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Härmä, H., Tong-Ochoa, N., van Adrichem, AJ., Jelesarov, I., Wennerberg, K. & Kopra, K. Toward universal protein post-translational modification detection in high throughput format. Chem Commun (Camb). 54, 2910-2913 (2018) . PMID: 29498735.
Samatanga, B., Cléry, A., Barraud, P., Allain, FH. & Jelesarov, I. Comparative analyses of the thermodynamic RNA binding signatures of different types of RNA recognition motifs. Nucleic Acids Res. 45, 6037-6050 (2017). PMID: 28334819.
Beyer, C., Christen, P., Jelesarov, I. & Fröhlich, J. Real-time assessment of possible electromagnetic-field-induced changes in protein conformation and thermal stability. Bioelectromagnetics 35, 470-8 (2014). PMID: 25123495.
Bischofberger, I., Calzolari, DC., De Los Rios, P., Jelezarov, I. & Trappe, V. Hydrophobic hydration of poly-N-isopropyl acrylamide: a matter of the mean energetic state of water. Sci Rep 4, 4377 (2014). PMID: 24625553.
Walczak, MJ., Samatanga, B., van Drogen, F., Peter, M., Jelesarov, I. & Wider, G. The RING Domain of the Scaffold Protein Ste5 Adopts a Molten Globular Character with High Thermal and Chemical Stability. Angew. Chem. Int. Ed. Engl. 53, 1320-3 (2014).
Beyer, C, Christen, P., Jelesarov, I. & Fröhlich, J. Experimental system for real-time assessment of potential changes in protein conformation induced by electromagnetic fields. Bioelectromagnetics 34, 419-428 (2013).
Bjelic, S. & Jelesarov, I. Probing the energetic and kinetic impact of topologically conserved interactions in the SIV gp41 six-helix bundle. Biophys Chem. 171, 54-62 (2013).
Samatanga, B., Dominguez, C., Jelesarov, I. & Allain, FH. The high kinetic stability of a G-quadruplex limits hn RNP F qRRM3 binding to G-tract RNA. Nucleic Acids Res. 41, 2505-2516 (2013).
Bloem, R., Koziol, K., Waldauer, SA., Buchli, B., Walser, R., Samatanga, B., Jelesarov, I. & Hamm, P. Ligand binding studied by 2D IR spectroscopy using the azidohomoalanine label. J Phys Chem B. 116, 13705-13712 (2012).
Dreier, B., Mikheeva, G., Belousova, N., Parizek, P., Boczek, E., Jelesarov, I., Forrer, P., Plückthun, A. & Krasnykh, V. Her2-specific multivalent adapters confer designed tropism to adenovirus for gene targeting. J. Mol. Biol. 405, 410-426 (2011).
De Groot, CO., Jelesarov, I., Damberger, FF., Bjelic, S., Schaerer, MA., Bhavesh, NS., Grigoriev, I., Buey, RM., Wüthrich, K., Capitani, G., Akhmanova, A. & Steinmetz, MO. Molecular insights into mammalian end binding protein heterodimerization. J Biol. Chem. 285, 5802-5814 (2010).
Falconer, RJ., Penkova, A., Jelesarov, I. & Collins, BM: Survey of the year 2008: applications of isothermal titration calorimetry. J. Mol. Recognit. 23, 395-413 (2010).
Shalaby, T., von Bueren, AO., Hürlimann, ML., Fiaschetti, G., Casteletti, D., Masayuki, T., Nagasawa, K., Arcaro, A., Jelesarov, I., Shin-ya, K. & Grotzer, M. Disabling c-Myc in childhood medulloblastoma and atypical teratoid/rhabdoid tumor cells by the potent G-quadruplex interactive agent S2T1-6OTD. Mol Cancer Ther. 9, 167-179 (2010).
Binter, A., Staunig, N., Jelesarov, I., Lohner, K., Palfey, BA., Deller, S., Gruber, K., & Macheroux, P. A single intersubunit salt bridge affects oligomerization and catalytic activity in a bacterial quinone. FEBS J. 276, 5263-5274 (2009).
Honnappa S, Gouveia SM, Weisbrich A, Damberger FF, Bhavesh NS, Jawhari H, Grigoriev I, van Rijssel FJ, Buey RM, Lawera A, Jelesarov I, Winkler FK, Wüthrich K, Akhmanova A & Steinmetz MO. An EB1-binding motic acts as a microtubule tip localization signal. Cell 138, 366-376 (2009).
