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International Journal of Molecular Sciences|December 8, 2020
Focus on DNA Glycosylases-A Set of Tightly Regulated Enzymes with a High Potential as Anticancer Drug TargetsFabienne Hans, Muge Senarisoy, Chandini Bhaskar Naidu, et al.
Molecular Biology of the Cell|June 5, 2009
Molecular distinctions between Aurora A and B: a single residue change transforms Aurora A into correctly localized and functional Aurora BFabienne Hans, Dimitrios A Skoufias, Stefan Dimitrov, et al.
Methods in Molecular Biology (Clifton, N.J.)|July 26, 2018
Erratum to: Characterizing Intact Macromolecular Complexes Using Native Mass SpectrometryElisabetta Boeri Erba, Luca Signor, Mizar F Oliva, et al.
Methods in Molecular Biology (Clifton, N.J.)|April 2, 2018
Characterizing Intact Macromolecular Complexes Using Native Mass SpectrometryElisabetta Boeri Erba, Luca Signor, Mizar F Oliva, et al.
Cell Cycle (Georgetown, Tex.)|September 20, 2008
Localization of aurora A and aurora B kinases during interphase: role of the N-terminal domainYoann Rannou, Marie-Bérengère Troadec, Clotilde Petretti, et al.
Scientific Reports|August 4, 2016
Fusion to a homo-oligomeric scaffold allows cryo-EM analysis of a small proteinFrancesca Coscia, Leandro F Estrozi, Fabienne Hans, et al.
Molecular Biology of the Cell|October 29, 2004
A small C-terminal sequence of Aurora B is responsible for localization and functionLaetitia Scrittori, Dimitrios A Skoufias, Fabienne Hans, et al.
Molecular Cell|April 30, 2003
The histone variant macroH2A interferes with transcription factor binding and SWI/SNF nucleosome remodelingDimitar Angelov, Annie Molla, Pierre-Yves Perche, et al.
Journal of Biochemistry|May 20, 2014
Centromeric histone variant CENP-A represses acetylation-dependent chromatin transcription that is relieved by histone chaperone NPM1Jayasha Shandilya, Parijat Senapati, Fabienne Hans, et al.
The Journal of Biological Chemistry|July 23, 2004
The histone octamer is invisible when NF-kappaB binds to the nucleosomeDimitar Angelov, François Lenouvel, Fabienne Hans, et al.
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