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Jalview Version 2—a multiple sequence alignment editor and analysis workbench
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Summary: Jalview Version 2 is a system for interactive WYSIWYG editing, analysis and annotation of multiple sequence alignments. Core features include keyboard and mouse-based editing, multiple views and alignment overviews, and linked structure display with Jmol. Jalview 2 is available in two forms: a lightweight Java applet for use in web applications, and a powerful desktop application that employs web services for sequence alignment, secondary structure prediction and the retrieval of alignments, sequences, annotation and structures from public databases and any DAS 1.53 compliant sequence or annotation server. Availability: The Jalview 2 Desktop application and JalviewLite applet are made freely available under the GPL, and can be downloaded from www.jalview.org Contact: g.j.barton@dundee.ac.uk
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Finn, R. D., Bateman, A., Clements, J., Coggill, P., Eberhardt, R. Y., Eddy, S. R., Heger, A., Hetherington, K., Holm, L., Mistry, J., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gkt1223 · Cited by 6,148
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Adzhubei, I., Jordan, D. M., & Sunyaev, S. R. (2013) · Current Protocols in Human Genetics · doi:10.1002/0471142905.hg0720s76 · Cited by 3,705
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De Cecco, M., Ito, T., Petrashen, A. P., Elias, A. E., Skvir, N. J., Criscione, S. W., Caligiana, A., Brocculi, G., Adney, E. M., Boeke, J. D., et al. (2019) · Nature · doi:10.1038/s41586-018-0784-9 · Cited by 1,255
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Bryant, P., Pozzati, G., & Elofsson, A. (2021) · doi:10.1101/2021.09.15.460468 · Cited by 1,022
Züst, R., Cervantes-Barragan, L., Habjan, M., Maier, R., Neuman, B. W., Ziebuhr, J., Szretter, K. J., Baker, S. C., Barchet, W., Diamond, M. S., et al. (2011) · Nature Immunology · doi:10.1038/ni.1979 · Cited by 811
Haplotype-resolved diverse human genomes and integrated analysis of structural variation
Ebert, P., Audano, P. A., Zhu, Q., Rodriguez-Martin, B., Porubsky, D., Bonder, M. J., Sulovari, A., Ebler, J., Zhou, W., Serra Mari, R., et al. (2021) · Science · doi:10.1126/science.abf7117 · Cited by 702
LINE-1 Retrotransposition Activity in Human Genomes
Beck, C. R., Collier, P., Macfarlane, C., Malig, M., Kidd, J. M., Eichler, E. E., Badge, R. M., & Moran, J. V. (2010) · Cell · doi:10.1016/j.cell.2010.05.021 · Cited by 632
PLEKHM1 Regulates Autophagosome-Lysosome Fusion through HOPS Complex and LC3/GABARAP Proteins
McEwan, D. G., Popovic, D., Gubas, A., Terawaki, S., Suzuki, H., Stadel, D., Coxon, F. P., Miranda de Stegmann, D., Bhogaraju, S., Maddi, K., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2014.11.006 · Cited by 563
cGAS senses long and HMGB/TFAM-bound U-turn DNA by forming protein-DNA ladders
Andreeva, L., Hiller, B., Kostrewa, D., Lässig, C., de Oliveira Mann, C. C., Jan Drexler, D., Maiser, A., Gaidt, M., Leonhardt, H., Hornung, V., et al. (2017) · Nature · doi:10.1038/nature23890 · Cited by 511
Cas1–Cas2 complex formation mediates spacer acquisition during CRISPR–Cas adaptive immunity
Nuñez, J. K., Kranzusch, P. J., Noeske, J., Wright, A. V., Davies, C. W., & Doudna, J. A. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2820 · Cited by 458
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Saxton, R. A., Knockenhauer, K. E., Wolfson, R. L., Chantranupong, L., Pacold, M. E., Wang, T., Schwartz, T. U., & Sabatini, D. M. (2016) · Science · doi:10.1126/science.aad2087 · Cited by 457
Evolution of human-specific neural SRGAP2 genes by incomplete segmental duplication
