{"id":76,"date":"2017-09-15T11:49:29","date_gmt":"2017-09-15T11:49:29","guid":{"rendered":"http:\/\/web.vu.lt\/bti\/v.smirnovas\/?page_id=76"},"modified":"2026-08-26T09:15:20","modified_gmt":"2026-08-26T09:15:20","slug":"publications","status":"publish","type":"page","link":"http:\/\/web.vu.lt\/bti\/v.smirnovas\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"

Rapalyt\u0117, S.; Karalkevi\u010di\u016bt\u0117, V.; Baronait\u0117, I.; Veiveris, D.; Smirnovas, V.; \u017diaunys, M.; \u0160ulskis, D. Liquid-Liquid Phase Separation and Amyloid Aggregation in the 14-3-3 Protein Family. International Journal of Biological Macromolecules<\/i> 2026<\/b>, 368<\/i>, 152660. https:\/\/doi.org\/10.1016\/j.ijbiomac.2026.152660<\/a>.
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\nSnie\u010dkut\u0117, R.; \u0160ulskis, D.; Jocyt\u0117, A.; Venclovait\u0117, U.; Tamulyt\u0117, R.; \u017diaunys, M.; Smirnovas, V.; Sakalauskas, A. Formation of Condition-Dependent Alpha-Synuclein Fibril Strain in Artificial Cerebrospinal Fluid. Advanced Science<\/i> 2026<\/b>, 13<\/i> (7), e05228. https:\/\/doi.org\/10.1002\/advs.202505228<\/a>.
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\nSzwachta, G.; Sulskis, D.; Konopka, A.; Jalonicka, E.; Struniawski, K.; Mikalauskaite, K.; Sakalauskas, A.; Kozera, R.; Smirnovas, V.; Stsiapura, V.; Ziaunys, M.; Hanczyc, P. Collective Methodological Emission Assay of Thioflavin T for Qualitative \u03b1-Synuclein Fibril Structures Discrimination. International Journal of Biological Macromolecules<\/i> 2026<\/b>, 335<\/i>, 148994. https:\/\/doi.org\/10.1016\/j.ijbiomac.2025.148994<\/a>.
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\nKrasauskas, L.; Veiveris, D.; \u017diaunys, M.; \u0160ulskis, D.; Sakalauskas, A.; Smirnovas, V. Tau Enhances Aggregation of S100A9 Protein and Further Association of Its Fibrils. International Journal of Molecular Sciences<\/i> 2025<\/b>, 26<\/i> (18), 8961. https:\/\/doi.org\/10.3390\/ijms26188961<\/a>.
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\nKaralkevi\u010di\u016bt\u0117, V.; Baronait\u0117, I.; Pe\u0161tenyt\u0117, A.; Veiveris, D.; Usevi\u010dius, G.; \u0160im\u0117nas, M.; \u017diaunys, M.; Smirnovas, V.; \u0160ulskis, D. Calcium-Dependent S100A8 Amyloid Fibril Formation via S100A1-Mediated Transient Interaction. ACS Chem. Neurosci.<\/i> 2025<\/b>, 16<\/i> (14), 2592\u20132601. https:\/\/doi.org\/10.1021\/acschemneuro.5c00086<\/a>.
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\nVeiveris, D.; Kopustas, A.; Sulskis, D.; Mikalauskaite, K.; Alsamsam, M. N.; Tutkus, M.; Smirnovas, V.; Ziaunys, M. Heterotypic Droplet Formation by Pro-Inflammatory S100A9 and Neurodegenerative Disease-Related \u03b1-Synuclein. Biomacromolecules<\/i> 2025<\/b>, 26<\/i> (6), 3525\u20133537. https:\/\/doi.org\/10.1021\/acs.biomac.5c00130<\/a>.
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\nPampuscenko, K.; Jankeviciute, S.; Morkuniene, R.; Sulskis, D.; Smirnovas, V.; Brown, G. C.; Borutaite, V. S100A9 Protein Activates Microglia and Stimulates Phagocytosis, Resulting in Synaptic and Neuronal Loss. Neurobiology of Disease<\/i> 2025<\/b>, 206<\/i>, 106817. https:\/\/doi.org\/10.1016\/j.nbd.2025.106817<\/a>.
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\nTamulyt\u0117, R.; Baronait\u0117, I.; \u0160ulskis, D.; Smirnovas, V.; Jankunec, M. Pro-Inflammatory S100A8 Protein Exhibits a Detergent-like Effect on Anionic Lipid Bilayers, as Imaged by High-Speed AFM. ACS Appl. Mater. Interfaces<\/i> 2025<\/b>, 17<\/i> (1), 2635\u20132647. https:\/\/doi.org\/10.1021\/acsami.4c18749<\/a>.
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\nMisi\u016bnait\u0117, I.; Mikalauskait\u0117, K.; Paulauskait\u0117, M.; Snie\u010dkut\u0117, R.; Smirnovas, V.; Bruk\u0161tus, A.; \u017diaunys, M.; \u017dutaut\u0117, I. Imidazo[2,1-b][1,3]Thiazine Derivatives as Potential Modulators of Alpha-Synuclein Amyloid Aggregation. ACS Chem. Neurosci.<\/i> 2024<\/b>, 15<\/i> (24), 4418\u20134430. https:\/\/doi.org\/10.1021\/acschemneuro.4c00451<\/a>.
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\nZiaunys, M.; Sulskis, D.; Veiveris, D.; Sakalauskas, A.; Mikalauskaite, K.; Smirnovas, V. Diverse Effects of Fluorescent Labels on Alpha-Synuclein Condensate Formation during Liquid-Liquid Phase Separation. International Journal of Biological Macromolecules<\/i> 2024<\/b>, 283<\/i>, 137688. https:\/\/doi.org\/10.1016\/j.ijbiomac.2024.137688<\/a>.
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\n\u017dvirblis, M.; Sakalauskas, A.; Ali Janvand, S. H.; Dudutien\u0117, V.; \u017diaunys, M.; Snie\u010dkut\u0117, R.; Otzen, D. E.; Smirnovas, V.; Matulis, D. Structure-Activity Relationship of Fluorinated Benzenesulfonamides as Inhibitors of Amyloid-\u03b2 Aggregation. Chemistry \u2013 A European Journal<\/i> 2024<\/b>, n\/a<\/i> (n\/a), e202402330. https:\/\/doi.org\/10.1002\/chem.202402330<\/a>.
