Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Sophie L Mader"'
Autor:
Kahlan E Newman, Sarah N Tindall, Sophie L Mader, Syma Khalid, Gavin H Thomas, Marjan W Van Der Woude
Publikováno v:
eLife, Vol 12 (2023)
Acylation of diverse carbohydrates occurs across all domains of life and can be catalysed by proteins with a membrane bound acyltransferase-3 (AT3) domain (PF01757). In bacteria, these proteins are essential in processes including symbiosis, resistan
Externí odkaz:
https://doaj.org/article/9849aac2dd3d4b87b58d6130bbf696ab
Autor:
Mona Baumgart, Michael Röpke, Max E. Mühlbauer, Sam Asami, Sophie L. Mader, Kai Fredriksson, Michael Groll, Ana P. Gamiz-Hernandez, Ville R. I. Kaila
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-9 (2021)
Buried charged networks in proteins are often important for their biological functionality and are believed to destabilise the protein fold. Here, the authors combine computational design, MD simulations, biophysical experiments, NMR and X-ray crysta
Externí odkaz:
https://doaj.org/article/0e77cdff4a874a32b8c39f0694e34a3c
Autor:
Punam Rattu, Flo Glencross, Sophie L. Mader, Chris-Kriton Skylaris, Stephen J. Matthews, Sarah L. Rouse, Syma Khalid
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 19, Iss , Pp 6417-6430 (2021)
Two proteins of the Escherichia coli membrane protein complex, CsgG and CsgF, are studied as proteinaceous nanopores for DNA sequencing. It is highly desirable to control the DNA as it moves through the pores, this requires characterisation of DNA tr
Externí odkaz:
https://doaj.org/article/fd4ef18f4e964d0f82717acf95699cd1
Autor:
Sophie L. Mader, Abraham Lopez, Jannis Lawatscheck, Qi Luo, Daniel A. Rutz, Ana P. Gamiz-Hernandez, Michael Sattler, Johannes Buchner, Ville R. I. Kaila
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
The chaperone Hsp90 uses the free energy from ATP hydrolysis to control the folding of client proteins in eukaryotic cells. Here the authors provide mechanistic insights into how its catalytic activity is coupled to conformational changes by combinin
Externí odkaz:
https://doaj.org/article/b87ff0e02f1548cc99bb836c5ec50ea7
Autor:
Alexandra Rehn, Jannis Lawatscheck, Marie-Lena Jokisch, Sophie L. Mader, Qi Luo, Franziska Tippel, Birgit Blank, Klaus Richter, Kathrin Lang, Ville R. I. Kaila, Johannes Buchner
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
Methylation of a lysine residue in Hsp90 is a recently discovered post-translational modification but the mechanistic effects of this modification have remained unknown so far. Here the authors combine biochemical and biophysical approaches, molecula
Externí odkaz:
https://doaj.org/article/e58f3663006545cf9df6166e474e1b1b
Autor:
Punam Rattu, Flo Glencross, Sophie L. Mader, Chris-Kriton Skylaris, Stephen J. Matthews, Sarah L. Rouse, Syma Khalid
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 20, Iss , Pp 1027- (2022)
Externí odkaz:
https://doaj.org/article/237975da14904d9a883d4d7d50bfed58
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-8 (2018)
The catalytic activity of dioxygenase AsqJ is strictly relying on the methylation of quinolone substrates. Here, the authors apply molecular simulations, X-ray crystallography and in vitro biochemical studies to the engineering of dioxygenase AsqJ wi
Externí odkaz:
https://doaj.org/article/774a7713e65b4a69a86781a9fc86afcc
Autor:
Rudolf Wachtel, Bastian Bräuning, Sophie L. Mader, Felix Ecker, Ville R. I. Kaila, Michael Groll, Aymelt Itzen
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
The bacterial protease GtgE is involved in the establishment of Salmonellosis. Here the authors provide a structural and biochemical analysis of GtgE that sheds light on the molecular mechanisms of reprogramming infected host cells via site-specific
Externí odkaz:
https://doaj.org/article/b1737a5a57314d0189c7e7ac298e8846
Autor:
Dirk Auman, Felix Ecker, Sophie L. Mader, Kevin M. Dorst, Alois Bräuer, Göran Widmalm, Michael Groll, Ville R. I. Kaila
Publikováno v:
Journal of the American Chemical Society. 144:15622-15632
Dioxygenases catalyze stereoselective oxygen atom transfer in metabolic pathways of biological, industrial, and pharmaceutical importance, but their precise chemical principles remain controversial. The α-ketoglutarate (αKG)-dependent dioxygenase A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e7a3c34bb7e556c742a3dc2012f3fad7
https://doi.org/10.1021/jacs.2c05650
https://doi.org/10.1021/jacs.2c05650
Autor:
Alexandra Rehn, Jannis Lawatscheck, Marie-Lena Jokisch, Sophie L. Mader, Qi Luo, Franziska Tippel, Birgit Blank, Klaus Richter, Kathrin Lang, Ville R. I. Kaila, Johannes Buchner
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-1 (2020)
An amendment to this paper has been published and can be accessed via a link at the top of the paper.
Externí odkaz:
https://doaj.org/article/9000f64049f1435abef4e720c2f80539