{"id":2,"date":"2020-05-15T09:15:16","date_gmt":"2020-05-15T09:15:16","guid":{"rendered":"http:\/\/www.amyloid.bti.vu.lt\/?page_id=2"},"modified":"2026-02-25T11:23:06","modified_gmt":"2026-02-25T09:23:06","slug":"publikacijos","status":"publish","type":"page","link":"http:\/\/www.amyloid.bti.vu.lt\/en\/publikacijos\/","title":{"rendered":"Publications"},"content":{"rendered":"\n

88. Karalkevi\u010di\u016bt\u0117, V., Rapalyt\u0117, S., Baronait\u0117, I., Veiveris, D., Smirnovas, V., \u017diaunys, M., and \u0160ulskis, D<\/strong>. (2026). Liquid-liquid phase separation and amyloid aggregation in the 14-3-3 protein family<\/a><\/strong>. Preprint at bioRxiv<\/em>, <\/p>\n\n\n\n

87. Snie\u010dkut\u0117, R., \u0160ulskis, D., Jocyt\u0117, A., Venclovait\u0117, U.,<\/strong> Tamulyt\u0117, R., \u017diaunys, M., Smirnovas, V., and Sakalauskas, A<\/strong>. (2025). Formation of Condition-Dependent Alpha-Synuclein Fibril Strain in Artificial Cerebrospinal Fluid<\/a><\/strong>. Advanced Science<\/em> , e05228. B<\/a>ioRxiv preprint version<\/a><\/strong><\/p>\n\n\n\n

86. Szwachta, G., Sulskis, D<\/strong>., Konopka, A., Ja\u0142onicka, E., Struniawski, K., Mikalauskaite, K., Sakalauskas, A<\/strong>., Kozera, R., Smirnovas, V<\/strong>., Stsiapura, V., Ziaunys M<\/strong>. and Hanczyc P. (2025). Collective methodological emission assay of Thioflavin T for qualitative \u03b1-synuclein fibril structures discrimination<\/a><\/strong>. International Journal of Biological Macromolecules<\/em>, 148994. <\/p>\n\n\n\n

85. Krasauskas, L., Veiveris, D., \u017diaunys, M., \u0160ulskis, D., Sakalauskas, A., and Smirnovas, V<\/strong>. (2025). Tau Enhances Aggregation of S100A9 Protein and Further Association of Its Fibrils<\/a><\/strong>. International Journal of Molecular Sciences<\/em> 26<\/em>, 8961. <\/p>\n\n\n\n

84. Pintado-Grima, C., B\u00e1rcenas, O., Arribas-Ruiz, E., Iglesias, V., Burdukiewicz, M<\/strong>., and Ventura, S. (2025). Comprehensive protein datasets and benchmarking for liquid\u2013liquid phase separation studies<\/a><\/strong>. Genome Biology<\/em> 26<\/em>, 198.<\/p>\n\n\n\n

83. Karalkevi\u010diu\u0305t\u0117, V., Baronait\u0117, I.<\/strong>, Pe\u0161tenyt\u0117, A., Veiveris, D<\/strong>., Usevi\u010dius, G., \u0160im\u0117nas, M., \u017diaunys, M., Smirnovas, V., and \u0160ulskis, D.<\/strong> (2025). Calcium-Dependent S100A8 Amyloid Fibril Formation via S100A1-Mediated Transient Interaction<\/a><\/strong>. ACS Chem. Neurosci.<\/em> 16<\/em>, 2592\u20132601. BioRxiv preprint version<\/a><\/strong><\/p>\n\n\n\n

82. Kalitnik, A., Lassota, A., Pola\u0144ska, O., G\u0105sior-G\u0142ogowska, M., Szefczyk, M., Barbach, A., Chilimoniuk, J., J\u0119\u015bkowiak-Kossakowska, I., Wojciechowska, A.W., Wojciechowski, J.W., et al. Burdukiewicz, M<\/strong> (2025). Experimental methods for studying amyloid cross-interactions<\/a><\/strong>. Protein Science<\/em> 34<\/em>, e70151.<\/p>\n\n\n\n

81. Veiveris, D<\/strong>., Kopustas, A., Sulskis, D., Mikalauskaite, K.<\/strong>, Alsamsam, M.N., Tutkus, M., Smirnovas, V., and Ziaunys, M<\/strong>. (2025). Heterotypic Droplet Formation by Pro-Inflammatory S100A9 and Neurodegenerative Disease-Related \u03b1-Synuclein.<\/a><\/strong> Biomacromolecules<\/em> 26<\/em>, 3525\u20133537. BioRxiv preprint version<\/a><\/strong><\/p>\n\n\n\n

80. \u017ditkus, E., \u010ciplys, E., \u017diaunys, M., Sakalauskas, A<\/strong>., and Slibinskas, R. (2025). Development of an efficient expression system for human chaperone BiP in Pichia pastoris: production optimization and functional validation<\/a><\/strong>. Microbial Cell Factories<\/em> 24<\/em>, 66. <\/p>\n\n\n\n

79. Pucha\u0142a, W., Kistowski, M., Zhukova, L., Burdukiewicz, M.<\/strong>, and Dadlez, M. (2025). HRaDeX: R Package and Web Server for Computing High-Resolution Deuterium Uptake Rates for HDX-MS Data<\/a><\/strong>. J Proteome Res 24<\/em>, 1688\u20131700.<\/p>\n\n\n\n

78. Pampuscenko, K., Jankeviciute, S., Morkuniene, R., Sulskis, D., Smirnovas<\/strong>, V., Brown, G.C., and Borutaite, V. (2025). S100A9 protein activates microglia and stimulates phagocytosis, resulting in synaptic and neuronal loss<\/a><\/strong>. Neurobiology of Disease<\/em> 206<\/em>, 106817. <\/p>\n\n\n\n

77. Tamulyt\u0117, R., Baronait\u0117, I., \u0160ulskis, D., Smirnovas, V<\/strong>., and Jankunec, M. (2025). Pro-inflammatory S100A8 Protein Exhibits a Detergent-like Effect on Anionic Lipid Bilayers, as Imaged by High-Speed AFM<\/a><\/strong>. ACS Appl. Mater. Interfaces<\/em>. 17<\/em>, 2635\u20132647.<\/p>\n\n\n\n

