N-Myristoyltransferase Inhibition Induces ER-Stress, Cell Cycle Arrest, and Apoptosis in Cancer Cells

Autor: Thinon, E, Morales Sanfrutos, J, Mann, D, Tate, EW

Publikováno v: ACS Chemical Biology

N-Myristoyltransferase (NMT) covalently attaches a C14-fatty acid to the N-terminal glycine of proteins and has been proposed as a therapeutic target in cancer. We have recently shown that selective NMT inhibition leads to dose-responsive loss of N-m

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::f3a3eb82ee2b7a158f05650ad49d8b6d
http://europepmc.org/articles/PMC5077176

Targeting n-myristoyltransferases promotes a pan-Mammarenavirus inhibition through the degradation of the Z matrix protein.

Autor: Carnec, Xavier^1,2 (AUTHOR), Borges-Cardoso, Virginie^1,2 (AUTHOR), Reynard, Stéphanie^1,2 (AUTHOR), Kowalski, Heinrich³ (AUTHOR), Gaillard, Jean-Charles⁴ (AUTHOR), Mateo, Mathieu^1,2 (AUTHOR), Armengaud, Jean⁴ (AUTHOR), Baize, Sylvain^1,2 (AUTHOR) sylvain.baize@pasteur.fr

Publikováno v: PLoS Pathogens. 12/3/2024, Vol. 20 Issue 12, p1-28. 28p.

A palmitoyl transferase chemical-genetic system to map ZDHHC-specific S-acylation.

Autor: Ocasio CA; The Francis Crick Institute, London, UK., Baggelaar MP; The Francis Crick Institute, London, UK.; Imperial College London, Department of Chemistry, Molecular Sciences Research Hub, London, UK.; Utrecht University, Biomolecular Mass Spectrometry & Proteomics Group, Utrecht, The Netherlands., Sipthorp J; The Francis Crick Institute, London, UK.; Imperial College London, Department of Chemistry, Molecular Sciences Research Hub, London, UK., Losada de la Lastra A; The Francis Crick Institute, London, UK.; Imperial College London, Department of Chemistry, Molecular Sciences Research Hub, London, UK., Tavares M; The Francis Crick Institute, London, UK.; Imperial College London, Department of Chemistry, Molecular Sciences Research Hub, London, UK., Volarić J; Imperial College London, Department of Chemistry, Molecular Sciences Research Hub, London, UK., Soudy C; The Francis Crick Institute, London, UK., Storck EM; King's College London, Randall Centre for Cell and Molecular Biophysics, School of Basic and Medical Biosciences and Department of Chemistry, London, UK., Houghton JW; The Francis Crick Institute, London, UK., Palma-Duran SA; The Francis Crick Institute, London, UK.; Department of Food Science, Research Center in Food and Development A.C., Hermosillo, Mexico., MacRae JI; The Francis Crick Institute, London, UK., Tomić G; The Francis Crick Institute, London, UK., Carr L; The Francis Crick Institute, London, UK., Downward J; The Francis Crick Institute, London, UK., Eggert US; King's College London, Randall Centre for Cell and Molecular Biophysics, School of Basic and Medical Biosciences and Department of Chemistry, London, UK., Tate EW; The Francis Crick Institute, London, UK. e.tate@imperial.ac.uk.; Imperial College London, Department of Chemistry, Molecular Sciences Research Hub, London, UK. e.tate@imperial.ac.uk.

Publikováno v: Nature biotechnology [Nat Biotechnol] 2024 Oct; Vol. 42 (10), pp. 1548-1558. Date of Electronic Publication: 2024 Jan 08.

Targeting N-myristoyl transferase-1 in cancer using peptide microarrays

Autor: Thinon, E, Mann, D, Tate, EW

Publikováno v: S75

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______1032::726f269983132f42c3923610de3c23be
http://hdl.handle.net/10044/1/26845

BFSP1 C-terminal domains released by post-translational processing events can alter significantly the calcium regulation of AQP0 water permeability.

Autor: Tapodi A; Department of Biosciences, The University of Durham, South Road, Durham, DH1 3LE, UK., Clemens DM; Physiology and Biophysics, UC Irvine, Irvine, CA, USA., Uwineza A; Department of Biosciences, The University of Durham, South Road, Durham, DH1 3LE, UK., Jarrin M; Department of Biosciences, The University of Durham, South Road, Durham, DH1 3LE, UK., Goldberg MW; Department of Biosciences, The University of Durham, South Road, Durham, DH1 3LE, UK., Thinon E; Department of Chemistry, Molecular Sciences Research Hub, Imperial College London, Wood Lane, London, W12 0BZ, UK; Institute of Chemical Biology, Molecular Sciences Research Hub, Imperial College London, Wood Lane, London, W12 0BZ, UK., Heal WP; Department of Chemistry, Molecular Sciences Research Hub, Imperial College London, Wood Lane, London, W12 0BZ, UK; Institute of Chemical Biology, Molecular Sciences Research Hub, Imperial College London, Wood Lane, London, W12 0BZ, UK., Tate EW; Department of Chemistry, Molecular Sciences Research Hub, Imperial College London, Wood Lane, London, W12 0BZ, UK; Institute of Chemical Biology, Molecular Sciences Research Hub, Imperial College London, Wood Lane, London, W12 0BZ, UK., Nemeth-Cahalan K; Physiology and Biophysics, UC Irvine, Irvine, CA, USA., Vorontsova I; Physiology and Biophysics, UC Irvine, Irvine, CA, USA., Hall JE; Physiology and Biophysics, UC Irvine, Irvine, CA, USA. Electronic address: jhall@uci.edu., Quinlan RA; Department of Biosciences, The University of Durham, South Road, Durham, DH1 3LE, UK; Biophysical Sciences Institute, The University of Durham, South Road, Durham, DH1 3LE, UK. Electronic address: r.a.quinlan@durham.ac.uk.

Publikováno v: Experimental eye research [Exp Eye Res] 2019 Aug; Vol. 185, pp. 107585. Date of Electronic Publication: 2019 Feb 18.