Dennis, M. Y., Nuttle, X., Sudmant, P. H., Antonacci, F., Graves, T. A., Nefedov, M., Rosenfeld, J. A., Sajjadian, S., Malig, M., Kotkiewicz, H., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.033 · Cited by 407
Structure of activated transcription complex Pol II–DSIF–PAF–SPT6
Vos, S. M., Farnung, L., Boehning, M., Wigge, C., Linden, A., Urlaub, H., & Cramer, P. (2018) · Nature · doi:10.1038/s41586-018-0440-4 · Cited by 432
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Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors
Yoshimura, S.-I., Gerondopoulos, A., Linford, A., Rigden, D. J., & Barr, F. A. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201008051 · Cited by 317
Auxin-related gene families in abiotic stress response in Sorghum bicolor
Wang, S., Bai, Y., Shen, C., Wu, Y., Zhang, S., Jiang, D., Guilfoyle, T. J., Chen, M., & Qi, Y. (2010) · Functional & Integrative Genomics · doi:10.1007/s10142-010-0174-3 · Cited by 297
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Uversky, V. N., Davé, V., Iakoucheva, L. M., Malaney, P., Metallo, S. J., Pathak, R. R., & Joerger, A. C. (2014) · Chemical Reviews · doi:10.1021/cr400713r · Cited by 288
In-cell architecture of an actively transcribing-translating expressome
O’Reilly, F. J., Xue, L., Graziadei, A., Sinn, L., Lenz, S., Tegunov, D., Blötz, C., Singh, N., Hagen, W. J. H., Cramer, P., et al. (2020) · Science · doi:10.1126/science.abb3758 · Cited by 284
The prdm family: expanding roles in stem cells and development
Hohenauer, T., & Moore, A. W. (2012) · Development · doi:10.1242/dev.070110 · Cited by 265
A heterochromatin-dependent transcription machinery drives piRNA expression
Andersen, P. R., Tirian, L., Vunjak, M., & Brennecke, J. (2017) · Nature · doi:10.1038/nature23482 · Cited by 280
Structure of the HIV-1 RNA packaging signal
Keane, S. C., Heng, X., Lu, K., Kharytonchyk, S., Ramakrishnan, V., Carter, G., Barton, S., Hosic, A., Florwick, A., Santos, J., et al. (2015) · Science · doi:10.1126/science.aaa9266 · Cited by 278
Structural mechanism of cGAS inhibition by the nucleosome
Pathare, G. R., Decout, A., Glück, S., Cavadini, S., Makasheva, K., Hovius, R., Kempf, G., Weiss, J., Kozicka, Z., Guey, B., et al. (2020) · Nature · doi:10.1038/s41586-020-2750-6 · Cited by 273
Structural basis for iron piracy by pathogenic Neisseria
Noinaj, N., Easley, N. C., Oke, M., Mizuno, N., Gumbart, J., Boura, E., Steere, A. N., Zak, O., Aisen, P., Tajkhorshid, E., et al. (2012) · Nature · doi:10.1038/nature10823 · Cited by 262
Pinto, R. M., Dragileva, E., Kirby, A., Lloret, A., Lopez, E., St. Claire, J., Panigrahi, G. B., Hou, C., Holloway, K., Gillis, T., et al. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003930 · Cited by 250
Steinegger, M., & Salzberg, S. L. (2020) · Genome Biology · doi:10.1186/s13059-020-02023-1 · Cited by 246
Sequencing Y Chromosomes Resolves Discrepancy in Time to Common Ancestor of Males Versus Females
Poznik, G. D., Henn, B. M., Yee, M.-C., Sliwerska, E., Euskirchen, G. M., Lin, A. A., Snyder, M., Quintana-Murci, L., Kidd, J. M., Underhill, P. A., et al. (2013) · Science · doi:10.1126/science.1237619 · Cited by 248
Bachman, P. M., Bolognesi, R., Moar, W. J., Mueller, G. M., Paradise, M. S., Ramaseshadri, P., Tan, J., Uffman, J. P., Warren, J., Wiggins, B. E., et al. (2013) · Transgenic Research · doi:10.1007/s11248-013-9716-5 · Cited by 242
Thompson, J. D., Linard, B., Lecompte, O., & Poch, O. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018093 · Cited by 242
Gene family innovation, conservation and loss on the animal stem lineage
(2018) · doi:10.7554/elife.34226 · Cited by 226
Marchais-Oberwinkler, S., Henn, C., Möller, G., Klein, T., Negri, M., Oster, A., Spadaro, A., Werth, R., Wetzel, M., Xu, K., et al. (2011) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2010.12.013 · Cited by 216
Transferrin receptor 1 is a reticulocyte-specific receptor for Plasmodium vivax