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\nKitoka, K.; Lends, A.; Kucinskas, G.; Bula, A. L.; Krasauskas, L.; Smirnovas, V.; Zilkova, M.; Kovacech, B.; Skrabana, R.; Hritz, J.; Jaudzems, K. dGAE(297-391) Tau Fragment Promotes Formation of Chronic Traumatic Encephalopathy-Like Tau Filaments. Angewandte Chemie International Edition<\/i> 2024<\/b>, n\/a<\/i> (n\/a), e202407821. https:\/\/doi.org\/10.1002\/anie.202407821<\/a>.
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\nZiaunys, M.; Mikalauskaite, K.; Sakalauskas, A.; Smirnovas, V. Study of Insulin Aggregation and Fibril Structure under Different Environmental Conditions. International Journal of Molecular Sciences<\/i> 2024<\/b>, 25<\/i> (17), 9406. https:\/\/doi.org\/10.3390\/ijms25179406<\/a>.
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\nZiaunys, M.; Sulskis, D.; Veiveris, D.; Kopustas, A.; Snieckute, R.; Mikalauskaite, K.; Sakalauskas, A.; Tutkus, M.; Smirnovas, V. Liquid\u2013Liquid Phase Separation of Alpha-Synuclein Increases the Structural Variability of Fibrils Formed during Amyloid Aggregation. The FEBS Journal<\/i> 2024<\/b>, 291<\/i> (20), 4522\u20134538. https:\/\/doi.org\/10.1111\/febs.17244<\/a>.
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\nLeri, M.; Sun, D.; Svedru\u017eic, \u017d. M.; \u0160ulskis, D.; Smirnovas, V.; Stefani, M.; Morozova-Roche, L.; Bucciantini, M. Pro-Inflammatory Protein S100A9 Targeted by a Natural Molecule to Prevent Neurodegeneration Onset. International Journal of Biological Macromolecules<\/i> 2024<\/b>, 276<\/i>, 133838. https:\/\/doi.org\/10.1016\/j.ijbiomac.2024.133838<\/a>.
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\nZiaunys, M.; Sulskis, D.; Mikalauskaite, K.; Sakalauskas, A.; Snieckute, R.; Smirnovas, V. S100A9 Inhibits and Redirects Prion Protein 89-230 Fragment Amyloid Aggregation. Archives of Biochemistry and Biophysics<\/i> 2024<\/b>, 758<\/i>, 110087. https:\/\/doi.org\/10.1016\/j.abb.2024.110087<\/a>.
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\nToleikis, Z.; Paluch, P.; Kuc, E.; Petkus, J.; Sulskis, D.; Org-Tago, M.-L.; Samoson, A.; Smirnovas, V.; Stanek, J.; Lends, A. Solid-State NMR Backbone Chemical Shift Assignments of \u03b1-Synuclein Amyloid Fibrils at Fast MAS Regime. Biomol NMR Assign<\/i> 2024<\/b>. https:\/\/doi.org\/10.1007\/s12104-024-10186-2<\/a>.
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\nBaronait\u0117, I.; \u0160ulskis, D.; Kopu Stas, A.; Tutkus, M.; Smirnovas, V. Formation of Calprotectin Inhibits Amyloid Aggregation of S100A8 and S100A9 Proteins. ACS Chem Neurosci<\/em> 2024<\/strong>, 15<\/em> (9), 1915\u20131925. https:\/\/doi.org\/10.1021\/acschemneuro.4c00093<\/a>.
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\nGhosh, S.; Tamilselvi, S.; Williams, C.; Jayaweera, S. W.; Iashchishyn, I. A.; \u0160ulskis, D.; Gilthorpe, J. D.; Olofsson, A.; Smirnovas, V.; Svedru\u017ei\u0107, \u017d. M.; Morozova-Roche, L. A. ApoE Isoforms Inhibit Amyloid Aggregation of Proinflammatory Protein S100A9. International Journal of Molecular Sciences<\/em> 2024<\/strong>, 25<\/em> (4), 2114. https:\/\/doi.org\/10.3390\/ijms25042114<\/a>.
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\nNaaman, E.; Qarawani, A.; Ben-Zvi Elimelech, R.; Harel, M.; Sigal-Dror, S.; Safuri, S.; Smirnovas, V.; Baronaite, I.; Romanova, N. V.; Morozova-Roche, L. A.; Zayit-Soudry, S. The Surprising Nonlinear Effects of S100A9 Proteins in the Retina. ACS Chem. Neurosci.<\/em> 2024<\/strong>. https:\/\/doi.org\/10.1021\/acschemneuro.3c00650<\/a>.
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\n\u0160ulskis, D.; \u017diaunys, M.; Sakalauskas, A.; Snie\u010dkut\u0117, R.; Smirnovas, V. Formation of Amyloid Fibrils by the Regulatory 14-3-3\u03b6 Protein. Open Biology<\/em> 2024<\/strong>, 14<\/em> (1), 230285. https:\/\/doi.org\/10.1098\/rsob.230285<\/a>.
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\nZiaunys, M.; Mikalauskaite, K.; Sakalauskas, A.; Smirnovas, V. Investigating Lysozyme Amyloid Fibril Formation and Structural Variability Dependence on Its Initial Folding State under Different pH Conditions. Protein Science<\/em> 2024<\/strong>, 33<\/em> (2), e4888. https:\/\/doi.org\/10.1002\/pro.4888<\/a>.
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\nSanders, E.; Csondor, R.; \u0160ulskis, D.; Baronait\u0117, I.; Smirnovas, V.; Maheswaran, L.; Horrocks, J.; Munro, R.; Georgiadou, C.; Horvath, I.; Morozova-Roche, L. A.; Williamson, P. T. F. The Stabilization of S100A9 Structure by Calcium Inhibits the Formation of Amyloid Fibrils. Int J Mol Sci<\/em> 2023<\/strong>, 24<\/em> (17), 13200. https:\/\/doi.org\/10.3390\/ijms241713200<\/a>.
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\nPampuscenko, K.; Morkuniene, R.; Krasauskas, L.; Smirnovas, V.; Brown, G. C.; Borutaite, V. Extracellular Tau Stimulates Phagocytosis of Living Neurons by Activated Microglia via Toll-like 4 Receptor-NLRP3 Inflammasome-Caspase-1 Signalling Axis. Sci Rep<\/em> 2023<\/strong>, 13<\/em> (1), 10813. https:\/\/doi.org\/10.1038\/s41598-023-37887-3<\/a>.
