The Phyre2 web portal for protein modeling, prediction and analysis

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

Altschul, S. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.17.3389 · Cited by 73,302

A method and server for predicting damaging missense mutations.

Adzhubei, I. A., Schmidt, S., Peshkin, L., Ramensky, V. E., Gerasimova, A., Bork, P., Kondrashov, A. S., & Sunyaev, S. R. (2010) · Nature Methods · doi:10.1038/nmeth0410-248 · Cited by 13,194

The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling

Arnold, K., Bordoli, L., Kopp, J., & Schwede, T. F. (2005) · Bioinformatics · doi:10.1093/bioinformatics/bti770 · Cited by 7,031

I-TASSER: a unified platform for automated protein structure and function prediction

Roy, A., Küçükural, A., & Zhang, Y. (2010) · Nature Protocols · doi:10.1038/nprot.2010.5 · Cited by 6,212

Protein secondary structure prediction based on position-specific scoring matrices 1 1Edited by G. Von Heijne

Jones, D. T. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3091 · Cited by 5,522

Protein structure prediction on the Web: a case study using the Phyre server

Kelley, L. A., & Sternberg, M. J. E. (2009) · Nature Protocols · doi:10.1038/nprot.2009.2 · Cited by 4,154

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

Davis, I., Leaver‐Fay, A., Chen, V. B., Block, J. N., Kapral, G. J., Wang, X., Murray, L. W., Arendall, W. B., Snoeyink, J. S., Richardson, J. S., et al. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm216 · Cited by 3,918

Protein homology detection by HMM–HMM comparison

Söding, J. (2004) · Bioinformatics · doi:10.1093/bioinformatics/bti125 · Cited by 2,459

SIFT web server: predicting effects of amino acid substitutions on proteins

Sim, N.-L., Kumar, P. N., Hu, J., Henikoff, S., Schneider, G., & Ng, P. C. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks539 · Cited by 2,419

HHblits: lightning-fast iterative protein sequence searching by HMM-HMM alignment

Remmert, M., Biegert, A., Hauser, A., & Söding, J. (2012) · Nature Methods · doi:10.1038/nmeth.1818 · Cited by 2,288

A Completely Reimplemented MPI Bioinformatics Toolkit with a New HHpred Server at its Core

Zimmermann, L., Stephens, A., Nam, S.-Z., Rau, D., Kübler, J., Lozajic, M., Gabler, F., Söding, J., Lupas, A. N., & Alva, V. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.12.007 · Cited by 2,522

Potent Neutralizing Antibodies against SARS-CoV-2 Identified by High-Throughput Single-Cell Sequencing of Convalescent Patients’ B Cells

Cao, Y., Su, B., Guo, X., Sun, W., Deng, Y., Bao, L., Zhu, Q., Zhang, X., Zheng, Y., Geng, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.025 · Cited by 1,188

The PSIPRED Protein Analysis Workbench: 20 years on

Buchan, D. W. A., & Jones, D. T. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz297 · Cited by 1,390

Systematic discovery of antiphage defense systems in the microbial pangenome

Doron, S., Melamed, S., Ofir, G., Leavitt, A., Lopatina, A., Keren, M., Amitai, G., & Sorek, R. (2018) · Science · doi:10.1126/science.aar4120 · Cited by 1,242

Asgard archaea illuminate the origin of eukaryotic cellular complexity

Zaremba-Niedzwiedzka, K., Caceres, E. F., Saw, J. H., Bäckström, D., Juzokaite, L., Vancaester, E., Seitz, K. W., Anantharaman, K., Starnawski, P., Kjeldsen, K. U., et al. (2017) · Nature · doi:10.1038/nature21031 · Cited by 1,226

DRAM for distilling microbial metabolism to automate the curation of microbiome function

Shaffer, M., Borton, M., McGivern, B. B., Zayed, A. A., Rosa, S. L. L., Solden, L., Liu, P., Narrowe, A. B., Rodríguez-Ramos, J. A., Bolduc, B., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa621 · Cited by 1,163

