Leri, M.; Sun, D.; Svedružic, Ž. M.; Šulskis, 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 2024, 276, 133838. https://doi.org/10.1016/j.ijbiomac.2024.133838.
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Ziaunys, 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 2024, 758, 110087. https://doi.org/10.1016/j.abb.2024.110087.
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Toleikis, 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 α-Synuclein Amyloid Fibrils at Fast MAS Regime. Biomol NMR Assign 2024. https://doi.org/10.1007/s12104-024-10186-2.
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Baronaitė, I.; Šulskis, D.; Kopu Stas, A.; Tutkus, M.; Smirnovas, V. Formation of Calprotectin Inhibits Amyloid Aggregation of S100A8 and S100A9 Proteins. ACS Chem Neurosci 2024, 15 (9), 1915–1925. https://doi.org/10.1021/acschemneuro.4c00093.
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Ghosh, S.; Tamilselvi, S.; Williams, C.; Jayaweera, S. W.; Iashchishyn, I. A.; Šulskis, D.; Gilthorpe, J. D.; Olofsson, A.; Smirnovas, V.; Svedružić, Ž. M.; Morozova-Roche, L. A. ApoE Isoforms Inhibit Amyloid Aggregation of Proinflammatory Protein S100A9. International Journal of Molecular Sciences 2024, 25 (4), 2114. https://doi.org/10.3390/ijms25042114.
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Naaman, 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. 2024. https://doi.org/10.1021/acschemneuro.3c00650.
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Šulskis, D.; Žiaunys, M.; Sakalauskas, A.; Sniečkutė, R.; Smirnovas, V. Formation of Amyloid Fibrils by the Regulatory 14-3-3ζ Protein. Open Biology 2024, 14 (1), 230285. https://doi.org/10.1098/rsob.230285.
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Ziaunys, 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 2024, 33 (2), e4888. https://doi.org/10.1002/pro.4888.
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Sanders, E.; Csondor, R.; Šulskis, D.; Baronaitė, 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 2023, 24 (17), 13200. https://doi.org/10.3390/ijms241713200.
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Pampuscenko, 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 2023, 13 (1), 10813. https://doi.org/10.1038/s41598-023-37887-3.
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Ziaunys, M.; Mikalauskaite, K.; Krasauskas, L.; Smirnovas, V. Conformation-Specific Association of Prion Protein Amyloid Aggregates with Tau Protein Monomers. International Journal of Molecular Sciences 2023, 24 (11), 9277. https://doi.org/10.3390/ijms24119277.
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Šulskis, D.; Šneiderienė, G.; Žiaunys, M.; Smirnovas, V. The Seeding Barrier between Human and Syrian Hamster Prion Protein Amyloid Fibrils Is Determined by Β2-Α2 Loop Sequence Elements. International Journal of Biological Macromolecules 2023, 238, 124038. https://doi.org/10.1016/j.ijbiomac.2023.124038.
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Sakalauskas, 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 2023, 24 (6), 5991. https://doi.org/10.3390/ijms24065991.
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Tamulytė, R.; Jankaitytė, E.; Toleikis, Z.; Smirnovas, V.; Jankunec, M. Pro-Inflammatory Protein S100A9 Alters Membrane Organization by Dispersing Ordered Domains. Biochimica et Biophysica Acta (BBA) – Biomembranes 2023, 1865 (3), 184113. https://doi.org/10.1016/j.bbamem.2022.184113.
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Hadi Ali Janvand, S.; Ladefoged, L. K.; Zubrienė, A.; Sakalauskas, A.; Christiansen, G.; Dudutienė, V.; Schiøtt, B.; Matulis, D.; Smirnovas, V.; Otzen, D. E. Inhibitory Effects of Fluorinated Benzenesulfonamides on Insulin Fibrillation. International Journal of Biological Macromolecules 2023, 227, 590–600. https://doi.org/10.1016/j.ijbiomac.2022.12.105.
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Andrade-Talavera, Y.; Chen, G.; Pansieri, J.; Arroyo-García, 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 2022, 102366. https://doi.org/10.1016/j.pneurobio.2022.102366.
