Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Sven Wernersson"'
Autor:
Maria Luisa Verteramo, Majda Misini Ignjatović, Rohit Kumar, Sven Wernersson, Vilhelm Ekberg, Johan Wallerstein, Göran Carlström, Veronika Chadimová, Hakon Leffler, Fredrik Zetterberg, Derek T. Logan, Ulf Ryde, Mikael Akke, Ulf J. Nilsson
Publikováno v:
iScience, Vol 27, Iss 4, Pp 109636- (2024)
Summary: Halogen bonding is increasingly utilized in efforts to achieve high affinity and selectivity of molecules designed to bind proteins, making it paramount to understand the relationship between structure, dynamics, and thermodynamic driving fo
Externí odkaz:
https://doaj.org/article/04a7dad9b6fc435daabaaf102e239b88
Autor:
Johan Wallerstein, Vilhelm Ekberg, Majda Misini Ignjatović, Rohit Kumar, Octav Caldararu, Kristoffer Peterson, Sven Wernersson, Ulrika Brath, Hakon Leffler, Esko Oksanen, Derek T. Logan, Ulf J. Nilsson, Ulf Ryde, Mikael Akke
Publikováno v:
JACS Au, Vol 1, Iss 4, Pp 484-500 (2021)
Externí odkaz:
https://doaj.org/article/2981db6db17549c9b3a2c12397786a4f
Autor:
Sven Wernersson, Romel Bobby, Liz Flavell, Alexander G. Milbradt, Geoffrey A. Holdgate, Kevin J. Embrey, Mikael Akke
Publikováno v:
Biochemistry. 61:2303-2318
The bromodomain and extra-terminal (BET) protein BRD4 regulates gene expression via recruitment of transcriptional regulatory complexes to acetylated chromatin. Like other BET proteins, BRD4 contains two bromodomains, BD1 and BD2, that can interact c
Autor:
Esko Oksanen, Majda Misini Ignjatović, Ulrika Brath, Octav Caldararu, Sven Wernersson, Kristoffer Peterson, Derek T. Logan, Ulf J. Nilsson, Ulf Ryde, Vilhelm Ekberg, Johan Wallerstein, Mikael Akke, Rohit Kumar, Hakon Leffler
Publikováno v:
JACS Au
JACS Au 1(4), 484-500 (2021). doi:10.1021/jacsau.0c00094
JACS Au, Vol 1, Iss 4, Pp 484-500 (2021)
JACS Au 1(4), 484-500 (2021). doi:10.1021/jacsau.0c00094
JACS Au, Vol 1, Iss 4, Pp 484-500 (2021)
JACS Au 1(4), 484-500 (2021). doi:10.1021/jacsau.0c00094
Molecular recognition is fundamental to biological signaling. A central question is how individual interactions between molecular moieties affect the thermodynamics of ligand binding to pr
Molecular recognition is fundamental to biological signaling. A central question is how individual interactions between molecular moieties affect the thermodynamics of ligand binding to pr
Multidimensional, heteronuclear NMR relaxation methods are used extensively to characterize the dynamics of biological macromolecules. Acquisition of relaxation datasets on proteins typically require significant measurement time, often several days.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d1c6ade1c0428d8a638c8e9262624345
https://doi.org/10.5194/mr-2021-46
https://doi.org/10.5194/mr-2021-46
Autor:
Cecilia Persson, Santosh Kumar Upadhyay, Viktoria Bågenholm, Henrik Stålbrand, Sven Wernersson, Mikael Akke
Publikováno v:
Biomolecular Nmr Assignments
Bacteroides ovatus is a member of the human gut microbiota. The importance of this microbial consortium involves the degradation of complex dietary glycans mainly conferred by glycoside hydrolases. In this study we focus on one such catabolic glycosi
Autor:
Johan Härmark, Yoran Weide, Michal Respondek, Peter Højrup, Hans Hebert, Christopher A. G. Söderberg, Cecilia Emanuelsson, Mikael Akke, Gudrun Rutsdottir, Morten Rasmussen, Sven Wernersson, Philip J.B. Koeck
Publikováno v:
The Journal of Biological Chemistry
Rutsdottir, G, Härmark, J, Weide, Y, Hebert, H, Rasmussen, M I, Wernersson, S, Respondek, M, Akke, M, Højrup, P, Koeck, P J B, Söderberg, C A G & Emanuelsson, C 2017, ' Structural model of dodecameric heat-shock protein Hsp21 : Flexible N-terminal arms interact with client proteins while C-terminal tails maintain the dodecamer and chaperone activity ', Journal of Biological Chemistry, vol. 292, no. 19, pp. 8103-8121 . https://doi.org/10.1074/jbc.M116.766816
Rutsdottir, G, Härmark, J, Weide, Y, Hebert, H, Rasmussen, M I, Wernersson, S, Respondek, M, Akke, M, Højrup, P, Koeck, P J B, Söderberg, C A G & Emanuelsson, C 2017, ' Structural model of dodecameric heat-shock protein Hsp21 : Flexible N-terminal arms interact with client proteins while C-terminal tails maintain the dodecamer and chaperone activity ', Journal of Biological Chemistry, vol. 292, no. 19, pp. 8103-8121 . https://doi.org/10.1074/jbc.M116.766816
Small heat-shock proteins (sHsps) prevent aggregation of thermosensitive client proteins in a first line of defense against cellular stress. The mechanisms by which they perform this function have been hard to define due to limited structural informa