Zobrazeno 1 - 10
of 150
pro vyhledávání: '"Henning D. Mootz"'
Publikováno v:
Frontiers in Chemistry, Vol 10 (2022)
The small ubiquitin-like modifier (SUMO) is involved in various cellular processes and mediates known non-covalent protein-protein interactions by three distinct binding surfaces, whose interactions are termed class I to class III. While interactors
Externí odkaz:
https://doaj.org/article/6ef8c5a0967a4ad9b64e20c089799196
Autor:
Christian Nienberg, Anika Retterath, Kira-Sophie Becher, Thorsten Saenger, Henning D. Mootz, Joachim Jose
Publikováno v:
Pharmaceuticals, Vol 9, Iss 3, p 36 (2016)
Human CK2 is a heterotetrameric constitutively active serine/threonine protein kinase and is an emerging target in current anti-cancer drug discovery. The kinase is composed of two catalytic CK2α subunits and two regulatory CK2β subunits. In order
Externí odkaz:
https://doaj.org/article/8ee74dcfae9b4295bd628a4313824a6c
Publikováno v:
The Journal of Physical Chemistry B. 127:3806-3815
Autor:
Tim Pasch, Alexander Schröder, Sabrina Kattelmann, Miriam Eisenstein, Shmuel Pietrokovski, Daniel Kümmel, Henning D. Mootz
Publikováno v:
Chemical Science. 14:5204-5213
Cysteine-less split inteins are very useful, but rare tools for protein engineering. Investigation of the novel PolB16 intein revealed a previously overlooked histidine as a conserved part for the serine-dependent mechanism.
Publikováno v:
Methods in Molecular Biology ISBN: 9781071632130
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ece5a1434264949b91db53a70312aaea
https://doi.org/10.1007/978-1-0716-3214-7_8
https://doi.org/10.1007/978-1-0716-3214-7_8
Autor:
Jennifer Rüschenbaum, Wieland Steinchen, Florian Mayerthaler, Anna‐Lena Feldberg, Henning D. Mootz
Publikováno v:
Angewandte Chemie (International ed. in English). 61(48)
Nonribosomal peptide synthetases (NRPSs) employ multiple domains, specifically arranged in modules, for the assembly-line biosynthesis of a plethora of bioactive peptides. It is poorly understood how catalysis is correlated with the domain interplay
Autor:
Annika Aust, Anna-Lena Feldberg, Henning D. Mootz, Pascal Meyer-Ahrens, Marie Reille-Seroussi
Publikováno v:
Angewandte Chemie (International Ed. in English)
The thiol group of the cysteine side chain is arguably the most versatile chemical handle in proteins. To expand the scope of established and commercially available thiol bioconjugation reagents, we genetically encoded a second such functional moiety
Autor:
Amke Trentmann, Debora A. Casolari, Maria V. Yusenko, Henning D. Mootz, Jan-Henrik Mikesch, Karl-Heinz Klempnauer, Mairin Lenz, Maria Francisca Arteaga, Richard J D'Andrea, Wolfgang Dörner, Stefan Klempnauer, Thomas J. Schmidt, Luca Abdel Ghani, Melanie Horn, Carsten Müller-Tidow, Thomas J. Gonda
Publikováno v:
Oncogene
Transcription factor MYB has recently emerged as a promising drug target for the treatment of acute myeloid leukemia (AML). Here, we have characterized a group of natural sesquiterpene lactones (STLs), previously shown to suppress MYB activity, for t
Autor:
Wieland Steinchen, Florian Mayerthaler, Xun Sun, Jonas Alfermann, Henning D. Mootz, Haw Yang, Anna Lena Feldberg
Publikováno v:
RSC Chemical Biology
Nonribosomal peptide synthetases (NRPSs) are multifunctional megaenzymes that govern the stepwise biosynthesis of pharmaceutically important peptides. In an ATP-dependent assembly-line mechanism dedicated domains are responsible for each catalytic st
Autor:
Henning D. Mootz, Shubhendu Palei
Publikováno v:
Chemical Communications. 57:4194-4197
A dual-intein approach for the preparation of head-to-tail macrocyclic peptides is reported, where synthetic and genetically encoded fragments are ligated by two native peptide bonds. A split intein ligates the synthetic and genetically encoded pepti