76. Ziaunys, M., Sulskis, D., Veiveris, D., Sakalauskas, A., Mikalauskaite, K., <\/strong>and Smirnovas, V<\/strong>. (2024). Diverse effects of fluorescent labels on alpha-synuclein condensate formation during liquid-liquid phase separation<\/a><\/strong>. International Journal of Biological Macromolecules<\/em> 283<\/em>, 137688. BioRxiv preprint version<\/a><\/strong><\/p>\n\n\n\n

75. Iglesias, V., Chilimoniuk, J., Pintado-Grima, C., B\u00e1rcenas, O., Ventura, S., and Burdukiewicz, M<\/strong>. (2024). Aggregating amyloid resources: A comprehensive review of databases on amyloid-like aggregation.<\/a><\/strong> Computational and Structural Biotechnology Journal<\/em> 23<\/em>, 4011\u20134018. <\/p>\n\n\n\n

74. Misiu\u0305nait\u0117, I., Mikalauskait\u0117, K<\/strong>., Paulauskait\u0117, M., Snie\u010dkut\u0117, R., Smirnovas, V<\/strong>., Bruk\u0161tus, A., \u017diaunys, M<\/strong>., and \u017dutaut\u0117, I. (2024). Imidazo[2,1-b][1,3]thiazine Derivatives as Potential Modulators of Alpha-Synuclein Amyloid Aggregation<\/a><\/strong>. ACS Chem. Neurosci<\/em>. 15<\/em>, 4418\u20134430. <\/p>\n\n\n\n

73. Kitoka, K., Lends, A., Kucinskas, G., Bula, A.L., Krasauskas, L., Smirnovas, V<\/strong>., Zilkova, M., Kovacech, B., Skrabana, R., Hritz, J., et al. (2024). dGAE(297-391) Tau Fragment Promotes Formation of Chronic Traumatic Encephalopathy-Like Tau Filaments.<\/a><\/strong> Angewandte Chemie International Edition<\/em>, e202407821. BioRxiv preprint version<\/a><\/strong><\/p>\n\n\n\n

72. \u017dvirblis, M., Sakalauskas, A<\/strong>., Ali Janvand, S.H., Dudutien\u0117, V., \u017diaunys, M., Snie\u010dkut\u0117, R<\/strong>., Otzen, D.E., Smirnovas, V<\/strong>., and Matulis, D. (2024). Structure-Activity Relationship of Fluorinated Benzenesulfonamides as Inhibitors of Amyloid-\u03b2 Aggregation<\/a><\/strong>. Chemistry \u2013 A European Journal<\/em>, e202402330. <\/p>\n\n\n\n

71. Ziaunys, M., Mikalauskaite, K., Sakalauskas, A., and Smirnovas, V<\/strong>. (2024). Study of Insulin Aggregation and Fibril Structure under Different Environmental Conditions<\/a><\/strong>. International Journal of Molecular Sciences<\/em> 25<\/em>, 9406. <\/p>\n\n\n\n

70. Ziaunys, M., Sulskis, D., Veiveris, D<\/strong>., Kopustas, A., Snieckute, R., Mikalauskaite, K., Sakalauskas, A<\/strong>., Tutkus, M., and Smirnovas, V<\/strong>. (2024). Liquid\u2013liquid phase separation of alpha-synuclein increases the structural variability of fibrils formed during amyloid aggregation<\/a><\/strong>. The FEBS Journal<\/em> 291<\/em>, 4522\u20134538. BioRxiv preprint version<\/a><\/strong><\/p>\n\n\n\n

69. Leri, M., Sun, D., Svedru\u017eic, \u017d.M., \u0160ulskis, D., Smirnovas, V<\/strong>., Stefani, M., Morozova-Roche, L., and Bucciantini, M. (2024). Pro-inflammatory protein S100A9 targeted by a natural molecule to prevent neurodegeneration onset.<\/a><\/strong> International Journal of Biological Macromolecules<\/em>, 133838.<\/p>\n\n\n\n

68. Ziaunys, M., Sulskis, D., Mikalauskaite, K., Sakalauskas, A., Snieckute, R., and Smirnovas, V<\/strong>. (2024). S100A9 inhibits and redirects prion protein 89-230 fragment amyloid aggregation<\/a><\/strong>. Archives of Biochemistry and Biophysics<\/em> 758, 110087. BioRxiv preprint version<\/a><\/strong><\/p>\n\n\n\n

67. Toleikis, Z<\/strong>., Paluch, P., Kuc, E., Petkus, J., Sulskis, D<\/strong>., Org-Tago, M.-L., Samoson, A., Smirnovas, V<\/strong>., Stanek, J., and Lends, A. (2024). Solid-state NMR backbone chemical shift assignments of \u03b1-synuclein amyloid fibrils at fast MAS regime<\/a><\/strong>. Biomol NMR Assign<\/em>.<\/p>\n\n\n\n

66. Baronait\u0117, I., \u0160ulskis, D<\/strong>., Kopustas, A., Tutkus, M., and Smirnovas, V<\/strong>. (2024). Formation of Calprotectin Inhibits Amyloid Aggregation of S100A8 and S100A9 Proteins<\/a><\/strong>. ACS Chem Neurosci<\/em> 15<\/em>, 1915\u20131925.<\/p>\n\n\n\n

65. Ghosh, S., Tamilselvi, S., Williams, C., Jayaweera, S.W., Iashchishyn, I.A., \u0160ulskis, D<\/strong>., Gilthorpe, J.D., Olofsson, A., Smirnovas, V<\/strong>., Svedru\u017ei\u0107, \u017d.M., et al. (2024). ApoE Isoforms Inhibit Amyloid Aggregation of Proinflammatory Protein S100A9.<\/a><\/strong> International Journal of Molecular Sciences<\/em> 25<\/em>, 2114. <\/p>\n\n\n\n

64. Naaman, E., Qarawani, A., Ben-Zvi Elimelech, R., Harel, M., Sigal-Dror, S., Safuri, S., Smirnovas, V., Baronaite, I<\/strong>., Romanova, N.V., Morozova-Roche, L.A., et al. (2024). The Surprising Nonlinear Effects of S100A9 Proteins in the Retina<\/strong>.<\/a> ACS Chem. Neurosci<\/em>. 15<\/em>, 735\u2013744.<\/p>\n\n\n\n