Jelesarov, I. & Karshikoff, A. Defining the role of salt bridges in protein stability. In: Shriver, JW. Protein structures, stability and interactions. Totowa, NJ, Chapter 10, pp. 227-260. Book Series: Methods in Mol. Biol. 490, (2009).
Bjelic, S. & Jelesarov, I. A survey of the year 2007 literature on applications of isothermal titration calorimetry. J. Mol. Recognit. 21, 289-312 (2008).
Bjelic, S., Wieninger, S., Jelesarov, I. & Karshikoff, A. Electrostatic contribution to the thermodynamic and kinetic stability of the homotrimeric coiled coil Lpp-56: A computational study. Proteins 70, 810-822 (2008).
Jelesarov, I. & Karshikoff, A. Meet to fold: the peculiar folding of oligomeric proteins. Biotechnology and Biotechnological Equipment 22, 598-605 (2008).
Karshikoff, A. & Jelesarov, I. Salt bridges and conformational flexibility: effect on protein stability. Biotechnology and Biotechnological Equipment 22, 606-611 (2008).
Okhrimenko, O. & Jelesarov, I. A survey of the year 2006 literature on applications of isothermal titration calorimetry. J. Mol. Recognit. 21, 1-19 (2008).
Vamvaca, K., Jelesarov, I & Hilvert, D. Kinetics and thermodynamics of ligand binding to a molten globular enzyme and its native counterpart. J Mol Biol. 382, 971-977 (2008).
Jelesarov, I. & Bosshard, HR. Isothermal titration calorimetry in studies of protein binding and protein conformational transitions. In "Protein Structures: Methods in Protein Structure Analysis." (Uversky, V. N. and E. A. Permyakov, Eds.), Nova Science Publishers, Inc., Hauppauge, N. Y. Chapter 1.2, pp. 29-55(2007).
Meier-Andrejszki, L., Bjelic, S., Naud, JF., Lavigne, P. & Jelesarov, I.Thermodynamics of b-HLH-LZ protein binding to DNA: the energetic importance of protein-DNA contacts in site-specific E-box recognition by the complete gene product of the Max p21 transcription factor. Biochemistry 46, 12427-12440 (2007).
Milev, S., Bjelic, S., Georgiev, O.& Jelesarov, I. Energeticss of peptide recognition by the second PDZ domain of human protein phosphatise 1E. Biochemistry 46, 1064-1078 (2007).
Schubert, M., Lapouge, K., Duss, O., Oberstrass, F.C., Jelesarov, I., Haas, D. & Allain, F.H. Molecular basis of messenger RNA recognition by the specific bacterial repressing clamp RsmA/CsrA. Nat. Struct. Mol. Biol. 14, 807-813 (2007).
Steinmetz, MO., Jelesarov, I., Matousek, WM., Honnappa, S., Jahnke, W., Missimer, JH., Frank, S., Alexandrescu, AT. & Kammerer RA. Molecular basis of coiled-coil formation. PNAS U. S. A. 104, 7062-7067 (2007).
Weisbrich, A., Honnappa, S., Jaussi, R., Okhrimenko, O., Frey, D., Jelesarov, I., Akhmanova, A. & Steinmetz, M.O. Structure-function relationship of the CAP-Gly domains. Nat. Struct. Mol. Biol. 14, 959-967 (2007).
Bjelic, S., Karshikoff, A. & Jelesarov, I. Stability and folding/unfolding kinetics of the homotrimeric coiled coil Lpp-56. Biochemistry, 45, 8931-8939 (2006).
Devi, V. S., Sprecher, C. B., Hunziker, P., Mittl, P. R. E., Bosshard, H. R. & Jelesarov, I. Disulfide formation and stability of a cysteine-rich repeat protein from Helicobacter pylori. Biochemistry 45, 1599-1607 (2006).
Deller, S., Sollner, S., Trenker-El-Toukhy, R., Jelesarov, I., Gubitz, G. M. & Macheroux, P. Characterization of a Thermostable NADPH:FMN Oxidoreductase from the Mesophilic Bacterium Bacillus subtilis.Biochemistry 45, 7083-7091(2006).
Honnappa, S., Okhrimenko, O., Jaussi, R., Jawhari, H., Jelesarov, I., Winkler, F. K. and Steinmetz, M. O. Mol. Cell 23, 663-671 (2006).
