| Year |
Citation |
Score |
| 2022 |
Pardal AJ, Bowman AJ. A specific role for Importin-5 and NASP in the import and nuclear hand-off of monomeric H3. Elife. 11. PMID 36066346 DOI: 10.7554/eLife.81755 |
0.74 |
|
| 2019 |
Pardal AJ, Fernandes-Duarte F, Bowman AJ. The histone chaperoning pathway: from ribosome to nucleosome. Essays in Biochemistry. 63: 29-43. PMID 31015382 DOI: 10.1042/Ebc20180055 |
0.744 |
|
| 2018 |
Apta-Smith MJ, Hernandez-Fernaud JR, Bowman AJ. Evidence for the nuclear import of histones H3.1 and H4 as monomers. The Embo Journal. PMID 30177573 DOI: 10.15252/Embj.201798714 |
0.765 |
|
| 2017 |
Bowman A, Koide A, Goodman JS, Colling ME, Zinne D, Koide S, Ladurner AG. sNASP and ASF1A function through both competitive and compatible modes of histone binding. Nucleic Acids Research. 45: 643-656. PMID 28123037 DOI: 10.1093/Nar/Gkw892 |
0.8 |
|
| 2015 |
Bowman A, Lercher L, Singh HR, Zinne D, Timinszky G, Carlomagno T, Ladurner AG. The histone chaperone sNASP binds a conserved peptide motif within the globular core of histone H3 through its TPR repeats. Nucleic Acids Research. PMID 26673727 DOI: 10.1093/Nar/Gkv1372 |
0.791 |
|
| 2014 |
Bowman A, Hammond CM, Stirling A, Ward R, Shang W, El-Mkami H, Robinson DA, Svergun DI, Norman DG, Owen-Hughes T. The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution. Nucleic Acids Research. 42: 6038-51. PMID 24688059 DOI: 10.1093/Nar/Gku232 |
0.621 |
|
| 2013 |
Hondele M, Stuwe T, Hassler M, Halbach F, Bowman A, Zhang ET, Nijmeijer B, Kotthoff C, Rybin V, Amlacher S, Hurt E, Ladurner AG. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Nature. 499: 111-4. PMID 23698368 DOI: 10.1038/Nature12242 |
0.609 |
|
| 2013 |
Zhang W, Tyl M, Ward R, Sobott F, Maman J, Murthy AS, Watson AA, Fedorov O, Bowman A, Owen-Hughes T, El Mkami H, Murzina NV, Norman DG, Laue ED. Structural plasticity of histones H3-H4 facilitates their allosteric exchange between RbAp48 and ASF1. Nature Structural & Molecular Biology. 20: 29-35. PMID 23178455 DOI: 10.1038/Nsmb.2446 |
0.796 |
|
| 2012 |
Bowman A, Owen-Hughes T. 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. PMID 22183605 DOI: 10.1007/978-1-61779-477-3_22 |
0.625 |
|
| 2011 |
Bowman A, Ward R, Wiechens N, Singh V, El-Mkami H, Norman DG, Owen-Hughes T. The histone chaperones Nap1 and Vps75 bind histones H3 and H4 in a tetrameric conformation. Molecular Cell. 41: 398-408. PMID 21329878 DOI: 10.1016/J.Molcel.2011.01.025 |
0.81 |
|
| 2010 |
Bowman A, Ward R, El-Mkami H, Owen-Hughes T, Norman DG. Probing the (H3-H4)2 histone tetramer structure using pulsed EPR spectroscopy combined with site-directed spin labelling. Nucleic Acids Research. 38: 695-707. PMID 19914933 DOI: 10.1093/nar/gkp1003 |
0.648 |
|
| 2009 |
Ward R, Bowman A, El-Mkami H, Owen-Hughes T, Norman DG. Long distance PELDOR measurements on the histone core particle. Journal of the American Chemical Society. 131: 1348-9. PMID 19138067 DOI: 10.1021/Ja807918F |
0.668 |
|
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