Zobrazeno 1 - 10
of 45
pro vyhledávání: '"Brian T Weinert"'
Autor:
Brian T Weinert, Vytautas Iesmantavicius, Tarek Moustafa, Christian Schölz, Sebastian A Wagner, Christoph Magnes, Rudolf Zechner, Chunaram Choudhary
Publikováno v:
Molecular Systems Biology, Vol 11, Iss 10, Pp n/a-n/a (2015)
Externí odkaz:
https://doaj.org/article/39de75e09c464391a614ec474fc2edac
Autor:
Eri Maria Sol, Sebastian A Wagner, Brian T Weinert, Amit Kumar, Hyun-Seok Kim, Chu-Xia Deng, Chunaram Choudhary
Publikováno v:
PLoS ONE, Vol 7, Iss 12, p e50545 (2012)
Lysine acetylation is a posttranslational modification that is dynamically regulated by the activity of acetyltransferases and deacetylases. The human and mouse genomes encode 18 different lysine deacetylases (KDACs) which are key regulators of many
Externí odkaz:
https://doaj.org/article/06ab66031bf44bf5b802f8bc2d914fb9
Autor:
Daniel V. Lopez, Fatima A.H. Al-Jaberi, Nkerorema D. Damas, Brian T. Weinert, Urska Pus, Sara Torres-Rusillo, Anders Woetmann, Niels Ødum, Charlotte M. Bonefeld, Martin Kongsbak-Wismann, Carsten Geisler
Publikováno v:
Frontiers in Immunology, Vol 12 (2021)
Th22 cells constitute a recently described CD4+ T cell subset defined by its production of interleukin (IL)-22. The action of IL-22 is mainly restricted to epithelial cells. IL-22 enhances keratinocyte proliferation but inhibits their differentiation
Externí odkaz:
https://doaj.org/article/d83bab7d7d6f4ff597750b11914dab5c
Autor:
Bogi Karbech Hansen, Rajat Gupta, Linda Baldus, David Lyon, Takeo Narita, Michael Lammers, Chunaram Choudhary, Brian T. Weinert
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
Many human proteins are regulated by lysine acetylation, but the degree of acetylation at individual sites is poorly characterized. Here, the authors measure acetylation stoichiometry in the HeLa cell proteome, providing a resource to assess mechanis
Externí odkaz:
https://doaj.org/article/f689076cde19400e8edea6f60e39f647
Autor:
Alexander Hogrebe, Louise von Stechow, Dorte B. Bekker-Jensen, Brian T. Weinert, Christian D. Kelstrup, Jesper V. Olsen
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
Quantitative phosphoproteomics has become a standard method in molecular and cell biology. Here, the authors compare performance and parameters of phosphoproteome quantification by LFQ, SILAC, and MS2-/MS3-based TMT and introduce a TMT-adapted algori
Externí odkaz:
https://doaj.org/article/f431e2c01ad34cbfb3c87caf0080bc32
Autor:
Alicia Lundby, Kasper Lage, Brian T. Weinert, Dorte B. Bekker-Jensen, Anna Secher, Tine Skovgaard, Christian D. Kelstrup, Anatoliy Dmytriyev, Chunaram Choudhary, Carsten Lundby, Jesper V. Olsen
Publikováno v:
Cell Reports, Vol 2, Iss 2, Pp 419-431 (2012)
Lysine acetylation is a major posttranslational modification involved in a broad array of physiological functions. Here, we provide an organ-wide map of lysine acetylation sites from 16 rat tissues analyzed by high-resolution tandem mass spectrometry
Externí odkaz:
https://doaj.org/article/006192c743594305a477b563c8dd6c55
Autor:
Carsten Geisler, Sara Torres-Rusillo, Urska Pus, Niels Ødum, Martin Kongsbak-Wismann, Fatima A H Al-Jaberi, Daniel Villalba Lopez, Charlotte M. Bonefeld, Nkerorema D Damas, Brian T Weinert, Anders Woetmann
Publikováno v:
Frontiers in Immunology, Vol 12 (2021)
Lopez, D V, Al-Jaberi, F A H, Damas, N D, Weinert, B T, Pus, U, Torres-Rusillo, S, Woetmann, A, Ødum, N, Bonefeld, C M, Kongsbak-Wismann, M & Geisler, C 2021, ' Vitamin D Inhibits IL-22 Production Through a Repressive Vitamin D Response Element in the il22 Promoter ', Frontiers in Immunology, vol. 12, pp. 715059 . https://doi.org/10.3389/fimmu.2021.715059
Lopez, D V, Al-Jaberi, F A H, Damas, N D, Weinert, B T, Pus, U, Torres-Rusillo, S, Woetmann, A, Ødum, N, Bonefeld, C M, Kongsbak-Wismann, M & Geisler, C 2021, ' Vitamin D Inhibits IL-22 Production Through a Repressive Vitamin D Response Element in the il22 Promoter ', Frontiers in Immunology, vol. 12, 715059 . https://doi.org/10.3389/fimmu.2021.715059
