2023
Agirre J, Atanasova M, Bagdonas H, Ballard CB, Baslé A, Beilsten-Edmands J, Borges RJ, Brown DG, Burgos-Mármol JJ, Berrisford JM, Bond PS, Caballero I, Catapano L, Chojnowski G, Cook AG, Cowtan KD, Croll TI, Debreczeni JÉ, Devenish NE, Dodson EJ, Drevon TR, Emsley P, Evans G, Evans PR, Fando M, Foadi J, Fuentes-Montero L, Garman EF, Gerstel M, Gildea RJ, Hatti K, Hekkelman ML, Heuser P, Hoh SW, Hough MA, Jenkins HT, Jiménez E, Joosten RP, Keegan RM, Keep N, Krissinel EB, Kolenko P, Kovalevskiy O, Lamzin VS, Lawson DM, Lebedev AA, Leslie AGW, Lohkamp B, Long F, Malý M, McCoy AJ, McNicholas SJ, Medina A, Millán C, Murray JW, Murshudov GN, Nicholls RA, Noble MEM, Oeffner R, Pannu NS, Parkhurst JM, Pearce N, Pereira J, Perrakis A, Powell HR, Read RJ, Rigden DJ, Rochira W, Sammito M, Sánchez Rodríguez F, Sheldrick GM, Shelley KL, Simkovic F, Simpkin AJ, Skubak P, Sobolev E, Steiner RA, Stevenson K, Tews I, Thomas JMH, Thorn A, Valls JT, Uski V, Usón I, Vagin A, Velankar S, Vollmar M, Walden H, Waterman D, Wilson KS, Winn MD, Winter G, Wojdyr M, Yamashita K. The CCP4 suite: integrative software for macromolecular crystallography. (2023) Acta Crystallogr D Struct Biol. 79:449-461. doi: 10.1107/S2059798323003595. PMID: 37259835
Schöpp T, Prigozhin DM, Douse C, Kaji K, Cook AG, O'Carroll D. (2023) The DUF3715 domain has a conserved role in RNA-directed transposon silencing. RNA doi: 10.1261/rna.079693.123. PMID: 37433650
Haque N, Will A, Cook AG, Hogg JR (2023) A network of DZF protein controls alternative splicing regulation and fidelity. Nucl Acids Res. gkad351, https://doi.org/10.1093/nar/gkad351 PMID: 3714450
Watson JA, Pantier R, Jayachandran U, Chhatbar K, Alexander-Howden B, Kruusvee V, Prendecki M, Bird A, Cook AG (2023) Structure of SALL4 zinc finger domain reveals link between AT-rich DNA binding and Okihiro syndrome. Life Sci Alliance. 6(3):e202201588. doi: 10.26508/lsa.202201588. PMID: 3663504
2022
Deák G and Cook AG (2022) Missense Variants Reveal Functional Insights Into the Human ARID Family of Gene Regulators JMB 434(9):167529. doi: 10.1016/j.jmb.2022.167529 PMID: 35257783
Bayne RA, Jayachandran U, Kasprowicz A, Bresson S, Tollervey D, Wallace EWJ, Cook AG (2022) Yeast Ssd1 is a non-enzymatic member of the RNase II family with an alternative RNA recognition interface. Nucleic Acids Research 50(5)2923-2937, DOI: 10.1093/nar/gkab615. PMID: 34302485
2021
Pantier P, Chhatbar K, Quante T, Skourti-Stathaki K, Cholewa-Waclaw J, Alston G, Alexander-Howden B, Lee HY, Cook AG, Spruijt CG, Vermeulen M, Selfridge J, Bird A (2021) SALL4 controls cell fate in response to DNA base composition. Molecular Cell 2021 81:845–858.e8. doi: 10.1016/j.molcel.2020.11.046
Ballou ER, Cook AG, Wallace EWJ (2021) Repeated evolution of inactive pseudonucleases in a fungal branch of the Dis3/RNase II family of nucleases. Molecular Biology and Evolution 2021 38: 1837–1846. doi: 10.1093/molbev/msaa324
2020
Zoch A, Auchynnikava T, Berrens RV, Kabayama Y, Schöpp T, Heep M, Vasiliauskaitė L, Pérez-Rico YA, Cook AG, Shkumatava A, Rappsilber J, Allshire RC and O’Carroll D (2020) SPOCD1 is an essential executor of piRNA-directed de novo DNA methylation. Nature 584:635-639 doi: 10.1038/s41586-020-2557-5
