Biotechnologijos institutas yra  mokslinių tyrimų institucija, siekianti užtikrinti valstybės pažangą sparčiai besivystančiose gyvybės mokslų ir biotechnologijų srityse, plėtoti tarptautinio lygio molekulinės biotechnologijos tyrimus, skatinti tarpdisciplininius tyrimus bei mokslo ir verslo bendradarbiavimą

Biotermodinamikos ir vaistų tyrimo skyrius • Mokslinės publikacijos

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Straipsnių kalbos taisymui siūlome American Journal Experts

Petrauskas, V., Gylytė, J., Toleikis, Z., Cimmperman, P., Matulis, D. 2013. Volume of Hsp90 ligand binding and the unfolding phase diagram as a function of pressure and temperature.  Eur Biophys J, 42:355-362.

Baranauskienė, L., Matulis, D. 2012. Intrinsic thermodynamics of ethoxzolamide inhibitor binding to human carbonic anhydrase XIII.  BMC Biophys, 5:12.

Pirrie, L., McCarthy, A., Major, L., Morkūnaitė, V., Zubrienė, A., Matulis, D., Lain, S., Lebl, T., Westwood, N. 2012. Discovery and Validation of SIRT2 Inhibitors Based on Tenovin-6: Use of a 1H-NMR Method to Assess Deacetylase Activity. Molecules, 17:12206-12224.

Sharp, S., and Roe, M., Kazlauskas, E., Čikotienė, I., Workman, P., Matulis, D., Prodromou, C. 2012. Co-Crystalization and In Vitro Biological Characterization of 5-Aryl-4-(5-Substituted-2-4-Dihydroxyphenyl)-1,2,3-Thiadiazole Hsp90 Inhibitors. PLoS ONE, 7:e44642.

Čapkauskaitė, E., Zubrienė, A., Baranauskienė, L., Tamulaitienė, G., Manakova, E., Kairys, V., Gražulis, S., Tumkevičius, S., Matulis, D. 2012. Design of [(2-pyrimidinylthio)acetyl]benzenesulfonamides as inhibitors of human carbonic anhydrases. European Journal of Medicinal Chemistry, 51:259-270.

Toleikis, Z. and Cimmperman, P. and Petrauskas, V. and Matulis, D. 2012 Serum albumin ligand binding volumes using high pressure denaturation. Journal of Chemical Thermodynamics, 52:24-29.

Norvaišas, P., Petrauskas, V., Matulis, D. 2012 Thermodynamics of cationic and anionic surfactant interaction. J Phys Chem B, 116:2138-2144. 

Labanauskas, L., Dudutiene, V., Urbelis, G., Sarlauskas, J., Sudzius, J., Matulis, D., Striela, R., Zilinskas, A. 2012. Synthesis of substituted 2λ4δ2-[1,2,3]thiadiazolo[3,4-c]benzimid-azoles and 2λ4δ2-[1,2,3,5]thiatriazolo[3,4-c]benzimidazoles. ARKIVOC, VIII:17-26. 

Giessrigl, B., Krieger, S., Rosner, M., Huttary, N., Saiko, P., Alami, M., Messaoudi, S., Peyrat, J., and Maciuk, A., Gollinger, M., Kopf, S., Kazlauskas, E., Mazal, P., Szekeres, T., Hengstschläger, M., Matulis, D., Jäger, W., Krupitza, G. 2012. Hsp90 stabilises Cdc25A and counteracts heat shock mediated Cdc25A degradation and cell cycle attenuation in pancreatic carcinoma cells. Hum Mol Genet, 21: 4615-4627.

Kazlauskas, E., Petrikaite, V., Michailoviene, V., Revuckiene, J., Matuliene, J., Grinius, L., Matulis, D. 2012. Thermodynamics of Aryl-Dihydroxyphenyl-Thiadiazole Binding to Human Hsp90. PLoS ONE, 7:e36899.

Cimmperman, P. and Matulis, D. 2011. Protein Thermal Denaturation Measurements via a Fluorescent Dye. Invited review to the book: RSC Biomolecular Sciences No. 22. Biophysical Approaches Determining Ligand Binding to Biomolecular Targets: Detection, Measurement and Modelling. Edited by A. Podjarny, A. Dejaegere, and B. Kieffer. Royal Society of Chemistry. Chapter 8.

Petrikaite, V. and Matulis, D. 2011. Binding of natural and synthetic inhibitors to human heat shock protein 90 and their clinical application. Medicina (Kaunas), 47:413-420.

Zubriene, A. and Kazlauskas, E. and Baranauskiene, L. and Petrauskas, V. and Matulis, D. 2011. Isothermal titration calorimetry and thermal shift assay in drug design. European pharmaceutical review, 16:56-59.

Toleikis, Z., Cimmperman, P., Petrauskas, V., Matulis, D. 2011. Determination of the volume changes induced by ligand binding to heat shock protein 90 using high-pressure denaturation. Anal Biochem. 413(2):171-178.

