Publications describing MASSIF-1:

Svensson, O., Monaco, S., Popov, A. N., Nurizzo, D. & Bowler, M. W. (2015). The fully automatic characterization and data collection from crystals of biological macromolecules, Acta Cryst. D71, 1757-1767, http://dx.doi.org/10.1107/S1399004715011918

Bowler M.W., Nurizzo, D., Barrett, R., Beteva, A., Bodin, M., Caserotto, H., Delageniere, S., Dobias, F., Flot, D., Giraud, T., Guichard, N., Guijarro, M., Lentini, M., Leonard, G., McSweeney, S., Oskarsson, M., Schmidt, W., Snigirev, A., von Stetten, D., Surr, J., Svensson, O., Theveneau, P. and Mueller-Dieckmann, C. (2015) MASSIF-1: A beamline dedicated to the fully automatic characterisation and data collection from crystals of biological macromolecules J. Sync. Rad. 22 1540-1547 http://dx.doi.org/10.1107/S1600577515016604.

Bowler, M.W., Svensson, O. & Nurizzo, D. (2016): Fully automatic macromolecular crystallography: the impact of MASSIF-1 on the optimum acquisition and quality of data, Cryst. Rev., 22, 233–249 http://dx.doi.org/10.1080/0889311X.2016.1155050.

Nurizzo, D., Bowler M.W., Caserotto, H., Dobias, F., Giraud, T., Surr, J., Guichard, N., Papp, G., Guijarro, M., Mueller-Dieckmann, C., Flot, D., McSweeney, S. Cipriani, F, Theveneau, P. and Leonard, G. (2016) RoboDiff: combining a sample changer and goniometer for highly automated macromolecular crystallography experiments Acta Cryst D 72, 966-975, http://dx.doi.org/10.1107/S205979831601158X.

 

 

Publications that used data collected at MASSIF-1:

2017

65. Pflug, A., Gaudon, S., Resa-Infante, P., Lethier, M., Reich, S., Schulze, W. M. & Cusack, S. (2017). Capped RNA primer binding to influenza polymerase and implications for the mechanism of cap-binding inhibitors, Nucleic Acids Research gkx1210-gkx1210. https://doi.org/10.1093/nar/gkx1210

64. Gavory, G., O'Dowd, C. R., Helm, M. D., Flasz, J., Arkoudis, E., Dossang, A., Hughes, C., Cassidy, E., McClelland, K., Odrzywol, E., Page, N., Barker, O., Miel, H. & Harrison, T. (2017). Discovery and characterization of highly potent and selective allosteric USP7 inhibitors, Nature Chemical Biology. https://doi.org/10.1038/nchembio.2528

63. Naschberger, A., Orry, A., Lechner, S., Bowler, M.W., Nurizzo, D., Novokmet, M., Keller, M.A., Oemer, G., Seppi, D., Haslbeck, M., Pansi, K., Dieplinger, H. and Rupp, B. (2017) Structural evidence for a role of the multifunctional human glycoprotein afamin in Wnt transport Structure https://doi.org/10.1016/j.str.2017.10.006

62. Wouter Elings, Raffaella Tassoni, Steven A. van der Schoot, Wendy Luu, Josef P. Kynast, Lin Dai, Anneloes J. Blok, Monika Timmer, Bogdan I. Florea, Navraj S. Pannu, and Marcellus Ubbink (2017) Phosphate Promotes the Recovery of Mycobacterium tuberculosis β-Lactamase from Clavulanic Acid Inhibition Biochemistry DOI: 10.1021/acs.biochem.7b00556

61. Sulzenbacher G, Roig-Zamboni V, Lebrun R, Guérardel Y, Murat D, Mansuelle P, Yamakawa N, Quian XX, Vincentelli R, Bourne Y, Wu LF, Alberto F. Glycosylate and move! The glycosyltransferase Maf is involved in bacterial flagella formation. Environ Microbiol. 2017  doi:10.1111/1462-2920.13975

60. Morana Dulic, Nevena Cvetesic, Igor Zivkovic, Andrés Palencia, Stephen Cusack, Branimir Bertosa, Ita Gruic-Sovulj, Kinetic Origin of Substrate Specificity in Post-Transfer Editing by Leucyl-tRNA Synthetase, Journal of Molecular Biology, 2017, https://doi.org/10.1016/j.jmb.2017.10.024