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Ziaunys, M.; Sakalauskas, A.; Mikalauskaite, K.; Smirnovas, V. Rapid Restructurization of Conformationally-Distinct Alpha-Synuclein Amyloid Fibrils at an Elevated Temperature. PeerJ 2022, 10, e14137. https://doi.org/10.7717/peerj.14137.
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Toleikis, 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 2022, 23 (12), 6781. https://doi.org/10.3390/ijms23126781.
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Ziaunys, M.; Smirnovas, V. Exploring Epigallocatechin-3-Gallate Autoxidation Products: Specific Incubation Times Required for Emergence of Anti-Amyloid Properties. Antioxidants 2022, 11 (10), 1887. https://doi.org/10.3390/antiox11101887.
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Sakalauskas, A.; Janoniene, A.; Zvinys, G.; Mikalauskaite, K.; Ziaunys, M.; Smirnovas, V. Exploring the Formation of Polymers with Anti-Amyloid Properties within the 2′3′-Dihydroxyflavone Autoxidation Process. Antioxidants 2022, 11 (9), 1711. https://doi.org/10.3390/antiox11091711.
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Mikalauskaite, K.; Ziaunys, M.; Smirnovas, V. Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State. International Journal of Molecular Sciences 2022, 23 (10), 5421. https://doi.org/10.3390/ijms23105421.
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Nagaraj, M.; Najarzadeh, Z.; Pansieri, J.; Biverstål, 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. 2022, 13 (2), 536–553. https://doi.org/10.1039/D1SC05790A.
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Ziaunys, 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 2022, 715, 109096. https://doi.org/10.1016/j.abb.2021.109096.
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Ziaunys, 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 2021, 22 (22), 12382. https://doi.org/10.3390/ijms222212382.
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Ziaunys, M.; Mikalauskaite, K.; Sakalauskas, A.; Smirnovas, V. Interplay between Epigallocatechin-3-Gallate and Ionic Strength during Amyloid Aggregation. PeerJ 2021, 9, e12381. https://doi.org/10.7717/peerj.12381.
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Arabuli, L.; Iashchishyn, I. A.; Romanova, N. V.; Musteikyte, G.; Smirnovas, V.; Chaudhary, H.; Svedružić, Ž. 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 2021, 22 (16), 8556. https://doi.org/10.3390/ijms22168556.
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Strazdaite, S.; Roeters, S. J.; Sakalauskas, A.; Sneideris, T.; Kirschner, J.; Pedersen, K. B.; Schiøtt, B.; Jensen, F.; Weidner, T.; Smirnovas, V.; Niaura, G. Interaction of Amyloid-β-(1–42) Peptide and Its Aggregates with Lipid/Water Interfaces Probed by Vibrational Sum-Frequency Generation Spectroscopy. J. Phys. Chem. B 2021. https://doi.org/10.1021/acs.jpcb.1c04882.
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Sakalauskas, A.; Ziaunys, M.; Snieckute, R.; Smirnovas, V. Autoxidation Enhances Anti-Amyloid Potential of Flavone Derivatives. Antioxidants 2021, 10 (9), 1428. https://doi.org/10.3390/antiox10091428.
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Toleikis, 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 2021, 22 (15), 7972. https://doi.org/10.3390/ijms22157972.
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Fridmanis, J.; Toleikis, Z.; Sneideris, T.; Ziaunys, M.; Bobrovs, R.; Smirnovas, V.; Jaudzems, K. Aggregation Condition–Structure Relationship of Mouse Prion Protein Fibrils. International Journal of Molecular Sciences 2021, 22 (17), 9635. https://doi.org/10.3390/ijms22179635.
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Čiplys, E.; Paškevičius, T.; Žitkus, E.; Bielskis, J.; Ražanskas, R.; Šneideris, T.; Smirnovas, V.; Kaupinis, A.; Tester, D. J.; Ackerman, M. J.; Højrup, P.; Michalak, M.; Houen, G.; Slibinskas, R. Mapping Human Calreticulin Regions Important for Structural Stability. Biochimica et Biophysica Acta (BBA) – Proteins and Proteomics 2021, 1869 (11), 140710. https://doi.org/10.1016/j.bbapap.2021.140710.