63. Ziaunys, M., Mikalauskaite, K., Sakalauskas, A., and Smirnovas, V.<\/strong> (2024). Investigating lysozyme amyloid fibril formation and structural variability dependence on its initial folding state under different pH conditions<\/a><\/strong>. Protein Science<\/em> 33<\/em>, e4888.<\/p>\n\n\n\n

62. \u0160ulskis, D., \u017diaunys, M., Sakalauskas, A., Snie\u010dkut\u0117, R., and Smirnovas, V<\/strong>. (2024). Formation of amyloid fibrils by the regulatory 14-3-3\u03b6 protein<\/a><\/strong>. Open Biology<\/em> 14<\/em>, 230285. BioRxiv preprint version<\/a><\/strong><\/p>\n\n\n\n

61. Sanders, E., Csondor, R., \u0160ulskis, D., Baronait\u0117, I., Smirnovas, V<\/strong>., Maheswaran, L., Horrocks, J., Munro, R., Georgiadou, C., Horvath, I., et al. (2023). The Stabilization of S100A9 Structure by Calcium Inhibits the Formation of Amyloid Fibrils<\/a><\/strong>. International Journal of Molecular Sciences<\/em> 24<\/em>, 13200. <\/p>\n\n\n\n

60. Pampuscenko, K., Morkuniene, R., Krasauskas, L., Smirnovas<\/strong>, V., Brown, G.C., and Borutaite, V. (2023). Extracellular tau stimulates phagocytosis of living neurons by activated microglia via Toll-like 4 receptor-NLRP3 inflammasome-caspase-1 signalling axis<\/a><\/strong>. Scientific Reports<\/em> 13<\/em>, 10813. <\/p>\n\n\n\n

59. Ziaunys, M., Mikalauskaite, K., Krasauskas, L., and Smirnovas, V<\/strong>. (2023). Conformation-Specific Association of Prion Protein Amyloid Aggregates with Tau Protein Monomers<\/a><\/strong>. International Journal of Molecular Sciences<\/em> 24<\/em>, 9277.<\/p>\n\n\n\n

58. \u0160ulskis, D., \u0160neiderien\u0117, G., \u017diaunys, M., and Smirnovas, V<\/strong>. (2023). The seeding barrier between human and Syrian hamster prion protein amyloid fibrils is determined by \u03b22-\u03b12 loop sequence elements<\/a><\/strong>. International Journal of Biological Macromolecules<\/em> 238<\/em>, 124038. <\/p>\n\n\n\n

57. Sakalauskas, A., Ziaunys, M., Snieckute, R., Janoniene, A., Veiveris, D.<\/strong>, Zvirblis, M., Dudutiene, V., and Smirnovas, V<\/strong>. (2023). The Major Components of Cerebrospinal Fluid Dictate the Characteristics of Inhibitors against Amyloid-Beta Aggregation<\/a><\/strong>. International Journal of Molecular Sciences<\/em> 24<\/em>, 5991.<\/p>\n\n\n\n

56. Tamulyt\u0117, R., Jankaityt\u0117, E., Toleikis, Z., Smirnovas, V.<\/strong>, and Jankunec, M. (2023). Pro-inflammatory protein S100A9 alters membrane organization by dispersing ordered domains<\/a><\/strong>. Biochimica et Biophysica Acta (BBA) – Biomembranes<\/em> 1865<\/em>, 184113.<\/p>\n\n\n\n

55. Hadi Ali Janvand, S., Ladefoged, L.K., Zubrien\u0117, A., Sakalauskas, A<\/strong>., Christiansen, G., Dudutien\u0117, V., Schi\u00f8tt, B., Matulis, D., Smirnovas, V<\/strong>., and Otzen, D.E. (2023). Inhibitory effects of fluorinated benzenesulfonamides on insulin fibrillation<\/a><\/strong>. International Journal of Biological Macromolecules<\/em> 227<\/em>, 590\u2013600.<\/p>\n\n\n\n

54. Andrade-Talavera, Y., Chen, G., Pansieri, J., Arroyo-Garc\u00eda, L.E., Toleikis, Z., Smirnovas, V<\/strong>., Johansson, J., Morozova-Roche, L., and Fisahn, A. (2022). S100A9 amyloid growth and S100A9 fibril-induced impairment of gamma oscillations in area CA3 of mouse hippocampus ex vivo is prevented by Bri2 BRICHOS<\/a><\/strong>. Progress in Neurobiology<\/em>, 102366.<\/p>\n\n\n\n

53. Ziaunys, M., Sakalauskas, A., Mikalauskaite, K., and Smirnovas, V<\/strong>. (2022). Rapid restructurization of conformationally-distinct alpha-synuclein amyloid fibrils at an elevated temperature<\/a><\/strong>. PeerJ<\/em> 10<\/em>, e14137.<\/p>\n\n\n\n

52. Ziaunys, M., and Smirnovas, V<\/strong>. (2022). Exploring Epigallocatechin-3-Gallate Autoxidation Products: Specific Incubation Times Required for Emergence of Anti-Amyloid Properties<\/a><\/strong>. Antioxidants<\/em> 11<\/em>, 1887.<\/p>\n\n\n\n

51. Sakalauskas, A., Janoniene, A.<\/strong>, Zvinys, G., Mikalauskaite, K., Ziaunys, M., and Smirnovas, V<\/strong>. (2022). Exploring the Formation of Polymers with Anti-Amyloid Properties within the 2\u20323\u2032-Dihydroxyflavone Autoxidation Process<\/a><\/strong>. Antioxidants<\/em> 11<\/em>, 1711.<\/p>\n\n\n\n

50. Toleikis, Z<\/strong>., Bobrovs, R., Janoniene, A<\/strong>., Lends, A., Ziaunys, M., Baronaite, <\/strong>I., Petrauskas, V., Kitoka, K., Smirnovas, V<\/strong>., and Jaudzems, K. (2022). Interactions between S100A9 and Alpha-Synuclein: Insight from NMR Spectroscopy<\/strong><\/a>. International Journal of Molecular Sciences<\/em> 23<\/em>, 6781. <\/p>\n\n\n\n

49. Mikalauskaite, K., Ziaunys, M., and Smirnovas, V<\/strong>. (2022). Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State<\/a><\/strong>. International Journal of Molecular Sciences 23<\/em>, 5421.<\/p>\n\n\n\n