59. Pinotsis, N. and Waksman, G. (2017), Crystal structure of the Legionella pneumophila Lpg2936 in complex with the cofactor S-adenosyl-L-methionine reveals novel insights into the mechanism of RsmE family methyltransferases. Protein Science. http://dx.doi.org/10.1002/pro.3305

58. Schulze, W. M. & Cusack, S. (2017). Structural basis for mutually exclusive co-transcriptional nuclear cap-binding complexes with either NELF-E or ARS2. Nature Communications 8,

57. Koromyslova AD, Hansman GS (2017) Nanobodies targeting norovirus capsid reveal functional epitopes and potential mechanisms of neutralization. PLoS Pathog 13  e1006636. https://doi.org/10.1371/journal.ppat.1006636

56. Ampaw, A., Carroll, M., von Velsen, J., Bhattasali, D., Cohen, A., Bowler, M.W. and Jakeman, D.L. Observing enzyme ternary transition state analogue complexes by 19F NMR spectroscopy (2017) Chemical Science, 10.1039/C7SC04204C

55. Drexler, D. J., Müller, M., Rojas-Cordova, C. A., Bandera, A. M. & Witte, G. Structural and Biophysical Analysis of the Soluble DHH/DHHA1-Type Phosphodiesterase TM1595 from Thermotoga maritima, Structure. http://dx.doi.org/10.1016/j.str.2017.10.001

54. Chu, Yindi, Tu, Tao, Penttinen, Leena, Xue, Xianli, Wang, Xiaoyu, Yi, Zhuolin, Gong, Li, Rouvinen, Juha, Luo, Huiying, Hakulinen, Nina, Yao, Bin and Su, Xiaoyun (2017) Insights into the roles of non-catalytic residues in the active site of a GH10 xylanase with activity on cellulose J. Biol. Chem 10.1074/jbc.M117.807768

53. Francesca Magnani, Simone Nenci, Elisa Millana Fananas, Marta Ceccon, Elvira Romero, Marco W. Fraaije, and Andrea Mattevi (2017) Crystal structures and atomic model of NADPH oxidase Proceedings of the National Academy of Sciences 114, 6764-6769

52. Polino, Mariella, Carvalho, Ana Luı́sa, Juknaitė, Lina Portugal, Carla A. M., Coelhoso, Isabel M. Romão, Maria João, Crespo, João G. Ion-Exchange Membranes for Stable Derivatization of Protein Crystals Crystal Growth & Design 2017 17, 4563-4572

51. Sorigué, D., Légeret, B., Cuiné, S., Blangy, S., Moulin, S., Billon, E., Richaud, P., Brugière, S., Couté, Y., Nurizzo, D., Müller, P., Brettel, K., Pignol, D., Arnoux, P., Li-Beisson, Y., Peltier, G. & Beisson, F. (2017). An algal photoenzyme converts fatty acids to hydrocarbons, Science 357, 903-907.

50. Lobner, E., Humm, A.-S., Mlynek, G., Kubinger, K., Kitzmüller, M., Traxlmayr, M. W., Djinović-Carugo, K. & Obinger, C. (2017). Two-Faced Fcab Prevents Polymerization with VEGF and Reveals Thermodynamics and the 2.15 Å Crystal Structure of the Complex, mAbs . 10.1080/19420862.2017.136482

49. Roversi, P., Marti, L., Caputo, A. T., Alonzi, D. S., Hill, J. C., Dent, K. C., Kumar, A., Levasseur, M. D., Lia, A., Waksman, T., Basu, S., Soto Albrecht, Y., Qian, K., McIvor, J. P., Lipp, C. B., Siliqi, D., Vasiljević, S., Mohammed, S., Lukacik, P., Walsh, M. A., Santino, A. & Zitzmann, N. (2017). Interdomain conformational flexibility underpins the activity of UGGT, the eukaryotic glycoprotein secretion checkpoint, Proceedings of the National Academy of Sciences. 10.1073/pnas.1703682114

48. Hiruma, Y., Koch, A., Hazraty, N., Tsakou, F., Medema, R. H., Joosten, R. P. & Perrakis, A. (2017). Understanding inhibitor resistance in Mps1 kinase through novel biophysical assays and structures, J. Biol. Chem. 10.1074/jbc.M117.783555

