Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Maximilian Zinke"'
Autor:
Maximilian Zinke, Maylis Lejeune, Ariel Mechaly, Benjamin Bardiaux, Ivo Gomperts Boneca, Philippe Delepelaire, Nadia Izadi-Pruneyre
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-12 (2024)
Abstract Active nutrient uptake is fundamental for survival and pathogenicity of Gram-negative bacteria, which operate a multi-protein Ton system to transport essential nutrients like metals and vitamins. This system harnesses the proton motive force
Externí odkaz:
https://doaj.org/article/ca4be11f6ba64ea48c98ad01dc70f542
Autor:
Maximilian Zinke, Katrin A. A. Sachowsky, Carl Öster, Sophie Zinn-Justin, Raimond Ravelli, Gunnar F. Schröder, Michael Habeck, Adam Lange
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
Bacteriophages of the Siphoviridae family have a long, flexible, non-contractile tail that has been difficult to characterize structurally. Here, the authors present the atomic structure of the tail tube of one of these phages, showing a hollow flexi
Externí odkaz:
https://doaj.org/article/62511668bbbc4a978e77f31884983fd0
Publikováno v:
The Journal of Biological Chemistry
The journal of biological chemistry 298(1), 101472-(2022). doi:10.1016/j.jbc.2021.101472
The journal of biological chemistry 298(1), 101472-(2022). doi:10.1016/j.jbc.2021.101472
Technological advances in cryo-EM in recent years have given rise to detailed atomic structures of bacteriophage tail tubes—a class of filamentous protein assemblies that could previously only be studied on the atomic scale in either their monomeri
Autor:
Songhwan Hwang, Dietmar Riedel, Pascal Fricke, Adam Lange, Karin Giller, Maximilian Zinke, Joseph S. Wall, Stefan Becker
Publikováno v:
Journal of Structural Biology
Intra-neuronal aggregation of alpha-synuclein into fibrils is the molecular basis for alpha-synucleinopathies, such as Parkinson's disease. The atomic structure of human alpha-synuclein (hAS) fibrils was recently determined by Tuttle et al. using sol
Autor:
Raimond B. G. Ravelli, Adam Lange, Maximilian Zinke, Sophie Zinn-Justin, Michael Habeck, Carl Öster, Katrin A. A. Sachowsky, Gunnar F. Schröder
Publikováno v:
Nature Communications, 11(1):5759. Nature Publishing Group
Nature Communications
Nature Communications, 2020, 11 (1), pp.5759. ⟨10.1038/s41467-020-19611-1⟩
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
Nature Communications 11(1), 5759 (2020). doi:10.1038/s41467-020-19611-1
Nature Communications, Nature Publishing Group, 2020, 11 (1), pp.5759. ⟨10.1038/s41467-020-19611-1⟩
Nature Communications
Nature Communications, 2020, 11 (1), pp.5759. ⟨10.1038/s41467-020-19611-1⟩
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
Nature Communications 11(1), 5759 (2020). doi:10.1038/s41467-020-19611-1
Nature Communications, Nature Publishing Group, 2020, 11 (1), pp.5759. ⟨10.1038/s41467-020-19611-1⟩
Bacteriophage SPP1 is a double-stranded DNA virus of the Siphoviridae family that infects the bacterium Bacillus subtilis. This family of phages features a long, flexible, non-contractile tail that has been difficult to characterize structurally. Her
Autor:
G. F. Schroeder, Maximilian Zinke, Adam Lange, Sophie Zinn-Justin, C. Oester, Michael Habeck, K.A.A. Sachowsky, R. Ravelli
Phage therapy has recently regained attention at combating multidrug-resistant bacteria. In 2019, tailed bacteriophages of the Siphoviridae family were engineered to successfully treat a disseminated bacterial infection after all other drugs had fail
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::512888edfef9fae809526ee94c5f9d22
https://doi.org/10.1101/2020.06.23.166439
https://doi.org/10.1101/2020.06.23.166439
Publikováno v:
ChemPhysChem
ChemPhysChem, Wiley-VCH Verlag, 2018, 19 (19), pp.2457--2460. ⟨10.1002/cphc.201800542⟩
Chemphyschem
ChemPhysChem, 2018, 19 (19), pp.2457--2460. ⟨10.1002/cphc.201800542⟩
ChemPhysChem, Wiley-VCH Verlag, 2018, 19 (19), pp.2457--2460. ⟨10.1002/cphc.201800542⟩
Chemphyschem
ChemPhysChem, 2018, 19 (19), pp.2457--2460. ⟨10.1002/cphc.201800542⟩
International audience; Proton detection and fast magic-angle spinning have advanced biological solid-state NMR, allowing for the backbone assignment of complex protein assemblies with high sensitivity and resolution. However, so far no method has be
Autor:
Anke Böhmer, Norbert Maassen, Erik Hanff, Janine Niebuhr, Volker Endeward, Dimitrios Tsikas, Maximilian Zinke, Mirja Maassen
Publikováno v:
Analytical Biochemistry. 550:132-136
The most widely recognized activity of the large family of the metalloenzyme carbonic anhydrases (CAs) is the diffusion-controlled hydration of CO2 to HCO3- and one proton, and the less rapid dehydration of HCO3- to CO2: CO2 + H2O ⇆ HCO3- + H+. CAs
Autor:
Johann P. Klare, Adrian Ricke, Sascha Lange, Julia Ruta, Thomas Eitinger, Sinah N. Pecina, Mario Gäde, Michael Sippach, Elena Bondarenko, Heinz-Jürgen Steinhoff, Adam Lange, Maximilian Zinke, Friedrich Finkenwirth
Publikováno v:
Biochimica et biophysica acta. Biomembranes. 1862(2)
Energy-coupling factor (ECF) transporters for uptake of vitamins and transition-metal ions into prokaryotic cells share a common architecture consisting of a substrate-specific integral membrane protein (S), a transmembrane coupling protein (T) and t
Publikováno v:
Amino Acids. 48:245-255
The intrinsic activity of carbonic anhydrase (CA) is the hydration of CO2 to carbonic acid and its dehydration to CO2. CA may also function as esterase and phosphatase. Recently, we demonstrated that renal CA is mainly responsible for the reabsorptio