Andrew J Bowman

2011-2015 LMU - Munich 
 2015- Warwick University, UK 
"Andrew Bowman"
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Pardal AJ, Bowman AJ. (2022) A specific role for Importin-5 and NASP in the import and nuclear hand-off of monomeric H3. Elife. 11
Pardal AJ, Fernandes-Duarte F, Bowman AJ. (2019) The histone chaperoning pathway: from ribosome to nucleosome. Essays in Biochemistry. 63: 29-43
Apta-Smith MJ, Hernandez-Fernaud JR, Bowman AJ. (2018) Evidence for the nuclear import of histones H3.1 and H4 as monomers. The Embo Journal
Bowman A, Koide A, Goodman JS, et al. (2017) sNASP and ASF1A function through both competitive and compatible modes of histone binding. Nucleic Acids Research. 45: 643-656
Bowman A, Lercher L, Singh HR, et al. (2015) The histone chaperone sNASP binds a conserved peptide motif within the globular core of histone H3 through its TPR repeats. Nucleic Acids Research
Bowman A, Hammond CM, Stirling A, et al. (2014) The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution. Nucleic Acids Research. 42: 6038-51
Hondele M, Stuwe T, Hassler M, et al. (2013) Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Nature. 499: 111-4
Zhang W, Tyl M, Ward R, et al. (2013) Structural plasticity of histones H3-H4 facilitates their allosteric exchange between RbAp48 and ASF1. Nature Structural & Molecular Biology. 20: 29-35
Bowman A, Owen-Hughes T. (2012) Sulfyhydryl-reactive site-directed cross-linking as a method for probing the tetrameric structure of histones H3 and H4. Methods in Molecular Biology (Clifton, N.J.). 833: 373-87
Bowman A, Ward R, Wiechens N, et al. (2011) The histone chaperones Nap1 and Vps75 bind histones H3 and H4 in a tetrameric conformation. Molecular Cell. 41: 398-408
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