Lopez, D V, Al-Jaberi, F A H, Damas, N D, Weinert, B T, Pus, U, Torres-Rusillo, S, Woetmann, A, Ødum, N, Bonefeld, C M, Kongsbak-Wismann, M & Geisler, C 2021, ' Vitamin D Inhibits IL-22 Production Through a Repressive Vitamin D Response Element in the il22 Promoter ', Frontiers in Immunology, vol. 12, pp. 715059 . https://doi.org/10.3389/fimmu.2021.715059
Lopez, D V, Al-Jaberi, F A H, Damas, N D, Weinert, B T, Pus, U, Torres-Rusillo, S, Woetmann, A, Ødum, N, Bonefeld, C M, Kongsbak-Wismann, M & Geisler, C 2021, ' Vitamin D Inhibits IL-22 Production Through a Repressive Vitamin D Response Element in the il22 Promoter ', Frontiers in Immunology, vol. 12, 715059 . https://doi.org/10.3389/fimmu.2021.715059
Th22 cells constitute a recently described CD4+ T cell subset defined by its production of interleukin (IL)-22. The action of IL-22 is mainly restricted to epithelial cells. IL-22 enhances keratinocyte proliferation but inhibits their differentiation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4eeac749e031a9d9e9a6f8fe09fd6f9e
https://www.frontiersin.org/articles/10.3389/fimmu.2021.715059/full
https://www.frontiersin.org/articles/10.3389/fimmu.2021.715059/full
Autor:
Takeo Narita, Bogi Karbech Hansen, David Lyon, Rajat Gupta, Linda Baldus, Chunaram Choudhary, Michael Lammers, Brian T. Weinert
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
Nature Communications
Hansen, B K, Gupta, R, Baldus, L, Lyon, D, Narita, T, Lammers, M, Choudhary, C & Weinert, B T 2019, ' Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation ', Nature Communications, vol. 10, 1055 . https://doi.org/10.1038/s41467-019-09024-0
Nature Communications
Hansen, B K, Gupta, R, Baldus, L, Lyon, D, Narita, T, Lammers, M, Choudhary, C & Weinert, B T 2019, ' Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation ', Nature Communications, vol. 10, 1055 . https://doi.org/10.1038/s41467-019-09024-0
Lysine acetylation is a reversible posttranslational modification that occurs at thousands of sites on human proteins. However, the stoichiometry of acetylation remains poorly characterized, and is important for understanding acetylation-dependent me
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dba28b383f0bd0610777aa2f77365b8e
http://link.springer.com/article/10.1038/s41467-019-09024-0
http://link.springer.com/article/10.1038/s41467-019-09024-0
Autor:
Atul S. Deshmukh, Morten Hostrup, Alba Gonzalez-Franquesa, Ben Stocks, Brian T Weinert, Jens Bangsbo, Martin Thomassen, Anders Krogh Lemminger, Jeppe Kjærgaard Larsen
Publikováno v:
SSRN Electronic Journal.
Exercise is an effective strategy in the prevention and treatment of metabolic diseases. Alterations in the skeletal muscle proteome, including post-translational modifications, regulate its metabolic adaptations to exercise. Here, we examined the ef
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::904b8ca8a416d54b3d125b99be3503a4
https://doi.org/10.2139/ssrn.3800386
https://doi.org/10.2139/ssrn.3800386
Publikováno v:
Narita, T, Weinert, B T & Choudhary, C 2019, ' Functions and mechanisms of non-histone protein acetylation ', Nature Reviews. Molecular Cell Biology, vol. 20, pp. 156-174 . https://doi.org/10.1038/s41580-018-0081-3
Nature Reviews Molecular Cell Biology
Nature Reviews Molecular Cell Biology
Nε-lysine acetylation was discovered more than half a century ago as a post-translational modification of histones and has been extensively studied in the context of transcription regulation. In the past decade, proteomic analyses have revealed that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ec009c7c3b4a27e6d971c09b0871883
https://doi.org/10.1038/s41580-018-0081-3
https://doi.org/10.1038/s41580-018-0081-3