Coarse-Grained Protein Models and Their Applications

Kmiecik, S., Gront, D., Koliński, M., Wieteska, Ł., Badaczewska-Dawid, A. E., & Koliński, A. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00163 · Cited by 1,113

Accurate De Novo Prediction of Protein Contact Map by Ultra-Deep Learning Model

Wang, S., Sun, S., Li, Z., Zhang, R., & Xu, J. (2017) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1005324 · Cited by 931

RNA-Induced Conformational Switching and Clustering of G3BP Drive Stress Granule Assembly by Condensation

Guillén‐Boixet, J., Kopach, A., Holehouse, A. S., Wittmann, S., Jahnel, M., Schlüßler, R., Kim, K., Trussina, I. R. E. A., Wang, J., Matějů, D., et al. (2020) · Cell · doi:10.1016/j.cell.2020.03.049 · Cited by 869

Atomic structures of respiratory complex III2, complex IV, and supercomplex III2-IV from vascular plants

Maldonado, M., Guo, F., & Letts, J. A. (2021) · eLife · doi:10.7554/elife.62047 · Cited by 833

Structural mechanism for NEK7-licensed activation of NLRP3 inflammasome

Sharif, H., Wang, L., Wang, W. L., Magupalli, V. G., Andreeva, L., Qiao, Q., Hauenstein, A. V., Wu, Z., Núñez, G., Mao, Y., et al. (2019) · Nature · doi:10.1038/s41586-019-1295-z · Cited by 824

A Genome-wide CRISPR Screen in Toxoplasma Identifies Essential Apicomplexan Genes

Sidik, S. M., Huet, D., Ganesan, S. M., Huynh, M., Wang, T., Nasamu, A. S., Thiru, P., Saeij, J. P. J., Carruthers, V. B., Niles, J. C., et al. (2016) · Cell · doi:10.1016/j.cell.2016.08.019 · Cited by 761

Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains

Yuan, Y., Cao, D., Zhang, Y., Ma, J., Qi, J., Wang, Q., Lu, G., Wu, Y., Yan, J., Shi, Y., et al. (2017) · Nature Communications · doi:10.1038/ncomms15092 · Cited by 756

mRNA circularization by METTL3–eIF3h enhances translation and promotes oncogenesis

Choe, J., Lin, S., Zhang, W. C., Liu, Q., Wang, L., Ramírez-Moya, J., Du, P., Kim, W., Tang, S., Piotr Sliz, A., et al. (2018) · Nature · doi:10.1038/s41586-018-0538-8 · Cited by 766

Transcriptome-wide off-target RNA editing induced by CRISPR-guided DNA base editors

Grünewald, J., Zhou, R., Garcia, S. P., Iyer, S., Lareau, C. A., Aryee, M. J., & Joung, J. K. (2019) · Nature · doi:10.1038/s41586-019-1161-z · Cited by 663

The SARM1 toll/interleukin-1 receptor domain possesses intrinsic NAD(+) cleavage activity that promotes pathological axonal degeneration

Essuman, K., Summers, D. W., Sasaki, Y., Mao, X., DiAntonio, A., & Milbrandt, J. (2017) · Neuron · doi:10.1016/j.neuron.2017.02.022 · Cited by 619

COFACTOR: improved protein function prediction by combining structure, sequence and protein–protein interaction information

Zhang, C., Freddolino, L., & Zhang, Y. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx366 · Cited by 606

Computational methods in drug discovery

Leelananda, S. P., & Lindert, S. (2016) · Beilstein Journal of Organic Chemistry · doi:10.3762/bjoc.12.267 · Cited by 675

In silico methods and tools for drug discovery

Shaker, B., Ahmad, S., Lee, J., Jung, C., & Na, D. (2021) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2021.104851 · Cited by 669

Structural Basis for Guide RNA Processing and Seed-Dependent DNA Targeting by CRISPR-Cas12a

