B. Castaing

发表

Molecular principles of recruitment and dynamics of guest proteins in liquid droplets

Y. Levy, K. Kamagata, Saori Kanbayashi, 2021, Scientific Reports.

Model of a DNA-Protein Complex of the Architectural Monomeric Protein MC1 from Euryarchaea

K. Loth, F. Culard, B. Castaing, 2014, PloS one.

New protein-DNA complexes in archaea: a small monomeric protein induces a sharp V-turn DNA structure

K. Loth, F. Culard, B. Castaing, 2018, Scientific Reports.

Fpg protein of Escherichia coli is a zinc finger protein whose cysteine residues have a structural and/or functional role.

G. de Murcia, T. O'Connor, B. Castaing, 1993, The Journal of biological chemistry.

Radiation Affects Binding of Fpg Repair Protein to an Abasic Site Containing DNA

B. Castaing, M. Spotheim-Maurizot, N. Gillard, 2004, Radiation research.

Location and base selectivity on fragmentation of brominated oligodeoxynucleotides.

B. Castaing, A. Delmas, C. Buré, 2006, Journal of mass spectrometry : JMS.

Microwave-Assisted Suzuki-Miyaura and Sonogashira Coupling of 4-Chloro-2-(trifluoromethyl)pyrido[1,2-e ]purine Derivatives

N. Biteau, B. Castaing, Vincent Roy, 2019, European Journal of Organic Chemistry.

Structure-dependent recruitment and diffusion of guest proteins in liquid droplets of FUS

K. Kamagata, Saori Kanbayashi, Nanako Iwaki, 2022, Scientific Reports.

An alternative flexible conformation of the E. coli HUβ2 protein: structural, dynamics, and functional aspects

K. Loth, B. Castaing, R. Augustyniak, 2011, European Biophysics Journal.

Crystallization and preliminary X‐ray diffraction analysis of the homodimeric form α2 of the HU protein from Escherichia coli

B. Castaing, J. Oberto, C. Zelwer, 1999 .

Cleavage and binding of a DNA fragment containing a single 8-oxoguanine by wild type and mutant FPG proteins.

B. Castaing, S. Boiteux, H. Seliger, 1993, Nucleic acids research.

Crystal Structure of Lactococcus lactis Formamido-pyrimidine DNA Glycosylase (alias Fpg or MutM) Non Covalently Bound to an AP Site Containing DNA.

B. Castaing, L. Serre, S. Boiteux, 2002 .

Three‐dimensional structures of avian beta‐microseminoproteins: insight from the chicken egg‐specific beta‐microseminoprotein 3 paralog

K. Loth, B. Castaing, V. Labas, 2021, FEBS open bio.

5-Hydroxy-5-methylhydantoin DNA lesion, a molecular trap for DNA glycosylases

T. Carell, Y. Le Bihan, F. Culard, 2011, Nucleic acids research.

Structural Basis for the Recognition of the FapydG Lesion (2,6-Diamino-4-hydroxy-5-formamidopyrimidine) by Formamidopyrimidine-DNA Glycosylase*

T. Carell, B. Castaing, S. Boiteux, 2004, Journal of Biological Chemistry.

Bacterial base excision repair enzyme Fpg recognizes bulky N7-substituted-FapydG lesion via unproductive binding mode.

T. Carell, Y. Le Bihan, B. Castaing, 2008, Chemistry & biology.

The orientation of the C-terminal domain of the Saccharomyces cerevisiae Rap1 protein is determined by its binding to DNA

Y. Le Bihan, B. Castaing, S. Zinn-Justin, 2011, Nucleic acids research.

Crystal structure of the Lactococcus lactis formamidopyrimidine‐DNA glycosylase bound to an abasic site analogue‐containing DNA

B. Castaing, L. Serre, S. Boiteux, 2002, The EMBO journal.

Evidence of a thermal unfolding dimeric intermediate for the Escherichia coli histone-like HU proteins: thermodynamics and structure.

J. Ramstein, B. Castaing, J. Oberto, 2003, Journal of molecular biology.

OGG1 competitive inhibitors show important off-target effects by directly inhibiting efflux pumps and disturbing mitotic progression

B. Castaing, A. D. Di Guilmi, G. Pinna, 2023, Frontiers in Cell and Developmental Biology.

HU Protein of Escherichia coli Binds Specifically to DNA That Contains Single-strand Breaks or Gaps (*)

B. Castaing, S. Boiteux, J. Laval, 1995, The Journal of Biological Chemistry.

Repair of 8‐oxo‐7,8‐dihydroguanine in prokaryotic and eukaryotic cells: Properties and biological roles of the Fpg and OGG1 DNA N‐glycosylases☆

B. Castaing, S. Boiteux, F. Coste, 2017, Free radical biology & medicine.

Thiopurine Derivative-Induced Fpg/Nei DNA Glycosylase Inhibition: Structural, Dynamic and Functional Insights

Virginie Gaudon, B. Castaing, V. Aucagne, 2020, International journal of molecular sciences.