48. Nagaraj, M., Najarzadeh, Z., Pansieri, J., Biverst\u00e5l, H., Musteikyte, G., Smirnovas, V<\/strong>., Matthews, S., Emanuelsson, C., Johansson, J., Buxbaum, J.N., et al. (2022). Chaperones mainly suppress primary nucleation during formation of functional amyloid required for bacterial biofilm formation. <\/a><\/strong>Chem. Sci<\/em>. 13<\/em>, 536\u2013553. <\/p>\n\n\n\n

47. Ziaunys, M., Mikalauskaite, K., Veiveris, D., Sakalauskas, A., and Smirnovas, V<\/strong>. (2022). Superoxide dismutase-1 alters the rate of prion protein aggregation and resulting fibril conformation<\/a><\/strong>. Archives of Biochemistry and Biophysics<\/em> 715<\/em>, 109096.<\/p>\n\n\n\n

46. Ziaunys, M., Sakalauskas, A., Mikalauskaite, K., and Smirnovas, V<\/strong>. (2021). Polymorphism of Alpha-Synuclein Amyloid Fibrils Depends on Ionic Strength and Protein<\/a><\/strong> Concentration. International Journal of Molecular Sciences<\/em> 22<\/em>, 12382.<\/p>\n\n\n\n

45. Ziaunys, M., Mikalauskaite, K., Sakalauskas, A., and Smirnovas, V<\/strong>. (2021). Interplay between epigallocatechin-3-gallate and ionic strength during amyloid aggregation<\/a><\/strong>. PeerJ<\/em> 9<\/em>, e12381.<\/p>\n\n\n\n

44. Arabuli, L., Iashchishyn, I.A., Romanova, N.V., Musteikyte, G., Smirnovas, V<\/strong>., Chaudhary, H., Svedru\u017ei\u0107, \u017d.M., and Morozova-Roche, L.A. (2021). Co-Aggregation of S100A9 with DOPA and Cyclen-Based Compounds Manifested in Amyloid Fibril Thickening without Altering Rates of Self-Assembly<\/a><\/strong>. International Journal of Molecular Sciences 22<\/em>, 8556.<\/p>\n\n\n\n

43. Strazdaite, S., Roeters, S.J., Sakalauskas, A., Sneideris, T<\/strong>., Kirschner, J., Pedersen, K.B., Schi\u00f8tt, B., Jensen, F., Weidner, T., Smirnovas, V<\/strong>., et al. (2021). Interaction of Amyloid-\u03b2-(1\u201342) Peptide and Its Aggregates with Lipid\/Water Interfaces Probed by Vibrational Sum-Frequency Generation Spectroscopy<\/a><\/strong>. J. Phys. Chem. B<\/em> 125<\/em>, 11208\u201311218.<\/p>\n\n\n\n

42. Sakalauskas, A., Ziaunys, M., Snieckute, R., and Smirnovas, V<\/strong>. (2021). Autoxidation Enhances Anti-Amyloid Potential of Flavone Derivatives<\/a><\/strong>. Antioxidants<\/em> 10<\/em>, 1428.<\/p>\n\n\n\n

41. Toleikis, Z., Ziaunys, M<\/strong>., Baranauskiene, L<\/strong>., Petrauskas, V., Jaudzems, K., and Smirnovas, V<\/strong>. (2021). S100A9 Alters the Pathway of Alpha-Synuclein Amyloid Aggregation. <\/a><\/strong>International Journal of Molecular Sciences<\/em> 22<\/em>, 7972. <\/p>\n\n\n\n

40. Fridmanis, J., Toleikis, Z., Sneideris, T., Ziaunys, M<\/strong>., Bobrovs, R., Smirnovas, V<\/strong>., and Jaudzems, K. (2021). Aggregation Condition\u2013Structure Relationship of Mouse Prion Protein Fibrils<\/a><\/strong>. International Journal of Molecular Sciences<\/em> 22<\/em>, 9635.<\/p>\n\n\n\n

39. Chaudhary, H., Iashchishyn, I.A., Romanova, N.V., Rambaran, M.A., Musteikyte, G., Smirnovas, V<\/strong>., Holmboe, M., Ohlin, C.A., Svedru\u017ei\u0107, \u017d.M., and Morozova-Roche, L.A. (2021). Polyoxometalates as Effective Nano-inhibitors of Amyloid Aggregation of Pro-inflammatory S100A9 Protein Involved in Neurodegenerative Diseases<\/a><\/strong>. ACS Appl. Mater. Interfaces<\/em> 13<\/em>, 26721\u201326734.<\/p>\n\n\n\n

38. Leri, M., Chaudhary, H., Iashchishyn, I.A., Pansieri, J., Svedru\u017ei\u0107, \u017d.M., G\u00f3mez Alcalde, S., Musteikyte, G., Smirnovas, V<\/strong>., Stefani, M., Bucciantini, M., et al. (2021). Natural Compound from Olive Oil Inhibits S100A9 Amyloid Formation and Cytotoxicity: Implications for Preventing Alzheimer\u2019s Disease<\/a><\/strong>. ACS Chem. Neurosci<\/em>. 12<\/em>, 1905\u20131918.<\/p>\n\n\n\n

37. Ziaunys, M., Mikalauskaite, K., Sakalauskas, A., and Smirnovas, V<\/strong>. (2021). Using lysozyme amyloid fibrils as a means of scavenging aggregation-inhibiting compounds<\/a><\/strong>. Biotechnology Journal 16<\/em>, 2100138.<\/p>\n\n\n\n

36. Kasho, K., Krasauskas, L., Smirnovas, V<\/strong>., Stojkovi\u010d, G., Morozova-Roche, L.A., and Wanrooij, S. (2021). Human Polymerase \u03b4-Interacting Protein 2 (PolDIP2) Inhibits the Formation of Human Tau Oligomers and Fibrils<\/a><\/strong>. International Journal of Molecular Sciences<\/em> 22<\/em>, 5768. <\/p>\n\n\n\n

35. Ziaunys, M., Sakalauskas, A., Mikalauskaite, K., Snieckute, R., and Smirnovas, V.<\/strong> (2021). Temperature-Dependent Structural Variability of Prion Protein Amyloid Fibrils<\/a><\/strong>. International Journal of Molecular Sciences<\/em> 22<\/em>, 5075.<\/p>\n\n\n\n