Swarts, D. C., John van der, O. O. S. T., & Jínek, M. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.03.016 · Cited by 625

SARS-CoV-2 Nsp1 binds the ribosomal mRNA channel to inhibit translation

Schubert, K. N., Karousis, E. D., Jomaa, A., Scaiola, A., Echeverria, B., Gurzeler, L., Leibundgut, M., Thiel, V., Mühlemann, O., & Ban, N. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0511-8 · Cited by 605

VPS13A and VPS13C are lipid transport proteins differentially localized at ER contact sites

Kumar, N., Leonzino, M., Hancock-Cerutti, W. F., Horenkamp, F. A., Li, P., Lees, J. A., Wheeler, H., Reinisch, K. M., & Camilli, P. V. D. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201807019 · Cited by 596

New CRISPR–Cas systems from uncultivated microbes

Burstein, D. E., Harrington, L. B., Strutt, S. C., Probst, A. J., Anantharaman, K., Thomas, B. C., Doudna, J. A., & Banfield, J. F. (2016) · Nature · doi:10.1038/nature21059 · Cited by 583

Resequencing of 243 diploid cotton accessions based on an updated A genome identifies the genetic basis of key agronomic traits

Du, X., Huang, G., He, S., Yang, Z., Sun, G., Ma, X., Li, N., Zhang, X., Sun, J., Liu, M., et al. (2018) · Nature Genetics · doi:10.1038/s41588-018-0116-x · Cited by 569

Protein Structure and Function Prediction Using I‐TASSER

Yang, J., & Zhang, Y. (2015) · Current Protocols in Bioinformatics · doi:10.1002/0471250953.bi0508s52 · Cited by 568

Cyclic GMP–AMP signalling protects bacteria against viral infection

Cohen, D., Melamed, S., Millman, A., Shulman, G., Oppenheimer-Shaanan, Y., Kacen, A., Doron, S., Amitai, G., & Sorek, R. (2019) · Nature · doi:10.1038/s41586-019-1605-5 · Cited by 535

The Chara Genome: Secondary Complexity and Implications for Plant Terrestrialization

Nishiyama, T., Sakayama, H., de Vries, J., Buschmann, H., Saint‐Marcoux, D., Ullrich, K. K., Haas, F. B., Vanderstraeten, L., Becker, D., Lang, D., et al. (2018) · Cell · doi:10.1016/j.cell.2018.06.033 · Cited by 522

Molecular Structure of the Human CFTR Ion Channel

Liu, F., Zhang, Z., Csanády, L., Gadsby, D. C., & Chen, J. (2017) · Cell · doi:10.1016/j.cell.2017.02.024 · Cited by 544

I-TASSER-MTD: a deep-learning-based platform for multi-domain protein structure and function prediction

Zhou, X., Zheng, W. H., Li, Y., Pearce, R., Zhang, C., Bell, E. W., Zhang, G., & Zhang, Y. (2022) · Nature Protocols · doi:10.1038/s41596-022-00728-0 · Cited by 538

Atomic structure of the entire mammalian mitochondrial complex I

Fiedorczuk, K., Letts, J. A., Degliesposti, G., Kaszuba, K., Skehel, M. J., & Sazanov, L. A. (2016) · Nature · doi:10.1038/nature19794 · Cited by 527

Identification of Novel Mobilized Colistin Resistance Gene mcr-9 in a Multidrug-Resistant, Colistin-Susceptible Salmonella enterica Serotype Typhimurium Isolate

Carroll, L. M., Gaballa, A., Guldimann, C., Sullivan, G., Henderson, L. O., & Wiedmann, M. (2019) · mBio · doi:10.1128/mbio.00853-19 · Cited by 506

Taxonomic profiling and populational patterns of bacterial bile salt hydrolase (BSH) genes based on worldwide human gut microbiome