Milev, S., Bosshard, H. R. & Jelesarov, I. Enthalpic and entropic effects of salt and polyol osmolytes on site-specific protein-DNA association: The integrase Tn916-DNA complex. Biochemistry 44, 285-293 (2005).
Nishiyama, M., Horst, R., Eidam, O., Herrmann, T., Ignatov, O., Vetsch, M., Bettendorff, P., Jelesarov, I., Grutter, M. G., Wuthrich, K., Glockshuber, R. & Capitani, G. Structural basis of chaperone-subunit complex recognition by the type 1 pilus assembly platform FimD. EMBO J. 24, 2075-2086 (2005).
Bosshard, H. R., Marti, D. N. & Jelesarov, I. Protein stabilization by salt bridges: concepts, experimental approaches and clarification of some misunderstandings. J. Mol. Recognit. 17, 1-16 (2004).
Cranz, S., Berger, C., Baici, A., Jelesarov, I. & Bosshard, H. R. Monomeric and dimeric bZIP transcription factor GCN4 bind at the same rate to their target DNA site. Biochemistry 43, 718-727 (2004).
Devi, V. S., Binz, H. K., Stumpp, M. T., Pluckthun, A., Bosshard, H. R. & Jelesarov, I. Folding of a designed simple ankyrin repeat protein. Protein Sci. 13, 2864-2870 (2004).
Gorfe, A. A., Caflisch, A. & Jelesarov, I. The role of flexibility and hydration on the sequence-specific DNA recognition by the Tn916 integrase protein: a molecular dynamics analysis. J. Mol. Recognit. 17, 120-131 (2004).
Marti, D. N., Bjelic, S., Lu, M., Bosshard, H. R. & Jelesarov, I. Fast folding of the HIV-1 and SIV gp41 six-helix bundles. J. Mol. Biol. 336, 1-8 (2004).
Milev, S., Bosshard, H. R. & Jelesarov, I. in Biocalorimetry 2: Applications of Calorimetry in Biological Sciences (eds. Ladbury, J. E. & Doyle, M.) 189-202 (John Wiley & Sons, 2004).
Nasser, I., Mohsen, A. W., Jelesarov, I., Vockley, J., Macheroux, P. & Ghisla, S. Thermal unfolding of medium-chain acyl-CoA dehydrogenase and iso(3)valeryl-CoA dehydrogenase: study of the effect of genetic defects on enzyme stability. BBA-Molecular Basis of Disease 1690, 22-32 (2004).
Thomas, A. M., Ginj, C., Jelesarov, I., Amrhein, N. & Macheroux, P. Role of K22 and R120 in the covalent binding of the antibiotic fosfomycin and the substrate-induced conformational change in UDP-N-acetylglucosamine enolpyruvyl transferase. Eur. J. Biochem. 271, 2682-2690 (2004).
Gorfe, A. A. & Jelesarov, I. Energetics of sequence-specific protein-DNA association: Computational analysis of integrase Tn916 binding to its target DNA. Biochemistry 42, 11568-11576 (2003).
Grimshaw, J. P. A., Jelesarov, I., Siegenthaler, R. K. & Christen, P. Thermosensor action of GrpE - The DnaK chaperone system at heat shock temperatures. J. Biol. Chem. 278, 19048-19053 (2003).
Milev, S., Gorfe, A. A., Karshikoff, A., Clubb, R. T., Bosshard, H. R. & Jelesarov, I. Energetics of sequence-specific protein-DNA association: Conformational stability of the DNA binding domain of integrase Tn916 and its cognate DNA duplex. Biochemistry 42, 3492-3502 (2003).
Milev, S., Gorfe, A. A., Karshikoff, A., Clubb, R. T., Bosshard, H. R. & Jelesarov, I. Energetics of sequence-specific Protein-DNA association: Binding of integrase Tn916 to its target DNA. Biochemistry 42, 3481-3491 (2003).
Nishlyama, M., Vetsch, M., Puorger, C., Jelesarov, I. & Glockshuber, R. Identification and characterization of the chaperone-subunit complex-binding domain from the type 1 pilus assembly platform FimD. J. Mol. Biol. 330, 513-525 (2003).
Ellgaard, L., Bettendorff, P., Braun, D., Herrmann, T., Fiorito, F., Jelesarov, M., Guntert, P., Helenius, A. & Wuthrich, K. NMR structures of 36 and 73-residue fragments of the calreticulin P-domain. J. Mol. Biol. 322, 773-784 (2002).