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\nZiaunys, M.; Mikalauskaite, K.; Krasauskas, L.; Smirnovas, V. Conformation-Specific Association of Prion Protein Amyloid Aggregates with Tau Protein Monomers. International Journal of Molecular Sciences<\/em> 2023<\/strong>, 24<\/em> (11), 9277. https:\/\/doi.org\/10.3390\/ijms24119277<\/a>.
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\n\u0160ulskis, D.; \u0160neiderien\u0117, G.; \u017diaunys, M.; Smirnovas, V. The Seeding Barrier between Human and Syrian Hamster Prion Protein Amyloid Fibrils Is Determined by \u03922-\u03912 Loop Sequence Elements. International Journal of Biological Macromolecules<\/em> 2023<\/strong>, 238<\/em>, 124038. https:\/\/doi.org\/10.1016\/j.ijbiomac.2023.124038<\/a>.
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\nSakalauskas, A.; Ziaunys, M.; Snieckute, R.; Janoniene, A.; Veiveris, D.; Zvirblis, M.; Dudutiene, V.; Smirnovas, V. The Major Components of Cerebrospinal Fluid Dictate the Characteristics of Inhibitors against Amyloid-Beta Aggregation. International Journal of Molecular Sciences<\/em> 2023<\/strong>, 24<\/em> (6), 5991. https:\/\/doi.org\/10.3390\/ijms24065991<\/a>.
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\nTamulyt\u0117, R.; Jankaityt\u0117, E.; Toleikis, Z.; Smirnovas, V.; Jankunec, M. Pro-Inflammatory Protein S100A9 Alters Membrane Organization by Dispersing Ordered Domains. Biochimica et Biophysica Acta (BBA) – Biomembranes<\/em> 2023<\/strong>, 1865<\/em> (3), 184113. https:\/\/doi.org\/10.1016\/j.bbamem.2022.184113<\/a>.
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\nHadi Ali Janvand, S.; Ladefoged, L. K.; Zubrien\u0117, A.; Sakalauskas, A.; Christiansen, G.; Dudutien\u0117, V.; Schi\u00f8tt, B.; Matulis, D.; Smirnovas, V.; Otzen, D. E. Inhibitory Effects of Fluorinated Benzenesulfonamides on Insulin Fibrillation. International Journal of Biological Macromolecules<\/em> 2023<\/strong>, 227<\/em>, 590\u2013600. https:\/\/doi.org\/10.1016\/j.ijbiomac.2022.12.105<\/a>.
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\nAndrade-Talavera, Y.; Chen, G.; Pansieri, J.; Arroyo-Garc\u00eda, L. E.; Toleikis, Z.; Smirnovas, V.; Johansson, J.; Morozova-Roche, L.; Fisahn, A. S100A9 Amyloid Growth and S100A9 Fibril-Induced Impairment of Gamma Oscillations in Area CA3 of Mouse Hippocampus Ex Vivo Is Prevented by Bri2 BRICHOS. Progress in Neurobiology<\/em> 2022<\/strong>, 102366. https:\/\/doi.org\/10.1016\/j.pneurobio.2022.102366<\/a>.
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\nZiaunys, M.; Sakalauskas, A.; Mikalauskaite, K.; Smirnovas, V. Rapid Restructurization of Conformationally-Distinct Alpha-Synuclein Amyloid Fibrils at an Elevated Temperature. PeerJ<\/em> 2022<\/strong>, 10<\/em>, e14137. https:\/\/doi.org\/10.7717\/peerj.14137<\/a>.
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\nToleikis, Z.; Bobrovs, R.; Janoniene, A.; Lends, A.; Ziaunys, M.; Baronaite, I.; Petrauskas, V.; Kitoka, K.; Smirnovas, V.; Jaudzems, K. Interactions between S100A9 and Alpha-Synuclein: Insight from NMR Spectroscopy. International Journal of Molecular Sciences<\/em> 2022<\/strong>, 23<\/em> (12), 6781. https:\/\/doi.org\/10.3390\/ijms23126781<\/a>.
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\nZiaunys, M.; Smirnovas, V. Exploring Epigallocatechin-3-Gallate Autoxidation Products: Specific Incubation Times Required for Emergence of Anti-Amyloid Properties. Antioxidants<\/em> 2022<\/strong>, 11<\/em> (10), 1887. https:\/\/doi.org\/10.3390\/antiox11101887<\/a>.
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\nSakalauskas, A.; Janoniene, A.; Zvinys, G.; Mikalauskaite, K.; Ziaunys, M.; Smirnovas, V. Exploring the Formation of Polymers with Anti-Amyloid Properties within the 2\u20323\u2032-Dihydroxyflavone Autoxidation Process. Antioxidants<\/em> 2022<\/strong>, 11<\/em> (9), 1711. https:\/\/doi.org\/10.3390\/antiox11091711<\/a>.
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\nMikalauskaite, K.; Ziaunys, M.; Smirnovas, V. Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State. International Journal of Molecular Sciences<\/em> 2022<\/strong>, 23<\/em> (10), 5421. https:\/\/doi.org\/10.3390\/ijms23105421<\/a>.
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\nNagaraj, M.; Najarzadeh, Z.; Pansieri, J.; Biverst\u00e5l, H.; Musteikyte, G.; Smirnovas, V.; Matthews, S.; Emanuelsson, C.; Johansson, J.; Buxbaum, J. N.; Morozova-Roche, L.; Otzen, D. E. Chaperones Mainly Suppress Primary Nucleation during Formation of Functional Amyloid Required for Bacterial Biofilm Formation. Chem. Sci.<\/em> 2022<\/strong>, 13<\/em> (2), 536\u2013553. https:\/\/doi.org\/10.1039\/D1SC05790A<\/a>.
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\nZiaunys, M.; Mikalauskaite, K.; Veiveris, D.; Sakalauskas, A.; Smirnovas, V. Superoxide Dismutase-1 Alters the Rate of Prion Protein Aggregation and Resulting Fibril Conformation. Archives of Biochemistry and Biophysics<\/em> 2022<\/strong>, 715<\/em>, 109096. https:\/\/doi.org\/10.1016\/j.abb.2021.109096<\/a>.
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\nZiaunys, M.; Sakalauskas, A.; Mikalauskaite, K.; Smirnovas, V. Polymorphism of Alpha-Synuclein Amyloid Fibrils Depends on Ionic Strength and Protein Concentration. International Journal of Molecular Sciences<\/em> 2021<\/strong>, 22<\/em> (22), 12382. https:\/\/doi.org\/10.3390\/ijms222212382<\/a>.
