M. Ziaunys, T. Sneideris, and V. Smirnovas, “Self-inhibition of insulin amyloid-like aggregation,” , Physical Chemistry Chemical Physics, vol. 20, no. 43, pp. 27638–27645, 2018.

C. Kim et al., “Artificial strain of human prions created in vitro,” Nature Communications, vol. 9, no. 1, p. 2166, 2018.

I. A. Iashchishyn, D. Sulskis, M. Nguyen Ngoc, V. Smirnovas, and L. A. Morozova-Roche, “Finke–Watzky Two-Step Nucleation–Autocatalysis Model of S100A9 Amyloid Formation: Protein Misfolding as ‘Nucleation’ Event,” ACS Chemical Neuroscience, vol. 8, no. 10, pp. 2152–2158, 2017.

J. Smirnovienė, V. Smirnovas, and D. Matulis, “Picomolar inhibitors of carbonic anhydrase: Importance of inhibition and binding assays,” Analytical Biochemistry, vol. 522, pp. 61–72, 2017.

T. Sneideris, K. Milto, and V. Smirnovas, “Polymorphism of amyloid-like fibrils can be defined by the concentration of seeds.,” PeerJ, vol. 3, pp. e1207–e1207, 2015.

T. Sneideris, D. Darguzis, A. Botyriute, M. Grigaliunas, R. Winter, and V. Smirnovas, “pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils.,” PloS one, vol. 10, no. 8, pp. e0136602–e0136602, 2015.

T. Šneideris, L. Baranauskienė, J. G. Cannon, R. Rutkienė, R. Meškys, and V. Smirnovas, “Looking for a generic inhibitor of amyloid-like fibril formation among flavone derivatives.,” PeerJ, vol. 3, pp. e1271–e1271, 2015.

R. Malisauskas, A. Botyriute, J. G. Cannon, and V. Smirnovas, “Flavone derivatives as inhibitors of insulin amyloid-like fibril formation.,” PloS one, vol. 10, no. 3, pp. e0121231–e0121231, 2015.

K. Milto, K. Michailova, and V. Smirnovas, “Elongation of mouse prion protein amyloid-like fibrils: Effect of temperature and denaturant concentration,” PLoS ONE, vol. 9, no. 4, pp. e94469–e94469, 2014.

V. Dudutienė et al., “Discovery and Characterization of Novel Selective Inhibitors of Carbonic Anhydrase IX,” Journal of Medicinal Chemistry, vol. 57, no. 22, pp. 9435–9446, 2014.

N. J. Cobb, M. I. Apostol, S. Chen, V. Smirnovas, and W. K. Surewicz, “Conformational stability of mammalian prion protein amyloid fibrils is dictated by a packing polymorphism within the core region,” Journal of Biological Chemistry, vol. 289, no. 5, pp. 2643–2650, 2014.

K. Milto, A. Botyriute, and V. Smirnovas, “Amyloid-Like Fibril Elongation Follows Michaelis-Menten Kinetics,” PLoS ONE, vol. 8, no. 7, pp. e68684–e68684, 2013.

V. Smirnovas, G. S. Baron, D. K. Offerdahl, G. J. Raymond, B. Caughey, and W. K. Surewicz, “Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange.,” Nature structural & molecular biology, vol. 18, pp. 504–506, 2011.

V. Smirnovas, J. I. Kim, X. Lu, R. Atarashi, B. Caughey, and W. K. Surewicz, “Distinct structures of scrapie prion protein (PrPSc)-seeded versus spontaneous recombinant prion protein fibrils revealed by hydrogen/deuterium exchange,” Journal of Biological Chemistry, vol. 284, no. 36, pp. 24233–24241, 2009.

V. Smirnovas and R. Winter, “Revealing different aggregation pathways of amyloidogenic proteins by ultrasound velocimetry.,” Biophysical journal, vol. 94, no. 8, pp. 3241–3246, 2008.

D. Radovan, V. Smirnovas, and R. Winter, “Effect of pressure on islet amyloid polypeptide aggregation: Revealing the polymorphic nature of the fibrillation process,” Biochemistry, vol. 47, no. 24, pp. 6352–6360, 2008.

