CASTAING Bertrand

email : bertrand.castaing@cnrs-orleans.fr

Phone : +33 2.38.25.78.43

Office D211

Research director, responsible of the thematic group “DNA repair: structure, fonction and dynamic”

 



32 documents

Article dans une revue

  • Martine Beaufour, David Ginguené, Rémy Le Meur, Bertrand Castaing, Martine Cadène. Liquid Native MALDI Mass Spectrometry for the Detection of Protein-Protein Complexes. Journal of The American Society for Mass Spectrometry, Springer Verlag (Germany), 2018, 29 (10), pp.1981-1994. ⟨hal-01965971⟩
  • Serge Boiteux, Franck Coste, Bertrand Castaing. Repair of 8-oxo-7,8-dihydroguanine in prokaryotic and eukaryotic cells: Properties and biological roles of the Fpg and OGG1 DNA N -glycosylases. Free Radical Biology and Medicine, Elsevier, 2017, 107, pp.179 - 201. ⟨10.1016/j.freeradbiomed.2016.11.042⟩. ⟨hal-01618166⟩
  • R. Le Meur, F. Culard, V. Nadan, S. Goffinont, F. Coste, et al.. The nucleoid-associated protein HU enhances 8-oxoguanine base excision by the formamidopyrimidine-DNA glycosylase. Biochemical Journal, Portland Press, 2015, 471 (1), pp.13-23. ⟨10.1042/BJ20150387⟩. ⟨hal-01216639⟩
  • Rémy Le Meur, Karine Loth, Françoise Culard, Bertrand Castaing, Céline Landon. Backbone assignment of the three dimers of HU from Escherichia coli at 293 K: EcHUα2, EcHUβ2 and EcHUαβ. Biomolecular NMR Assignments, Springer, 2015, 9 (2), pp.359-363. ⟨10.1007/s12104-015-9610-6⟩. ⟨hal-01171467⟩
  • F. d'Heygere, A. Schwartz, F. Coste, B. Castaing, M. Boudvillain. ATP-dependent motor activity of the transcription termination factor Rho from Mycobacterium tuberculosis. Nucleic Acids Research, Oxford University Press, 2015, 43, pp.6099-60111. ⟨10.1093/nar/gkv505⟩. ⟨hal-01171219⟩
  • Françoise Paquet, Olivier Delalande, Stephane Goffinont, Françoise Culard, Karine Loth, et al.. Model of a DNA-protein complex of the architectural monomeric protein MC1 from Euryarchaea. PLoS ONE, Public Library of Science, 2014, 9 (2), pp.e88809. ⟨10.1371/journal.pone.0088809⟩. ⟨hal-01063974⟩
  • E. Rusaouën, X. Riedinger, J.-C. Tisserand, F. Seychelles, J. Salort, et al.. Laminar and Intermittent flow in a tilted heat pipe. European Physical Journal E: Soft matter and biological physics, EDP Sciences: EPJ, 2014, 37 (1), pp.4. ⟨10.1140/epje/i2014-14004-7⟩. ⟨hal-01612392⟩
  • A. Biela, F. Coste, F. Culard, M. Guerin, S. Goffinont, et al.. Zinc finger oxidation of Fpg/Nei DNA glycosylases by 2-thioxanthine: biochemical and X-ray structural characterization. Nucleic Acids Research, Oxford University Press, 2014, 42 (16), pp.doi: 10.1093/nar/gku613. ⟨10.1093/nar/gku613⟩. ⟨hal-01175522⟩
  • L. Chevillard, B. Castaing, A. Arneodo, E. Leveque, J. F. Pinton, et al.. A phenomenological theory of Eulerian and Lagrangian velocity fluctuations in turbulent flows. Comptes Rendus Physique, Elsevier Masson, 2012, 13 (9-10), pp.899-928. ⟨10.1016/j.crhy.2012.09.002⟩. ⟨hal-01557081⟩
  • Sylvie Baucheron, Franck Coste, Sylvie Canepa, Marie-Christine Maurel, Etienne Giraud, et al.. Binding of the RamR repressor to wild-type and mutated promoters of the RamA gene involved in efflux-mediated multidrug resistance in Salmonella enterica serovar Typhimurium.. Antimicrobial Agents and Chemotherapy, American Society for Microbiology, 2012, 56 (2), pp.942-8. ⟨10.1128/AAC.05444-11⟩. ⟨hal-00721770⟩
  • Béatrice Matot, Yann-Vaï Le Bihan, Rachel Lescasse, Javier Pérez, Simona Miron, et al.. The orientation of the C-terminal domain of the Saccharomyces cerevisiae Rap1 protein is determined by its binding to DNA.. Nucleic Acids Research, Oxford University Press, 2012, 40 (7), pp.3197-207. ⟨10.1093/nar/gkr1166⟩. ⟨hal-00720647⟩
  • Norbert Garnier, Karine Loth, Franck Coste, Rafal Augustyniak, Virginie Nadan, et al.. An alternative flexible conformation of the E. coli HU beta(2) protein: structural, dynamics, and functional aspects. European Biophysics Journal, Springer Verlag (Germany), 2011, 40 (2), pp.117-129. ⟨10.1007/s00249-010-0630-y⟩. ⟨hal-00602370⟩
  • Yann Vei Le Bihan, Angeles M. Izquierdo, Franck Coste, Pierre Aller, Françoise Culard, et al.. 5-Hydroxy-5-methylhydantoin DNA lesion, a molecular trap for DNA glycosylases. Nucleic Acids Research, Oxford University Press, 2011, 39 (14), pp.6277-6290. ⟨10.1093/nar/gkr215⟩. ⟨hal-00614943⟩