47. Risso, V. A. et al. De novo active sites for resurrected Precambrian enzymes. (2017). Nature Communications. 8, 16113 http://dx.doi.org/10.1038/ncomms16113 

46. Perveen, S., Rashid, N., Tang, X.-F., Imanaka, T. & Papageorgiou, A. C. (2017) Anthranilate phosphoribosyltransferase from the hyperthermophillic archaeon Thermococcus kodakarensis shows maximum activity with zinc and forms a unique dimeric structure, FEBS Open Bio

45. Jonnalagadda, S.V.R., Ornithopoulou, E., Orr, A., Mossou, E., Forsyth, T., Mitchell, E.P., Bowler, M.W., Mitraki, A.  and Tamamis, P. (2017) Computational Design of Amyloid Self-Assembling Peptides Bearing Aromatic Residues and the Cell Adhesive Motif Arg-Gly-Asp Mol. Syst. Des. Eng., 10.1039/C7ME00016B

44. Lai, X., Wichers, H. J., Soler-Lopez, M. & Dijkstra, B. W. (2017) Structure of Human Tyrosinase Related Protein 1 Reveals a Binuclear Zinc Active Site Important for Melanogenesis, Angewandte Chemie International Edition

43. Handramouli, S., Malito, E., Nguyen, T., Luisi, K., Donnarumma, D., Xing, Y., Norais, N., Yu, D. and Carfi, A. (2017) Structural basis for potent antibody-mediated neutralization of human cytomegalovirus, Science Immunology, 2, 10.1126/sciimmunol.aan1457

42. Hutchinson, J. P., Rowland, P., Taylor, M. R. D., Christodoulou, E. M., Haslam, C., Hobbs, C. I., Holmes, D. S., Homes, P., Liddle, J., Mole, D. J., Uings, I., Walker, A. L., Webster, S. P., Mowat, C. G. & Chung, C.-w. (2017). Structural and mechanistic basis of differentiated inhibitors of the acute pancreatitis target kynurenine-3-monooxygenase, Nature communications 8, 15827.

41. Bezerra, G. A., Ohara-Nemoto, Y., Cornaciu, I., Fedosyuk, S., Hoffmann, G., Round, A., Márquez, J. A., Nemoto, T. K. & Djinović-Carugo, K. (2017). Bacterial protease uses distinct thermodynamic signatures for substrate recognition, Scientific Reports 7, 2848.

40. Blanchet, G., Alili, D., Protte, A., Upert, G., Gilles, N., Tepshi, L., Stura, E. A., Mourier, G. & Servent, D. (2017). Ancestral protein resurrection and engineering opportunities of the mamba aminergic toxins, Scientific Reports 7, 2701.

39. Mietton, F., Ferri, E., Champleboux, M., Zala, N., Maubon, D., Zhou, Y., Harbut, M., Spittler, D., Garnaud, C., Courçon, M., Chauvel, M., d’Enfert, C., Kashemirov, B. A., Hull, M., Cornet, M., McKenna, C. E., Govin, J. & Petosa, C. (2017). Selective BET bromodomain inhibition as an antifungal therapeutic strategy, Nature communications 8, 15482.

38. Uitdehaag, J. C. M., de Man, J., Willemsen-Seegers, N., Prinsen, M. B. W., Libouban, M. A. A., Sterrenburg, J. G., de Wit, J. J. P., de Vetter, J. R. F., de Roos, J. A. D. M., Buijsman, R. C. & Zaman, G. J. R. (2017). Target Residence Time-Guided Optimization on TTK Kinase Results in Inhibitors with Potent Anti-Proliferative Activity, Journal of Molecular Biology 429, 2211-2230.

37. Pellegrini, E., Signor, L., Singh, S., Boeri Erba, E. & Cusack, S. (2017). Structures of the inactive and active states of RIP2 kinase inform on the mechanism of activation, PLOS ONE 12, e0177161

36. Frandsen, K. E. H., Poulsen, J.-C. N., Tandrup, T. & Lo Leggio, L. Unliganded and substrate bound structures of the cellooligosaccharide active lytic polysaccharide monooxygenase LsAA9A at low pH, Carbohydrate Research.