34. Szulc, N., Burdukiewicz, M., G\u0105sior-G\u0142ogowska, M., Wojciechowski, J.W., Chilimoniuk, J., Mackiewicz, P., \u0160neideris, T., Smirnovas, V<\/strong>., and Kotulska, M. (2021). Bioinformatics methods for identification of amyloidogenic peptides show robustness to misannotated training data<\/a><\/strong>. Scientific Reports<\/em> 11<\/em>, 8934.<\/p>\n\n\n\n

33. Jurgelevi\u010di\u016bt\u0117, J., Bi\u010dkovas, N., Sakalauskas, A<\/strong>., Novickij, V., Smirnovas, V<\/strong>., and Lastauskien\u0117, E. (2021). Effects of Pulsed Electric Fields on Yeast with Prions and the Structure of Amyloid Fibrils<\/a><\/strong>. Applied Sciences<\/em> 11<\/em>, 2684. <\/p>\n\n\n\n

32. Ziaunys, M., Sakalauskas, A., Sneideris, T., and Smirnovas, V<\/strong>. (2021). Lysozyme Fibrils Alter the Mechanism of Insulin Amyloid Aggregation<\/a><\/strong>. International Journal of Molecular Sciences<\/em> 22<\/em>, 1775. <\/p>\n\n\n\n

31. Ziaunys, M., Sakalauskas, A., Mikalauskaite, K., and Smirnovas, V<\/strong>. (2021). Exploring the occurrence of thioflavin-T-positive insulin amyloid aggregation intermediates<\/a><\/strong>. PeerJ<\/em> 9<\/em>, e10918.<\/p>\n\n\n\n

30. Cataldi, R., Chia, S., Pisani, K., Ruggeri, F.S., Xu, C.K., \u0160neideris, T<\/strong>., Perni, M., Sarwat, S., Joshi, P., Kumita, J.R., et al. (2021). A dopamine metabolite stabilizes neurotoxic amyloid-\u03b2 oligomers<\/a><\/strong>. Communications Biology<\/em> 4<\/em>, 1\u201310.<\/p>\n\n\n\n

29. Martins, 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., et al. (2020). MIRRAGGE \u2013 Minimum Information Required for Reproducible AGGregation Experiments<\/strong><\/a>. Frontiers in Molecular Neurosci<\/em>ence 13<\/em>.<\/p>\n\n\n\n

28. Mikalauskaite, K., Ziaunys, M., Sneideris, T., and Smirnovas, V<\/strong>. (2020). Effect of Ionic Strength on Thioflavin-T Affinity to Amyloid Fibrils and its Fluorescence Intensity<\/a><\/strong>. International Journal of Molecular Sciences<\/em> 21<\/em>, 8916.<\/p>\n\n\n\n

27. Ziaunys, M., Sakalauskas, A., and Smirnovas, V.<\/strong> (2020). Identifying Insulin Fibril Conformational Differences by Thioflavin-T Binding Characteristics<\/strong><\/a>. Biomacromolecules<\/em> .<\/p>\n\n\n\n

26. Sneideris, T., Ziaunys, M<\/strong>., Chu, B.K.-Y., Chen, R.P.-Y., and Smirnovas, V<\/strong>. (2020). Self-Replication of Prion Protein Fragment 89-230 Amyloid Fibrils Accelerated by Prion Protein Fragment 107-143 Aggregates<\/a><\/strong>. International Journal of Molecular Sciences<\/em> 21<\/em>, 7410.<\/p>\n\n\n\n

25. Pampuscenko, K., Morkuniene, R., Krasauskas, L., Smirnovas, V<\/strong>., Tomita, T., and Borutaite, V. (2020). Distinct Neurotoxic Effects of Extracellular Tau Species in Primary Neuronal-Glial Cultures<\/a><\/strong>. Molecular Neurobiology<\/em>.<\/p>\n\n\n\n

24. Sakalauskas, A., Ziaunys, M., and Smirnovas, V. <\/strong>(2020). Gallic acid oxidation products alter the formation pathway of insulin amyloid fibrils<\/a>. <\/strong>Scientific Reports<\/em> 10<\/em>, e14466.<\/p>\n\n\n\n

23. Musteikyte, G., Ziaunys, M., and Smirnovas V.<\/strong> (2020). Methylene blue inhibits nucleation and elongation of SOD1 amyloid fibrils.<\/strong><\/a> PeerJ<\/em>, 8<\/em>, e9719.<\/p>\n\n\n\n

22. Talaikis, M., Strazdait\u0117, S., \u017diaunys, M<\/strong>., and Niaura, G. (2020). Far-Off Resonance: Multiwavelength Raman Spectroscopy Probing Amide Bands of Amyloid-\u03b2-(37\u201342) Peptide<\/a><\/strong>. Molecules<\/em> 25<\/em>, e3556.<\/p>\n\n\n\n

21. Pansieri, J., Iashchishyn, I.A., Fakhouri, H., Ostoji\u0107, L., Malisauskas, M., Musteikyte, G., Smirnovas, V.<\/strong>, Schneider, M.M., Scheidt, T., Xu, C.K., et al. (2020). Templating S100A9 amyloids on A\u03b2 fibrillar surfaces revealed by charge detection mass spectrometry, microscopy, kinetic and microfluidic analyses<\/strong><\/a>. Chemical Science<\/em> 11<\/em>, 7031\u20137039. BioRxiv preprint version<\/a><\/strong><\/p>\n\n\n\n

20. Strazdaite, S., Navakauskas, E., Kirschner, J., Sneideris, T<\/strong>., and Niaura, G. (2020). Structure Determination of Hen Egg-White Lysozyme Aggregates Adsorbed to Lipid\/Water and Air\/Water Interfaces<\/a><\/strong>. Langmuir<\/em> 36<\/em>, 4766\u20134775.<\/p>\n\n\n\n

19. Ziaunys, M., Sneideris, T., and Smirnovas, V.<\/strong> (2020). Formation of distinct prion protein amyloid fibrils under identical experimental conditions<\/strong><\/a>. Scientific Reports<\/em> 10<\/em>, e4572.<\/p>\n\n\n\n

18. Pampuscenko, K., Morkuniene, R., Sneideris, T., Smirnovas, V<\/strong>., Budvytyte, R., Valincius, G., Brown, G.C., and Borutaite, V. (2020). Extracellular tau induces microglial phagocytosis of living neurons in cell cultures<\/a><\/strong>. Journal of Neurochemistry<\/em> 154<\/em>, 316-329.<\/p>\n\n\n\n