Identification of key residues of the DNA glycosylase OGG1 controlling efficient DNA sampling and recruitment to oxidized bases in living cells

Catherine Chapuis, Virginie Gaudon, B. Castaing, 2022, bioRxiv.

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

B. Castaing, L. Serre, C. Zelwer, 2005, Nucleic acids research.

Crystallization and preliminary X-ray crystallographic studies of a complex between the Lactococcus lactis Fpg DNA-repair enzyme and an abasic site containing DNA.

B. Castaing, L. Serre, C. Zelwer, 2002, Acta crystallographica. Section D, Biological crystallography.

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

F. Culard, B. Castaing, M. Maurel, 2011, Antimicrobial Agents and Chemotherapy.

AP site structural determinants for Fpg specific recognition.

B. Castaing, S. Boiteux, C. Zelwer, 1999, Nucleic acids research.

The nucleoid-associated protein HU enhances 8-oxoguanine base excision by the formamidopyrimidine-DNA glycosylase.

K. Loth, F. Culard, B. Castaing, 2015, The Biochemical journal.

Zinc finger oxidation of Fpg/Nei DNA glycosylases by 2-thioxanthine: biochemical and X-ray structural characterization

T. Carell, F. Culard, B. Castaing, 2014, Nucleic acids research.

Recognition of Cyclonucleoside Lesions by the Lactococcus lactis FPG Protein

A. Favier, J. Cadet, B. Castaing, 2003, Nucleosides, nucleotides & nucleic acids.

DNA containing a chemically reduced apurinic site is a high affinity ligand for the E. coli formamidopyrimidine-DNA glycosylase.

B. Castaing, S. Boiteux, C. Zelwer, 1992, Nucleic acids research.

Monitoring RNA unwinding by the transcription termination factor Rho from Mycobacterium tuberculosis.

B. Castaing, M. Boudvillain, A. Schwartz, 2015, Methods in molecular biology.

Complex oligomeric structure of a truncated form of DdrA: a protein required for the extreme radiotolerance of Deinococcus.

B. Castaing, I. Gutsche, Xavier Siebert, 2008, Biochimica et biophysica acta.

Liquid Native MALDI Mass Spectrometry for the Detection of Protein-Protein Complexes

M. Cadene, B. Castaing, M. Beaufour, 2018, Journal of The American Society for Mass Spectrometry.

Synthesis of an Enantiomerically Pure Carbocyclic DNA Abasic Site Analogue

B. Castaing, C. Zelwer, J. Fourrey, 1999 .

Insights into the DNA repair process by the formamidopyrimidine‐DNA glycosylase investigated by molecular dynamics

P. Amara, B. Castaing, Aline Thomas, 2004, Protein science : a publication of the Protein Society.

ATP-dependent motor activity of the transcription termination factor Rho from Mycobacterium tuberculosis

B. Castaing, M. Boudvillain, A. Schwartz, 2015, Nucleic acids research.

Structure and Sequence Determinants Governing the Interactions of RNAs with Influenza A Virus Non-Structural Protein NS1

D. Marc, Virginie Gaudon, B. Castaing, 2020, Viruses.

Backbone assignment of the three dimers of HU from Escherichia coli at 293 K: EcHUα2, EcHUβ2 and EcHUαβ

K. Loth, F. Culard, B. Castaing, 2015, Biomolecular NMR Assignments.

Catalytic and DNA binding properties of the ogg1 protein of Saccharomyces cerevisiae: comparison between the wild type and the K241R and K241Q active-site mutant proteins.

B. Castaing, P. A. van der Kemp, S. Boiteux, 2000, Biochemistry.

Structural insights into the regulation of the human E2∼SUMO conjugate through analysis of its stable mimetic

Virginie Gaudon, B. Castaing, S. Goffinont, 2023, The Journal of biological chemistry.

Structural insights into the regulation of the human E2SUMO conjugate through analysis of its stable mimetic

Virginie Gaudon, B. Castaing, N. Garnier, 2023 .

Complex oligomeric structure of a truncated form of DdrA: a protein required for the extreme radiotolerance of Deinococcus.

B. Castaing, I. Gutsche, Xavier Siebert, 2008, Biochimica et biophysica acta.