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Chaudhary, H.; Iashchishyn, I. A.; Romanova, N. V.; Rambaran, M. A.; Musteikyte, G.; Smirnovas, V.; Holmboe, M.; Ohlin, C. A.; Svedružić, Ž. 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 2021, 13 (23), 26721–26734. https://doi.org/10.1021/acsami.1c04163.
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Leri, M.; Chaudhary, H.; Iashchishyn, I. A.; Pansieri, J.; Svedružić, Ž. M.; Gómez 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’s Disease. ACS Chem. Neurosci. 2021, 12 (11), 1905–1918. https://doi.org/10.1021/acschemneuro.0c00828.
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Ziaunys, M.; Mikalauskaite, K.; Sakalauskas, A.; Smirnovas, V. Using Lysozyme Amyloid Fibrils as a Means of Scavenging Aggregation-Inhibiting Compounds. Biotechnology Journal 2021, 16 (9), 2100138. https://doi.org/10.1002/biot.202100138.
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Kasho, K.; Krasauskas, L.; Smirnovas, V.; Stojkovič, G.; Morozova-Roche, L. A.; Wanrooij, S. Human Polymerase δ-Interacting Protein 2 (PolDIP2) Inhibits the Formation of Human Tau Oligomers and Fibrils. International Journal of Molecular Sciences 2021, 22 (11), 5768. https://doi.org/10.3390/ijms22115768.
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Ziaunys, M.; Sakalauskas, A.; Mikalauskaite, K.; Snieckute, R.; Smirnovas, V. Temperature-Dependent Structural Variability of Prion Protein Amyloid Fibrils. International Journal of Molecular Sciences 2021, 22 (10), 5075. https://doi.org/10.3390/ijms22105075.
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Szulc, N.; Burdukiewicz, M.; Gąsior-Głogowska, M.; Wojciechowski, J. W.; Chilimoniuk, J.; Mackiewicz, P.; Šneideris, T.; Smirnovas, V.; Kotulska, M. Bioinformatics Methods for Identification of Amyloidogenic Peptides Show Robustness to Misannotated Training Data. Scientific Reports 2021, 11 (1), 8934. https://doi.org/10.1038/s41598-021-86530-6.
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Ziaunys, M.; Sakalauskas, A.; Sneideris, T.; Smirnovas, V. Lysozyme Fibrils Alter the Mechanism of Insulin Amyloid Aggregation. International Journal of Molecular Sciences 2021, 22 (4), 1775. https://doi.org/10.3390/ijms22041775.
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Ziaunys, M.; Sakalauskas, A.; Mikalauskaite, K.; Smirnovas, V. Exploring the Occurrence of Thioflavin-T-Positive Insulin Amyloid Aggregation Intermediates. PeerJ 2021, 9, e10918. https://doi.org/10.7717/peerj.10918.
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Jurgelevičiūtė, J.; Bičkovas, N.; Sakalauskas, A.; Novickij, V.; Smirnovas, V.; Lastauskienė, E. Effects of Pulsed Electric Fields on Yeast with Prions and the Structure of Amyloid Fibrils. Applied Sciences 2021, 11 (6), 2684. https://doi.org/10.3390/app11062684.
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Ziaunys, M.; Sneideris, T.; Smirnovas, V. Formation of Distinct Prion Protein Amyloid Fibrils under Identical Experimental Conditions. Scientific Reports 2020, 10 (1), 4572. https://doi.org/10.1038/s41598-020-61663-2.
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Ziaunys, M.; Sakalauskas, A.; Smirnovas, V. Identifying Insulin Fibril Conformational Differences by Thioflavin-T Binding Characteristics. Biomacromolecules 2020, 21 (12), 4989–4997. https://doi.org/10.1021/acs.biomac.0c01178.
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Sneideris, 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 2020, 21 (19), 7410. https://doi.org/10.3390/ijms21197410.
