids cation-Hofmeister anion salts on cytochrome c. Int. J. Biol. Macromol. 164, 3808-3813. IF₂₀₁₉ 5.162 Q1
(69) Petrenčáková M., Filander F., Hovan A., Yassaghi G., Man P., Kožár T., Jancura D., Schwer M-S., Plückthun A., Novák P., Miškovský P., Bánó G., Sedlák E. (2020) Photoinduced damage of AsLOV2 domain is accompanied by increased singlet oxygen production due to flavin dissociation. Sci. Rep. 10: 4119. IF₂₀₁₈ 4.011 Q1
(68) Petrenčáková M., Varhač R., Nemergut M., Schwer M-S., Jancura D., Sedlák E. (2020) Conformational properties of LOV2 domain and its C450A variant within broad pH region. Biophys. Chem. 259, 106337. IF₂₀₁₈ 1.745 Q2
(67) Sedlák E., Sedláková D., Marek J., Hančár J., Garajová K., Žoldák G. (2019) Ion-specific protein/water interface determines Hofmeister effect on the kinetic stability of glucose oxidase. J. Phys. Chem. B 123, 7965-7973. IF₂₀₁₈ 2.923 Q1
(66) Šipošová K., Sedlák E., Kožár T., Nemergut M., Musatov A. (2019) Dual Effect of Non-ionic Detergent Triton X-100 on Insulin Amyloid Formation. Colloids and Surfaces B: Biointerfaces 173, 709-718. IF₂₀₁₇ 3.998 Q1
(65) Dušeková E., Garajová K., Yavaşer R., Varhač R., *Sedlák E. (2018) Hofmeister effect on catalytic properties of chymotrypsin is substrate-dependent. Biophys. Chem. 243, 8-16. IF₂₀₁₇ 1.870 Q2
(64) Tomášková N., Varhač R., Lysáková V., Musatov A., *Sedlák E. (2018) Peroxidase activity of cytochrome c in its compact state depends on dynamics of the heme region. Biochim. Biophys. Acta – Proteins & Proteomics 1866, 1073-1083. IF₂₀₁₇ 2.609 Q1
(63) ¹Schaefer J.V., ¹Sedlák E., Kast F., Nemergut M., *Plückthun A. (2018) Modification of kinetic stability of immunoglobin G by solvent additives. mAbs 10(4): 607-623. doi: 10.1080/ 19420862. IF₂₀₁₇ 5.165 Q
(62) *Sedlák E., Žoldák G., *Wittung-Stafshede P. (2018) Synergistic effects of copper sites on apparent stability of multicopper oxidase, Fet3p. Inter. J. Mol. Sci. 19, 269; doi: 10.3390/ ijms19010269. IF₂₀₁₇ 3.687 Q1
(61) Garajová K., Zimmermann M., Petrenčáková M., Dzurová L., Nemergut M., Škultéty Ľ, Žoldák G., *Sedlák E. (2017) The molten-globule residual structure is critical for reflavination of Glucose Oxidase. Biophys. Chem. 230, 74-83. IF₂₀₁₅ 2.402
(60) Nemergut M., Žoldák G., Schaefer J.V., Kast F., Miškovský P., *Plückthun A., *Sedlák E. (2017) Analysis of IgG kinetic stability by differential scanning calorimetry, probe fluorescence and light scattering. Protein Sci. 26, 2229-2239. IF₂₀₁₆ 2.523
(59) Sedlák E., *Musatov A. (2017) Inner mechanism of protection of mitochondrial electron-transfer proteins against oxidative damage. Focus on hydrogen peroxide decomposition. Minireview. Biochimie 142, 152-157. IF₂₀₁₆ 3.112
(58) Musatov A., *Sedlák E. (2017) Role of cardiolipin in stability of integral membrane proteins. Review. Biochimie 142, 102-111. IF₂₀₁₆ 3.112
(57) Žoldák G., Jancura D., *Sedlák E. (2017) Utilization of fluorescence ratio in determination of inflection point in pH, denaturant and temperature dependences. Protein Sci. 26(6), 1236-1239. IF₂₀₁₅ 3.039
(56) Garajová K., Balogová A., Dušeková E., Sedláková D., Sedlák E., *Varhač R. (2017) Correlation of lysozyme activity and stability in the presence of Hofmeister series anions. BBA – Proteins & Proteomics 1865(3), 281–288. IF₂₀₁₅ 3.016
