Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Jana Mrázková"'
Publikováno v:
PLoS ONE, Vol 14, Iss 7, p e0220318 (2019)
Lectins are a group of ubiquitous proteins which specifically recognize and reversibly bind sugar moieties of glycoprotein and glycolipid constituents on cell surfaces. The mutagenesis approach is often employed to characterize lectin binding propert
Externí odkaz:
https://doaj.org/article/1d7c1fe6c80f4e22861f83bf36273557
Autor:
Petra Bořilová Linhartová, Jana Mrázková, Jan Lochman, Petr Sistek, Zdeněk Daněk, Lydie Izakovičová Hollá
Publikováno v:
Diagnostics, Vol 11, Iss 301, p 301 (2021)
Diagnostics
Volume 11
Issue 2
Diagnostics
Volume 11
Issue 2
Mannose-binding lectin (MBL) deficiency caused by the variability in the MBL2 gene is responsible for the susceptibility to and severity of various infectious and autoimmune diseases. A combination of six single nucleotide polymorphisms (SNPs) has a
Autor:
Peter H. Seeberger, Xiaoqiang Guo, Jana Mrázková, Franck Fieschi, You Yang, Hidenori Tanaka, Bernd Lepenies, Chakkumkal Anish, Frank Schuhmacher, Michaela Wimmerová, Christoph Rademacher, Daniele Leonori, Heung Sik Hahm, João T. Monteiro, Claney L. Pereira, Anika Reinhardt, Sandip Pasari, Sharavathi Guddehalli Parameswarappa, Mark K. Schlegel, Dan Grünstein, Jeyakumar Kandasamy, Guozhi Xiao, Andreas Geissner, Timo Johannssen, Sebastian Götze, Christopher E. Martin, Michel Thépaut
Publikováno v:
Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2019, 116 (6), pp.1958-1967. ⟨10.1073/pnas.1800853116⟩
Proceedings of the National Academy of Sciences of the United States of America, 2019, 116 (6), pp.1958-1967. ⟨10.1073/pnas.1800853116⟩
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2019, 116 (6), pp.1958-1967. ⟨10.1073/pnas.1800853116⟩
Proceedings of the National Academy of Sciences of the United States of America, 2019, 116 (6), pp.1958-1967. ⟨10.1073/pnas.1800853116⟩
International audience; Interactions between glycans and glycan binding proteins are essential for numerous processes in all kingdoms of life. Glycan microarrays are an excellent tool to examine protein-glycan interactions. Here, we present a microbe
Publikováno v:
PLoS ONE, Vol 14, Iss 7, p e0220318 (2019)
PLoS ONE
PLoS ONE
Lectins are a group of ubiquitous proteins which specifically recognize and reversibly bind sugar moieties of glycoprotein and glycolipid constituents on cell surfaces. The mutagenesis approach is often employed to characterize lectin binding propert
Autor:
Sylva Hönigová, Jana Mrázková
Publikováno v:
TESTFÓRUM. 4:79-92
Článek popisuje proces identifikace a nápravy obtíží ve vzdělávání u žáka základní školy. Vychází z pojetí tzv. třístupňového modelu péče, který klade důraz právě na proces oproti jednorázovým zjištěním. Popisuje mož
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1498
Site-directed mutagenesis is a powerful technique which is used to understand the basis of interactions between proteins and their binding partners, as well as to modify these interactions. Methods of rational design that are based on detailed knowle
Autor:
Jana Mrazkova, Petr Sistek, Jan Lochman, Lydie Izakovicova Holla, Zdenek Danek, Petra Borilova Linhartova
Publikováno v:
Diagnostics, Vol 11, Iss 2, p 301 (2021)
Mannose-binding lectin (MBL) deficiency caused by the variability in the MBL2 gene is responsible for the susceptibility to and severity of various infectious and autoimmune diseases. A combination of six single nucleotide polymorphisms (SNPs) has a
Externí odkaz:
https://doaj.org/article/9fc89a6b9c3f43d0a710d858c33d4144
Autor:
Zdeněk Kříž, Jana Mrázková, Petros Zotos, Jaroslav Koča, Michaela Wimmerová, Thomais Chatzipavlou, Jan Adam
Publikováno v:
Journal of Computer-Aided Molecular Design
This article focuses on designing mutations of the PA-IIL lectin from Pseudomonas aeruginosa that lead to change in specificity. Following the previous results revealing the importance of the amino acid triad 22–23–24 (so-called specificity-bindi