Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Marret Müller"'
Publikováno v:
Cells, Vol 9, Iss 3, p 605 (2020)
Emerin is one of the best characterized proteins of the inner nuclear membrane, but can also occur at the level of the endoplasmic reticulum. We now use enhanced ascorbate peroxidase 2 (APEX2) to probe the environment of emerin. APEX2 can be used as
Externí odkaz:
https://doaj.org/article/7a22017d9f8b4d8d92a30a387823c1c8
Autor:
Henning Urlaub, Marret Müller, Christof Lenz, Ralph H. Kehlenbach, Martin W. Goldberg, Christina James
Publikováno v:
J Biol Chem
The Journal of Biological Chemistry
Journal of biological chemistry, 2019, Vol.294(44), pp.16241-16254 [Peer Reviewed Journal]
The Journal of Biological Chemistry
Journal of biological chemistry, 2019, Vol.294(44), pp.16241-16254 [Peer Reviewed Journal]
Vesicle-associated membrane protein–associated protein B (VAPB) is a tail-anchored protein that is present at several contact sites of the endoplasmic reticulum (ER). We now show by immunoelectron microscopy that VAPB also localizes to the inner nu
Autor:
Marret Müller, Falko Hochgräfe, Jan Pané-Farré, Chris J. Hamilton, Manuela Harms, Nguyen Thi Thu Huyen, Haike Antelmann, Vu Van Loi
Publikováno v:
Antioxidants & Redox Signaling
Aims: Bacillithiol (BSH) is utilized as a major thiol-redox buffer in the human pathogen Staphylococcus aureus. Under oxidative stress, BSH forms mixed disulfides with proteins, termed as S-bacillithiolation, which can be reversed by bacilliredoxins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::105e349741780b9a612ad6673179eded
https://ueaeprints.uea.ac.uk/id/eprint/59902/
https://ueaeprints.uea.ac.uk/id/eprint/59902/
Autor:
Henrike Pförtner, Marret Müller, Uwe Völker, Rabea Schlüter, Swantje Reiß, Jon Marles-Wright, Katharina Riedel, Anica Beyer, Wenke Reiß, Susanne Engelmann, Ulrike Mäder, Michael Hecker, Jan Pané-Farré, Richard J. Lewis
Publikováno v:
Molecular Microbiology.
Summary With about 25 000 molecules per cell, Asp23 is one of the most abundant proteins in Staphylococcus aureus. Asp23 has been characterized as a protein that, following an alkaline shock, accumulates in the soluble protein fraction. Transcription
Autor:
Marret, Müller, Swantje, Reiß, Rabea, Schlüter, Ulrike, Mäder, Anica, Beyer, Wenke, Reiß, Jon, Marles-Wright, Richard J, Lewis, Henrike, Pförtner, Uwe, Völker, Katharina, Riedel, Michael, Hecker, Susanne, Engelmann, Jan, Pané-Farré
Publikováno v:
Molecular microbiology. 93(6)
With about 25 000 molecules per cell, Asp23 is one of the most abundant proteins in Staphylococcus aureus. Asp23 has been characterized as a protein that, following an alkaline shock, accumulates in the soluble protein fraction. Transcription of the