Dr. Christophe DECROOS
Dr.
Christophe
DECROOS
AMU iSm2 Service 342
Campus Scientifique de St Jérôme
13397
Marseille cedex 20
Téléphone :
Courriel :
Entrée :
01/10/2015
Parcours :
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Enseignements :
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Thématiques :
Métalloenzymes à cuivre (LPMO)
Responsabilités administratives :
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Publications (13)
Reference
Résumé graphique
HAL
LPMO‐like activity of bioinspired copper complexes: from model substrate to extended polysaccharides
Rébecca Leblay, Rafael Delgadillo-Ruiz, Christophe Decroos, Christelle Hureau, Marius Réglier, Ivan Castillo Pérez, Bruno Faure, A. Jalila Simaan, ChemCatChem, 2023. <hal-04231361>
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Decoding the Ambiguous Electron Paramagnetic Resonance Signals in the Lytic Polysaccharide Monooxygenase from Photorhabdus luminescens
Rogelio Gómez-Piñeiro, Maria Drosou, Sylvain Bertaina, Christophe Decroos, A. Jalila Simaan, Dimitrios Pantazis, Maylis Orio, Inorganic Chemistry, 2022, 61, 8022-8035. <hal-03704221>
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Structural analysis of histone deacetylase 8 mutants associated with Cornelia de Lange Syndrome spectrum disorders
Jeremy Osko, Nicholas Porter, Christophe Decroos, Matthew Lee, Paris Watson, Sarah Raible, Ian Krantz, Matthew Deardorff, David Christianson, Journal of Structural Biology, 2021, 213, 107681. <hal-03106173>
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Characterization of a bacterial copper‐dependent lytic polysaccharide monooxygenase with an unusual second coordination sphere
Alessia Munzone, Bilal El Kerdi, Mathieu Fanuel, Hélène Rogniaux, David Ropartz, Marius Réglier, Antoine Royant, A. Jalila Simaan, Christophe Decroos, FEBS Journal, 2020, 287, 3298-3314. <hal-02467531>
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Understanding the g -tensors of perchlorotriphenylmethyl and Finland-type trityl radicals
Paul Demay-Drouhard, H.Y.V. Ching, Christophe Decroos, Régis Guillot, Yun Li, Leandro Tabares, Clotilde Policar, Helene C Bertrand, Sun Un, Physical Chemistry Chemical Physics, 2020. <hal-02938076>
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Phosphorylation of Histone Deacetylase 8: Structural and Mechanistic Analysis of the Phosphomimetic S39E Mutant
Katherine Welker Leng, Carol Ann Castañeda, Christophe Decroos, Barira Islam, Shozeb Haider, David W. Christianson, Carol Fierke, Biochemistry, 2019, 58, 4480-4493. <hal-02391044>
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Chemical Modification of 1-Aminocyclopropane Carboxylic Acid (ACC) Oxidase: Cysteine Mutational Analysis, Characterization, and Bioconjugation with a Nitroxide Spin Label
Sybille Tachon, Eugénie Fournier, Christophe Decroos, Pascal Mansuelle, Emilien Etienne, Marc Maresca, Marlène Martinho, Valérie Belle, Thierry Tron, Ariane Jalila Simaan, Molecular Biotechnology, 2019. <hal-02157289>
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Toward Stable Electron Paramagnetic Resonance Oximetry Probes: Synthesis, Characterization, and Metabolic Evaluation of New Ester Derivatives of a Tris-( para -carboxyltetrathiaaryl)methyl (TAM) Radical
Christophe Decroos, Véronique Balland, Jean-Luc Boucher, Gildas Bertho, Yun Xu-Li, Daniel Mansuy, Chemical Research in Toxicology, 2013, 26, 1561-1569. <hal-03684842>
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HDAC8 mutations in Cornelia de Lange syndrome affect the cohesin acetylation cycle.
