Zobrazeno 1 - 10
of 30
pro vyhledávání: '"Rune Busk Damgaard"'
Autor:
Nikolas Furthmann, Verian Bader, Lena Angersbach, Alina Blusch, Simran Goel, Ana Sánchez-Vicente, Laura J. Krause, Sarah A. Chaban, Prerna Grover, Victoria A. Trinkaus, Eva M. van Well, Maximilian Jaugstetter, Kristina Tschulik, Rune Busk Damgaard, Carsten Saft, Gisa Ellrichmann, Ralf Gold, Arend Koch, Benjamin Englert, Ana Westenberger, Christine Klein, Lisa Jungbluth, Carsten Sachse, Christian Behrends, Markus Glatzel, F. Ulrich Hartl, Ken Nakamura, Chadwick W. Christine, Eric J. Huang, Jörg Tatzelt, Konstanze F. Winklhofer
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-24 (2023)
Abstract NEMO is a ubiquitin-binding protein which regulates canonical NF-κB pathway activation in innate immune signaling, cell death regulation and host-pathogen interactions. Here we identify an NF-κB-independent function of NEMO in proteostasis
Externí odkaz:
https://doaj.org/article/254c39b4dc224a428f4f65c841b52060
Autor:
Rune Busk Damgaard, Paul R Elliott, Kirby N Swatek, Eamonn R Maher, Polina Stepensky, Orly Elpeleg, David Komander, Yackov Berkun
Publikováno v:
EMBO Molecular Medicine, Vol 11, Iss 3, Pp n/a-n/a (2019)
Abstract The deubiquitinase OTULIN removes methionine‐1 (M1)‐linked polyubiquitin signals conjugated by the linear ubiquitin chain assembly complex (LUBAC) and is critical for preventing TNF‐driven inflammation in OTULIN‐related autoinflammat
Externí odkaz:
https://doaj.org/article/6dc30199d4184d6c8ef04834bb9f3c12
Autor:
Matous Hrdinka, Berthe Katrine Fiil, Mattia Zucca, Derek Leske, Katrin Bagola, Monica Yabal, Paul R. Elliott, Rune Busk Damgaard, David Komander, Philipp J. Jost, Mads Gyrd-Hansen
Publikováno v:
Cell Reports, Vol 14, Iss 12, Pp 2846-2858 (2016)
Innate immune signaling relies on the deposition of non-degradative polyubiquitin at receptor-signaling complexes, but how these ubiquitin modifications are regulated by deubiquitinases remains incompletely understood. Met1-linked ubiquitin (Met1-Ub)
Externí odkaz:
https://doaj.org/article/8f642d40924c449d9119d8000a7664b1
Autor:
Monica Yabal, Nicole Müller, Heiko Adler, Nathalie Knies, Christina J. Groß, Rune Busk Damgaard, Hirokazu Kanegane, Marc Ringelhan, Thomas Kaufmann, Mathias Heikenwälder, Andreas Strasser, Olaf Groß, Jürgen Ruland, Christian Peschel, Mads Gyrd-Hansen, Philipp J. Jost
Publikováno v:
Cell Reports, Vol 7, Iss 6, Pp 1796-1808 (2014)
X-linked inhibitor of apoptosis protein (XIAP) has been identified as a potent regulator of innate immune responses, and loss-of-function mutations in XIAP cause the development of the X-linked lymphoproliferative syndrome type 2 (XLP-2) in humans. U
Externí odkaz:
https://doaj.org/article/9094fca13e624e00a0421a656f42b8b4
Publikováno v:
The FEBS Journal. 288:5903-5908
Ester-linked ubiquitination of serine or threonine residues - or even lipids - has emerged as a new regulatory earmark in cell signalling. Petrova et al. (2021) now reveal that ubiquitin esterification by the atypical ubiquitin ligase HOIL-1, a compo
Publikováno v:
Cell Death Differ
Post-translational modification of proteins with ubiquitin (ubiquitination) provides a rapid and versatile mechanism for regulating cellular signalling systems. Met1-linked (or ‘linear’) ubiquitin chains have emerged as a key regulatory signal th
Autor:
Susan E. Davies, Rune Busk Damgaard, David Komander, Helen E. Jolin, Andrew N J McKenzie, Michael Allison, Hannah Titheradge
Publikováno v:
Damgaard, R B, Jolin, H E, Allison, M E D, Davies, S E, Titheradge, H L, McKenzie, A N J & Komander, D 2020, ' OTULIN protects the liver against cell death, inflammation, fibrosis, and cancer ', Cell Death and Differentiation, vol. 27, pp. 1457-1474 . https://doi.org/10.1038/s41418-020-0532-1
Cell Death and Differentiation
Cell Death and Differentiation
Methionine-1 (M1)-linked polyubiquitin chains conjugated by the linear ubiquitin chain assembly complex (LUBAC) control NF-κB activation, immune homoeostasis, and prevents tumour necrosis factor (TNF)-induced cell death. The deubiquitinase OTULIN ne
Publikováno v:
Merklinger, L, Bauer, J, Pedersen, P A, Damgaard, R B & Morth, J P 2022, ' Phospholipids alter activity and stability of mitochondrial membrane-bound ubiquitin ligase MARCH5 ', Life Science Alliance, vol. 5, no. 8, e202101309 . https://doi.org/10.26508/lsa.202101309
Mitochondrial homeostasis is tightly controlled by ubiquitination. The mitochondrial integral membrane ubiquitin ligase MARCH5 is a crucial regulator of mitochondrial membrane fission, fusion, and disposal through mitophagy. In addition, the lipid co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9611c052cb58c9188d1dcdd4778dd332
https://curis.ku.dk/portal/da/publications/phospholipids-alter-activity-and-stability-of-mitochondrial-membranebound-ubiquitin-ligase-march5(b659faea-060d-40de-bd4b-1bd9d122937c).html
https://curis.ku.dk/portal/da/publications/phospholipids-alter-activity-and-stability-of-mitochondrial-membranebound-ubiquitin-ligase-march5(b659faea-060d-40de-bd4b-1bd9d122937c).html
Publikováno v:
Nature
Ubiquitylation, a wide-spread post-translational protein modification in eukaryotes, marks cytosol‐invading bacteria as cargo for anti-bacterial autophagy.(1–3) The identity of the ubiquitylated substrate on bacteria has remained unknown. Here we
Autor:
Rune Busk Damgaard
Publikováno v:
Cell Death Differ