(55) Musatov A., Varhač R., Hosler J.P., *Sedlák E. (2016) Delipidation of Cytochrome c Oxidase from Rhodobacter sphaeroides Destabilizes its Quaternary Structure. Biochimie 125, 23-31. IF₂₀₁₅ 3.017
(54) Schütz M., Schöppe J., Sedlák E., Hillebrand M., Nagy-Davidescu G., Egloff P, *Plückthun A. (2016) Directed evolution of G protein-coupled receptors in yeast for higher functional production in eukaryotic expression hosts. Sci. Reports. 6:21508. IF₂₀₁₅ 5.228
(53) Schütz M., Batyuk A. Klenk C., Kummer L., de Picciotto S., Gülbakan B., Wu Y., Newby G.A., Zosel F., Schöppe J., Sedlák E., Mittl P., Schuler B., Zenobi R., Wittrup K.D., *Plückthun A. (2016) Generation of fluorogen-activating designed ankyrin repeat proteins (FADAs) as versatile sensor tools. J. Mol. Biol. 428, 1272–1289. IF₂₀₁₅ 4.517
(52) Sedlák E. & *Robinson N.C. (2015) Destabilization of the Quaternary Structure of Bovine Heart Cytochrome c Oxidase upon Removal of Tightly Bound Cardiolipin. Biochemistry 54(36), 5569-77. IF₂₀₁₄ 3.015
(51) Poniková S., Antošová A., Demjen E, Sedláková D., Marek J., Varhač R., *Gažová Z. & *Sedlák E. (2015) Lysozyme stability and amyloid fibrillization dependence on Hofmeister anions in acidic pH. J. Biol. Inorg. Chem. 20, 921-933. IF₂₀₁₄ 2.538
(50) Varhač R., Sedláková D., Stupák M. & *Sedlák E. (2015) Non-two-state thermal denaturation of cytochrome c at neutral and slightly acidic pH. Biophys. Chem. 203-204, 41-50. doi: 10.1016/j.bpc.2015.05.002. IF₂₀₁₄ 1.986
(49) ¹Sedlák E., ¹Schaefer J.V., Marek J., Gimeson P. & *Plückthun A. (2015) Advanced Analyses of Kinetic Stabilities of IgGs modified by Mutations and Glycosylation. Protein Sci. 24(7), 1100-1113. doi: 10.1002/pro.2691. IF₂₀₁₄ 2.854
(48) *Sedlák E., Varhač R., Musatov A. & Robinson N.C. (2014) The Kinetic Stability of Cytochrome c Oxidase: Effect of Bound Phospholipid and Dimerization. Biophys. J. 107(12), 2932-2940. doi: 10.1016/j.bpj.2014.10.055. IF₂₀₁₃ 3.832
(47) Sedlák E., Fabián M., Robinson N.C. & *Musatov A. (2010) Ferricytochrome c Protects Cytochrome c Oxidase Against Hydrogen Peroxide-Induced Oxidative Damage. Free Radic. Biol. Med. 49(10), 1574-1581. IF₂₀₀₉ 6.081
(46) Ziegler L., Terzulli A, Sedlák E. & *Kosman D.J. (2010) Core Glycan in the Yeast Multicopper Ferroxidase, Fet3p: A Case Study of N-Linked Glycosylation, Protein Maturation and Stability. Protein Sci. 19, 1739-1750. IF₂₀₀₉ 2.937
(45) Auton M., Sowa K.E., Smith S.M., Sedlák E., Vijayan V. & *Cruz M.A. (2010) Destabilization of the A1 domain in Von Willebrand Factor dissociates the A1A2A3 tridomain and provokes spontaneous binding to Glycoprotein Ibα and platelet activation under shear stress. J. Biol. Chem. 285, 22831–22839. IF₂₀₀₉ 5.328
(44) Tomášková N., Varinská L. & *Sedlák E. (2010) Rate of oxidative damage of cytochrome c by hydrogen peroxide is modulated by Hofmeister anions. Gen. Phys. Biophys. 29, 255-265. IF₂₀₀₉ 0.741
(43) Tóth K., Sedlák E., Musatov A. & *Žoldák G. (2010) Activity of NADH oxidase from Thermus thermophilus in water/alcohol binary mixtures is limited by the stability of quaternary structure. J. Mol. Catal. B 64, 60–67. IF₂₀₀₉ 2.400
(42) *Sedlák E., Fedunová D., Veselá V., Sedláková D. & Antalík M. (2009) Polyanion hydrophobicity and protein basicity affect protein stability in protein-polyanion complexes. Biomacromolecules 10(9), 2533-2538.