Song, Z., Cai, Y., Lao, X., Wang, X., Lin, X., Cui, Y., Kalavagunta, P. K., Liao, J., Jin, L., Shang, J., et al. (2019) · Microbiome · doi:10.1186/s40168-019-0628-3 · Cited by 505

The architecture of respiratory supercomplexes

Letts, J. A., Fiedorczuk, K., & Sazanov, L. A. (2016) · Nature · doi:10.1038/nature19774 · Cited by 490

RAB31 marks and controls an ESCRT-independent exosome pathway

Wei, D., Zhan, W., Gao, Y., Huang, L., Gong, R., Wang, W., Zhang, R., Wu, Y., Gao, S., & Kang, T. (2020) · Cell Research · doi:10.1038/s41422-020-00409-1 · Cited by 512

The human 18S rRNA m6A methyltransferase METTL5 is stabilized by TRMT112

van Tran, N., Ernst, F. G. M., Hawley, B. R., Zorbas, C., Ulryck, N., Hackert, P., Bohnsack, K. E., Bohnsack, M. T., Jaffrey, S. R., Graille, M., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz619 · Cited by 507

ER-mitochondria tethering by PDZD8 regulates Ca 2+ dynamics in mammalian neurons

Hirabayashi, Y., Kwon, S., Paek, H., Pernice, W. M., Paul, M. A., Lee, J., Erfani, P., Raczkowski, A. M., Petrey, D. S., Pon, L. A., et al. (2017) · Science · doi:10.1126/science.aan6009 · Cited by 505

Can Predicted Protein 3D Structures Provide Reliable Insights into whether Missense Variants Are Disease Associated?

Ittisoponpisan, S., Islam, S. A., Khanna, T., Alhuzimi, E. M., David, A., & Sternberg, M. J. E. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.04.009 · Cited by 508

Phylogenetic Analysis and Structural Modeling of SARS-CoV-2 Spike Protein Reveals an Evolutionary Distinct and Proteolytically Sensitive Activation Loop

Jaimes, J. A., André, N. M., Chappie, J. S., Millet, J. K., & Whittaker, G. R. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.04.009 · Cited by 492

Plasmid-encoded tet(X) genes that confer high-level tigecycline resistance in Escherichia coli

Sun, J. G., Chen, C., Cui, C., Zhang, Y., Liu, X., Cui, Z.-H., Ma, X.-Y., Feng, Y., Fang, L., Lian, X.-L., et al. (2019) · Nature Microbiology · doi:10.1038/s41564-019-0496-4 · Cited by 492

Intestinal serotonin and fluoxetine exposure modulate bacterial colonization in the gut

Fung, T. C., Vuong, H. E., Luna, C. G. G., Pronovost, G. N., Aleksandrova, A. A., Riley, N. G., Vavilina, A., McGinn, J., Rendon, T. K., Forrest, L. R., et al. (2019) · Nature Microbiology · doi:10.1038/s41564-019-0540-4 · Cited by 492

Structure of the activated ROQ1 resistosome directly recognizing the pathogen effector XopQ

Martin, R., Qi, T., Zhang, H., Liu, F., King, M., Toth, C., Nogales, E., & Staskawicz, B. J. (2020) · Science · doi:10.1126/science.abd9993 · Cited by 457

Type III CRISPR–Cas systems produce cyclic oligoadenylate second messengers

Niewoehner, O., Garcia-Doval, C., Rostøl, J. T., Berk, C., Schwede, F., Bigler, L., Hall, J., Marraffini, L. A., & Jinek, M. (2017) · Nature · doi:10.1038/nature23467 · Cited by 509

ePlant: Visualizing and Exploring Multiple Levels of Data for Hypothesis Generation in Plant Biology

Waese, J., Fan, J., Pasha, A., Yu, H., Fucile, G., Shi, R., Cumming, M. N., Kelley, L. A., Sternberg, M. J. E., Krishnakumar, V., et al. (2017) · The Plant Cell · doi:10.1105/tpc.17.00073 · Cited by 464