Matthew A. Deardorff, Masashige Bando, Ryuichiro Nakato, Erwan Watrin, Takehiko Itoh, Masashi Minamino, Katsuya Saitoh, Makiko Komata, Yuki Katou, Dinah Clark, Kathryn E. Cole, Elfride de Baere, Christophe Decroos, Nataliya Di Donato, Sarah Ernst, Lauren J. Francey, Yolanda Gyftodimou, Kyotaro Hirashima, Melanie Hullings, Yuuichi Ishikawa, Christian Jaulin, Maninder Kaur, Tohru Kiyono, Patrick M. Lombardi, Laura Magnaghi-Jaulin, Geert R. Mortier, Naohito Nozaki, Michael B. Petersen, Hiroyuki Seimiya, Victoria M. Siu, Yutaka Suzuki, Kentaro Takagaki, Jonathan J. Wilde, Patrick J. Willems, Claude Prigent, Gabriele Gillessen-Kaesbach, David W. Christianson, Frank J. Kaiser, Laird G. Jackson, Toru Hirota, Ian D. Krantz, Katsuhiko Shirahige, Nature, 2012, 489, 313-7. <inserm-00728375>
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First Combined In Vivo X-ray Tomography And High-resolution Molecular Electron Paramagnetic Resonance (epr) Imaging Of The Mouse Knee Joint Taking Into Account The Disappearance Kinetics Of The Epr Probe.
Nicolas Bézière, Christophe Decroos, Karen Mkhitaryan, Elizabeth Kish, Frédéric Jp Richard, Stéphanie Bigot-Marchand, Sylvain Durand, Florence Cloppet, Caroline Chauvet, Marie-Thérèse Corvol, Francois Rannou, Yun Xu-Li, Daniel Mansuy, Fabienne Peyrot, Yves-Michel Frapart, Molecular Imaging, 2012, 11, epub ahead of print. <hal-00712106>
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Pages
Chapitres d'ouvrages (1)
Reference
Résumé graphique
HAL
A. Jalila Simaan, Alda Lisa Concia, Alessia Munzone, Maria-Chrysanthi Kafentzi, Amélie Kochem, et al.. Modeling the Mononuclear Copper Monooxygenase Active Site. Series on Chemistry, Energy and the Environment: Volume 5 Bioinspired Chemistry; From Enzymes to Synthetic Models, pp.185-263, 2019, ⟨10.1142/9789813274440_0008⟩. ⟨hal-02094996⟩
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Début
Début
Métalloenzymes à cuivre (LPMO)
Début
| Reference | Résumé graphique | HAL |
|---|---|---|
|
LPMO‐like activity of bioinspired copper complexes: from model substrate to extended polysaccharides |
|
✓ |
|
Decoding the Ambiguous Electron Paramagnetic Resonance Signals in the Lytic Polysaccharide Monooxygenase from Photorhabdus luminescens |
|
✓ |
|
Structural analysis of histone deacetylase 8 mutants associated with Cornelia de Lange Syndrome spectrum disorders |
|
✓ |
|
Characterization of a bacterial copper‐dependent lytic polysaccharide monooxygenase with an unusual second coordination sphere |
|
✓ |
|
Understanding the g -tensors of perchlorotriphenylmethyl and Finland-type trityl radicals |
|
✓ |
|
Phosphorylation of Histone Deacetylase 8: Structural and Mechanistic Analysis of the Phosphomimetic S39E Mutant |
|
✓ |
|
Chemical Modification of 1-Aminocyclopropane Carboxylic Acid (ACC) Oxidase: Cysteine Mutational Analysis, Characterization, and Bioconjugation with a Nitroxide Spin Label |
|
✓ |
|
Toward Stable Electron Paramagnetic Resonance Oximetry Probes: Synthesis, Characterization, and Metabolic Evaluation of New Ester Derivatives of a Tris-( para -carboxyltetrathiaaryl)methyl (TAM) Radical |
|
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|
HDAC8 mutations in Cornelia de Lange syndrome affect the cohesin acetylation cycle. |
|
✓ |
|
First Combined In Vivo X-ray Tomography And High-resolution Molecular Electron Paramagnetic Resonance (epr) Imaging Of The Mouse Knee Joint Taking Into Account The Disappearance Kinetics Of The Epr Probe. |
|
✓ |
Pages
| Reference | Résumé graphique | HAL |
|---|---|---|
|
A. Jalila Simaan, Alda Lisa Concia, Alessia Munzone, Maria-Chrysanthi Kafentzi, Amélie Kochem, et al.. Modeling the Mononuclear Copper Monooxygenase Active Site. Series on Chemistry, Energy and the Environment: Volume 5 Bioinspired Chemistry; From Enzymes to Synthetic Models, pp.185-263, 2019, ⟨10.1142/9789813274440_0008⟩. ⟨hal-02094996⟩ |
|
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