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\nZiaunys, M.; Mikalauskaite, K.; Sakalauskas, A.; Smirnovas, V. Interplay between Epigallocatechin-3-Gallate and Ionic Strength during Amyloid Aggregation. PeerJ<\/em> 2021<\/strong>, 9<\/em>, e12381. https:\/\/doi.org\/10.7717\/peerj.12381<\/a>.
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\nArabuli, L.; Iashchishyn, I. A.; Romanova, N. V.; Musteikyte, G.; Smirnovas, V.; Chaudhary, H.; Svedru\u017ei\u0107, \u017d. M.; Morozova-Roche, L. A. Co-Aggregation of S100A9 with DOPA and Cyclen-Based Compounds Manifested in Amyloid Fibril Thickening without Altering Rates of Self-Assembly. International Journal of Molecular Sciences<\/em> 2021<\/strong>, 22<\/em> (16), 8556. https:\/\/doi.org\/10.3390\/ijms22168556<\/a>.
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\nStrazdaite, S.; Roeters, S. J.; Sakalauskas, A.; Sneideris, T.; Kirschner, J.; Pedersen, K. B.; Schi\u00f8tt, B.; Jensen, F.; Weidner, T.; Smirnovas, V.; Niaura, G. Interaction of Amyloid-\u03b2-(1\u201342) Peptide and Its Aggregates with Lipid\/Water Interfaces Probed by Vibrational Sum-Frequency Generation Spectroscopy. J. Phys. Chem. B<\/em> 2021<\/strong>. https:\/\/doi.org\/10.1021\/acs.jpcb.1c04882<\/a>.
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\nSakalauskas, A.; Ziaunys, M.; Snieckute, R.; Smirnovas, V. Autoxidation Enhances Anti-Amyloid Potential of Flavone Derivatives. Antioxidants<\/em> 2021<\/strong>, 10<\/em> (9), 1428. https:\/\/doi.org\/10.3390\/antiox10091428<\/a>.
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\nToleikis, Z.; Ziaunys, M.; Baranauskiene, L.; Petrauskas, V.; Jaudzems, K.; Smirnovas, V. S100A9 Alters the Pathway of Alpha-Synuclein Amyloid Aggregation. International Journal of Molecular Sciences<\/em> 2021<\/strong>, 22<\/em> (15), 7972. https:\/\/doi.org\/10.3390\/ijms22157972<\/a>.
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\nFridmanis, J.; Toleikis, Z.; Sneideris, T.; Ziaunys, M.; Bobrovs, R.; Smirnovas, V.; Jaudzems, K. Aggregation Condition\u2013Structure Relationship of Mouse Prion Protein Fibrils. International Journal of Molecular Sciences<\/em> 2021<\/strong>, 22<\/em> (17), 9635. https:\/\/doi.org\/10.3390\/ijms22179635<\/a>.
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\n\u010ciplys, E.; Pa\u0161kevi\u010dius, T.; \u017ditkus, E.; Bielskis, J.; Ra\u017eanskas, R.; \u0160neideris, T.; Smirnovas, V.; Kaupinis, A.; Tester, D. J.; Ackerman, M. J.; H\u00f8jrup, P.; Michalak, M.; Houen, G.; Slibinskas, R. Mapping Human Calreticulin Regions Important for Structural Stability. Biochimica et Biophysica Acta (BBA) – Proteins and Proteomics<\/em> 2021<\/strong>, 1869<\/em> (11), 140710. https:\/\/doi.org\/10.1016\/j.bbapap.2021.140710<\/a>.
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\nChaudhary, H.; Iashchishyn, I. A.; Romanova, N. V.; Rambaran, M. A.; Musteikyte, G.; Smirnovas, V.; Holmboe, M.; Ohlin, C. A.; Svedru\u017ei\u0107, \u017d. M.; Morozova-Roche, L. A. Polyoxometalates as Effective Nano-Inhibitors of Amyloid Aggregation of Pro-Inflammatory S100A9 Protein Involved in Neurodegenerative Diseases. ACS Appl. Mater. Interfaces<\/em> 2021<\/strong>, 13<\/em> (23), 26721\u201326734. https:\/\/doi.org\/10.1021\/acsami.1c04163<\/a>.
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\nLeri, M.; Chaudhary, H.; Iashchishyn, I. A.; Pansieri, J.; Svedru\u017ei\u0107, \u017d. M.; G\u00f3mez Alcalde, S.; Musteikyte, G.; Smirnovas, V.; Stefani, M.; Bucciantini, M.; Morozova-Roche, L. A. Natural Compound from Olive Oil Inhibits S100A9 Amyloid Formation and Cytotoxicity: Implications for Preventing Alzheimer\u2019s Disease. ACS Chem. Neurosci.<\/em> 2021<\/strong>, 12<\/em> (11), 1905\u20131918. https:\/\/doi.org\/10.1021\/acschemneuro.0c00828<\/a>.
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\nZiaunys, M.; Mikalauskaite, K.; Sakalauskas, A.; Smirnovas, V. Using Lysozyme Amyloid Fibrils as a Means of Scavenging Aggregation-Inhibiting Compounds. Biotechnology Journal<\/em> 2021<\/strong>, 16<\/em> (9), 2100138. https:\/\/doi.org\/10.1002\/biot.202100138<\/a>.
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\nKasho, K.; Krasauskas, L.; Smirnovas, V.; Stojkovi\u010d, G.; Morozova-Roche, L. A.; Wanrooij, S. Human Polymerase \u03b4-Interacting Protein 2 (PolDIP2) Inhibits the Formation of Human Tau Oligomers and Fibrils. International Journal of Molecular Sciences<\/em> 2021<\/strong>, 22<\/em> (11), 5768. https:\/\/doi.org\/10.3390\/ijms22115768<\/a>.
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\nZiaunys, M.; Sakalauskas, A.; Mikalauskaite, K.; Snieckute, R.; Smirnovas, V. Temperature-Dependent Structural Variability of Prion Protein Amyloid Fibrils. International Journal of Molecular Sciences<\/em> 2021<\/strong>, 22<\/em> (10), 5075. https:\/\/doi.org\/10.3390\/ijms22105075<\/a>.
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\nSzulc, N.; Burdukiewicz, M.; G\u0105sior-G\u0142ogowska, M.; Wojciechowski, J. W.; Chilimoniuk, J.; Mackiewicz, P.; \u0160neideris, T.; Smirnovas, V.; Kotulska, M. Bioinformatics Methods for Identification of Amyloidogenic Peptides Show Robustness to Misannotated Training Data. Scientific Reports<\/em> 2021<\/strong>, 11<\/em> (1), 8934. https:\/\/doi.org\/10.1038\/s41598-021-86530-6<\/a>.