2017
Kruusvee V§, Lyst MJ§, Taylor C, Tarnauskaitė Ž, Bird AP$ and Cook AG$ (2017) Structure of the MeCP2-TBLR1 complex reveals a molecular basis for Rett syndrome and related disorders. PNAS 114:E3243-E3250. doi: 10.1073/pnas.1700731114 $Joint corresponding, § joint first author
2016
Pre-40S ribosome biogenesis factor Tsr1 is an inactive structural mimic of translational GTPases. McCaughan UM, Jayachandran U, Shchepachev V, Chen ZA, Rappsilber J, Tollervey D, Cook AG. (2016) Nat Commun. 7:11789 doi: 10.1038/ncomms11789. PMID: 27250689
2015
Nuclear factor 90 uses an ADAR2-like binding mode to recognize specific bases in dsRNA. Jayachandran U, Grey H, Cook AG. Nucleic Acids Res. (2015) doi: 10.1093/nar/gkv1508 PMID:26712564
The NF45/NF90 Heterodimer Contributes to the Biogenesis of 60S Ribosomal Subunits and Influences Nucleolar Morphology. Wandrey F, Montellese C, Koos K, Badertscher L, Bammert L, Cook AG, Zemp I, Horvath P, Kutay U. Mol Cell Biol. (2015) 35:3491-503. doi: 10.1128/MCB.00306-15.
2014
Snapshots of pre-rRNA structural flexibility reveal eukaryotic 40S assembly dynamics at nucleotide resolution. Hector RD, Burlacu E, Aitken S, Le Bihan T, Tuijtel M, Zaplatina A, Cook AG, Granneman S. Nucleic Acids Res. (2014) 42:12138-54. doi: 10.1093/nar/gku815.
2012
NF45 dimerizes with NF90, Zfr and SPNR via a conserved domain that has a nucleotidyltranserase fold. Wolkowicz UM and Cook AG Nucleic Acids Research (2012) PMID: 22833610
2010
Nuclear export complexes in the frame. Cook AG, Conti E. Curr Opin Struct Biol. (2010) 20:247-52 Review.
Nuclear import mechanism of the EJC component Mago-Y14 revealed by structural studies of importin 13. Bono F, Cook AG, Grünwald M, Ebert J, Conti E. Mol Cell. (2010) 37:211-22.
2009
Structures of the tRNA export factor in the nuclear and cytosolic states. Cook AG, Fukuhara N, Jinek M, Conti E. Nature. (2009) 461:60-5.
2007
Structural biology of nucleocytoplasmic transport. Cook A, Bono F, Jinek M, Conti E. Annu Rev Biochem. (2007) 76:647-71. Review.
2005
The structure of the nuclear export receptor Cse1 in its cytosolic state reveals a closed conformation incompatible with cargo binding. Cook A, Fernandez E, Lindner D, Ebert J, Schlenstedt G, Conti E. Mol Cell. (2005) 18:355-67.
Structural characterization of Ca2+/CaM in complex with the phosphorylase kinase PhK5 peptide. Cook AG, Johnson LN, McDonnell JM. FEBS J. (2005) 272:1511-22.
The structure of cyclin E1/CDK2: implications for CDK2 activation and CDK2-independent roles. Honda R, Lowe ED, Dubinina E, Skamnaki V, Cook A, Brown NR, Johnson LN. EMBO J. (2005) 24:452-63
2002
Structural studies on phospho-CDK2/cyclin A bound to nitrate, a transition state analogue: implications for the protein kinase mechanism. Cook A, Lowe ED, Chrysina ED, Skamnaki VT, Oikonomakos NG, Johnson LN. Biochemistry (2002) 41:7301-11.
2000
Structure of human transthyretin complexed with bromophenols: a newmode of binding. Ghosh M, Meerts IA, Cook A, Bergman A, Brouwer A, Johnson LN. Acta Crystallographica D (2000) 56:1085:95