Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Péter Ecsédi"'
Autor:
Dóra Nagy-Fazekas, Pál Stráner, Péter Ecsédi, Nóra Taricska, Adina Borbély, László Nyitray, András Perczel
Publikováno v:
Bioengineering, Vol 10, Iss 3, p 389 (2023)
Antibodies are key proteins of the immune system, and they are widely used for both research and theragnostic applications. Among them, camelid immunoglobulins (IgG) differ from the canonical human IgG molecules, as their light chains are completely
Externí odkaz:
https://doaj.org/article/532fcbcce04c4c5eaab7d71a9c0ff521
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2021)
S100 proteins are small, dimeric, Ca2+-binding proteins of considerable interest due to their associations with cancer and rheumatic and neurodegenerative diseases. They control the functions of numerous proteins by forming protein–protein complexe
Externí odkaz:
https://doaj.org/article/c170172c3e8c487d80be6acd490c2342
Autor:
Fanni Sebák, Péter Ecsédi, Dóra K. Menyhárd, Gyula Pálfy, László Nyitray, Erika F. Dudás, Andrea Bodor
Publikováno v:
ChemBioChem. 21:3087-3095
Conformationally flexible protein complexes represent a major challenge for structural and dynamical studies. We present herein a method based on a hybrid NMR/MD approach to characterize the complex formed between the disordered p53TAD1-60 and the me
Publikováno v:
Angewandte Chemie International Edition. 61
It is important to identify proline cis/trans isomers that appear in several regulatory mechanisms of proteins, and to characterize minor species that are present due to the conformational heterogeneity in intrinsically disordered proteins (IDPs). To
Publikováno v:
Angewandte Chemie. 134
Publikováno v:
Angewandte Chemie (International ed. in English). 61(1)
It is important to identify proline cis/trans isomers that appear in several regulatory mechanisms of proteins, and to characterize minor species that are present due to the conformational heterogeneity in intrinsically disordered proteins (IDPs). To
Publikováno v:
Frontiers in Molecular Biosciences
Frontiers in Molecular Biosciences, 2021, 8, pp.749052. ⟨10.3389/fmolb.2021.749052⟩
Frontiers in Molecular Biosciences, Vol 8 (2021)
Frontiers in Molecular Biosciences, 2021, 8, pp.749052. ⟨10.3389/fmolb.2021.749052⟩
Frontiers in Molecular Biosciences, Vol 8 (2021)
S100 proteins are small, dimeric, Ca2+-binding proteins of considerable interest due to their associations with cancer and rheumatic and neurodegenerative diseases. They control the functions of numerous proteins by forming protein–protein complexe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e425f53af94fdb4010a5d4608fdf5cf5
https://hal.science/hal-03706776/file/fmolb-08-749052.pdf
https://hal.science/hal-03706776/file/fmolb-08-749052.pdf
Autor:
Erika F, Dudás, Gyula, Pálfy, Dóra K, Menyhárd, Fanni, Sebák, Péter, Ecsédi, László, Nyitray, Andrea, Bodor
Publikováno v:
Chembiochem
Conformationally flexible protein complexes represent a major challenge for structural and dynamical studies. We present herein a method based on a hybrid NMR/MD approach to characterize the complex formed between the disordered p53TAD1–60 and the
Autor:
Márton A. Simon, Ádám Póti, Péter Ecsédi, Attila Reményi, Gábor M. Kovács, Gergő Gógl, József Kardos, László Nyitray
Publikováno v:
FEBS Journal
FEBS Journal, 2020, 287 (13), pp.2834-2846. ⟨10.1111/febs.15175⟩
FEBS Journal, 2020, 287 (13), pp.2834-2846. ⟨10.1111/febs.15175⟩
International audience; The calcium-binding, vertebrate-specific S100 protein family consists of 20 paralogs in humans (referred as the S100ome), with several clinically important members. To explore their protein-protein interactions (PPIs) quantita
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34196efc5fae669cabd3ec30fdbd3dd2
https://hal.science/hal-03700709/document
https://hal.science/hal-03700709/document
Publikováno v:
Structure
Structure, 2020, 28 (8), pp.943-953.e4. ⟨10.1016/j.str.2020.05.001⟩
Structure, 2020, 28 (8), pp.943-953.e4. ⟨10.1016/j.str.2020.05.001⟩
International audience; To fully understand the environmental factors that influence crystallization is an enormous task, therefore crystallographers are still forced to work "blindly" trying as many crystallizing conditions and mutations to improve