35. Carboni, F., Adamo, R., Fabbrini, M., De Ricco, R., Cattaneo, V., Brogioni, B., Veggi, D., Pinto, V., Passalacqua, I., Oldrini, D., Rappuoli, R., Malito, E., Margarit, I. y. R. & Berti, F. (2017). Structure of a protective epitope of group B Streptococcus type III capsular polysaccharide, Proceedings of the National Academy of Sciences 114, 5017-5022.

34. Skjoldager, N., Blanner Bang, M., Rykær, M., Björnberg, O., Davies, M. J., Svensson, B., Harris, P. & Hägglund, P. (2017). The structure of Lactococcus lactis thioredoxin reductase reveals molecular features of photo-oxidative damage, Scientific Reports 7, 46282.

33. Sander, B., Xu, W., Eilers, M., Popov, N. & Lorenz, S. (2017). A conformational switch regulates the ubiquitin ligase HUWE1, eLife 6, e21036.

32. Cao, L., Cantos-Fernandes, S. & Gigant, B. (2017). The structural switch of nucleotide-free kinesin, Scientific Reports 7, 42558.

31. Fernández, I., Cornaciu, I., Carrica, M. d. C., Uchikawa, E., Hoffmann, G., Sieira, R., Márquez, J. A. & Goldbaum, F. A. (2017). Three-Dimensional Structure of Full-Length NtrX, an Unusual Member of the NtrC Family of Response Regulators, Journal of Molecular Biology 429, 1192-1212.

30. Cheeseman, M. D., Chessum, N. E. A., Rye, C. S., Pasqua, A. E., Tucker, M. J., Wilding, B., Evans, L. E., Lepri, S., Richards, M., Sharp, S. Y., Ali, S., Rowlands, M., O’Fee, L., Miah, A., Hayes, A., Henley, A. T., Powers, M., te Poele, R., De Billy, E., Pellegrino, L., Raynaud, F., Burke, R., van Montfort, R. L. M., Eccles, S. A., Workman, P. & Jones, K. (2017). Discovery of a Chemical Probe Bisamide (CCT251236): An Orally Bioavailable Efficacious Pirin Ligand from a Heat Shock Transcription Factor 1 (HSF1) Phenotypic Screen, Journal of Medicinal Chemistry 60, 180-201.

29. Košak, U., Knez, D., Coquelle, N., Brus, B., Pišlar, A., Nachon, F., Brazzolotto, X., Kos, J., Colletier, J.-P. & Gobec, S. (2017). N-Propargylpiperidines with naphthalene-2-carboxamide or naphthalene-2-sulfonamide moieties: Potential multifunctional anti-Alzheimer’s agents, Bioorganic & Medicinal Chemistry 25, 633-645.

28. Kristariyanto, Y. A., Abdul Rehman, S. A., Weidlich, S., Knebel, A. & Kulathu, Y. (2017). A single MIU motif of MINDY‐1 recognizes K48‐linked polyubiquitin chains, EMBO reports 18, 392-402.

27. Na, Z., Yeo, S. P., Bharath, S. R., Bowler, M. W., Balikci, E., Wang, C.-I. & Song, H. (2017). Structural basis for blocking PD-1-mediated immune suppression by therapeutic antibody pembrolizumab, Cell Res 27, 147-150.

 

2016

26. Varshney, D., Petit, A.-P., Bueren-Calabuig, J. A., Jansen, C., Fletcher, D. A., Peggie, M., Weidlich, S., Scullion, P., Pisliakov, A. V. & Cowling, V. H. (2016). Molecular basis of RNA guanine-7 methyltransferase (RNMT) activation by RAM, Nucleic Acids Research 44, 10423-10436.

25. Fedosyuk, S., Bezerra, G. A., Radakovics, K., Smith, T. K., Sammito, M., Bobik, N., Round, A., Ten Eyck, L. F., Djinović-Carugo, K., Usón, I. & Skern, T. (2016). Vaccinia Virus Immunomodulator A46: A Lipid and Protein-Binding Scaffold for Sequestering Host TIR-Domain Proteins, PLOS Pathogens 12, e1006079.

24. Perveen, S., Rashid, N. & Papageorgiou, A. C. (2016). Crystal structure of a phosphoribosyl anthranilate isomerase from the hyperthermophilic archaeon Thermococcus kodakaraensis, Acta Crystallographica Section F 72, 804-812.