Gruszczyk, J., Kanjee, U., Chan, L.-J., Menant, S., Malleret, B., Lim, N. T. Y., Schmidt, C. Q., Mok, Y.-F., Lin, K.-M., Pearson, R. D., et al. (2018) · Science · doi:10.1126/science.aan1078 · Cited by 212
Molecular mechanism of APC/C activation by mitotic phosphorylation
Zhang, S., Chang, L., Alfieri, C., Zhang, Z., Yang, J., Maslen, S., Skehel, M., & Barford, D. (2016) · Nature · doi:10.1038/nature17973 · Cited by 203
Crystal structure of human stearoyl–coenzyme A desaturase in complex with substrate
Wang, H., Klein, M. G., Zou, H., Lane, W., Snell, G., Levin, I., Li, K., & Sang, B.-C. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3049 · Cited by 192
Activity-enhancing mutations in an E3 ubiquitin ligase identified by high-throughput mutagenesis
Starita, L. M., Pruneda, J. N., Lo, R. S., Fowler, D. M., Kim, H. J., Hiatt, J. B., Shendure, J., Brzovic, P. S., Fields, S., & Klevit, R. E. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1303309110 · Cited by 183
Anding, A. L., Wang, C., Chang, T.-K., Sliter, D. A., Powers, C. M., Hofmann, K., Youle, R. J., & Baehrecke, E. H. (2018) · Current Biology · doi:10.1016/j.cub.2017.11.064 · Cited by 172
Peroxisomal lactate dehydrogenase is generated by translational readthrough in mammals
Schueren, F., Lingner, T., George, R., Hofhuis, J., Dickel, C., Gärtner, J., & Thoms, S. (2014) · eLife · doi:10.7554/elife.03640 · Cited by 180
Marek, M., Kannan, S., Hauser, A.-T., Moraes Mourão, M., Caby, S., Cura, V., Stolfa, D. A., Schmidtkunz, K., Lancelot, J., Andrade, L., et al. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003645 · Cited by 173
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Zarrillo, S., Gaikwad, N., Lanaud, C., Powis, T., Viot, C., Lesur, I., Fouet, O., Argout, X., Guichoux, E., Salin, F., et al. (2018) · Nature Ecology & Evolution · doi:10.1038/s41559-018-0697-x · Cited by 173
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Grigg, J. C., Ukpabi, G., Gaudin, C. F. M., & Murphy, M. E. P. (2010) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2009.09.012 · Cited by 169
Haas, C. E., Rodionov, D. A., Kropat, J., Malasarn, D., Merchant, S. S., & de Crécy-Lagard, V. (2009) · BMC Genomics · doi:10.1186/1471-2164-10-470 · Cited by 159
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Vos, S. M., Farnung, L., Linden, A., Urlaub, H., & Cramer, P. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0437-1 · Cited by 160
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Loops Govern SH2 Domain Specificity by Controlling Access to Binding Pockets
Kaneko, T., Huang, H., Zhao, B., Li, L., Liu, H., Voss, C. K., Wu, C., Schiller, M. R., & Li, S. S.-C. (2010) · Science Signaling · doi:10.1126/scisignal.2000796 · Cited by 146
Weick, E.-M., Puno, M. R., Januszyk, K., Zinder, J. C., DiMattia, M. A., & Lima, C. D. (2018) · Cell · doi:10.1016/j.cell.2018.05.041 · Cited by 153
Mapping the Phosphoproteome of Influenza A and B Viruses by Mass Spectrometry
Hutchinson, E. C., Denham, E. M., Thomas, B., Trudgian, D. C., Hester, S. S., Ridlova, G., York, A., Turrell, L., & Fodor, E. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002993 · Cited by 151
Structure of the STRA6 receptor for retinol uptake
Chen, Y., Clarke, O. B., Kim, J., Stowe, S., Kim, Y.-K., Assur, Z., Cavalier, M., Godoy-Ruiz, R., von Alpen, D. C., Manzini, C., et al. (2016) · Science · doi:10.1126/science.aad8266 · Cited by 148
Regulation of lipid binding underlies the activation mechanism of class IA PI3-kinases
Hon, W.-C., Berndt, A., & Williams, R. L. (2012) · Oncogene · doi:10.1038/onc.2011.532 · Cited by 129
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Valsecchi, I., Dupres, V., Stephen-Victor, E., Guijarro, J., Gibbons, J., Beau, R., Bayry, J., Coppee, J.-Y., Lafont, F., Latgé, J.-P., et al. (2017) · Journal of Fungi · doi:10.3390/jof4010002 · Cited by 123