\n—
\nZiaunys, M.; Sakalauskas, A.; Sneideris, T.; Smirnovas, V. Lysozyme Fibrils Alter the Mechanism of Insulin Amyloid Aggregation. International Journal of Molecular Sciences<\/em> 2021<\/strong>, 22<\/em> (4), 1775. https:\/\/doi.org\/10.3390\/ijms22041775<\/a>.
\n—
\nZiaunys, M.; Sakalauskas, A.; Mikalauskaite, K.; Smirnovas, V. Exploring the Occurrence of Thioflavin-T-Positive Insulin Amyloid Aggregation Intermediates. PeerJ<\/em> 2021<\/strong>, 9<\/em>, e10918. https:\/\/doi.org\/10.7717\/peerj.10918<\/a>.
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\nJurgelevi\u010di\u016bt\u0117, J.; Bi\u010dkovas, N.; Sakalauskas, A.; Novickij, V.; Smirnovas, V.; Lastauskien\u0117, E. Effects of Pulsed Electric Fields on Yeast with Prions and the Structure of Amyloid Fibrils. Applied Sciences<\/em> 2021<\/strong>, 11<\/em> (6), 2684. https:\/\/doi.org\/10.3390\/app11062684<\/a>.
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\nZiaunys, M.; Sneideris, T.; Smirnovas, V. Formation of Distinct Prion Protein Amyloid Fibrils under Identical Experimental Conditions. Scientific Reports<\/em> 2020<\/strong>, 10<\/em> (1), 4572. https:\/\/doi.org\/10.1038\/s41598-020-61663-2<\/a>.
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\nZiaunys, M.; Sakalauskas, A.; Smirnovas, V. Identifying Insulin Fibril Conformational Differences by Thioflavin-T Binding Characteristics. Biomacromolecules<\/em> 2020<\/strong>, 21<\/em> (12), 4989\u20134997. https:\/\/doi.org\/10.1021\/acs.biomac.0c01178<\/a>.
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\nSneideris, T.; Ziaunys, M.; Chu, B. K.-Y.; Chen, R. P.-Y.; Smirnovas, V. Self-Replication of Prion Protein Fragment 89-230 Amyloid Fibrils Accelerated by Prion Protein Fragment 107-143 Aggregates. International Journal of Molecular Sciences<\/em> 2020<\/strong>, 21<\/em> (19), 7410. https:\/\/doi.org\/10.3390\/ijms21197410<\/a>.
\n—
\nSakalauskas, A.; Ziaunys, M.; Smirnovas, V. Gallic Acid Oxidation Products Alter the Formation Pathway of Insulin Amyloid Fibrils. Scientific Reports<\/em> 2020<\/strong>, 10<\/em> (1), 14466. https:\/\/doi.org\/10.1038\/s41598-020-70982-3<\/a>.
\n—
\nPansieri, J.; Iashchishyn, I. A.; Fakhouri, H.; Ostoji\u0107, L.; Malisauskas, M.; Musteikyte, G.; Smirnovas, V.; Schneider, M. M.; Scheidt, T.; Xu, C. K.; Meisl, G.; Knowles, T. P. J.; Gazit, E.; Antoine, R.; Morozova-Roche, L. A. Templating S100A9 Amyloids on A\u03b2 Fibrillar Surfaces Revealed by Charge Detection Mass Spectrometry, Microscopy, Kinetic and Microfluidic Analyses. Chem. Sci.<\/em> 2020<\/strong>, 11<\/em> (27), 7031\u20137039. https:\/\/doi.org\/10.1039\/C9SC05905A<\/a>.
\n—
\nPampuscenko, K.; Morkuniene, R.; Sneideris, T.; Smirnovas, V.; Budvytyte, R.; Valincius, G.; Brown, G. C.; Borutaite, V. Extracellular Tau Induces Microglial Phagocytosis of Living Neurons in Cell Cultures. Journal of Neurochemistry<\/em> 2020<\/strong>, 154<\/em> (3), 316\u2013329. https:\/\/doi.org\/10.1111\/jnc.14940<\/a>.
\n—
\nPampuscenko, K.; Morkuniene, R.; Krasauskas, L.; Smirnovas, V.; Tomita, T.; Borutaite, V. Distinct Neurotoxic Effects of Extracellular Tau Species in Primary Neuronal-Glial Cultures. Mol Neurobiol<\/em> 2020<\/strong>. https:\/\/doi.org\/10.1007\/s12035-020-02150-7<\/a>.
\n—
\nMusteikyte, G.; Ziaunys, M.; Smirnovas, V. Methylene Blue Inhibits Nucleation and Elongation of SOD1 Amyloid Fibrils. PeerJ<\/em> 2020<\/strong>, 8<\/em>, e9719. https:\/\/doi.org\/10.7717\/peerj.9719<\/a>.
\n—
\nMikalauskaite, K.; Ziaunys, M.; Sneideris, T.; Smirnovas, V. Effect of Ionic Strength on Thioflavin-T Affinity to Amyloid Fibrils and Its Fluorescence Intensity. International Journal of Molecular Sciences<\/em> 2020<\/strong>, 21<\/em> (23), 8916. https:\/\/doi.org\/10.3390\/ijms21238916<\/a>.
\n—
\nMartins, P. M.; Navarro, S.; Silva, A.; Pinto, M. F.; S\u00e1rk\u00e1ny, Z.; Figueiredo, F.; Pereira, P. J. B.; Pinheiro, F.; Bednarikova, Z.; Burdukiewicz, M.; Galzitskaya, O. V.; Gazova, Z.; Gomes, C. M.; Pastore, A.; Serpell, L. C.; Skrabana, R.; Smirnovas, V.; Ziaunys, M.; Otzen, D. E.; Ventura, S.; Macedo-Ribeiro, S. MIRRAGGE \u2013 Minimum Information Required for Reproducible AGGregation Experiments. Front. Mol. Neurosci.<\/em> 2020<\/strong>, 13<\/em>. https:\/\/doi.org\/10.3389\/fnmol.2020.582488<\/a>.
\n—
\nZiaunys, M.; Sneideris, T.; Smirnovas, V. Exploring the Potential of Deep-Blue Autofluorescence for Monitoring Amyloid Fibril Formation and Dissociation. PeerJ<\/em> 2019<\/strong>, 7<\/em>, e7554. https:\/\/doi.org\/10.7717\/peerj.7554<\/a>.