Frickel, E. M., Riek, R., Jelesarov, I., Helenius, A., Wuthrich, K. & Ellgaard, L. TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain. PNAS U.S.A. 99, 1954-1959 (2002).
Gorfe, A. A., Ferrara, P., Caflisch, A., Marti, D. N., Bosshard, H. R. & Jelesarov, I. Calculation of protein ionization equilibria with conformational sampling: pK(a) of a model leucine zipper, GCN4 and barnase. Proteins: Struct. Funct. Genet. 46, 41-60 (2002).
Phelan, P., Gorfe, A. A., Jelesarov, I., Marti, D. N., Warwicker, J. & Bosshard, H. R. Salt bridges destabilize a leucine zipper designed for maximized ion pairing between helices. Biochemistry 41, 2998-3008 (2002).
Bosshard, H. R., Durr, E., Hitz, T. & Jelesarov, I. Energetics of coiled coil folding: The nature of the transition states. Biochemistry 40, 3544-3552 (2001).
Fitzpatrick, T. B., Killer, P., Thomas, R. M., Jelesarov, I., Amrhein, N. & Macheroux, P. Chorismate synthase from the hyperthermophile Thermotoga maritima combines thermostability and increased rigidity with catalytic and spectral properties similar to mesophilic counterparts. J. Biol. Chem. 276, 18052-18059 (2001).
Grimshaw, J. P. A., Jelesarov, I., Schonfeld, H. J. & Christen, P. Reversible thermal transition in GrpE, the nucleotide exchange factor of the DnaK heat-shock system. J. Biol. Chem. 276, 6098-6104 (2001).
Jelesarov, I. & Lu, M. Thermodynamics of trimer-of-hairpins formation by the SIV gp41 envelope protein. J. Mol. Biol. 307, 637-656 (2001).
Samland, A. K., Jelesarov, I., Kuhn, R., Amrhein, N. & Macheroux, P. Thermodynamic characterization of ligand-induced conformational changes in UDP-N-acetylglucosamine enolpyruvyl transferase. Biochemistry 40, 9950-9956 (2001).
Durr, E. & Jelesarov, I. Thermodynamic analysis of cavity creating mutations in an engineered leucine zipper and energetics of glycerol-induced coiled coil stabilization. Biochemistry 39, 4472-4482 (2000).
Marti, D. N., Jelesarov, I. & Bosshard, H. R. Interhelical ion pairing in coiled coils: Solution structure of a heterodimeric leucine zipper and determination of pK(a) values of Glu side chains. Biochemistry 39, 12804-12818 (2000).
Perozzo, R., Jelesarov, I., Bosshard, H. R., Folkers, G. & Scapozza, L. Compulsory order of substrate binding to herpes simplex virus type 1 thymidine kinase - A calorimetric study. J. Biol. Chem. 275, 16139-16145 (2000).
Read, C. M. & Jelesarov, I. in Protein-DNA Interactions. Principles and Protocols. (ed. Moss, T.) (Humana Press, Totowa, NJ, 2000).
Durr, E., Jelesarov, I. & Bosshard, H. R. Extremely fast folding of a very stable leucine zipper with a strengthened hydrophobic core and lacking electrostatic interactions between helices. Biochemistry 38, 870-880 (1999).
Jelesarov, I., Crane-Robinson, C. & Privalov, P. L. The energetics of HMG box interactions with DNA: Thermodynamic description of the target DNA duplexes. J. Mol. Biol. 294, 981-995 (1999).
Jelesarov, I. & Bosshard, H. R. Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition. J. Mol. Recognit. 12, 3-18 (1999).
Privalov, P. L., Jelesarov, I., Read, C. M., Dragan, A. I. & Crane-Robinson, C. The energetics of HMG box interactions with DNA: Thermodynamics of the DNA binding of the HMG box from mouse Sox-5. J. Mol. Biol. 294, 997-1013 (1999).
Jelesarov, I., Durr, E., Thomas, R. M. & Bosshard, H. R. Salt effects on hydrophobic interaction and charge screening in the folding of a negatively charged peptide to a coiled coil (leucine zipper). Biochemistry 37, 7539-7550 (1998).
