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Jan 04

73. 1H, 13C, and 15N chemical shift assignments of the SUD domains of SARS-CoV-2 non-structural protein 3c: “The SUD-M & SUD-C domains”. Biomol. NMR Assign.  15, 165-171, (2021)

73. Α. Gallo, A.C. Tsika, N.K. Fourkiotis, F. Cantini F, L. Banci,  S. Sreeramulu, H. Schwalbe, G.A. Spyroulias. 1H, 13C, and 15N chemical shift assignments of the SUD domains of SARS-CoV-2 non-structural protein 3c: “The SUD-M & SUD-C domains”. Biomol. NMR Assign.  15, 165-171, (2021). https://doi.org/10.1007/s12104-020-10000-9

Jan 04

72. 1H, 13C, and 15N chemical shift assignments of the SUD domains of SARS-CoV-2 non-structural protein 3c: “The N-terminal domain-SUD-N”. Biomol. NMR Assign.  15, 85-89 (2021)

72. Α. Gallo, A.C. Tsika, N.K. Fourkiotis, F. Cantini F, L. Banci,  S. Sreeramulu, H. Schwalbe, G.A. Spyroulias. 1H, 13C, and 15N chemical shift assignments of the SUD domains of SARS-CoV-2 non-structural protein 3c: “The N-terminal domain-SUD-N”. Biomol. NMR Assign.  15, 85-89 (2021). https://doi.org/10.1007/s12104-020-09987-y

Jan 04

71. 1H, 13C and 15N backbone and side-chain resonance assignment of Nostoc sp. C139A variant of the Heme-Nitric Oxide/Oxygen Binding(H-NOX) domain in complex with cinaciguat (BAY 58-2667). Biomol. NMR Assign.  15, 53-57 (2021)

71. G. Dalkas, G.I.  Makrynitsa, A. Argyriou, M. Bantzi, S. Topouzis, P. Sandner, A. Giannis, A. Papapetropoulos, G.A. Spyroulias.  1H, 13C and 15N backbone and side-chain resonance assignment of Nostoc sp. C139A variant of the Heme-Nitric Oxide/Oxygen Binding(H-NOX) domain in complex with cinaciguat (BAY 58-2667). Biomol. NMR Assign.  15, 53-57 (2021). https://doi.org/10.1007/s12104-016-9707-6

Jan 04

70. A quantitative western blot technique using TMB: Comparison with a free quantification software. Electrophoresis  42, 786-792  (2021)

70. Α. Ntoukas, A. Niarchos, A.C. Tsika, S. Mantzoukas, G.A. Spyroulias,, K. Poulas.  A quantitative western blot technique using TMB: Comparison with a free quantification software. Electrophoresis  42, 786-792  (2021).  https://doi.org/10.1002/elps.202000306

Jan 04

69. Assessment of biodistribution of TAT-L-Sco2 Fusion Protein, towards a Protein Therapeutic approach for Mitochondrial Neurodegenerative Disorders, due to SCO2 Mutations. Mol. Genet. Metab. Rep., 25, 100683, (2020)

69. G.C. Kaiafas, D. Papagiannopoulou, Α.N. Miliotou, A.S. Tsingotjidou, P.C. Chalkidou, A.C. Tsika, G.A. Spyroulias, A.S. Tsiftsoglou, L.C. Papadopoulou. Assessment of biodistribution of TAT-L-Sco2 Fusion Protein, towards a Protein Therapeutic approach for Mitochondrial Neurodegenerative Disorders, due to SCO2 Mutations. Mol. Genet. Metab. Rep., 25, 100683, (2020). https://doi.org/10.1016/j.ymgmr.2020.100683

Jan 04

68. Identification of compounds that bind the centriolar protein SAS-6 and inhibit its oligomerisation. J. Biol. Chem. 295, 17922-17934, (2020)

68. J.M.C. Busch, M.-T. Matsoukas, M. Musgaard, G.A. Spyroulias, P.C. Biggin, I. Vakonakis. Identification of compounds that bind the centriolar protein SAS-6 and inhibit its oligomerisation. J. Biol. Chem. 295, 17922-17934, (2020). https://doi.org/10.1074/jbc.RA120.014780

Jan 04

67. Functional and structural aspects of La overexpression in lung cancer. J. Mol. Biol. 432, 166712 (2020)

67. E. Kaliatsi, A. Argyriou, G. Bouras, M. Apostolidi, P. Konstantinidou, A.-N. Sokat, G.A. Spyroulias, C. Stathopoulos. Functional and structural aspects of La overexpression in lung cancer. J. Mol. Biol. 432, 166712 (2020). https://doi.org/10.1016/j.jmb.2020.11.011

Jan 04

66. Discovery of a stable tripeptide targeting the N-domain of CRF1 receptor. Amino Acids  52, 1337-1351 (2020)

66. G. Liapakis, V. Karageorgos, J. Andreadelis, G.G. Holz, E. Dermitzaki, G.G. Kordopati, E.K. Stylos, K. Spyridaki, S. Poulaki, D. Ntountaniotis, S. Sakellaris, M. Vanioti, A. Kostagianni, K.D. Marousis, G. Leonis, G. Kokotos, M. Venihaki, G.A. Spyroulias, T. Tselios, A. Margioris, A. Tzakos, Τ. Mavromoustakos.  Discovery of a stable tripeptide targeting the N-domain of CRF1 receptor. Amino Acids  52, 1337-1351 (2020). https://doi.org/10.1007/s00726-020-02895-4

Jan 04

65. H, 13C, and 15N backbone chemical shift assignments of the apo and the ADP-ribose bound forms of the macrodomain of SARS-CoV-2 non-structural protein 3b Biomol. NMR Assign.  14, 339-346 (2020)

65. F. Cantini, L. Banci, N. Altincekic, J.K. Bains, K. Dhamotharan, C. Fuks, B. Fürtig, S.L. Gande, B. Hargittay, M. Hengesbach, M.T. Hutchison, S.M. Korn, N. Kubatova, F. Kutz, V. Linhard, F. Löhr, N. Meiser, D.J. Pyper, N.S. Qureshi, C. Richter, K. Saxena, A. Schlundt, H. Schwalbe, S. Sreeramulu, J.N. Tants, A. Wacker, J.E. Weigand, J. Wöhnert, A.C. Tsika, N. Fourkiotis, G.A. Spyroulias. 1H, 13C, and 15N backbone chemical shift assignments of the apo and the ADP-ribose bound forms of the macrodomain of SARS-CoV-2 non-structural protein 3b. Biomol. NMR Assign.  14, 339-346 (2020).  https://doi.org/10.1007/s12104-020-09973-4

Jan 04

64. Unsaturated fatty acid-induced conformational transitions and aggregation of the repeat domain of Tau. Molecules  25, 2716 (1-21), (2020)

64. C.G. Barracchia, R. Tira, F. Parolini, F. Munari, L. Bubacco, G.A. Spyroulias, M. D’Onofrio, M. Assfalg. Unsaturated fatty acid-induced conformational transitions and aggregation of the repeat domain of Tau. Molecules  25, 2716 (1-21), (2020). https://doi.org/10.3390/molecules25112716