Zobrazeno 1 - 10
of 100
pro vyhledávání: '"Carmela Giglione"'
Autor:
Xiaodi Gong, Jean-Baptiste Boyer, Simone Gierlich, Marlena Pożoga, Jonas Weidenhausen, Irmgard Sinning, Thierry Meinnel, Carmela Giglione, Yonghong Wang, Rüdiger Hell, Markus Wirtz
Publikováno v:
Cell Reports, Vol 43, Iss 2, Pp 113768- (2024)
Summary: The ribosome-tethered N-terminal acetyltransferase A (NatA) acetylates 52% of soluble proteins in Arabidopsis thaliana. This co-translational modification of the N terminus stabilizes diverse cytosolic plant proteins. The evolutionary conser
Externí odkaz:
https://doaj.org/article/ff204367416745e1aad4c13986b70397
Dual lysine and N‐terminal acetyltransferases reveal the complexity underpinning protein acetylation
Autor:
Willy V Bienvenut, Annika Brünje, Jean‐Baptiste Boyer, Jens S Mühlenbeck, Gautier Bernal, Ines Lassowskat, Cyril Dian, Eric Linster, Trinh V Dinh, Minna M Koskela, Vincent Jung, Julian Seidel, Laura K Schyrba, Aiste Ivanauskaite, Jürgen Eirich, Rüdiger Hell, Dirk Schwarzer, Paula Mulo, Markus Wirtz, Thierry Meinnel, Carmela Giglione, Iris Finkemeier
Publikováno v:
Molecular Systems Biology, Vol 16, Iss 7, Pp 1-23 (2020)
Abstract Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N‐α‐acetylation (NTA) and ε‐lysine acetylation (KA) are known to be catalyzed by distinct families o
Externí odkaz:
https://doaj.org/article/d26b41bab41445bf8117bc4fba9d0b24
Autor:
Cyril Dian, Inmaculada Pérez-Dorado, Frédéric Rivière, Thomas Asensio, Pierre Legrand, Markus Ritzefeld, Mengjie Shen, Ernesto Cota, Thierry Meinnel, Edward W. Tate, Carmela Giglione
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
N-terminal glycine myristoyl transferases (NMTs) catalyse the myristoylation of eukaryotic proteins. Here, the authors provide insights into the catalytic mechanism of NMTs by determining the crystal structures of human NMT1 in complex with reactive
Externí odkaz:
https://doaj.org/article/1d7d6b525886413db95bc8b3e99c1d00
Autor:
Thomas Asensio, Cyril Dian, Jean-Baptiste Boyer, Frédéric Rivière, Thierry Meinnel, Carmela Giglione
Publikováno v:
Frontiers in Plant Science, Vol 13 (2022)
Protein N-acetyltransferases (NATs) belong to the general control non-repressible 5 (Gcn5)-related N-acetyltransferases (GNATs) superfamily. GNATs catalyze the transfer of acetyl from acetyl-CoA to the reactive amine moiety of a wide range of accepto
Externí odkaz:
https://doaj.org/article/044863c5cbe247559d7511c662004e72
Autor:
Sonia Fieulaine, Adrien Boularot, Isabelle Artaud, Michel Desmadril, Frédéric Dardel, Thierry Meinnel, Carmela Giglione
Publikováno v:
PLoS Biology, Vol 9, Iss 5, p e1001066 (2011)
For several decades, molecular recognition has been considered one of the most fundamental processes in biochemistry. For enzymes, substrate binding is often coupled to conformational changes that alter the local environment of the active site to ali
Externí odkaz:
https://doaj.org/article/223f520af7824a7589a2e95b485fd722
Autor:
Laurent Mamelli, Sylvain Petit, Jacqueline Chevalier, Carmela Giglione, Aurélie Lieutaud, Thierry Meinnel, Isabelle Artaud, Jean-Marie Pagès
Publikováno v:
PLoS ONE, Vol 4, Iss 7, p e6443 (2009)
BACKGROUND: Multi-drug resistant (MDR) bacteria have become a major concern in hospitals worldwide and urgently require the development of new antibacterial molecules. Peptide deformylase is an intracellular target now well-recognized for the design
Externí odkaz:
https://doaj.org/article/d96febcb1a014fa5ab7ddfc7132ab1fd
Publikováno v:
Trends in Biochemical Sciences. 48:495-499
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::692c9610f2cb079cb5dc4aff02c531a0
https://doi.org/10.1016/j.tibs.2023.02.008
https://doi.org/10.1016/j.tibs.2023.02.008
Publikováno v:
Methods in Enzymology ISBN: 9780443157721
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::97152fb15c6dc895f731b0503055d549
https://doi.org/10.1016/bs.mie.2023.02.018
https://doi.org/10.1016/bs.mie.2023.02.018
Publikováno v:
Journal of Molecular Biology
Journal of Molecular Biology, 2022, 434 (22), pp.67843. ⟨10.1016/j.jmb.2022.167843⟩
Journal of Molecular Biology, 2022, 434 (22), pp.67843. ⟨10.1016/j.jmb.2022.167843⟩
International audience; N-myristoyltransferases (NMTs) catalyze protein myristoylation, a lipid modification crucial for cell survival and a range of pathophysiological processes. Originally thought to modify only N-terminal glycine α-amino groups (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63f689e57cc0796e6a5cd8cf357a7e7a
https://pubmed.ncbi.nlm.nih.gov/36181773
https://pubmed.ncbi.nlm.nih.gov/36181773
Autor:
Pavlína, Miklánková, Eric, Linster, Jean-Baptiste, Boyer, Jonas, Weidenhausen, Johannes, Mueller, Laura, Armbruster, Karine, Lapouge, Carolina, De La Torre, Willy, Bienvenut, Carsten, Sticht, Matthias, Mann, Thierry, Meinnel, Irmgard, Sinning, Carmela, Giglione, Rüdiger, Hell, Markus, Wirtz
Publikováno v:
Science advances. 8(24)
In humans, the Huntingtin yeast partner K (HYPK) binds to the ribosome-associated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::16228f889ba2c21d1dea4ac3987e1fe2
https://pubmed.ncbi.nlm.nih.gov/35704578
https://pubmed.ncbi.nlm.nih.gov/35704578