Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Helge M Magnussen"'
Autor:
James A. Daniel, Sofia Elizarova, Ali H. Shaib, Abed A. Chouaib, Helge M. Magnussen, Jianlong Wang, Nils Brose, JeongSeop Rhee, Marilyn Tirard
Publikováno v:
Frontiers in Molecular Neuroscience, Vol 16 (2023)
Advances in genome sequencing technologies have favored the identification of rare de novo mutations linked to neurological disorders in humans. Recently, a de novo autosomal dominant mutation in NACC1 was identified (NM_052876.3: c.892C > T, NP_4431
Externí odkaz:
https://doaj.org/article/3c62c49759234d74b4d0948ff66bd30b
Autor:
Helge M. Magnussen, Syed F. Ahmed, Gary. J. Sibbet, Ventzislava A. Hristova, Koji Nomura, Andreas K. Hock, Lewis J. Archibald, Andrew G. Jamieson, David Fushman, Karen H. Vousden, Allan M. Weissman, Danny T. Huang
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
p53 is an important tumor suppressor protein which is regulated by the E3 ubiquitin ligase MDM2. Here the authors reveal that DNA damage-induced Ser429 phosphorylation of MDM2 serve to boost the activity of MDM2 homodimer by stabilizing the active E2
Externí odkaz:
https://doaj.org/article/80e8bf383dda460bb88d16b6b1cd6555
Publikováno v:
Seminars in Cell & Developmental Biology
Stress is unavoidable and essential to cellular and organismal evolution and failure to adapt or restore homeostasis can lead to severe diseases or even death. At the cellular level, stress drives a plethora of molecular changes, of which variations
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec8ceb88ee56358b18247467635ee0d2
https://doi.org/10.1016/j.semcdb.2021.12.010
https://doi.org/10.1016/j.semcdb.2021.12.010
Autor:
Joshua J Peter, Helge M Magnussen, Paul A DaRosa, David Millrine, Stephen P Matthews, Frederic Lamoliatte, Ramasubramanian Sundaramoorthy, Ron R Kopito, Yogesh Kulathu
Publikováno v:
The EMBO Journal. 41
Protein UFMylation, i.e., post-translational modification with ubiquitin-fold modifier 1 (UFM1), is essential for cellular and endoplasmic reticulum homeostasis. Despite its biological importance, we have a poor understanding of how UFM1 is conjugate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35f13c92b89b4f7e58893f4e768a971d
https://doi.org/10.15252/embj.2022111015
https://doi.org/10.15252/embj.2022111015
Autor:
Joshua J. Peter, Helge M. Magnussen, Paul Anthony DaRosa, David Millrine, Stephen P Matthews, Frederic Lamoliatte, Ramasubramanian Sundaramoorthy, Ron R Kopito, Yogesh Kulathu
Protein UFMylation is emerging as a posttranslational modification essential for endoplasmic reticulum and cellular homeostasis. Despite its biological importance, we have a poor understanding of how UFM1 is conjugated onto substrates. Here, we use a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d3819ab41288e8e19a2c2323d5d08546
https://doi.org/10.1101/2022.01.31.478489
https://doi.org/10.1101/2022.01.31.478489
Autor:
David Millrine, Thomas Cummings, Stephen P. Matthews, Joshua J. Peter, Helge M. Magnussen, Sven M. Lange, Thomas Macartney, Frederic Lamoliatte, Axel Knebel, Yogesh Kulathu
Publikováno v:
Cell reports. 40(5)
An essential first step in the post-translational modification of proteins with UFM1, UFMylation, is the proteolytic cleavage of pro-UFM1 to expose a C-terminal glycine. Of the two UFM1-specific proteases (UFSPs) identified in humans, only UFSP2 is r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a5bcd4b20509cf2819421ac72b06319
https://pubmed.ncbi.nlm.nih.gov/35926457
https://pubmed.ncbi.nlm.nih.gov/35926457
Autor:
Douglas Strathdee, Sandeep Dhayade, Danny T. Huang, Helge M. Magnussen, Timothy J. Humpton, Andreas K. Hock, Karen H. Vousden, David A. Stevenson, Koji Nomura, Julia Weber, Colin Nixon, Karen Blyth
Publikováno v:
Genes Dev
The p53 tumor suppressor protein is a potent activator of proliferative arrest and cell death. In normal cells, this pathway is restrained by p53 protein degradation mediated by the E3-ubiquitin ligase activity of MDM2. Oncogenic stress releases p53
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::418c6c76197887cb49eaf802ced904e4
https://eprints.gla.ac.uk/231800/1/231800.pdf
https://eprints.gla.ac.uk/231800/1/231800.pdf
Autor:
Danny T. Huang, Helge M. Magnussen
Publikováno v:
Journal of Molecular Biology
Graphical abstract
Highlights • The MDM2 RING domain has a tendency to form aggregates, which is species dependent. • The structures of dimeric MDM2 RING domains from frog and fish are presented. • A G443T substitution strongly reduces agg
Highlights • The MDM2 RING domain has a tendency to form aggregates, which is species dependent. • The structures of dimeric MDM2 RING domains from frog and fish are presented. • A G443T substitution strongly reduces agg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de1d09f643ebb18e3d1991e060fd5fc3
https://pubmed.ncbi.nlm.nih.gov/33450248
https://pubmed.ncbi.nlm.nih.gov/33450248
Autor:
Andreas K. Hock, David A. Stevenson, Koji Nomura, Danny T. Huang, Karen H. Vousden, Helge M. Magnussen, Sandeep Dhayade, Timothy J. Humpton, Douglas Strathdee, Julia Weber, Karen Blyth, Colin Nixon
Publikováno v:
Genes Dev
The p53 tumor suppressor protein is a potent activator of proliferative arrest and cell death. In normal cells, this pathway is restrained by p53 protein degradation mediated by the E3-ubiquitin ligase activity of MDM2. Oncogenic stress releases p53
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e60176eddef2bb8c944fadcce0cd71b
https://doi.org/10.1101/gad.348692.121
https://doi.org/10.1101/gad.348692.121
Autor:
Syed Faisal Ahmed, Andrew G. Jamieson, Andreas K. Hock, Helge M. Magnussen, Karen H. Vousden, Ventzislava A. Hristova, Lewis J. Archibald, Danny T. Huang, Gary J. Sibbet, Koji Nomura, David Fushman, Allan M. Weissman
Publikováno v:
Nature Communications
Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
Phosphorylation of MDM2 by ATM upon DNA damage is an important mechanism for deregulating MDM2, thereby leading to p53 activation. ATM phosphorylates multiple residues near the RING domain of MDM2, but the underlying molecular basis for deregulation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2d3ed69811ec6623d16c2a382921ed6
https://pubmed.ncbi.nlm.nih.gov/32350255
https://pubmed.ncbi.nlm.nih.gov/32350255