M. Keerl, V. Smirnovas, R. Winter, and W. Richtering, “Interplay between hydrogen bonding and macromolecular architecture leading to unusual phase behavior in thermosensitive microgels,” Angewandte Chemie – International Edition, vol. 47, no. 2, pp. 338–341, 2008.

M. Keerl, V. Smirnovas, R. Winter, and W. Richtering, “Copolymer microgels from mono- And disubstituted acrylamides: Phase behavior and hydrogen bonds,” Macromolecules, vol. 41, no. 18, pp. 6830–6836, 2008.

J. Kraineva, V. Smirnovas, and R. Winter, “Effects of lipid confinement on insulin stability and amyloid formation,” Langmuir, vol. 23, no. 13, pp. 7118–7126, 2007.

S. Grudzielanek et al., “Cytotoxicity of Insulin within its Self-assembly and Amyloidogenic Pathways,” Journal of Molecular Biology, vol. 370, no. 2, pp. 372–384, 2007.

S. Grudzielanek, V. Smirnovas, and R. Winter, “The effects of various membrane physical-chemical properties on the aggregation kinetics of insulin,” Chemistry and Physics of Lipids, vol. 149, no. 1–2, pp. 28–39, 2007.

V. Smirnovas, R. Winter, T. Funck, and W. Dzwolak, “Protein amyloidogenesis in the context of volume fluctuations: A case study on insulin,” ChemPhysChem, vol. 7, no. 5, pp. 1046–1049, 2006.

S. Grudzielanek, V. Smirnovas, and R. Winter, “Solvation-assisted pressure tuning of insulin fibrillation: From novel aggregation pathways to biotechnological applications,” Journal of Molecular Biology, vol. 356, no. 2, pp. 497–509, 2006.

W. Dzwolak, A. Loksztejn, and V. Smirnovas, “New insights into the self-assembly of insulin amyloid fibrils: An H-D exchange FT-IR study,” Biochemistry, vol. 45, no. 26, pp. 8143–8151, 2006.

V. Smirnovas, R. Winter, T. Funck, and W. Dzwolak, “Thermodynamic properties underlying the α-helix-to-β-sheet transition, aggregation, and amyloidogenesis of polylysine as probed by calorimetry, densimetry, and ultrasound velocimetry,” Journal of Physical Chemistry B, vol. 109, no. 41, pp. 19043–19045, 2005.

W. Dzwolak and V. Smirnovas, “A conformational alpha-helix to beta-sheet transition accompanies racemic self-assembly of polylysine: An FT-IR spectroscopic study,” Biophysical Chemistry, vol. 115, no. 1, pp. 49–54, 2005.

W. Dzwolak, R. Jansen, V. Smirnovas, A. Loksztejn, S. Porowski, and R. Winter, “Template-controlled conformational patterns of insulin fibrillar self-assembly reflect history of solvation of the amyloid nuclei.,” Physical chemistry chemical physics : PCCP, vol. 7, no. 7, pp. 1349–1351, 2005.

W. Dzwolak et al., “Ethanol-perturbed amyloidogenic self-assembly of insulin: Looking for origins of amyloid strains,” Biochemistry, vol. 44, no. 25, pp. 8948–8958, 2005.

W. Dzwolak, V. Smirnovas, R. Jansen, and R. Winter, “Insulin forms amyloid in a strain-dependent manner: an FT-IR spectroscopic study.,” Protein science, vol. 13, no. 7, pp. 1927–1932, 2004.

Z. Bumeliene et al., “Determination of the dissociation constant and stoichiometry of a complex of the protein interferon alpha-2b with cibacron blue F3G-A,” Journal of Analytical Chemistry, vol. 58, no. 11, pp. 1038–1041, 2003.

M. Kažemėkaitė, A. Bulovas, V. Smirnovas, G. Niaura, E. Butkus, and V. Razumas, “Synthesis of new SAM-forming ferrocene derivatives and their interfacial properties on gold,” Tetrahedron Letters, vol. 42, no. 43, pp. 7691–7694, Oct. 2001.