\n—
\nZiaunys, M.; Smirnovas, V. Emergence of Visible Light Optical Properties of L-Phenylalanine Aggregates. PeerJ<\/em> 2019<\/strong>, 7<\/em>, e6518. https:\/\/doi.org\/10.7717\/peerj.6518<\/a>.
\n—
\nZiaunys, M.; Smirnovas, V. Additional Thioflavin-T Binding Mode in Insulin Fibril Inner Core Region. J. Phys. Chem. B<\/em> 2019<\/strong>, 123<\/em> (41), 8727\u20138732. https:\/\/doi.org\/10.1021\/acs.jpcb.9b08652<\/a>.
\n—
\nZiaunys, M.; Mikalauskaite, K.; Smirnovas, V. Amyloidophilic Molecule Interactions on the Surface of Insulin Fibrils: Cooperative Binding and Fluorescence Quenching. Scientific Reports<\/em> 2019<\/strong>, 9<\/em> (1), 20303. https:\/\/doi.org\/10.1038\/s41598-019-56788-y<\/a>.
\n—
\nSneideris, T.; Sakalauskas, A.; Sternke-Hoffmann, R.; Peduzzo, A.; Ziaunys, M.; Buell, A. K.; Smirnovas, V. The Environment Is a Key Factor in Determining the Anti-Amyloid Efficacy of EGCG. Biomolecules<\/em> 2019<\/strong>, 9<\/em> (12), 855. https:\/\/doi.org\/10.3390\/biom9120855<\/a>.
\n—
\nSakalauskas, A.; Ziaunys, M.; Smirnovas, V. Concentration-Dependent Polymorphism of Insulin Amyloid Fibrils. PeerJ<\/em> 2019<\/strong>, 7<\/em>, e8208. https:\/\/doi.org\/10.7717\/peerj.8208<\/a>.
\n—
\nPansieri, J.; Ostoji\u0107, L.; Iashchishyn, I. A.; Magzoub, M.; Wallin, C.; W\u00e4rml\u00e4nder, S. K. T. S.; Gr\u00e4slund, A.; Nguyen Ngoc, M.; Smirnovas, V.; Svedru\u017ei\u0107, \u017d.; Morozova-Roche, L. A. Pro-Inflammatory S100A9 Protein Aggregation Promoted by NCAM1 Peptide Constructs. ACS Chem. Biol.<\/em> 2019<\/strong>, 14<\/em> (7), 1410\u20131417. https:\/\/doi.org\/10.1021\/acschembio.9b00394<\/a>.
\n—
\nZiaunys, M.; Sneideris, T.; Smirnovas, V. Self-Inhibition of Insulin Amyloid-like Aggregation. Physical Chemistry Chemical Physics<\/em> 2018<\/strong>, 20<\/em> (43), 27638\u201327645. https:\/\/doi.org\/10.1039\/C8CP04838J<\/a>.
\n—
\nKim, C.; Xiao, X.; Chen, S.; Haldiman, T.; Smirnovas, V.; Kofskey, D.; Warren, M.; Surewicz, K.; Maurer, N. R.; Kong, Q.; Surewicz, W.; Safar, J. G. Artificial Strain of Human Prions Created in Vitro. Nature Communications<\/em> 2018<\/strong>, 9<\/em> (1), 2166. https:\/\/doi.org\/10.1038\/s41467-018-04584-z<\/a>.
\n—
\nSmirnovien\u0117, J.; Smirnovas, V.; Matulis, D. Picomolar Inhibitors of Carbonic Anhydrase: Importance of Inhibition and Binding Assays. Analytical Biochemistry<\/em> 2017<\/strong>, 522<\/em>, 61\u201372. https:\/\/doi.org\/10.1016\/j.ab.2017.01.022<\/a>.
\n—
\nIashchishyn, I. A.; Sulskis, D.; Nguyen Ngoc, M.; Smirnovas, V.; Morozova-Roche, L. A. Finke\u2013Watzky Two-Step Nucleation\u2013Autocatalysis Model of S100A9 Amyloid Formation: Protein Misfolding as \u201cNucleation\u201d Event. ACS Chemical Neuroscience<\/em> 2017<\/strong>, 8<\/em> (10), 2152\u20132158. https:\/\/doi.org\/10.1021\/acschemneuro.7b00251<\/a>.
\n—
\nSneideris, T.; Milto, K.; Smirnovas, V. Polymorphism of Amyloid-like Fibrils Can Be Defined by the Concentration of Seeds. PeerJ<\/em> 2015<\/strong>, 3<\/em>, e1207\u2013e1207. https:\/\/doi.org\/10.7717\/peerj.1207<\/a>.
\n—
\nSneideris, T.; Darguzis, D.; Botyriute, A.; Grigaliunas, M.; Winter, R.; Smirnovas, V. PH-Driven Polymorphism of Insulin Amyloid-Like Fibrils. PloS one<\/em> 2015<\/strong>, 10<\/em> (8), e0136602\u2013e0136602. https:\/\/doi.org\/10.1371\/journal.pone.0136602<\/a>.
\n—
\n\u0160neideris, T.; Baranauskien\u0117, L.; Cannon, J. G.; Rutkien\u0117, R.; Me\u0161kys, R.; Smirnovas, V. Looking for a Generic Inhibitor of Amyloid-like Fibril Formation among Flavone Derivatives. PeerJ<\/em> 2015<\/strong>, 3<\/em>, e1271\u2013e1271. https:\/\/doi.org\/10.7717\/peerj.1271<\/a>.
\n—
\nMalisauskas, R.; Botyriute, A.; Cannon, J. G.; Smirnovas, V. Flavone Derivatives as Inhibitors of Insulin Amyloid-like Fibril Formation. PloS one<\/em> 2015<\/strong>, 10<\/em> (3), e0121231. https:\/\/doi.org\/10.1371\/journal.pone.0121231<\/a>.
\n—
\nMilto, K.; Michailova, K.; Smirnovas, V. Elongation of Mouse Prion Protein Amyloid-like Fibrils: Effect of Temperature and Denaturant Concentration. PLoS ONE<\/em> 2014<\/strong>, 9<\/em> (4), e94469. https:\/\/doi.org\/10.1371\/journal.pone.0094469<\/a>.