Mejhert, N., Kuruvilla, L., Gabriel, K. R., Elliott, S. D., Guie, M.-A., Wang, H., Lai, Z. W., Lane, E. A., Christiano, R., Danial, N. N., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.01.014 · Cited by 121
The social and structural architecture of the yeast protein interactome
Michaelis, A. C., Brunner, A.-D., Zwiebel, M., Meier, F., Strauss, M. T., Bludau, I., & Mann, M. (2023) · Nature · doi:10.1038/s41586-023-06739-5 · Cited by 119
Conformational buffering underlies functional selection in intrinsically disordered protein regions
González-Foutel, N. S., Glavina, J., Borcherds, W. M., Safranchik, M., Barrera-Vilarmau, S., Sagar, A., Estaña, A., Barozet, A., Garrone, N. A., Fernandez-Ballester, G., et al. (2022) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00811-w · Cited by 118
Structural basis for transcriptional start site control of HIV-1 RNA fate
Brown, J. D., Kharytonchyk, S., Chaudry, I., Iyer, A. S., Carter, H., Becker, G., Desai, Y., Glang, L., Choi, S. H., Singh, K., et al. (2020) · Science · doi:10.1126/science.aaz7959 · Cited by 118
Medin co-aggregates with vascular amyloid-β in Alzheimer’s disease
Wagner, J., Degenhardt, K., Veit, M., Louros, N., Konstantoulea, K., Skodras, A., Wild, K., Liu, P., Obermüller, U., Bansal, V., et al. (2022) · Nature · doi:10.1038/s41586-022-05440-3 · Cited by 110
Gunter, H. M., Fan, S., Xiong, F., Franchini, P., Fruciano, C., & Meyer, A. (2013) · Molecular Ecology · doi:10.1111/mec.12417 · Cited by 109
Beattie, S. R., Mark, K. M. K., Thammahong, A., Ries, L. N. A., Dhingra, S., Caffrey-Carr, A. K., Cheng, C., Black, C. C., Bowyer, P., Bromley, M. J., et al. (2017) · PLOS Pathogens · doi:10.1371/journal.ppat.1006340 · Cited by 103
Bravo Ruiz, G., Ross, Z. K., Gow, N. A. R., & Lorenz, A. (2020) · mSphere · doi:10.1128/msphere.00151-20 · Cited by 101
Neuropeptide repertoire and 3D anatomy of the ctenophore nervous system
Sachkova, M. Y., Nordmann, E.-L., Soto-Àngel, J. J., Meeda, Y., Górski, B., Naumann, B., Dondorp, D., Chatzigeorgiou, M., Kittelmann, M., & Burkhardt, P. (2021) · Current Biology · doi:10.1016/j.cub.2021.09.005 · Cited by 95
Carberry, C. A., Waters, S. M., Kenny, D. A., & Creevey, C. J. (2014) · Applied and Environmental Microbiology · doi:10.1128/aem.03131-13 · Cited by 100
Gómez Daglio, L., & Dawson, M. N. (2017) · Invertebrate Systematics · doi:10.1071/is16055 · Cited by 98
Hfq CLASH uncovers sRNA-target interaction networks linked to nutrient availability adaptation
Iosub, I. A., van Nues, R. W., McKellar, S. W., Nieken, K. J., Marchioretto, M., Sy, B., Tree, J. J., Viero, G., & Granneman, S. (2020) · eLife · doi:10.7554/elife.54655 · Cited by 98
Differential evolution of voltage-gated sodium channels in tetrapods and teleost fishes
Widmark, J., Sundstrom, G., Ocampo Daza, D., & Larhammar, D. (2011) · Molecular Biology and Evolution · doi:10.1093/molbev/msq257 · Cited by 88
ATP synthase evolution on a cross-braced dated tree of life
Mahendrarajah, T. A., Moody, E. R. R., Schrempf, D., Szánthó, L. L., Dombrowski, N., Davín, A. A., Pisani, D., Donoghue, P. C. J., Szöllősi, G. J., Williams, T. A., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42924-w · Cited by 86
Parsons, C., Stüeken, E. E., Rosen, C. J., Mateos, K., & Anderson, R. E. (2021) · Geobiology · doi:10.1111/gbi.12419 · Cited by 91
Evolutionary analysis of the most polymorphic gene family in falciparum malaria
Otto, T. D., Assefa, S. A., Böhme, U., Sanders, M. J., Kwiatkowski, D. P., Pf3k consortium, Berriman, M., & Newbold, C. (2019) · Wellcome Open Research · doi:10.12688/wellcomeopenres.15590.1 · Cited by 90
Design of highly functional genome editors by modeling the universe of CRISPR-Cas sequences
Ruffolo, J. A., Nayfach, S., Gallagher, J., Bhatnagar, A., Beazer, J., Hussain, R., Russ, J., Yip, J., Hill, E., Pacesa, M., et al. (2024) · doi:10.1101/2024.04.22.590591 · Cited by 90
MacKenzie, D. A., Tailford, L. E., Hemmings, A. M., & Juge, N. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.040907 · Cited by 88