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Sakalauskas, A.; Ziaunys, M.; Smirnovas, V. Gallic Acid Oxidation Products Alter the Formation Pathway of Insulin Amyloid Fibrils. Scientific Reports 2020, 10 (1), 14466. https://doi.org/10.1038/s41598-020-70982-3.
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Pansieri, J.; Iashchishyn, I. A.; Fakhouri, H.; Ostojić, 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 Aβ Fibrillar Surfaces Revealed by Charge Detection Mass Spectrometry, Microscopy, Kinetic and Microfluidic Analyses. Chem. Sci. 2020, 11 (27), 7031–7039. https://doi.org/10.1039/C9SC05905A.
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Pampuscenko, 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 2020, 154 (3), 316–329. https://doi.org/10.1111/jnc.14940.
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Pampuscenko, 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 2020. https://doi.org/10.1007/s12035-020-02150-7.
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Musteikyte, G.; Ziaunys, M.; Smirnovas, V. Methylene Blue Inhibits Nucleation and Elongation of SOD1 Amyloid Fibrils. PeerJ 2020, 8, e9719. https://doi.org/10.7717/peerj.9719.
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Mikalauskaite, 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 2020, 21 (23), 8916. https://doi.org/10.3390/ijms21238916.
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Martins, P. M.; Navarro, S.; Silva, A.; Pinto, M. F.; Sárkány, 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 – Minimum Information Required for Reproducible AGGregation Experiments. Front. Mol. Neurosci. 2020, 13. https://doi.org/10.3389/fnmol.2020.582488.
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Ziaunys, M.; Sneideris, T.; Smirnovas, V. Exploring the Potential of Deep-Blue Autofluorescence for Monitoring Amyloid Fibril Formation and Dissociation. PeerJ 2019, 7, e7554. https://doi.org/10.7717/peerj.7554.
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Ziaunys, M.; Smirnovas, V. Emergence of Visible Light Optical Properties of L-Phenylalanine Aggregates. PeerJ 2019, 7, e6518. https://doi.org/10.7717/peerj.6518.
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Ziaunys, M.; Smirnovas, V. Additional Thioflavin-T Binding Mode in Insulin Fibril Inner Core Region. J. Phys. Chem. B 2019, 123 (41), 8727–8732. https://doi.org/10.1021/acs.jpcb.9b08652.
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Ziaunys, M.; Mikalauskaite, K.; Smirnovas, V. Amyloidophilic Molecule Interactions on the Surface of Insulin Fibrils: Cooperative Binding and Fluorescence Quenching. Scientific Reports 2019, 9 (1), 20303. https://doi.org/10.1038/s41598-019-56788-y.
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Sneideris, 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 2019, 9 (12), 855. https://doi.org/10.3390/biom9120855.
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Sakalauskas, A.; Ziaunys, M.; Smirnovas, V. Concentration-Dependent Polymorphism of Insulin Amyloid Fibrils. PeerJ 2019, 7, e8208. https://doi.org/10.7717/peerj.8208.
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Pansieri, J.; Ostojić, L.; Iashchishyn, I. A.; Magzoub, M.; Wallin, C.; Wärmländer, S. K. T. S.; Gräslund, A.; Nguyen Ngoc, M.; Smirnovas, V.; Svedružić, Ž.; Morozova-Roche, L. A. Pro-Inflammatory S100A9 Protein Aggregation Promoted by NCAM1 Peptide Constructs. ACS Chem. Biol. 2019, 14 (7), 1410–1417. https://doi.org/10.1021/acschembio.9b00394.
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Ziaunys, M.; Sneideris, T.; Smirnovas, V. Self-Inhibition of Insulin Amyloid-like Aggregation. Physical Chemistry Chemical Physics 2018, 20 (43), 27638–27645. https://doi.org/10.1039/C8CP04838J.
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Kim, 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 2018, 9 (1), 2166. https://doi.org/10.1038/s41467-018-04584-z.
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Smirnovienė, J.; Smirnovas, V.; Matulis, D. Picomolar Inhibitors of Carbonic Anhydrase: Importance of Inhibition and Binding Assays. Analytical Biochemistry 2017, 522, 61–72. https://doi.org/10.1016/j.ab.2017.01.022.