23. Gógl, G., Alexa, A., Kiss, B., Katona, G., Kovács, M., Bodor, A., Reményi, A. & Nyitray, L. (2016). Structural Basis of Ribosomal S6 Kinase 1 (RSK1) Inhibition by S100B Protein: MODULATION OF THE EXTRACELLULAR SIGNAL-REGULATED KINASE (ERK) SIGNALING CASCADE IN A CALCIUM-DEPENDENT WAY, Journal of Biological Chemistry 291, 11-27.

22. Altegoer, F., Rensing, S. A. & Bange, G. (2016). Structural basis for the CsrA-dependent modulation of translation initiation by an ancient regulatory protein, Proceedings of the National Academy of Sciences 113, 10168-10173

21. Volbeda, A., Darnault, C., Renoux, O., Reichmann, D., Amara, P., Ollagnier de Choudens, S. & Fontecilla-Camps, J. C. (2016). Crystal Structures of Quinolinate Synthase in Complex with a Substrate Analogue, the Condensation Intermediate, and Substrate-Derived Product, Journal of the American Chemical Society 138, 11802-11809

20. Kristensen, O., Kristensen, Lise B., Møllerud, S., Frydenvang, K., Pickering, Darryl S. & Kastrup, Jette S. (2016). The Structure of a High-Affinity Kainate Receptor: GluK4 Ligand-Binding Domain Crystallized with Kainate, Structure 24, 1582-1589.

19. Nuti, E., Cuffaro, D., D'Andrea, F., Rosalia, L., Tepshi, L., Fabbi, M., Carbotti, G., Ferrini, S., Santamaria, S., Camodeca, C., Ciccone, L., Orlandini, E., Nencetti, S., Stura, E. A., Dive, V. & Rossello, A. (2016). Sugar-Based Arylsulfonamide Carboxylates as Selective and Water-Soluble Matrix Metalloproteinase-12 Inhibitors, ChemMedChem 11, 1626-1637.

18. Borsari, C., Luciani, R., Pozzi, C., Poehner, I., Henrich, S., Trande, M., Cordeiro-da-Silva, A., Santarem, N., Baptista, C., Tait, A., Di Pisa, F., Dello Iacono, L., Landi, G., Gul, S., Wolf, M., Kuzikov, M., Ellinger, B., Reinshagen, J., Witt, G., Gribbon, P., Kohler, M., Keminer, O., Behrens, B., Costantino, L., Tejera Nevado, P., Bifeld, E., Eick, J., Clos, J., Torrado, J., Jiménez-Antón, M. D., Corral, M. J., Alunda, J. M., Pellati, F., Wade, R. C., Ferrari, S., Mangani, S. & Costi, M. P. (2016). Profiling of Flavonol Derivatives for the Development of Antitrypanosomatidic Drugs, Journal of Medicinal Chemistry 59, 7598-7616.

17. Caputo, A. T., Alonzi, D. S., Marti, L., Reca, I.-B., Kiappes, J. L., Struwe, W. B., Cross, A., Basu, S., Lowe, E. D., Darlot, B., Santino, A., Roversi, P. & Zitzmann, N. (2016). Structures of mammalian ER α-glucosidase II capture the binding modes of broad-spectrum iminosugar antivirals, Proceedings of the National Academy of Sciences 113, E4630-E4638.

16. Hafstrand, I., Doorduijn, E.M., Duru, A.D., Buratto, J., Oliveira, C.C., Sandalova, T., van Hall, T., and Achour, A. (2016). The MHC Class I Cancer-Associated Neoepitope Trh4 Linked with Impaired Peptide Processing Induces a Unique Noncanonical TCR Conformer. The Journal of Immunology 196, 2327-2334.