(41) Sedlák E. & *Robinson N.C. (2009) Sequential dissociation of subunits from bovine heart cytochrome c oxidase by urea. Biochemistry 48, 8143-8150.
(40) Varhač R., Tomášková N., Fabián M. & *Sedlák E. (2009) Kinetics of cyanide binding as a probe of local stability/flexibility of cytochrome c. Biophys. Chem. 144(1-2), 21-26.
(39) Auton M., Sedlák E., Marek J., Wu T., Zu C, Moake J. & *Cruz M.A. (2009) Correlations Between Structural Stability and Catch to Slip Bond Transitions: Changes in Thermodynamic Stability of VWF caused by Type 2B (R1306Q and I1309V) and 2M (G1324S) von Willebrand Disease Mutations Differentially Affect the Force Dependent Binding to Platelet GPIb. Biophys. J. 97, 618–627.
(38) Sedlák E., Ziegler L., Kossman D.J. & *Wittung-Stafshede P. (2008) In vitro unfolding of yeast multi-copper oxidase Fet3p variants reveals unique role of each metal site. Proc. Natl. Acad. Sci. U.S.A. 105, 19257-19262.
(37) Rodriguez-Granillo A., Sedlák E. & Wittung-Stafshede P. (2008) Stability and ATP binding of the nucleotide-binding domain of the Wilson disease protein: Effect of the common H1069Q mutation. J. Mol. Biol. 383, 1097-1111.
(36) Sedlák E., Stagg L. & Wittung-Stafshede P. (2008) Effect of Hofmeister ions on protein thermal stability: Role of ion hydration and peptide groups? Arch. Biochem. Biophys. 479(1), 69-73.
(35) Sedlák E., Stagg L. & Wittung-Stafshede P. (2008) Role of cations of Desulfovibrio desulfuricans apoflavodoxin at neutral pH. Arch. Biochem. Biophys. 474(1), 128- 35.
(34) Žoldák G., *Sedlák E., Wolfrum A., Musatov A., Fedunová D., Szkaradkiewicz K. & Sprinzl M. (2008) Multi-domain initiation factor 2 from Thermus thermophilus consists of the individual autonomous domains. Biochemistry 47(17), 4992-5005.
(33) Tóth K., Sedlák E., Sprinzl M. & *Žoldák G. (2008) Hofmeister monovalent cation effect on function and stability of NADH oxidase from Thermus thermophilus. Biochim. Biophys. Acta 1784(5), 789-795.
(32) Sedlák E., Žoldák G. & *Wittung-Stafshede P. (2008) Role of copper in thermal stability of human ceruloplasmin. Biophys. J. 94, 1384–1391.
(31) Hussain F., Sedlák E. & *Wittung-Stafshede P. (2007) Role of copper in folding and stability of the cupredoxin-like copper carrier protein CopC. Arch. Biochem. Biophys. 467(1), 58-66.
(30) Sedlák E. & *Wittung-Stafshede P. (2007) Discrete Roles of Copper Ions in Chemical Unfolding of Human Ceruloplasmin. Biochemistry 46(33), 9638-9644.
(29) Staničová J., Sedlák E., Musatov A. & *Robinson N.C. (2007) Differential Stability of Dimeric and Monomeric Cytochrome c Oxidase Exposed to Elevated Hydrostatic Pressure. Biochemistry 46, 7146-7152.