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Iashchishyn, I. A.; Sulskis, D.; Nguyen Ngoc, M.; Smirnovas, V.; Morozova-Roche, L. A. Finke–Watzky Two-Step Nucleation–Autocatalysis Model of S100A9 Amyloid Formation: Protein Misfolding as “Nucleation” Event. ACS Chemical Neuroscience 2017, 8 (10), 2152–2158. https://doi.org/10.1021/acschemneuro.7b00251.
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Sneideris, T.; Milto, K.; Smirnovas, V. Polymorphism of Amyloid-like Fibrils Can Be Defined by the Concentration of Seeds. PeerJ 2015, 3, e1207–e1207. https://doi.org/10.7717/peerj.1207.
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Sneideris, T.; Darguzis, D.; Botyriute, A.; Grigaliunas, M.; Winter, R.; Smirnovas, V. PH-Driven Polymorphism of Insulin Amyloid-Like Fibrils. PloS one 2015, 10 (8), e0136602–e0136602. https://doi.org/10.1371/journal.pone.0136602.
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Šneideris, T.; Baranauskienė, L.; Cannon, J. G.; Rutkienė, R.; Meškys, R.; Smirnovas, V. Looking for a Generic Inhibitor of Amyloid-like Fibril Formation among Flavone Derivatives. PeerJ 2015, 3, e1271–e1271. https://doi.org/10.7717/peerj.1271.
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Malisauskas, R.; Botyriute, A.; Cannon, J. G.; Smirnovas, V. Flavone Derivatives as Inhibitors of Insulin Amyloid-like Fibril Formation. PloS one 2015, 10 (3), e0121231. https://doi.org/10.1371/journal.pone.0121231.
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Milto, K.; Michailova, K.; Smirnovas, V. Elongation of Mouse Prion Protein Amyloid-like Fibrils: Effect of Temperature and Denaturant Concentration. PLoS ONE 2014, 9 (4), e94469. https://doi.org/10.1371/journal.pone.0094469.
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Dudutienė, V.; Matulienė, J.; Smirnov, A.; Timm, D. D.; Zubrienė, A.; Baranauskienė, L.; Morku̅naitė, V.; Smirnovienė, J.; Michailovienė, V.; Juozapaitienė, V.; Mickevičiu̅tė, A.; Kazokaitė, J.; Bakšytė, S.; Kasiliauskaitė, A.; Jachno, J.; Revuckienė, J.; Kišonaitė, M.; Pilipuitytė, V.; Ivanauskaitė, E.; Milinavičiu̅tė, G.; Smirnovas, V.; Petrikaitė, V.; Kairys, V.; Petrauskas, V.; Norvaišas, P.; Lingė, D.; Gibieža, P.; Čapkauskaitė, E.; Zakšauskas, A.; Kazlauskas, E.; Manakova, E.; Gražulis, S.; Ladbury, J. E.; Matulis, D. Discovery and Characterization of Novel Selective Inhibitors of Carbonic Anhydrase IX. Journal of Medicinal Chemistry 2014, 57 (22), 9435–9446. https://doi.org/10.1021/jm501003k.
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Cobb, 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 2014, 289 (5), 2643–2650. https://doi.org/10.1074/jbc.M113.520718.
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Milto, K.; Botyriute, A.; Smirnovas, V. Amyloid-Like Fibril Elongation Follows Michaelis-Menten Kinetics. PLoS ONE 2013, 8 (7), e68684. https://doi.org/10.1371/journal.pone.0068684.
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Smirnovas, 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 2011, 18, 504–506. https://doi.org/10.1038/nsmb.2035.
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Smirnovas, 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 2009, 284 (36), 24233–24241. https://doi.org/10.1074/jbc.M109.036558.
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Smirnovas, V.; Winter, R. Revealing Different Aggregation Pathways of Amyloidogenic Proteins by Ultrasound Velocimetry. Biophysical journal 2008, 94 (8), 3241–3246. https://doi.org/10.1529/biophysj.107.123133.