15. Siitonen V, Selvaraj B, Niiranen L, Lindqvist Y, Schneider G, Metsä-Ketelä M (2016) Divergent non-heme iron enzymes in the nogalamycin biosynthetic pathway. Proc. Natl. Acad. Sci USA 113, 5251-5256

14. Zander U, Hoffmann G, Cornaciu I, Marquette J-P, Papp G, Landret C, Seroul G, Sinoir J, Rower M, Felisaz F, Rodriguez-Puente S, Mariaule V, Murphy P, Mathieu M, Cipriani F, Marquez JA (2016) Automated harvesting and processing of protein crystals through laser photoablation. Acta Cryst. D72, 454-466

13. Heggelund JE, Burschowsky D, Bjørnestad VA, Hodnik V, Anderluh G, Krengel U (2016) High-Resolution Crystal Structures Elucidate the Molecular Basis of Cholera Blood Group Dependence. PLoS Pathogens 12 : e1005567. doi:10.1371/journal.ppat.1005567

12. Thierry E, Guilligay D, Kosinski J, Bock T, Gaudon S, Round A, Pflug A, Hengrung N, El Omari K, Baudin F, Hart DJ, Beck M, Cusack S (2016). Influenza Polymerase Can Adopt an Alternative Configuration Involving a Radical Repacking of PB2 Domains, Molecular Cell. 61, 125-37, doi:10.1016/j.molcel.2015.11.016

11. Muir K, Kschonsak M, Li Y, Metz J, Haering Christian H, Panne D (2016) Structure of the Pds5-Scc1 Complex and Implications for Cohesin Function. Cell reports 14, 2116-2126

10. Neudegger T, Verghese J, Hayer-Hart M, Hartl FU, Bracher A (2016). Structure of human heat-shock transcription factor 1 in complex with DNA, Nature Structural & Molecular Biology, doi:10.1038/nsmb.3149

9. Forsberg Z, Nelson CE, Dalhus B, Mekasha S, Loose JS, Crouch LI, Rohr AK, Gardner JG, Eijsink VG, Vaaje-Kolstad G (2016) Structural and Functional Analysis of a Lytic Polysaccharide Monooxygenase Important for Efficient Utilization of Chitin in Cellvibrio japonicus. J. Biol. Chem 291, 7300-7312

8. Frandsen KEH, Simmons TJ, Dupree P, Poulsen J-CN, Hemsworth GR, Ciano L, Johnston EM, Tovborg M, Johansen KS, von Freiesleben P, Marmuse L, Fort S, Cottaz S, Driguez H, Henrissat B, Lenfant N, Tuna F, Baldansuren A, Davies GJ, Lo Leggio L, Walton PH (2016) The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases. Nature Chemical Biology 12, 298-303

7. Camara-Artigas A, Plaza-Garrido M, Martinez-Rodriguez S, Bacarizo J (2016) New crystal form of human ubiquitin in the presence of magnesium. Acta Cryst. F72, 29-35

6. Papageorgiou N, Lichiere J, Baklouti A, Ferron F, Sevajol M, Canard B, Coutard B (2016) Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering. Acta Cryst. D72, 192-202

5. Mourier G, Salinas M, Kessler P, Stura EA, Leblanc M, Tepshi L, Besson T, Diochot S, Baron A, Douguet D, Lingueglia E, Servent D (2016) Mambalgin-1 Pain-relieving Peptide, Stepwise Solid-phase Synthesis, Crystal Structure, and Functional Domain for Acid-sensing Ion Channel 1a Inhibition.  J. Biol. Chem 291, 2616-2629

 

2015

4. Marton, Z., Guillon, R., Krimm, I., Preeti, Rahimova, R., Egron, D., Jordheim, L.P., Aghajari, N., Dumontet, C., Périgaud, C., et al. (2015). Identification of Noncompetitive Inhibitors of Cytosolic 5′-Nucleotidase II Using a Fragment-Based Approach. Journal of Medicinal Chemistry 58, 9680-9696.

3. Koromyslova AD, Leuthold MM, Bowler MW, Hansman GS. (2015) The sweet quartet: Binding of fucose to the norovirus capsid. Virology 483, 203-208. doi: 10.1016/j.virol.2015.04.006

2. Pathak S, Alonso J, Schimpl M, Rafie K, Blair DE, Borodkin VS, Schuttelkopf AW, Albarbarawi O, van Aalten DMF (2015) The active site of O-GlcNAc transferase imposes constraints on substrate sequence. Nature Structural & Molecular Biology 22, 744-750

1. Kharde S, Calviño FR, Gumiero A, Wild K, Sinning I (2015). The structure of Rpf2-Rrs1 explains its role in ribosome biogenesis, Nucleic Acids Res. 43, 7083–95, doi:10.1093/nar/gkv640