17. Ziaunys, M., Mikalauskaite, K., and Smirnovas, V.<\/strong> (2019). Amyloidophilic Molecule Interactions on the Surface of Insulin Fibrils: Cooperative Binding and Fluorescence Quenching<\/a><\/strong>. Scientific Reports<\/em> 9<\/em>, e20303.<\/p>\n\n\n\n

16. Sneideris, T., Sakalauskas, A<\/strong>., Sternke-Hoffmann, R., Peduzzo, A., Ziaunys, M.<\/strong>, Buell, A.K., and Smirnovas, V.<\/strong> (2019). The Environment Is a Key Factor in Determining the Anti-Amyloid Efficacy of EGCG<\/a><\/strong>. Biomolecules<\/em> 9<\/em>, e855.<\/p>\n\n\n\n

15. Sakalauskas, A., Ziaunys, M., and Smirnovas, V<\/strong>. (2019). Concentration-dependent polymorphism of insulin amyloid fibrils<\/a><\/strong>. PeerJ<\/em> 7<\/em>, e8208.<\/p>\n\n\n\n

14 Ziaunys, M., and Smirnovas, V<\/strong>. (2019). Additional Thioflavin-T Binding Mode in Insulin Fibril Inner Core Region<\/a><\/strong>. Journal of Physical Chemistry B<\/em> 123<\/em>, 8727\u20138732.<\/p>\n\n\n\n

13. Ruggeri, F.S., \u0160neideris, T.<\/strong>, Chia, S., Vendruscolo, M., and Knowles, T.P.J. (2019). Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy<\/a><\/strong>. JoVE (Journal of Visualized Experiments)<\/em> e60108.<\/p>\n\n\n\n

12. Ziaunys, M., Sneideris, T., and Smirnovas, V<\/strong>. (2019). Exploring the potential of deep-blue autofluorescence for monitoring amyloid fibril formation and dissociation<\/a><\/strong>. PeerJ<\/em> 7<\/em>, e7554.<\/p>\n\n\n\n

11. Pansieri, 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.<\/strong>, Svedru\u017ei\u0107, \u017d., et al. (2019). Pro-Inflammatory S100A9 Protein Aggregation Promoted by NCAM1 P<\/a><\/strong>eptide Constructs. ACS Chemical Biology<\/em> 14<\/em>, 1410\u20131417.<\/p>\n\n\n\n

10. Ruggeri, F.S., \u0160neideris, T.<\/strong>, Vendruscolo, M., and Knowles, T.P.J. (2019). Atomic force microscopy for single molecule characterisation of protein aggregation<\/a><\/strong>. Archives of Biochemistry and Biophysics<\/em> 664<\/em>, 134\u2013148.<\/p>\n\n\n\n

9. Ziaunys, M., and Smirnovas, V<\/strong>. (2019). Emergence of visible light optical properties of L-phenylalanine aggregates<\/a><\/strong>. PeerJ<\/em> 7<\/em>, e6518.<\/p>\n\n\n\n

8. Ziaunys, M., Sneideris, T., and Smirnovas, V<\/strong>. (2018). Self-inhibition of insulin amyloid-like aggregation<\/a><\/strong>. Physical Chemistry Chemical Physics<\/em> 20<\/em>, 27638\u201327645.<\/p>\n\n\n\n

7. Iashchishyn, I.A., Sulskis, D., Nguyen Ngoc, M., Smirnovas, V<\/strong>., and Morozova-Roche, L.A. (2017). Finke\u2013Watzky Two-Step Nucleation\u2013Autocatalysis Model of S100A9 Amyloid Formation: Protein Misfolding as \u201cNucleation\u201d Event<\/a><\/strong>. ACS Chemical Neuroscience<\/em> 8<\/em>, 2152\u20132158.<\/p>\n\n\n\n

6. \u0160neideris, T., Baranauskien\u0117, L<\/strong>., Cannon, J.G., Rutkien\u0117, R., Me\u0161kys, R., and Smirnovas, V<\/strong>. (2015). Looking for a generic inhibitor of amyloid-like fibril formation among flavone derivatives<\/a><\/strong>. PeerJ<\/em> 3<\/em>, e1271.<\/p>\n\n\n\n

5. Sneideris, T., Milto, K., and Smirnovas, V<\/strong>. (2015). Polymorphism of amyloid-like fibrils can be defined by the concentration of seeds<\/a><\/strong>. PeerJ<\/em> 3<\/em>, e1207.<\/p>\n\n\n\n

4. Sneideris, T., Darguzis, D., Botyriute, A., Grigaliunas, M<\/strong>., Winter, R., and Smirnovas, V<\/strong>. (2015). pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils<\/a><\/strong>. PloS One<\/em> 10<\/em>, e0136602.<\/p>\n\n\n\n

3. Malisauskas, R., Botyriute, A<\/strong>., Cannon, J.G., and Smirnovas, V<\/strong>. (2015). Flavone derivatives as inhibitors of insulin amyloid-like fibril formation<\/a><\/strong>. PloS One<\/em> 10<\/em>, e0121231.<\/p>\n\n\n\n

2. Milto, K., Michailova, K., and Smirnovas, V<\/strong>. (2014). Elongation of mouse prion protein amyloid-like fibrils: Effect of temperature and denaturant concentration<\/a><\/strong>. PLoS One<\/em> 9<\/em>, e94469.<\/p>\n\n\n\n

1. Milto, K., Botyriute, A., and Smirnovas, V<\/strong>. (2013). Amyloid-Like Fibril Elongation Follows Michaelis-Menten Kinetics<\/a><\/strong>. PLoS One<\/em> 8<\/em>, e68684.<\/p>\n","protected":false},"excerpt":{"rendered":"