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Radovan, D.; Smirnovas, V.; Winter, R. Effect of Pressure on Islet Amyloid Polypeptide Aggregation: Revealing the Polymorphic Nature of the Fibrillation Process. Biochemistry 2008, 47 (24), 6352–6360. https://doi.org/10.1021/bi800503j.
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Lopes, 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 2008, 121 (11), 112002–112002. https://doi.org/10.1088/1742-6596/121/11/112002.
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Keerl, 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 2008, 47 (2), 338–341. https://doi.org/10.1002/anie.200703728.
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Keerl, M.; Smirnovas, V.; Winter, R.; Richtering, W. Copolymer Microgels from Mono- And Disubstituted Acrylamides: Phase Behavior and Hydrogen Bonds. Macromolecules 2008, 41 (18), 6830–6836. https://doi.org/10.1021/ma800785w.
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Kraineva, J.; Smirnovas, V.; Winter, R. Effects of Lipid Confinement on Insulin Stability and Amyloid Formation. Langmuir 2007, 23 (13), 7118–7126. https://doi.org/10.1021/la700405y.
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Grudzielanek, 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 2007, 370 (2), 372–384. https://doi.org/10.1016/j.jmb.2007.04.053.
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Grudzielanek, S.; Smirnovas, V.; Winter, R. The Effects of Various Membrane Physical-Chemical Properties on the Aggregation Kinetics of Insulin. Chemistry and Physics of Lipids 2007, 149 (1–2), 28–39. https://doi.org/10.1016/j.chemphyslip.2007.05.006.
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Smirnovas, V.; Winter, R.; Funck, T.; Dzwolak, W. Protein Amyloidogenesis in the Context of Volume Fluctuations: A Case Study on Insulin. ChemPhysChem 2006, 7 (5), 1046–1049. https://doi.org/10.1002/cphc.200500717.
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Grudzielanek, S.; Smirnovas, V.; Winter, R. Solvation-Assisted Pressure Tuning of Insulin Fibrillation: From Novel Aggregation Pathways to Biotechnological Applications. Journal of Molecular Biology 2006, 356 (2), 497–509. https://doi.org/10.1016/j.jmb.2005.11.075.
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Dzwolak, W.; Loksztejn, A.; Smirnovas, V. New Insights into the Self-Assembly of Insulin Amyloid Fibrils: An H-D Exchange FT-IR Study. Biochemistry 2006, 45 (26), 8143–8151. https://doi.org/10.1021/bi060341a.
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Smirnovas, V.; Winter, R.; Funck, T.; Dzwolak, W. 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 2005, 109 (41), 19043–19045. https://doi.org/10.1021/jp053283w.
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Dzwolak, W.; Smirnovas, V. A Conformational Alpha-Helix to Beta-Sheet Transition Accompanies Racemic Self-Assembly of Polylysine: An FT-IR Spectroscopic Study. Biophysical Chemistry 2005, 115 (1), 49–54. https://doi.org/10.1016/j.bpc.2005.01.003.
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Dzwolak, 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 : PCCP 2005, 7 (7), 1349–1351. https://doi.org/10.1039/b502255j.
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Dzwolak, 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 2005, 44 (25), 8948–8958. https://doi.org/10.1021/bi050281t.
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Dzwolak, W.; Smirnovas, V.; Jansen, R.; Winter, R. Insulin Forms Amyloid in a Strain-Dependent Manner: An FT-IR Spectroscopic Study. Protein science : a publication of the Protein Society 2004, 13 (7), 1927–1932. https://doi.org/10.1110/ps.03607204.
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Bumeliene, 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 2003, 58 (11), 1038–1041. https://doi.org/10.1023/A:1027325120597.
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Bumelis, V. A.; Bumeliene, Z.; Gedminiene, G.; Smirnovas, V.; Sereikaite, J.; Medelyte, I. Investigation of Thermal Stability of Recombinant Human Interferon-Gamma. Biologija 2002, 3 (2), 37–41.
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Kažemėkaitė, 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 2001, 42 (43), 7691–7694. https://doi.org/10.1016/S0040-4039(01)01625-2.