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pro vyhledávání: '"Jan Byska"'
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 18, Iss , Pp 532-547 (2020)
N-terminal acetyltransferases (NATs) belong to the superfamily of acetyltransferases. They are enzymes catalysing the transfer of an acetyl group from acetyl coenzyme A to the N-terminus of polypeptide chains. N-terminal acetylation is one of the mos
Externí odkaz:
https://doaj.org/article/c0bab6a947cb4e70817490881c617cf5
Autor:
Katarína Furmanová, Jan Byška, Eduard M. Gröller, Ivan Viola, Jan J. Paleček, Barbora Kozlíková
Publikováno v:
BMC Bioinformatics, Vol 19, Iss 1, Pp 1-17 (2018)
Abstract Background Studying the patterns of protein-protein interactions (PPIs) is fundamental for understanding the structure and function of protein complexes. The exploration of the vast space of possible mutual configurations of interacting prot
Externí odkaz:
https://doaj.org/article/1313da42c8184e1cbb49ce6ddf24bd2e
Autor:
Pavol Ulbrich, Manuela Waldner, Katarina Furmanova, Sergio M. Marques, David Bednar, Barbora Kozlikova, Jan Byska
Publikováno v:
IEEE Transactions on Visualization and Computer Graphics
We present sMolBoxes, a dataflow representation for the exploration and analysis of long molecular dynamics (MD) simulations. When MD simulations reach millions of snapshots, a frame-by-frame observation is not feasible anymore. Thus, biochemists rel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe8eb300a63407ed17f693844c5359c3
http://arxiv.org/abs/2209.11771
http://arxiv.org/abs/2209.11771
Autor:
Joan Planas-Iglesias, Filip Opaleny, Pavol Ulbrich, Jan Stourac, Zainab Sanusi, Gaspar P Pinto, Andrea Schenkmayerova, Jan Byska, Jiri Damborsky, Barbora Kozlikova, David Bednar
Publikováno v:
Nucleic acids research
The transplantation of loops between structurally related proteins is a compelling method to improve the activity, specificity and stability of enzymes. However, despite the interest of loop regions in protein engineering, the available methods of lo
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2074
Networks of protein-protein interactions (PPI) constitute either stable or transient complexes in every cell. Most of the cellular complexes keep their function, and therefore stay similar, during evolution. The evolutionary constraints preserve most