  • Franck Coste, Matthias Ober, Yann-Vaï Le Bihan, Maria Angeles Izquierdo, Nadège Hervouet, et al.. Bacterial base excision repair enzyme Fpg recognizes bulky N7-substituted-FapydG lesion via unproductive binding mode.. Chemistry & Biology / Chemistry and Biology; CHEMISTRY & BIOLOGY, 2008, 15 (7), pp.706-17. ⟨10.1016/j.chembiol.2008.05.014⟩. ⟨hal-00408047⟩
  • Irina Gutsche, Andreja Vujicić-Zagar, Xavier Siebert, Pascale Servant, Françoise Vannier, et al.. Complex oligomeric structure of a truncated form of DdrA: A protein required for the extreme radiotolerance of Deinococcus.. Biochimica et Biophysica Acta - Molecular Cell Research, Elsevier, 2008, 1784 (7-8), pp.1050-8. ⟨10.1016/j.bbapap.2008.03.009⟩. ⟨hal-00297143⟩
  • C. BurÉ, B. Castaing, C. Lange, A.F. Delmas. Location and base selectivity on fragmentation of brominated oligodeoxynucleotides. Journal of Mass Spectrometry, Wiley-Blackwell, 2006, 41 (1), pp.84-90. ⟨10.1002/jms.967⟩. ⟨hal-00088837⟩
  • Stéphane Boiteux, Bertrand Castaing, J.P. Radicella. BER: (Base excision repair): molecular mechanisms and biological roles. Biofutur, Elsevier - Cachan : Lavoisier, 2006, 25 (271), pp.35-39. ⟨hal-00387927⟩
  • F. Coste, M. Ober, T. Carrell, S. Boiteux, C. Zelwer, et al.. Structural basis for the recognition of the FapydG lesion (2,6-diamino-4-hydroxy-5-formamidopyrimidine) by Formamidopyrimidine-DNA glycosylase. Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2006, 279 (42), pp.44074-44083. ⟨10.1074/jbc.M405928200⟩. ⟨hal-00114389⟩
  • Marie Davídková, Viktorie Stísová, Stéphane Goffinont, Nathalie Gillard, Bertrand Castaing, et al.. Modification of DNA radiolysis by DNA-binding proteins: structural aspects. Radiation Protection Dosimetry, Oxford University Press (OUP), 2006, 122 (1-4), pp.100-105. ⟨10.1093/rpd/ncl442⟩. ⟨hal-00168743⟩
  • K. Pereira de Jesus, L. Serre, C. Zelwer, B. Castaing. Structural insights into abasic site for Fpg specific binding and catalysis: comparative high-resolution crystallographic studies of Fpg bound to various models of abasic site analogues containing DNA. Nucleic Acids Research, Oxford University Press, 2005, 33, pp.5936-5944. ⟨hal-00088666⟩
  • M. BÉgusovÀ, N. Gillard, D. Sy, B. Castaing, M. Charlier, et al.. Radiolysis of DNA-protein complexes. Radiation Physics and Chemistry, Elsevier, 2005, 72, pp.265-270. ⟨hal-00088505⟩
  • Patricia Amara, Laurence Serre, B. Castaing, A. Thomas. Insights into the DNA repair process by the formamidopyrimidine-DNA glycosylase investigated by molecular dynamics. Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2004, 13 (8), pp.2009-2021. ⟨10.1110/ps.04772404⟩. ⟨hal-00088335⟩
  • N. Gillard, M. BÉgusovÀ, B. Castaing, M. Spotheim-Maurizot. Radiation affects binding of Fpg repair protein to an abasic site containing DNA. Radiation Research, Radiation Research Society, 2004, 162, pp.566-571. 2.0.CO;2">⟨10.1043/0033-7587(2004)162<0566:RABOFR>2.0.CO;2⟩. ⟨hal-00113044⟩
  • Charles Ramstein, Nadège Hervouet, Franck Coste, Charles Zelwer, Jacques Oberto, et al.. Evidence of a thermal unfolding dimeric intermediate for the Escherichia coli histone-like HU proteins: thermodynamics and structure.. Journal of Molecular Biology, Elsevier, 2003, 331 (1), pp.101-21. ⟨hal-02127656⟩
  • E. Muller, D. Gasparutto, B. Castaing, A. Favier, J. Cadet. Recognition of cyclonucleoside lesions by the Lactococcus lactis FPG protein. Nucleosides, Nucleotides and Nucleic Acids, Taylor & Francis, 2003, 22, pp.1563-1565. ⟨hal-00088198⟩
  • Franck Coste, N. Hervouet, J. Oberto, C. Zelwer, Bertrand Castaing. Crystallization and preliminary X-ray diffraction analysis of the homodimeric form alpha2 of the HU protein from Escherichia coli.. Acta Crystallographica Section D: Biological Crystallography, International Union of Crystallography, 1999, 55 (Pt 11), pp.1952-4. ⟨hal-02127644⟩
  • A. Arneodo, C. Baudet, F. Belin, R. Benzi, B. Castaing, et al.. Structure functions in turbulence, in various flow configurations, at Reynolds number between 30 and 5000, using extended self-similarity. EPL - Europhysics Letters, European Physical Society/EDP Sciences/Società Italiana di Fisica/IOP Publishing, 1996, 34 (6), pp.411-416. ⟨10.1209/epl/i1996-00472-2⟩. ⟨hal-01557131⟩