88. Karalkevi\u010di\u016bt\u0117, V., Rapalyt\u0117, S., Baronait\u0117, I., Veiveris, D., Smirnovas, V., \u017diaunys, M., and \u0160ulskis, D. (2026). Liquid-liquid phase separation and amyloid aggregation in the 14-3-3 protein family. Preprint at bioRxiv, 87. Snie\u010dkut\u0117, R., \u0160ulskis, D., Jocyt\u0117, A., Venclovait\u0117, U., Tamulyt\u0117, R., \u017diaunys, M., Smirnovas, V., and Sakalauskas, A. (2025). Formation of Condition-Dependent Alpha-Synuclein Fibril […]<\/p>\n","protected":false},"author":1,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"open","template":"","meta":{"footnotes":""},"class_list":["post-2","page","type-page","status-publish","hentry"],"blocksy_meta":[],"rise-blocks_excerpt":"88. Karalkevi\u010di\u016bt\u0117, V., Rapalyt\u0117, S., Baronait\u0117, I., Veiveris, D., Smirnovas, V., \u017diaunys, M., and \u0160ulskis, D. (2026). Liquid-liquid phase separation and amyloid aggregation in the 14-3-3 protein family. Preprint at bioRxiv, 87. Snie\u010dkut\u0117, R., \u0160ulskis, D., Jocyt\u0117, A., Venclovait\u0117, U., Tamulyt\u0117, R., \u017diaunys, M., Smirnovas, V., and Sakalauskas, A. (2025). Formation of Condition-Dependent Alpha-Synuclein Fibril Strain in Artificial Cerebrospinal Fluid...","yoast_head":"\nPublikacijos - Amiloid\u0173 tyrimo sektorius<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"http:\/\/www.amyloid.bti.vu.lt\/en\/publikacijos\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Publikacijos - Amiloid\u0173 tyrimo sektorius\" \/>\n<meta property=\"og:description\" content=\"88. Karalkevi\u010di\u016bt\u0117, V., Rapalyt\u0117, S., Baronait\u0117, I., Veiveris, D., Smirnovas, V., \u017diaunys, M., and \u0160ulskis, D. (2026). Liquid-liquid phase separation and amyloid aggregation in the 14-3-3 protein family. Preprint at bioRxiv, 87. Snie\u010dkut\u0117, R., \u0160ulskis, D., Jocyt\u0117, A., Venclovait\u0117, U., Tamulyt\u0117, R., \u017diaunys, M., Smirnovas, V., and Sakalauskas, A. (2025). Formation of Condition-Dependent Alpha-Synuclein Fibril […]\" \/>\n<meta property=\"og:url\" content=\"http:\/\/www.amyloid.bti.vu.lt\/en\/publikacijos\/\" \/>\n<meta property=\"og:site_name\" content=\"Amiloid\u0173 tyrimo sektorius\" \/>\n<meta property=\"article:modified_time\" content=\"2026-02-25T09:23:06+00:00\" \/>\n<meta property=\"og:image\" content=\"http:\/\/www.amyloid.bti.vu.lt\/wp-content\/uploads\/2024\/04\/g6.png\" \/>\n\t<meta property=\"og:image:width\" content=\"887\" \/>\n\t<meta property=\"og:image:height\" content=\"442\" \/>\n\t<meta property=\"og:image:type\" content=\"image\/png\" \/>\n<meta name=\"twitter:card\" content=\"summary_large_image\" \/>\n<meta name=\"twitter:label1\" content=\"Est. reading time\" \/>\n\t<meta name=\"twitter:data1\" content=\"13 minutes\" \/>\n<script type=\"application\/ld+json\" class=\"yoast-schema-graph\">{\"@context\":\"https:\\\/\\\/schema.org\",\"@graph\":[{\"@type\":\"WebPage\",\"@id\":\"http:\\\/\\\/www.amyloid.bti.vu.lt\\\/publikacijos\\\/\",\"url\":\"http:\\\/\\\/www.amyloid.bti.vu.lt\\\/publikacijos\\\/\",\"name\":\"Publikacijos - Amiloid\u0173 tyrimo sektorius\",\"isPartOf\":{\"@id\":\"http:\\\/\\\/www.amyloid.bti.vu.lt\\\/#website\"},\"datePublished\":\"2020-05-15T09:15:16+00:00\",\"dateModified\":\"2026-02-25T09:23:06+00:00\",\"breadcrumb\":{\"@id\":\"http:\\\/\\\/www.amyloid.bti.vu.lt\\\/publikacijos\\\/#breadcrumb\"},\"inLanguage\":\"en-US\",\"potentialAction\":[{\"@type\":\"ReadAction\",\"target\":[\"http:\\\/\\\/www.amyloid.bti.vu.lt\\\/publikacijos\\\/\"]}]},{\"@type\":\"BreadcrumbList\",\"@id\":\"http:\\\/\\\/www.amyloid.bti.vu.lt\\\/publikacijos\\\/#breadcrumb\",\"itemListElement\":[{\"@type\":\"ListItem\",\"position\":1,\"name\":\"Home\",\"item\":\"http:\\\/\\\/www.amyloid.bti.vu.lt\\\/\"},{\"@type\":\"ListItem\",\"position\":2,\"name\":\"Publikacijos\"}]},{\"@type\":\"WebSite\",\"@id\":\"http:\\\/\\\/www.amyloid.bti.vu.lt\\\/#website\",\"url\":\"http:\\\/\\\/www.amyloid.bti.vu.lt\\\/\",\"name\":\"Amiloid\u0173 tyrimo grup\u0117\",\"description\":\"Gyvyb\u0117s moksl\u0173 centras, Saul\u0117tekio al. 7, Vilnius\",\"publisher\":{\"@id\":\"http:\\\/\\\/www.amyloid.bti.vu.lt\\\/#organization\"},\"potentialAction\":[{\"@type\":\"SearchAction\",\"target\":{\"@type\":\"EntryPoint\",\"urlTemplate\":\"http:\\\/\\\/www.amyloid.bti.vu.lt\\\/?s={search_term_string}\"},\"query-input\":{\"@type\":\"PropertyValueSpecification\",\"valueRequired\":true,\"valueName\":\"search_term_string\"}}],\"inLanguage\":\"en-US\"},{\"@type\":\"Organization\",\"@id\":\"http:\\\/\\\/www.amyloid.bti.vu.lt\\\/#organization\",\"name\":\"Amiloid\u0173 tyrimo grup\u0117\",\"url\":\"http:\\\/\\\/www.amyloid.bti.vu.lt\\\/\",\"logo\":{\"@type\":\"ImageObject\",\"inLanguage\":\"en-US\",\"@id\":\"http:\\\/\\\/www.amyloid.bti.vu.lt\\\/#\\\/schema\\\/logo\\\/image\\\/\",\"url\":\"http:\\\/\\\/www.amyloid.bti.vu.lt\\\/wp-content\\\/uploads\\\/2024\\\/04\\\/g6.png\",\"contentUrl\":\"http:\\\/\\\/www.amyloid.bti.vu.lt\\\/wp-content\\\/uploads\\\/2024\\\/04\\\/g6.png\",\"width\":887,\"height\":442,\"caption\":\"Amiloid\u0173 tyrimo grup\u0117\"},\"image\":{\"@id\":\"http:\\\/\\\/www.amyloid.bti.vu.lt\\\/#\\\/schema\\\/logo\\\/image\\\/\"},\"sameAs\":[\"https:\\\/\\\/www.linkedin.com\\\/company\\\/93628208\\\/\"]}]}<\/script>\n<!