Structural and mechanistic basis of the EMC-dependent biogenesis of distinct transmembrane clients
Miller-Vedam, L. E., Bräuning, B., Popova, K. D., Schirle Oakdale, N. T., Bonnar, J. L., Prabu, J. R., Boydston, E. A., Sevillano, N., Shurtleff, M. J., Stroud, R. M., et al. (2020) · eLife · doi:10.7554/elife.62611 · Cited by 87
Kim, J.-H., Dilthey, A. T., Nagaraja, R., Lee, H.-S., Koren, S., Dudekula, D., Wood III, W. H., Piao, Y., Ogurtsov, A. Y., Utani, K., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky442 · Cited by 86
Gupta, M., Azumaya, C. M., Moritz, M., Pourmal, S., Diallo, A., Merz, G. E., Jang, G., Bouhaddou, M., Fossati, A., Brilot, A. F., et al. (2021) · doi:10.1101/2021.05.10.443524 · Cited by 89
SARS-CoV-2 Nsp16 activation mechanism and a cryptic pocket with pan-coronavirus antiviral potential
Vithani, N., Ward, M. D., Zimmerman, M. I., Novak, B., Borowsky, J. H., Singh, S., & Bowman, G. R. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.03.024 · Cited by 84
Chen, Z., Shiozaki, M., Haas, K. M., Skinner, W. M., Zhao, S., Guo, C., Polacco, B. J., Yu, Z., Krogan, N. J., Lishko, P. V., et al. (2023) · Cell · doi:10.1016/j.cell.2023.09.017 · Cited by 82
Dietary- and host-derived metabolites are used by diverse gut bacteria for anaerobic respiration
Little, A. S., Younker, I. T., Schechter, M. S., Bernardino, P. N., Méheust, R., Stemczynski, J., Scorza, K., Mullowney, M. W., Sharan, D., Waligurski, E., et al. (2024) · Nature Microbiology · doi:10.1038/s41564-023-01560-2 · Cited by 80
pico‐ PLAZA , a genome database of microbial photosynthetic eukaryotes
Vandepoele, K., Van Bel, M., Richard, G., Van Landeghem, S., Verhelst, B., Moreau, H., Van de Peer, Y., Grimsley, N., & Piganeau, G. (2013) · Environmental Microbiology · doi:10.1111/1462-2920.12174 · Cited by 76
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Deneke, V. E., Blaha, A., Lu, Y., Suwita, J. P., Draper, J. M., Phan, C. S., Panser, K., Schleiffer, A., Jacob, L., Humer, T., et al. (2024) · Cell · doi:10.1016/j.cell.2024.09.035 · Cited by 78
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Noddings, C. M., Johnson, J. L., & Agard, D. A. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01128-y · Cited by 75
Xu, F., Jerlström-Hultqvist, J., Einarsson, E., Ástvaldsson, Á., Svärd, S. G., & Andersson, J. O. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004053 · Cited by 74
Schou, K. B., Mogensen, J. B., Morthorst, S. K., Nielsen, B. S., Aleliunaite, A., Serra-Marques, A., Fürstenberg, N., Saunier, S., Bizet, A. A., Veland, I. R., et al. (2017) · Nature Communications · doi:10.1038/ncomms14177 · Cited by 72
Specificity of Staphyloferrin B Recognition by the SirA Receptor from Staphylococcus aureus
Grigg, J. C., Cheung, J., Heinrichs, D. E., & Murphy, M. E. P. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.172924 · Cited by 71
New genomic data and analyses challenge the traditional vision of animal epithelium evolution
Belahbib, H., Renard, E., Santini, S., Jourda, C., Claverie, J.-M., Borchiellini, C., & Le Bivic, A. (2018) · BMC Genomics · doi:10.1186/s12864-018-4715-9 · Cited by 71
Zhang, D., Zhang, J., Kalimuthu, S., Liu, J., Song, Z.-M., He, B.-B., Cai, P., Zhong, Z., Feng, C., Neelakantan, P., et al. (2023) · Microbiome · doi:10.1186/s40168-023-01540-y · Cited by 72
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Metadata
- Authors
- Waterhouse, A. M., Procter, J. B., Martin, D. M. A., Clamp, M., & Barton, G. J.
- Venue
- Bioinformatics
- Publisher
- Oxford University Press (OUP)
- Published
- 2009-01-16
- Volume
- 25
- Issue
- 9
- Pages
- 1189-1191
- ISSN
- 1367-4803 (ISSN-L)
- 1367-4811
- OpenAlex
- W2120772351
- Cited by
- 10,235
- References
- 0
- FWCI
- 110.90
- Type
- journal article
- Language
- en
- Open access
- hybrid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.