\n—
\nDudutien\u0117, V.; Matulien\u0117, J.; Smirnov, A.; Timm, D. D.; Zubrien\u0117, A.; Baranauskien\u0117, L.; Morku\u0305nait\u0117, V.; Smirnovien\u0117, J.; Michailovien\u0117, V.; Juozapaitien\u0117, V.; Mickevi\u010diu\u0305t\u0117, A.; Kazokait\u0117, J.; Bak\u0161yt\u0117, S.; Kasiliauskait\u0117, A.; Jachno, J.; Revuckien\u0117, J.; Ki\u0161onait\u0117, M.; Pilipuityt\u0117, V.; Ivanauskait\u0117, E.; Milinavi\u010diu\u0305t\u0117, G.; Smirnovas, V.; Petrikait\u0117, V.; Kairys, V.; Petrauskas, V.; Norvai\u0161as, P.; Ling\u0117, D.; Gibie\u017ea, P.; \u010capkauskait\u0117, E.; Zak\u0161auskas, A.; Kazlauskas, E.; Manakova, E.; Gra\u017eulis, S.; Ladbury, J. E.; Matulis, D. Discovery and Characterization of Novel Selective Inhibitors of Carbonic Anhydrase IX. Journal of Medicinal Chemistry<\/em> 2014<\/strong>, 57<\/em> (22), 9435\u20139446. https:\/\/doi.org\/10.1021\/jm501003k<\/a>.
\n—
\nCobb, N. J.; Apostol, M. I.; Chen, S.; Smirnovas, V.; Surewicz, W. K. Conformational Stability of Mammalian Prion Protein Amyloid Fibrils Is Dictated by a Packing Polymorphism within the Core Region. Journal of Biological Chemistry<\/em> 2014<\/strong>, 289<\/em> (5), 2643\u20132650. https:\/\/doi.org\/10.1074\/jbc.M113.520718<\/a>.
\n—
\nMilto, K.; Botyriute, A.; Smirnovas, V. Amyloid-Like Fibril Elongation Follows Michaelis-Menten Kinetics. PLoS ONE<\/em> 2013<\/strong>, 8<\/em> (7), e68684. https:\/\/doi.org\/10.1371\/journal.pone.0068684<\/a>.
\n—
\nSmirnovas, V.; Baron, G. S.; Offerdahl, D. K.; Raymond, G. J.; Caughey, B.; Surewicz, W. K. Structural Organization of Brain-Derived Mammalian Prions Examined by Hydrogen-Deuterium Exchange. Nature structural & molecular biology<\/em> 2011<\/strong>, 18<\/em>, 504\u2013506. https:\/\/doi.org\/10.1038\/nsmb.2035<\/a>.
\n—
\nSmirnovas, V.; Kim, J. I.; Lu, X.; Atarashi, R.; Caughey, B.; Surewicz, W. K. Distinct Structures of Scrapie Prion Protein (PrPSc)-Seeded versus Spontaneous Recombinant Prion Protein Fibrils Revealed by Hydrogen\/Deuterium Exchange. Journal of Biological Chemistry<\/em> 2009<\/strong>, 284<\/em> (36), 24233\u201324241. https:\/\/doi.org\/10.1074\/jbc.M109.036558<\/a>.
\n—
\nSmirnovas, V.; Winter, R. Revealing Different Aggregation Pathways of Amyloidogenic Proteins by Ultrasound Velocimetry. Biophysical journal<\/em> 2008<\/strong>, 94<\/em> (8), 3241\u20133246. https:\/\/doi.org\/10.1529\/biophysj.107.123133<\/a>.
\n—
\nRadovan, D.; Smirnovas, V.; Winter, R. Effect of Pressure on Islet Amyloid Polypeptide Aggregation: Revealing the Polymorphic Nature of the Fibrillation Process. Biochemistry<\/em> 2008<\/strong>, 47<\/em> (24), 6352\u20136360. https:\/\/doi.org\/10.1021\/bi800503j<\/a>.
\n—
\nLopes, D. H. J.; Smirnovas, V.; Winter, R. Islet Amyloid Polypeptide and High Hydrostatic Pressure: Towards an Understanding of the Fibrillization Process. Journal of Physics: Conference Series<\/em> 2008<\/strong>, 121<\/em> (11), 112002\u2013112002. https:\/\/doi.org\/10.1088\/1742-6596\/121\/11\/112002<\/a>.
\n—
\nKeerl, M.; Smirnovas, V.; Winter, R.; Richtering, W. Interplay between Hydrogen Bonding and Macromolecular Architecture Leading to Unusual Phase Behavior in Thermosensitive Microgels. Angewandte Chemie – International Edition<\/em> 2008<\/strong>, 47<\/em> (2), 338\u2013341. https:\/\/doi.org\/10.1002\/anie.200703728<\/a>.
\n—
\nKeerl, M.; Smirnovas, V.; Winter, R.; Richtering, W. Copolymer Microgels from Mono- And Disubstituted Acrylamides: Phase Behavior and Hydrogen Bonds. Macromolecules<\/em> 2008<\/strong>, 41<\/em> (18), 6830\u20136836. https:\/\/doi.org\/10.1021\/ma800785w<\/a>.
\n—
\nKraineva, J.; Smirnovas, V.; Winter, R. Effects of Lipid Confinement on Insulin Stability and Amyloid Formation. Langmuir<\/em> 2007<\/strong>, 23<\/em> (13), 7118\u20137126. https:\/\/doi.org\/10.1021\/la700405y<\/a>.
\n—
\nGrudzielanek, S.; Velkova, A.; Shukla, A.; Smirnovas, V.; Tatarek-Nossol, M.; Rehage, H.; Kapurniotu, A.; Winter, R. Cytotoxicity of Insulin within Its Self-Assembly and Amyloidogenic Pathways. Journal of Molecular Biology<\/em> 2007<\/strong>, 370<\/em> (2), 372\u2013384. https:\/\/doi.org\/10.1016\/j.jmb.2007.04.053<\/a>.
\n—
\nGrudzielanek, S.; Smirnovas, V.; Winter, R. The Effects of Various Membrane Physical-Chemical Properties on the Aggregation Kinetics of Insulin. Chemistry and Physics of Lipids<\/em> 2007<\/strong>, 149<\/em> (1\u20132), 28\u201339. https:\/\/doi.org\/10.1016\/j.chemphyslip.2007.05.006<\/a>.
\n—
\nSmirnovas, V.; Winter, R.; Funck, T.; Dzwolak, W. Protein Amyloidogenesis in the Context of Volume Fluctuations: A Case Study on Insulin. ChemPhysChem<\/em> 2006<\/strong>, 7<\/em> (5), 1046\u20131049. https:\/\/doi.org\/10.1002\/cphc.200500717<\/a>.
