Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Eric Schulze-Niemand"'
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2021)
Externí odkaz:
https://doaj.org/article/8988b3cf9f574e979df35ad11a13d8bc
Publikováno v:
Journal of Chemical Information and Modeling
Autor:
Eric Schulze-Niemand, Michael Naumann
Publikováno v:
Trends in Biochemical Sciences. 48:82-95
The COP9 signalosome (CSN) is a universal regulator of Cullin-RING ubiquitin ligases (CRLs) - a family of modular enzymes that control various cellular processes via timely degradation of key signaling proteins. The CSN, with its eight-subunit archit
Autor:
Kevin Böhm, Eric Schulze‐Niemand, Thilo Kähne, Elisa Siddiqui, Christian Täger, Daniel Ramsbeck, Mirko Buchholz, Michael Naumann
Publikováno v:
Archiv der Pharmazie.
Autor:
Martynas Gavutis, Eric Schulze-Niemand, Hung-Hsun Lee, Bo Liedberg, Matthias Stein, Ramūnas Valiokas
Publikováno v:
Nanoscale
Our study is the first report on the details of tBLM formation covering the entire time frame of the process as well as different phases of the anchoring interface.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62a8e86d4e2961f07cc4ac75cd855392
https://hdl.handle.net/21.11116/0000-000D-575A-D21.11116/0000-000D-575C-B
https://hdl.handle.net/21.11116/0000-000D-575A-D21.11116/0000-000D-575C-B
Autor:
Robert Creutznacher, Eric Schulze-Niemand, Patrick König, Vesna Stanojlovic, Alvaro Mallagaray, Thomas Peters, Matthias Stein, Mario Schubert
Publikováno v:
Biochemistry
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::775d56a266e9852b52327b3295a2f1ad
https://hdl.handle.net/21.11116/0000-000C-BC20-C21.11116/0000-000C-B6E7-2
https://hdl.handle.net/21.11116/0000-000C-BC20-C21.11116/0000-000C-B6E7-2
Autor:
Dawadschargal Dubiel, Paula C.A. da Fonseca, Leoš Shivaya Valášek, Eric Schulze-Niemand, Michael Naumann
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1870:119402
Publikováno v:
Proteins: Structure, Function, and Bioinformatics
Deubiquitinylases (DUBs) catalyze the peptide bond cleavage of specific ubiquitin linkages at distinct protein substrates. Pathogens from viruses and bacteria independently developed effector proteins with DUB activity to mimic host DUB functions and
Publikováno v:
Trends in microbiology. 30(1)
With the aim of overcoming host immune responses, and to permit persistence, numerous bacterial and viral pathogens have evolved effective strategies to control the activity of ovarian tumor domain proteases (OTUs), a group of deubiquitinylases cruci