Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Frederic Lamoliatte"'
Autor:
Rathan Jadav, Florian Weiland, Sylvie M. Noordermeer, Thomas Carroll, Yuandi Gao, Jianming Wang, Houjiang Zhou, Frederic Lamoliatte, Ivan Muñoz, Rachel Toth, Thomas Macartney, Fiona Brown, C. James Hastie, Constance Alabert, Haico van Attikum, Frank Zenke, Jean-Yves Masson, John Rouse
The ATR kinase protects cells against DNA damage and replication stress and represents a promising anti-cancer drug target. The ATR inhibitors (ATRi) berzosertib and gartisertib are in clinical trials for treatment of advanced solid tumours as monoth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7bd865751b8d79266f27737bf29508de
https://doi.org/10.1101/2023.04.03.535285
https://doi.org/10.1101/2023.04.03.535285
Autor:
Syed Arif Abdul Rehman, Elena Di Nisio, Chiara Cazzaniga, Odetta Antico, Axel Knebel, Clare Johnson, Frederic Lamoliatte, Rodolfo Negri, Miratul Muqit MK, Virginia De Cesare
E2 conjugating enzymes (E2s) play a central role in the enzymatic cascade that leads to the attachment of ubiquitin to a substrate. This process, termed ubiquitylation is fundamental for maintaining cellular homeostasis and impacts almost all cellula
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5213529c293d7dae87454baf4c9f7290
https://doi.org/10.1101/2023.03.05.531151
https://doi.org/10.1101/2023.03.05.531151
Autor:
Sven M. Lange, Matthew R. McFarland, Frederic Lamoliatte, Dominika Kwaśna, Linnan Shen, Iona Wallace, Isobel Cole, Lee A. Armstrong, Axel Knebel, Clare Johnson, Virginia De Cesare, Yogesh Kulathu
Branched ubiquitin (Ub) chains make up a significant proportion of Ub polymers in human cells and are formed when two or more sites on a single Ub molecule are modified with Ub creating bifurcated architectures. Despite their abundance, we have a poo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e35913596d7c4ef61fc79481ed7099a7
https://doi.org/10.1101/2023.01.10.523363
https://doi.org/10.1101/2023.01.10.523363
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
Autor:
Mateusz Gregorczyk, Graziana Pastore, Pawel Lis, Sven Lange, Frederic Lamoliatte, Thomas Macartney, Rachel Toth, Fiona Brown, James Hastie, Daniel Durocher, John Rouse
NEK1 is a pleiotropic protein kinase implicated in mitosis, ciliogenesis and DNA repair but little is known about its regulation or targets. Its relevance for human health is underscored by the association of NEK1 mutations with human diseases includ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a568ee4e04f21dcfae357e50206dab43
https://doi.org/10.1101/2022.08.31.505651
https://doi.org/10.1101/2022.08.31.505651
Publikováno v:
The Biochemical journal. 479(20)
SummaryADP-heptose activates the protein kinase ALPK1 triggering TIFA phosphorylation at Thr9, the recruitment of TRAF6 and the subsequent production of inflammatory mediators. Here, we demonstrate that ADP-heptose also stimulates the formation of Ly
Functional characterization of C21ORF2 association with the NEK1 kinase mutated in human in diseases
Autor:
Mateusz Gregorczyk, Graziana Pastore, Ivan Muñoz, Thomas Carroll, Johanna Streubel, Meagan Munro, Pawel Lis, Sven Lange, Frederic Lamoliatte, Thomas Macartney, Rachel Toth, Fiona Brown, James Hastie, Gislene Pereira, Daniel Durocher, John Rouse
Publikováno v:
Life Science Alliance. 6:e202201740
The NEK1 kinase controls ciliogenesis, mitosis, and DNA repair, andNEK1mutations cause human diseases including axial spondylometaphyseal dysplasia and amyotrophic lateral sclerosis.C21ORF2mutations cause a similar pattern of human diseases, suggesti
Autor:
Alexander Agrotis, Frederic Lamoliatte, Thomas D Williams, Ailsa Black, Rhuari Horberry, Adrien Rousseau
Publikováno v:
Life Science Alliance. 6:e202201642
The homohexameric p97 complex, composed of Cdc48 subunits in yeast, is a crucial component of protein quality control pathways including ER-associated degradation. The complex acts to segregate protein complexes in an ATP-dependent manner, requiring
Autor:
David Millrine, Thomas Cummings, Stephen P. Matthews, Joshua J. Peter, Helge Magnussen, Thomas Macartney, Frederic Lamoliatte, Axel Knebel, Yogesh Kulathu
An essential first step in the posttranslational 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 re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::200f779f47f0cc6fb3b9f60bf35b7886
https://doi.org/10.1101/2022.02.28.482207
https://doi.org/10.1101/2022.02.28.482207
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