Chapitre d'ouvrage

  • F. d'Heygère, A. Schwartz, F. Coste, B. Castaing, M. Boudvillain. Monitoring RNA Unwinding by the Transcription Termination Factor Rho from Mycobacterium tuberculosis. Methods in Mecular Biology, 1259, Springer, pp.293-311, 2015, RNA remodelling proteins (Boudvillain, ed), 978-1-4939-2213-0. ⟨10.1007/978-1-4939-2214-7_18⟩. ⟨hal-01174055⟩
  • L. Chevillard, B. Castaing, E. Leveque, A. Arneodo. Phenomenological relation between the Kolmogorov constant and the skewness in turbulence. Eckhardt, B. Advances in Turbulence Xii - Proceedings of the 12th Euromech European Turbulence Conference, 132, Springer-Verlag Berlin, pp.719-720, 2009, Springer Proceedings in Physics, 978-3-642-03085-7; 978-3-642-03084-0. ⟨10.1007/978-3-642-03085-7_174⟩. ⟨hal-01557098⟩
  • Evelyne Sage, Bertrand Castaing. Radiation damage to biomolecules, radioprotection and radiotherapy. Genome maintenance mechanisms in response to radiation-induced DNA damage. Mélanie Spotheim-Maurizot. Radiation chemistry from basics to applications in material and life sciences, EDP Sciences, pp.219-232, 2008. ⟨hal-00284342⟩
  • E. Sage, B. Castaing. Genome maintenance mechanisms in response to radiation-induced DNA damage.. Spotheim-Maurizot, M., Mostafavi, M., Douki, T., Belloni, J. Radiation chemistry from basics to applications in material and life sciences, EDP Sciences, Les Ulis, pp.219-232, 2008. ⟨hal-00623595⟩

Autre publication

  • Kadija Essalhi, L. Gellon, Julie Berthault, Françoise Culard, Martine Guerrin, et al.. Ogg1, a Saccharomyces cerevisiae bifunctional DNA glycosylase involved in base excision repair of oxidative DNA damage, interacts with the replicative DNA polymerase, Pol epsilon. 2011, pp.409. ⟨hal-00614891⟩