-- \/ Yoast SEO plugin. -->","yoast_head_json":{"title":"Publikacijos - Amiloid\u0173 tyrimo sektorius","robots":{"index":"index","follow":"follow","max-snippet":"max-snippet:-1","max-image-preview":"max-image-preview:large","max-video-preview":"max-video-preview:-1"},"canonical":"http:\/\/www.amyloid.bti.vu.lt\/en\/publikacijos\/","og_locale":"en_US","og_type":"article","og_title":"Publikacijos - Amiloid\u0173 tyrimo sektorius","og_description":"88. Karalkevi\u010di\u016bt\u0117, V., Rapalyt\u0117, S., Baronait\u0117, I., Veiveris, D., Smirnovas, V., \u017diaunys, M., and \u0160ulskis, D. (2026). Liquid-liquid phase separation and amyloid aggregation in the 14-3-3 protein family. Preprint at bioRxiv, 87. Snie\u010dkut\u0117, R., \u0160ulskis, D., Jocyt\u0117, A., Venclovait\u0117, U., Tamulyt\u0117, R., \u017diaunys, M., Smirnovas, V., and Sakalauskas, A. (2025). Formation of Condition-Dependent Alpha-Synuclein Fibril […]","og_url":"http:\/\/www.amyloid.bti.vu.lt\/en\/publikacijos\/","og_site_name":"Amiloid\u0173 tyrimo sektorius","article_modified_time":"2026-02-25T09:23:06+00:00","og_image":[{"width":887,"height":442,"url":"http:\/\/www.amyloid.bti.vu.lt\/wp-content\/uploads\/2024\/04\/g6.png","type":"image\/png"}],"twitter_card":"summary_large_image","twitter_misc":{"Est. reading time":"13 minutes"},"schema":{"@context":"https:\/\/schema.org","@graph":[{"@type":"WebPage","@id":"http:\/\/www.amyloid.bti.vu.lt\/publikacijos\/","url":"http:\/\/www.amyloid.bti.vu.lt\/publikacijos\/","name":"Publikacijos - Amiloid\u0173 tyrimo sektorius","isPartOf":{"@id":"http:\/\/www.amyloid.bti.vu.lt\/#website"},"datePublished":"2020-05-15T09:15:16+00:00","dateModified":"2026-02-25T09:23:06+00:00","breadcrumb":{"@id":"http:\/\/www.amyloid.bti.vu.lt\/publikacijos\/#breadcrumb"},"inLanguage":"en-US","potentialAction":[{"@type":"ReadAction","target":["http:\/\/www.amyloid.bti.vu.lt\/publikacijos\/"]}]},{"@type":"BreadcrumbList","@id":"http:\/\/www.amyloid.bti.vu.lt\/publikacijos\/#breadcrumb","itemListElement":[{"@type":"ListItem","position":1,"name":"Home","item":"http:\/\/www.amyloid.bti.vu.lt\/"},{"@type":"ListItem","position":2,"name":"Publikacijos"}]},{"@type":"WebSite","@id":"http:\/\/www.amyloid.bti.vu.lt\/#website","url":"http:\/\/www.amyloid.bti.vu.lt\/","name":"Amyloid Research Group","description":"Life Sciences Center, Sauletekio 7, Vilnius, Lithuania","publisher":{"@id":"http:\/\/www.amyloid.bti.vu.lt\/#organization"},"potentialAction":[{"@type":"SearchAction","target":{"@type":"EntryPoint","urlTemplate":"http:\/\/www.amyloid.bti.vu.lt\/?s={search_term_string}"},"query-input":{"@type":"PropertyValueSpecification","valueRequired":true,"valueName":"search_term_string"}}],"inLanguage":"en-US"},{"@type":"Organization","@id":"http:\/\/www.amyloid.bti.vu.lt\/#organization","name":"Amyloid Research Group","url":"http:\/\/www.amyloid.bti.vu.lt\/","logo":{"@type":"ImageObject","inLanguage":"en-US","@id":"http:\/\/www.amyloid.bti.vu.lt\/#\/schema\/logo\/image\/","url":"http:\/\/www.amyloid.bti.vu.lt\/wp-content\/uploads\/2024\/04\/g6.png","contentUrl":"http:\/\/www.amyloid.bti.vu.lt\/wp-content\/uploads\/2024\/04\/g6.png","width":887,"height":442,"caption":"Amiloid\u0173 tyrimo grup\u0117"},"image":{"@id":"http:\/\/www.amyloid.bti.vu.lt\/#\/schema\/logo\/image\/"},"sameAs":["https:\/\/www.linkedin.com\/company\/93628208\/"]}]}},"_links":{"self":[{"href":"http:\/\/www.amyloid.bti.vu.lt\/en\/wp-json\/wp\/v2\/pages\/2","targetHints":{"allow":["GET"]}}],"collection":[{"href":"http:\/\/www.amyloid.bti.vu.lt\/en\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"http:\/\/www.amyloid.bti.vu.lt\/en\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"http:\/\/www.amyloid.bti.vu.lt\/en\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"http:\/\/www.amyloid.bti.vu.lt\/en\/wp-json\/wp\/v2\/comments?post=2"}],"version-history":[{"count":68,"href":"http:\/\/www.amyloid.bti.vu.lt\/en\/wp-json\/wp\/v2\/pages\/2\/revisions"}],"predecessor-version":[{"id":1102,"href":"http:\/\/www.amyloid.bti.vu.lt\/en\/wp-json\/wp\/v2\/pages\/2\/revisions\/1102"}],"wp:attachment":[{"href":"http:\/\/www.amyloid.bti.vu.lt\/en\/wp-json\/wp\/v2\/media?parent=2"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}