Publications

Sneideris, M. Ziaunys, B. K.-Y. Chu, R. P.-Y. Chen, and V. Smirnovas, “Self-Replication of Prion Protein Fragment 89-230 Amyloid Fibrils Accelerated by Prion Protein Fragment 107-143 Aggregates,” International Journal of Molecular Sciences, vol. 21, no. 19, doi: 10.3390/ijms21197410.

Sakalauskas, M. Ziaunys, and V. Smirnovas, “Gallic acid oxidation products alter the formation pathway of insulin amyloid fibrils,” Scientific Reports, vol. 10, Art. no. 14466, Sep. 2020, doi: 10.1038/s41598-020-70982-3.

Pampuscenko, R. Morkuniene, L. Krasauskas, V. Smirnovas, T. Tomita, and V. Borutaite, “Distinct Neurotoxic Effects of Extracellular Tau Species in Primary Neuronal-Glial Cultures,” Mol Neurobiol, Oct. 2020, doi: 10.1007/s12035-020-02150-7.

Musteikyte, M. Ziaunys, and V. Smirnovas, “Methylene blue inhibits nucleation and elongation of SOD1 amyloid fibrils,” PeerJ, vol. 8, p. e9719, Aug. 2020, doi: 10.7717/peerj.9719.

J. Pansieri et al., “Templating S100A9 amyloids on Aβ fibrillar surfaces revealed by charge detection mass spectrometry, microscopy, kinetic and microfluidic analyses,” Chem. Sci., Jun. 2020, doi: 10.1039/C9SC05905A.

Ziaunys, T. Sneideris, and V. Smirnovas, “Formation of distinct prion protein amyloid fibrils under identical experimental conditions,” Sci Rep, vol. 10, no. 1, pp. e4572, Mar. 2020, doi: 10.1038/s41598-020-61663-2.

Pampuscenko et al., “Extracellular tau induces microglial phagocytosis of living neurons in cell cultures,” Journal of Neurochemistry, e14940, Dec. 2019, doi: 10.1111/jnc.14940.

Ziaunys, K. Mikalauskaite, and V. Smirnovas, “Amyloidophilic Molecule Interactions on the Surface of Insulin Fibrils: Cooperative Binding and Fluorescence Quenching,” Sci Rep, vol. 9, no. 1, pp. e20303, Dec. 2019, doi: 10.1038/s41598-019-56788-y.

Sneideris et al., “The Environment Is a Key Factor in Determining the Anti-Amyloid Efficacy of EGCG,” Biomolecules, vol. 9, no. 12, p. 855, Dec. 2019, doi: 10.3390/biom9120855.

Sakalauskas, M. Ziaunys, and V. Smirnovas, “Concentration-dependent polymorphism of insulin amyloid fibrils,” PeerJ, vol. 7, p. e8208, Dec. 2019, doi: 10.7717/peerj.8208.

Ziaunys, T. Sneideris, and V. Smirnovas, “Exploring the potential of deep-blue autofluorescence for monitoring amyloid fibril formation and dissociation,” PeerJ, vol. 7, p. e7554, Aug. 2019, doi: 10.7717/peerj.7554.

Ziaunys and V. Smirnovas, “Emergence of visible light optical properties of L-phenylalanine aggregates,” PeerJ, vol. 7, p. e6518, Feb. 2019, doi: 10.7717/peerj.6518.

Ziaunys and V. Smirnovas, “Additional Thioflavin-T Binding Mode in Insulin Fibril Inner Core Region,” J. Phys. Chem. B, vol. 123, no. 41, pp. 8727–8732, Oct. 2019, doi: 10.1021/acs.jpcb.9b08652.

Pansieri et al., “Pro-Inflammatory S100A9 Protein Aggregation Promoted by NCAM1 Peptide Constructs,” ACS Chem. Biol., vol. 14, no. 7, pp. 1410–1417, Jul. 2019, doi: 10.1021/acschembio.9b00394.

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, doi: 10.1039/C8CP04838J.