(28) *Sedlák E. (2007) Characterization of polyanion-induced molten globule-like state of cytochrome c. Biopolymers 86(2), 119-126.
(27) Žoldák G, Redecke L, Svergun D, Konarev P, Vörtler S, Dobbek H, Sedlák E & *Sprinzl M. (2007) Release Factors 2 from Escherichia coli and Thermus thermophilus: structural, spectroscopic and microcalorimetric studies. Nucleic Acid Res. 35(4), 1343-1353.
(26) Tomášková N., Varhač R., Žoldák G., Olekšáková L., Sedláková D. & *Sedlák E. (2007) Conformational stability and dynamics of cytochrome c affect its alkaline isomerization. J. Biol. Inorg. Chem. 12(2), 257-266.
(25) Žoldák G., *Sedlák E., Valušová E., Wolfrum A., Marek J., Antalík M. & Sprinzl M. (2006) Irreversible thermal denaturation of elongation factor Ts from Thermus thermophilus. Effect of the residual structure and intermonomer disulphide bond. Biochim. Biophys. Acta 1764, 1277-1285.
(24) Hritz J., Žoldák G. & *Sedlák E. (2006) Cofactor assisted gating mechanism in the active site of NADH oxidase from Thermus thermophilus. Proteins 64(2), 465-476.
(23) Stupák M., Žoldák G., Musatov A., Sprinzl M. & *Sedlák E. (2006) Unusual effect of salts on the homodimeric structure of NADH oxidase from Thermus thermophilus in acidic pH. Biochim. Biophys. Acta 1764, 129-137.
(22) Sedlák E., Panda M., Dale M.P., Weintraub S.T. & Robinson N.C. (2006) Photo-Labeling the Cardiolipin Binding Subunits within Bovine Heart Cytochrome c Oxidase. Biochemistry 45(3), 746-754.
(21) Žoldák G., Musatov A., Stupák M., Sprinzl M. & *Sedlák E. (2005) pH-induced changes in activity and conformation of NADH oxidase from Thermus thermophilus. Gen. Phys. Biophys. 24(3), 279-298.
(20) Fedurco M., Augustynski J., Indiani C., Smulevich G., Antalík M., Bánó M., Sedlák E., Glascock M.C. & Dawson J.H. (2005) Electrochemistry of unfolded cytochrome c in neutral and acidic urea solutions. J. Am. Chem. Soc. 127(20), 7638-7646.
(19) Žoldák G., Zubrik A., Musatov A., Stupák M. & ^*Sedlák E. (2004) Irreversible thermal denaturation of Glucose oxidase from Aspergillus niger is the transition to the denatured state with residual structure. J. Biol. Chem. 279, 47601-47609.
(18) Fedurco M., Augustynski J., Indiani C., Smulevich G., Antalík M., Bánó M., Sedlák E., Glascock M.C. & Dawson J.H. (2004) The heme iron coordination structure of unfolded ferric and ferrous cytochrome c in neutral and acidic urea solutions. Spectroscopic and electrochemical studies. Biochim. Biophys. Acta-Proteins & Proteomics 1703, 31-41.
(17) Kristian P., Balentová E., Bernát J., Imrich J., Sedlák E., Danihel I., Böhm S., Prónayová N., Klika K.D., Pihlaja K. & Baranová J. (2004) Fluorescence and Structure of Methylated Acridin-9-yl thioureas. Chem. Pap. 58(4), 268-275.
(16) Balentová E., Bernát J., Kristian P., Imrich J., Sedlák E., Danihel I., Böhm S., Prónayová N., Pihlaja K., Klika K. D. (2004) Some interesting problems of acridin-9-yl thioureas methylation. Structure, fluorescence and biological properties of the obtained products. Collect. Czech. Chem. Commun. 69, 833-849.
(15) Žoldák G., Sprinzl M. & ^*Sedlák E. (2004) Modulation of activity of NADH oxidase from Thermus thermophilus through change in flexibility in the enzyme active site induced by Hofmeister series anions. Eur. J. Biochem. 271, 48-57.
