Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Tatsiana Charnavets"'
Autor:
Phuong Ngoc Pham, Maroš Huličiak, Lada Biedermannová, Jiří Černý, Tatsiana Charnavets, Gustavo Fuertes, Štěpán Herynek, Lucie Kolářová, Petr Kolenko, Jiří Pavlíček, Jiří Zahradník, Pavel Mikulecky, Bohdan Schneider
Publikováno v:
Viruses, Vol 13, Iss 2, p 190 (2021)
Engineered small non-antibody protein scaffolds are a promising alternative to antibodies and are especially attractive for use in protein therapeutics and diagnostics. The advantages include smaller size and a more robust, single-domain structural f
Externí odkaz:
https://doaj.org/article/ca7c6b6725114b919d25f73d80bebe28
Autor:
Mikhail Makarov, Alma C. Sanchez Rocha, Robin Krystufek, Ivan Cherepashuk, Volha Dzmitruk, Tatsiana Charnavets, Anneliese M. Faustino, Michal Lebl, Kosuke Fujishima, Stephen D. Fried, Klara Hlouchova
Publikováno v:
Journal of the American Chemical Society. 145:5320-5329
Whereas modern proteins rely on a quasi-universal repertoire of 20 canonical amino acids (AAs), numerous lines of evidence suggest that ancient proteins relied on a limited alphabet of 10 ‘early’ AAs, and that the 10 ‘late’ AAs were products
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2ca8cb37b64e3946b9527babfc6bab5
https://doi.org/10.1021/jacs.2c12987
https://doi.org/10.1021/jacs.2c12987
Autor:
Miroslav Janata, Eva Čadová, Pavla Angelisová, Tatsiana Charnavets, Václav Hořejší, Vladimír Raus
Publikováno v:
Macromolecular bioscience. 22(10)
Low-molecular weight (MW) amphiphilic copolymers have been recently introduced as a powerful tool for the detergent-free isolation of cell membrane proteins. Herein, a screening approach is used to identify a new copolymer type for this application.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ceafa0a339f64a6d13f493c551753295
https://pubmed.ncbi.nlm.nih.gov/35964154
https://pubmed.ncbi.nlm.nih.gov/35964154
Publikováno v:
Acta Crystallographica. Section D, Structural Biology
Two investigated DNA 18-mers indicate a dynamic equilibrium of conformations in solution and crystallize as duplexes with two consecutive T–T mismatches. Neither these mismatched nucleotides nor others found in the PDB exhibit unique structural fea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::664a58de4189dbacb3c63f277722f66f
https://doi.org/10.1107/s2059798320014151
https://doi.org/10.1107/s2059798320014151
Autor:
Tatsiana Charnavets, Yoav Peleg, Tamar Unger, Petr Kolenko, Lucie Kolářová, Silvie Svidenská, Jiří Zahradník, Joel L. Sussman, Bohdan Schneider
Publikováno v:
The FEBS Journal. 286:3858-3873
Interleukin 24 (IL-24) is a cytokine with the potential to be an effective treatment for autoimmune diseases and cancer. However, its instability and difficulties in its production have hampered detailed biological and biophysical studies. We approac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9feda0923f4c3d897d929ab635692a92
https://doi.org/10.1111/febs.14945
https://doi.org/10.1111/febs.14945
Autor:
Štěpán Herynek, Lucie Kolářová, Gustavo Fuertes, Jiří Černý, Phuong Ngoc Pham, Bohdan Schneider, Petr Kolenko, Pavel Mikulecky, Jiří Zahradník, Jiří Pavlíček, Tatsiana Charnavets, Lada Biedermannová, Maroš Huličiak
Publikováno v:
Viruses
Volume 13
Issue 2
Viruses, Vol 13, Iss 190, p 190 (2021)
Volume 13
Issue 2
Viruses, Vol 13, Iss 190, p 190 (2021)
Engineered small non-antibody protein scaffolds are a promising alternative to antibodies and are especially attractive for use in protein therapeutics and diagnostics. The advantages include smaller size and a more robust, single-domain structural f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c5bb7d198b0b5b05b03a626be9a1597
Autor:
Lucie Bednárová, Jiri Vondrasek, Jiri Vymetal, Janne E. Reseland, Ondřej Vaněk, Petra Sázelová, Monika Zouharova, Václav Kašička, Tatsiana Charnavets, Michaela Rumlová, Kristyna Bousova, Jaroslav Srp, Klara Postulkova, Veronika Vetyskova
Publikováno v:
International Journal of Molecular Sciences
Volume 21
Issue 23
International Journal of Molecular Sciences, Vol 21, Iss 9293, p 9293 (2020)
Volume 21
Issue 23
International Journal of Molecular Sciences, Vol 21, Iss 9293, p 9293 (2020)
Ameloblastin (Ambn) as an intrinsically disordered protein (IDP) stands for an important role in the formation of enamel&mdash
the hardest biomineralized tissue commonly formed in vertebrates. The human ameloblastin (AMBN) is expressed in two is
the hardest biomineralized tissue commonly formed in vertebrates. The human ameloblastin (AMBN) is expressed in two is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc8201677c44bd851e172c5e66bc2244
http://hdl.handle.net/10852/81567
http://hdl.handle.net/10852/81567
Autor:
Lukas Traxler, Felix Faschinger, Michael Stadlbauer, Hermann J. Gruber, Peter Hinterdorfer, Tatsiana Charnavets, Marc Fahrner, Christoph Romanin, Petr Rathner, Norbert Müller
Publikováno v:
Angewandte Chemie. 129:15962-15967
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b2a7d00d7a1b76514b34436f9429733c
https://doi.org/10.1002/ange.201708667
https://doi.org/10.1002/ange.201708667
Autor:
Jaroslav Nunvar, Jens Völker, Tatsiana Charnavets, Kenneth J. Breslauer, Bohdan Schneider, Iva Nečasová
Publikováno v:
Biopolymers
Repetitive extragenic palindrome (REP)—associated tyrosine transposase enzymes (RAYTs) bind REP DNA domains and catalyze their cleavage. Genomic sequence analyses identify potential noncoding REP sequences associated with RAYT-encoding genes. To pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c13f67baeb56d704ae0918c3592392e3
https://doi.org/10.1002/bip.22666
https://doi.org/10.1002/bip.22666
Autor:
Lukas, Traxler, Petr, Rathner, Marc, Fahrner, Michael, Stadlbauer, Felix, Faschinger, Tatsiana, Charnavets, Norbert, Müller, Christoph, Romanin, Peter, Hinterdorfer, Hermann J, Gruber
Publikováno v:
Angewandte Chemie (International ed. in English). 56(49)
Calmodulin (CaM) binds most of its targets by wrapping around an amphipathic α-helix. The N-terminus of Orai proteins contains a conserved CaM-binding segment but the binding mechanism has been only partially characterized. Here, microscale thermoph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::746d824513db65132fbb592bbcb1a2ba
https://pubmed.ncbi.nlm.nih.gov/29024298
https://pubmed.ncbi.nlm.nih.gov/29024298