Petrikaite, V. and Matulis, D. 2011. Thermodynamics of Natural and Synthetic Inhibitor Binding to Human Hsp90. Knygoje "Application of Thermodynamics to Biological and Materials Science" Redag. Mizutani Tadashi, p. 77-92, ISBN: 978-953-307-980-6.

Rink, C., Sasse, F., Zubrienė, A., Matulis, D., Maier, ME. 2010. Probing the influence of an allylic methyl group in zearalenone analogues on binding to Hsp90. Chemistry. 16(48):14469-14478.

Zubrienė, A., Gutkowska, M., Matulienė, J., Chaleckis, R., Michailovienė, V., Voroncova, A., Venclovas, C., Zylicz, A., Zylicz, M., Matulis, D. 2010. Thermodynamics of radicicol binding to human Hsp90 alpha and beta isoforms. Biophys Chem, 152(1-3):153-163.

Čapkauskaitė, E., Baranauskienė, L., Golovenko, D., Manakova, E., Gražulis, S., Tumkevičius, S., Matulis, D. 2010. Indapamide-like benzenesulfonamides as inhibitors of carbonic anhydrases I, II, VII, and XIII. Bioorg Med Chem, 18(21):7357-7364.

Sūdžius, J., Baranauskienė, L., Golovenko, D., Matulienė, J., Michailovienė, V., Torresan, J., Jachno, J., Sukackaitė, R., Manakova, E., Gražulis, S., Tumkevičius, S., Matulis, D. 2010. 4-[N-(substituted 4-pyrimidinyl)amino]benzenesulfonamides as inhibitors of carbonic anhydrase isozymes I, II, VII, and XIII. Bioorg Med Chem, 18(21):7413-7421.

Baranauskienė, L., Hilvo, M., Matulienė, J., Golovenko, D., Manakova, E., Dudutienė, V., Michailovienė, V., Torresan, J., Jachno, J., Parkkila, S., Maresca, A., Supuran, C. T., Gražulis, S., and Matulis, D. 2010. Inhibition and binding studies of carbonic anhydrase isozymes I, II and IX with benzimidazo[1,2-c][1,2,3]thiadiazole-7-sulfonamides, J Enz Inhib Med Chem, 25(6):863-870.

Zurawska, A., Urbanski, J., Matulienė, J., Baraniak, J., Klejman, M. P., Filipek, S., Matulis, D., Bieganowski, P. 2010, Mutations that increase both Hsp90 ATPase activity in vitro and Hsp90 drug resistance in vivo. BBA – Molec Cell Res, 1803(5):575-583.
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Labanauskas, L., Dudutienė, V., Matulis, D., Urbelis, G. 2009, Synthesis of a new heterocyclic system: 3 phenylbenzimidazo [1,2-c]-[1,2,3]selenadiazole . Chem Heterocycl Comp No. 9, 1435-1436.

Ugele, M., Sasse, F., Knapp, S., Fedorov, O., Zubriene, A., Matulis, D., Maier ME. 2009. Propionate Analogues of Zearalenone Bind to Hsp90. Chembiochem, 10(13):2203-2212. Supp

Baranauskienė, L., Petrikaitė, V., Matulienė, J., Matulis, D. 2009. Titration Calorimetry Standards and the Precision of Isothermal Titration Calorimetry Data. Int J Mol Sci, 10:2752-2762.

Zubrienė, A., Matulienė, J., Baranauskienė, L., Jachno, J., Torresan, J., Michailovienė, V., Cimmperman, P., Matulis, D. 2009. Measurement of Nanomolar Dissociation Constants by Titration Calorimetry and Thermal Shift Assay – Radicicol Binding to Hsp90 and Ethoxzolamide Binding to CAII. Int J Mol Sci, 10:2662-2680.

Cikotiene, I., Kazlauskas, E., Matuliene, J., Michailoviene, V.,Torresan, J., Jachno, J., Matulis, D. 2009. 5-Aryl-4-(5-substituted-2,4- dihydroxyphenyl)-1,2,3-thiadiazoles as inhibitors of Hsp90 chaperone. Bioorg Med Chem Lett, 19:1089-1092.

Hilvo, M., Baranauskiene, L., Salzano, A.M., Scaloni, A., Matulis, D., Innocenti, A., Scozzafava, A., Monti, S.M., Di Fiore, A., De Simone, G., Lindfors, M., Jänis, J., Valjakka, J., Pastoreková, S., Pastorek, J., Kulomaa, M.S., Nordlund, H.R., Supuran, C.T., Parkkila, S. 2008 Biochemical characterization of CA IX: one of the most active carbonic anhydrase isozymes J Biol Chem, 283: 27799-27809. [+Suppl.]