(14) Žoldák G., Šuťák R., Antalík M., Sprinzl M. & ^*Sedlák E. (2003) Role of conformational flexibility for enzymatic activity in NADH oxidase from Thermus thermophilus. Eur. J. Biochem. 270, 4887-4897.
(13) ^*Sedlák E. & Antalík M. (2002). Effect of polyanion on the acidic conformational transition of native and denatured ferricytochrome c. Circular Dichroism study. Gen. Phys. Biophys. 21, 175-188.
(12) Janovec L., Suchár G., Imrich J., Kristian P., Sasinková V., Alföldi J. & Sedlák E. (2002) 9-isothiocyanatoanthracene as a versatile starting compound in the chemistry of anthracen-9-yl derivatives. Collect. Czech. Chem. Commun. 67, 665-678.
(11) ^*Sedlák E., Žoldák G., Antalík M. & Sprinzl M. (2002). Thermodynamic properties of nucleotide-free EF-Tu from Thermus thermophilus in the presence of low-molecular weight effectors of its GTPase activity. Biochim. Biophys. Acta- Protein Struct. Mol. Enzymol. 1597, 22-27.
(10) ^*Sedlák E., Sprinzl M., Grillenbeck N. & Antalík M. (2002) Microcalorimetric study of elongation factor Tu from Thermus thermophilus in nucleotide-free, GDP and GTP forms and in the presence of elongation factor Ts. Biochim. Biophys. Acta-Protein Struct. Mol. Enzymol. 1596, 357-365.
(9) Sedlák E., Valušová E., Nesper-Brock, M., Antalík M. & Sprinzl M. (2001) Effect of the central disulfide bond on the unfolding behavior of Elongation factor Ts from Thermus thermophilus. Biochemistry 40(32), 9579-9586.
(8) Valušová E., Sedlák E., Antalík M., Nock S. & Sprinzl M. (2001) Effect of N-domain on the stability of elongation factor Ts from Thermus thermophilus. Biochim. Biophys. Acta- Protein Struct. Mol. Enzymol.1547, 117-126.
(7) Kristian P., Bernát J., Imrich J., Sedlák E., Alföldi J. & Čornanič M. (2001) New approach to synthesis of N-substituted 9-amino/iminoacridines with important fluorescence properties. Heterocycles 55(2), 279-290.
(6) Sedlák E. & Robinson N.C. (1999) Phospholipase A₂ Digestion of Cardiolipin Bound to Bovine Cytochrome c Oxidase Alters both Activity and Quaternary Structure. Biochemistry 38(45), 14966-14972.
(5) Sedlák E. & Antalík M. (1999). Molten globule-like state of cytochrome c induced by polyanion poly(vinylsulphate) in slightly acidic pH. Biochim. Biophys. Acta 1434(2), 347-355.
(4) Nesper M., Nock S., Sedlák E., Antalík M., Podhradský D. & Sprinzl M. (1998) Dimers of Thermus thermophilus elongation factor Ts are required for its function as a nucleotide exchange factor of elongation factor Tu. Eur. J. Biochem. 255, 81-86.
(3) Sedlák E. & Antalík M. (1998) Coulombic and Noncoulombic Effect of Polyanions on Cytochrome c Structure. Biopolymers 46(3), 145-154.
(2) Sedlák E., Antalík M., Bágeľová J. & Fedurco M. (1997) Interaction of ferricytochrome c with polyanion Nafion. Biochim. Biophys. Acta-Bioenergetics 1319, 258-266.
(1) Sedlák E. (1997) Effect of polyanions on ferricytochrome c. Biochem. Mol. Biol. Int. 41(1), 25-32.

The best scientific work or collection of works of young scientist (under 35 years) in biophysics (granted by Slovak Biophysical Society; 2004)
Award of Minister of Education of Slovak Republic for Science and Technique in category of Established results of young workers in science and development to 35 years; 2004.
Marie-Curie Intra-European Fellowship (~200,000 Eur) (2009-2011) in laboratory of Prof. Dr. Andreas Plückthun, University of Zürich. Project: “ Conversion of integral membrane receptors into soluble forms