Kim et al., “Artificial strain of human prions created in vitro,” Nature Communications, vol. 9, no. 1, p. 2166, Jun. 2018, doi: 10.1038/s41467-018-04584-z.

Smirnovienė, V. Smirnovas, and D. Matulis, “Picomolar inhibitors of carbonic anhydrase: Importance of inhibition and binding assays,” Analytical Biochemistry, vol. 522, pp. 61–72, Apr. 2017, doi: 10.1016/j.ab.2017.01.022.

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, Aug. 2017, doi: 10.1021/acschemneuro.7b00251.

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, Aug. 2015, doi: 10.7717/peerj.1207.

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, doi: 10.1371/journal.pone.0136602.

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, Sep. 2015, doi: 10.7717/peerj.1271.

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, doi: 10.1371/journal.pone.0121231.

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, Jan. 2014, doi: 10.1371/journal.pone.0094469.

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, Nov. 2014, doi: 10.1021/jm501003k.

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, Jan. 2014, doi: 10.1074/jbc.M113.520718.

Milto, A. Botyriute, and V. Smirnovas, “Amyloid-Like Fibril Elongation Follows Michaelis-Menten Kinetics,” PLoS ONE, vol. 8, no. 7, pp. e68684–e68684, Jul. 2013, doi: 10.1371/journal.pone.0068684.

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, Mar. 2011, doi: 10.1038/nsmb.2035.

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, Sep. 2009, doi: 10.1074/jbc.M109.036558.

Smirnovas and R. Winter, “Revealing different aggregation pathways of amyloidogenic proteins by ultrasound velocimetry.,” Biophysical journal, vol. 94, no. 8, pp. 3241–3246, Apr. 2008, doi: 10.1529/biophysj.107.123133.

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, Jun. 2008, doi: 10.1021/bi800503j.

H. J. Lopes, V. Smirnovas, and R. Winter, “Islet amyloid polypeptide and high hydrostatic pressure: towards an understanding of the fibrillization process,” Journal of Physics: Conference Series, vol. 121, no. 11, pp. 112002–112002, Jul. 2008, doi: 10.1088/1742-6596/121/11/112002.

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, Jan. 2008, doi: 10.1002/anie.200703728.

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, Sep. 2008, doi: 10.1021/ma800785w.

Kraineva, V. Smirnovas, and R. Winter, “Effects of lipid confinement on insulin stability and amyloid formation,” Langmuir, vol. 23, no. 13, pp. 7118–7126, Jun. 2007, doi: 10.1021/la700405y.

Grudzielanek et al., “Cytotoxicity of Insulin within its Self-assembly and Amyloidogenic Pathways,” Journal of Molecular Biology, vol. 370, no. 2, pp. 372–384, Jul. 2007, doi: 10.1016/j.jmb.2007.04.053.

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, doi: 10.1016/j.chemphyslip.2007.05.006.

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, May 2006, doi: 10.1002/cphc.200500717.

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, Mar. 2006, doi: 10.1016/j.jmb.2005.11.075.

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, Jul. 2006, doi: 10.1021/bi060341a.

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, Oct. 2005, doi: 10.1021/jp053283w.

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, May 2005, doi: 10.1016/j.bpc.2005.01.003.

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, Apr. 2005, doi: 10.1039/b502255j.

Dzwolak et al., “Ethanol-perturbed amyloidogenic self-assembly of insulin: Looking for origins of amyloid strains,” Biochemistry, vol. 44, no. 25, pp. 8948–8958, Jun. 2005, doi: 10.1021/bi050281t.

Dzwolak, V. Smirnovas, R. Jansen, and R. Winter, “Insulin forms amyloid in a strain-dependent manner: an FT-IR spectroscopic study.,” Protein science : a publication of the Protein Society, vol. 13, no. 7, pp. 1927–1932, Jul. 2004, doi: 10.1110/ps.03607204.

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, doi: 10.1023/A:1027325120597.

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, doi: 10.1016/S0040-4039(01)01625-2.