\n—
\nGrudzielanek, S.; Smirnovas, V.; Winter, R. Solvation-Assisted Pressure Tuning of Insulin Fibrillation: From Novel Aggregation Pathways to Biotechnological Applications. Journal of Molecular Biology<\/em> 2006<\/strong>, 356<\/em> (2), 497\u2013509. https:\/\/doi.org\/10.1016\/j.jmb.2005.11.075<\/a>.
\n—
\nDzwolak, W.; Loksztejn, A.; Smirnovas, V. New Insights into the Self-Assembly of Insulin Amyloid Fibrils: An H-D Exchange FT-IR Study. Biochemistry<\/em> 2006<\/strong>, 45<\/em> (26), 8143\u20138151. https:\/\/doi.org\/10.1021\/bi060341a<\/a>.
\n—
\nSmirnovas, V.; Winter, R.; Funck, T.; Dzwolak, W. Thermodynamic Properties Underlying the \u03b1-Helix-to-\u03b2-Sheet Transition, Aggregation, and Amyloidogenesis of Polylysine as Probed by Calorimetry, Densimetry, and Ultrasound Velocimetry. Journal of Physical Chemistry B<\/em> 2005<\/strong>, 109<\/em> (41), 19043\u201319045. https:\/\/doi.org\/10.1021\/jp053283w<\/a>.
\n—
\nDzwolak, W.; Smirnovas, V. A Conformational Alpha-Helix to Beta-Sheet Transition Accompanies Racemic Self-Assembly of Polylysine: An FT-IR Spectroscopic Study. Biophysical Chemistry<\/em> 2005<\/strong>, 115<\/em> (1), 49\u201354. https:\/\/doi.org\/10.1016\/j.bpc.2005.01.003<\/a>.
\n—
\nDzwolak, W.; Jansen, R.; Smirnovas, V.; Loksztejn, A.; Porowski, S.; Winter, R. Template-Controlled Conformational Patterns of Insulin Fibrillar Self-Assembly Reflect History of Solvation of the Amyloid Nuclei. Physical chemistry chemical physics\u202f: PCCP<\/em> 2005<\/strong>, 7<\/em> (7), 1349\u20131351. https:\/\/doi.org\/10.1039\/b502255j<\/a>.
\n—
\nDzwolak, W.; Grudzielanek, S.; Smirnovas, V.; Ravindra, R.; Nicolini, C.; Jansen, R.; Loksztejn, A.; Porowski, S.; Winter, R. Ethanol-Perturbed Amyloidogenic Self-Assembly of Insulin: Looking for Origins of Amyloid Strains. Biochemistry<\/em> 2005<\/strong>, 44<\/em> (25), 8948\u20138958. https:\/\/doi.org\/10.1021\/bi050281t<\/a>.
\n—
\nDzwolak, W.; Smirnovas, V.; Jansen, R.; Winter, R. Insulin Forms Amyloid in a Strain-Dependent Manner: An FT-IR Spectroscopic Study. Protein science\u202f: a publication of the Protein Society<\/em> 2004<\/strong>, 13<\/em> (7), 1927\u20131932. https:\/\/doi.org\/10.1110\/ps.03607204<\/a>.
\n—
\nBumeliene, Z.; Sereikaite, I.; Bumelis, V. a.; Smirnovas, V.; Gedminiene, G.; Braziunaite, L.; Bajorunaite, E. 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<\/em> 2003<\/strong>, 58<\/em> (11), 1038\u20131041. https:\/\/doi.org\/10.1023\/A:1027325120597<\/a>.
\n—
\nBumelis, V. A.; Bumeliene, Z.; Gedminiene, G.; Smirnovas, V.; Sereikaite, J.; Medelyte, I. Investigation of Thermal Stability of Recombinant Human Interferon-Gamma. Biologija<\/em> 2002<\/strong>, 3<\/em> (2), 37\u201341.
\n—
\nKa\u017eem\u0117kait\u0117, M.; Bulovas, A.; Smirnovas, V.; Niaura, G.; Butkus, E.; Razumas, V. Synthesis of New SAM-Forming Ferrocene Derivatives and Their Interfacial Properties on Gold. Tetrahedron Letters<\/em> 2001<\/strong>, 42<\/em> (43), 7691\u20137694. https:\/\/doi.org\/10.1016\/S0040-4039(01)01625-2<\/a>.<\/p>\n","protected":false},"excerpt":{"rendered":"

Rapalyt\u0117, S.; Karalkevi\u010di\u016bt\u0117, V.; Baronait\u0117, I.; Veiveris, D.; Smirnovas, V.; \u017diaunys, M.; \u0160ulskis, D. Liquid-Liquid Phase Separation and Amyloid Aggregation in the 14-3-3 Protein Family. International Journal of Biological Macromolecules 2026, 368, 152660. https:\/\/doi.org\/10.1016\/j.ijbiomac.2026.152660. — Snie\u010dkut\u0117, R.; \u0160ulskis, D.; Jocyt\u0117, A.; Venclovait\u0117, U.; Tamulyt\u0117, R.; \u017diaunys, M.; Smirnovas, V.; Sakalauskas, A. Formation of Condition-Dependent Alpha-Synuclein Fibril Strain in Artificial Cerebrospinal Fluid. Advanced Science 2026, 13 (7), e05228. https:\/\/doi.org\/10.1002\/advs.202505228. — Szwachta, G.; Sulskis, D.; Konopka, A.; Jalonicka, E.; Struniawski, K.; Mikalauskaite, . . .<\/span><\/a><\/p>\n","protected":false},"author":1,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-76","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"http:\/\/web.vu.lt\/bti\/v.smirnovas\/wp-json\/wp\/v2\/pages\/76","targetHints":{"allow":["GET"]}}],"collection":[{"href":"http:\/\/web.vu.lt\/bti\/v.smirnovas\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"http:\/\/web.vu.lt\/bti\/v.smirnovas\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"http:\/\/web.vu.lt\/bti\/v.smirnovas\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"http:\/\/web.vu.lt\/bti\/v.smirnovas\/wp-json\/wp\/v2\/comments?post=76"}],"version-history":[{"count":61,"href":"http:\/\/web.vu.lt\/bti\/v.smirnovas\/wp-json\/wp\/v2\/pages\/76\/revisions"}],"predecessor-version":[{"id":812,"href":"http:\/\/web.vu.lt\/bti\/v.smirnovas\/wp-json\/wp\/v2\/pages\/76\/revisions\/812"}],"wp:attachment":[{"href":"http:\/\/web.vu.lt\/bti\/v.smirnovas\/wp-json\/wp\/v2\/media?parent=76"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}