Cimmperman, P., Baranauskiene, L., Jachimoviciute, S.,Jachno, J., Torresan, J., Michailoviene, V., Matuliene, J., Sereikaite, J., Bumelis, V., Matulis, D. 2008. A Quantitative Model of Thermal Stabilization and Destabilization of Proteins by Ligands. Biophys J, 95:3222-3231.

Baranauskienė, L., Matulienė, J., Matulis, D. 2008. Determination of the thermodynamics of carbonic anhydrase acid-unfolding by titration calorimetry. J Biochem Biophys Meth, 70:1043–1047.

Zaveckas, M., Žvirblienė, A., Žvirblis, G., Chmieliauskaitė, V., Bumelis, V., Pesliakas, H. 2007. Effect of surface histidine mutations and their number on the partitioning and refolding of recombinant human granulocyte-colony stimulating factor (Cys17Ser) in aqueous two-phase systems containing chelated metal ions. J Chromatogr B, 852:409-419.

Dudutienė, V., Baranauskienė, L., Matulis, D. 2007. Benzimidazo[1,2-c][1,2,3]thiadiazole-7-sulfonamides as inhibitors of carbonic anhydrase. Bioorg Med Chem Lett, 17: 3335-3338.

Matulis, D., Kranz, J., Salemme, F.R., and Todd, M.J. 2005. Thermodynamic stability of carbonic anhydrase: measurements of binding affinity and stoichiometry using ThermoFluor. Biochemistry, 44, 5258-66.

Matulis, D. and Todd, M. 2004. Thermodynamics – structure correlations of sulfonamide inhibitor binding to carbonic anhydrase. In “Biocalorimetry 2“, eds. Ladbury, J.E. and Doyle, M.L. Wiley. 107-132.

Matulis, D., Rouzina, I., and Bloomfield, V. 2002. Thermodynamics of cationic lipid binding to DNA and DNA condensation: Roles of electrostatics and hydrophobicity. J Am Chem Soc, 124, 7331-7342.

Matulis, D., and Bloomfield, V. 2001. Thermodynamics of the hydrophobic effect. I. Coupling of aggregation and pKa shifts in solutions of aliphatic amines. Biophys Chem, 93: 37-51.

Matulis, D., and Bloomfield, V. 2001. Thermodynamics of the hydrophobic effect. II. Calorimetric measurement of enthalpy, entropy, and heat capacity of aggregation of alkylamines and long aliphatic chains. Biophys Chem, 93: 53-65.

Matulis, D. 2001. Thermodynamics of the hydrophobic effect. III. Condensation and aggregation of alkanes, alcohols, and alkylamines. Biophys Chem, 93: 67-82.

Lovrien, R., Wu, C., and Matulis, D. 2000. Ligand - protein coprecipitative isolation by matrix stacking and entanglement. Sep Sci Technol, 35(11): 1795-1811.

Matulis, D., Rouzina, I., and Bloomfield, V. 2000. Thermodynamics of DNA binding and condensation: isothermal titration calorimetry and electrostatic mechanism. J Mol Biol, 296: 1053-1063.

Matulis, D., Baumann, C., Bloomfield, V., and Lovrien, R. 1999. 1-Anilino-8-naphthalene sulfonate as a protein conformational tightening agent. Biopol, 49: 451-458.

Matulis, D., Wu, C., Pham, T., Guy, C., and, Lovrien, R. 1999. Protection of enzymes by aromatic sulfonates from inactivation by acid and elevated temperatures. J Molec Catalysis B: Enzymatic. 7: 21-36.

Matulis, D., and Lovrien, R. 1998. 1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation. Biophys J, 74: 422-429.

Wu, C., Lovrien, R., and Matulis, D. 1998. Lectin coprecipitative isolation from crudes by little rock orange ligand. Analyt Biochem, 257: 33-39.

Rubikas, J., and Matulis, D. 1998. Nickel resistance in Escherichia coli V38 isolated from city sewage sludge. Ekologija. 9: 24-28. 3. Rubikas, J., and Matulis, D. 1998. Nickel ion efflux is the main mechanism of resistance in Escherichia coli V38. Ekologija, 9: 29-32.

Matulis, D., Lovrien, R. 1997. Selective Precipitation of Proteins. Curr Prot Prot Sc: 4.5.1-4.5.36.

Rubikas, J., Matulis, D., Leipus, A., and Urbaitienė, D. 1997. Nickel resistance in Escherichia Coli V38 is dependent on the concentration used for induction. FEMS Microbiol Lett, 155: 193-198.

Matulis, D., Richardson, T., and Lovrien, R. 1996. Coprecipitation of proteins with matrix ligands: scaleable protein isolation. J Molec Recogn, 9: 433-443.

Matulis, D., Lovrien, R. 1995. Assays for Total Protein. Curr Prot Prot Sc: 3.4.1-3.4.4.


Petrikaite, V., Kazlauskas, E., Matuliene, J., Matulis, D. 2011. Development of Hsp90 inhibitors as anticancer compounds. F1000 Posters.

 

 

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