Weber-Bornhauser, S., Eggenberger, J., Jelesarov, I., Bernard, A., Berger, C. & Bosshard, H. R. Thermodynamics and kinetics of the reaction of a single-chain antibody fragment (scFv) with the leucine zipper domain of transcription factor GCN4. Biochemistry 37, 13011-13020 (1998).
Wendt, H., Leder, L., Harma, H., Jelesarov, I., Baici, A. & Bosshard, H. R. Very rapid, ionic strength-dependent association and folding of a heterodimeric leucine zipper. Biochemistry 36, 204-213 (1997).
Jelesarov, I., Leder, L. & Bosshard, H. R. Probing the energetics of antigen-antibody recognition by titration microcalorimetry. METHODS: A Companion to Meth. Enzymol. 9, 533-541 (1996).
Jelesarov, I. & Bosshard, H. R. in Protein Structures: Methods in Protein Structure Analysis (eds. Uversky, V. N. & Permyakov, E. A.) in press (Nova Science Publishers, Hauppauge, NY, 1996).
Jelesarov, I. & Bosshard, H. R. Thermodynamic characterization of the coupled folding and association of heterodimeric coiled coils (Leucine tippers). J. Mol. Biol. 263, 344-358 (1996).
Jelesarov, I. & Bosshard, H. R. Folding energetics of a heterodimeric leucine zipper. Prog. Biophys. Mol. Biol. 65, Pa402-Pa402 (1996).
Berger, C., Jelesarov, I. & Bosshard, H. R. Coupled folding and site-specific binding of the GCN4-bZIP transcription factor to the AP-1 and ATF/CREB DNA sites studied by microcalorimetry. Biochemistry 35, 14984-14991 (1996).
Bisang, C., Weber, C., Inglis, J., Schiffer, C. A., Vangunsteren, W. F., Jelesarov, I., Bosshard, H. R. & Robinson, J. A. Stabilization of Type-I Beta-Turn Conformations in Peptides Containing the Npna-Repeat Motif of the Plasmodium-Falciparum Circumsporozoite Protein by Substituting Proline for (S)-Alpha-Methylproline. J. Am. Chem. Soc. 117, 7904-7915 (1995).
Jelesarov, I. & Bosshard, H. R. in Perspectives on Protein Engineering (eds. Geisow, M. J. & Epton, R.) 273-274 (1995).
Leder, L., Berger, C., Bornhauser, S., Wendt, H., Ackermann, F., Jelesarov, I. & Bosshard, H. R. Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide antibody recognition. Biochemistry 34, 16509-16518 (1995).
Jelesarov, I. & Bosshard, H. R. Thermodynamics of Ferredoxin Binding to Ferredoxin-Nadp(+) Reductase and the Role of Water at the Complex Interface. Biochemistry 33, 13321-13328 (1994).
Leder, L., Wendt, H., Schwab, C., Jelesarov, I., Bornhauser, S., Ackermann, F. & Bosshard, H. R. Genuine and Apparent Cross-Reaction of Polyclonal Antibodies to Proteins and Peptides. Eur. J. Biochem. 219, 73-81 (1994).
Jelesarov, I., Depascalis, A. R., Koppenol, W. H., Hirasawa, M., Knaff, D. B. & Bosshard, H. R. Ferredoxin Binding-Site on Ferredoxin - Nadp+ Reductase - Differential Chemical Modification of Free and Ferredoxin-Bound Enzyme. Eur. J. Biochem. 216, 57-66 (1993).
De Pascalis, A. R., Jelesarov, I., Ackermann, F., Koppenol, W. H., Hirasawa, M., Knaff, D. B. & Bosshard, H. R. Binding of Ferredoxin to Ferredoxin-Nadp+ Oxidoreductase - the Role of Carboxyl Groups, Electrostatic Surface-Potential, and Molecular Dipole-Moment. Protein Sci. 2, 1126-1135 (1993).
Tchilian, E., Jelesarov, I. & Hadjiivanova, H. Effect of ginsenoside Rg1 on insulin binding in mice liver and brain membranes. Phytotherapy Res. 5, 46-48 (1991).
Tchilian, E., Jelesarov, I., Ilkov, A. & Kojouharova, M. A purified insulin receptor as a probe for its immunochemical study. Comptes Renduz. Bulg. Acad. Sci. 43, 57-60 (1990).
Tchilian, E., Jelesarov, I. & Hadjiivanova, H. 125-I-Insulin binding is decreased in olfactory bulbs of aged rats. Neuropeptides 17, 193-196 (1990).