Architecture of African swine fever virus and implications for viral assembly

Wang, N., Zhao, D., Wang, J., Zhang, Y., Wang, M., Gao, Y., Li, F., Wang, J., Bu, Z., Rao, Z., et al. (2019) · Science · doi:10.1126/science.aaz1439 · Cited by 454

Identification of novel mobile colistin resistance gene mcr-10

Wang, C., Feng, Y., Liu, L., Wei, L., Kang, M., & Zong, Z. (2020) · Emerging Microbes & Infections · doi:10.1080/22221751.2020.1732231 · Cited by 459

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

Vitamin D-Mediated Hypercalcemia: Mechanisms, Diagnosis, and Treatment

Tebben, P. J., Singh, R. J., & Kumar, R. (2016) · Endocrine Reviews · doi:10.1210/er.2016-1070 · Cited by 443

Architecture of the type IVa pilus machine

Chang, Y., Rettberg, L. A., Treuner‐Lange, A., Iwasa, J., Søgaard‐Andersen, L., & Jensen, G. J. (2016) · Science · doi:10.1126/science.aad2001 · Cited by 405

The architecture of the mammalian respirasome

Gu, J., Wu, M., Guo, R., Yan, K., Lei, J., Gao, N., & Yang, M. (2016) · Nature · doi:10.1038/nature19359 · Cited by 372

MINDY-1 Is a Member of an Evolutionarily Conserved and Structurally Distinct New Family of Deubiquitinating Enzymes

Rehman, S. A. A., Kristariyanto, Y. A., Choi, S., Nkosi, P. J., Weidlich, S., Labib, K. P. M., Hofmann, K., & Kulathu, Y. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.009 · Cited by 367

Enterococcus peptidoglycan remodeling promotes checkpoint inhibitor cancer immunotherapy

Griffin, M. E., Espinosa, J., Becker, J. L., Luo, J.-D., Carroll, T. S., Jha, J. K., Fanger, G. R., & Hang, H. C. (2021) · Science · doi:10.1126/science.abc9113 · Cited by 366

Homology modeling in drug discovery: Overview, current applications, and future perspectives

Muhammed, M. T., & Aki, E. (2018) · Chemical Biology & Drug Design · doi:10.1111/cbdd.13388 · Cited by 381

TMC1 Forms the Pore of Mechanosensory Transduction Channels in Vertebrate Inner Ear Hair Cells

Pan, B., Akyuz, N., Liu, X.-P., Asai, Y., Nist-Lund, C. A., Kurima, K., Derfler, B. H., György, B., Limapichat, W., Walujkar, S., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.07.033 · Cited by 356

Architecture of human mTOR complex 1

Aylett, C. H. S., Sauer, E., Imseng, S., Boehringer, D., Hall, M. N., Ban, N., & Maier, T. (2016) · Science · doi:10.1126/science.aaa3870 · Cited by 344

HotSpot Wizard 3.0: web server for automated design of mutations and smart libraries based on sequence input information

Sumbalova, L., Štourač, J., Martínek, T., Bednář, D., & Damborský, J. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky417 · Cited by 346

Structure of nucleosome-bound human BAF complex

He, S., Wu, Z., Tian, Y., Yu, Z., Yu, J., Wang, X., Li, J., Liu, B., & Xu, Y. (2020) · Science · doi:10.1126/science.aaz9761 · Cited by 351

DISARM is a widespread bacterial defence system with broad anti-phage activities

Ofir, G., Melamed, S., Sberro, H., Mukamel, Z., Silverman, S., Yaakov, G., Doron, S., & Sorek, R. (2017) · Nature Microbiology · doi:10.1038/s41564-017-0051-0 · Cited by 350

MFN1 structures reveal nucleotide-triggered dimerization critical for mitochondrial fusion

Cao, Y.-L., Meng, S., Chen, Y., Feng, J.-X., Gu, D.-D., Yu, B., Li, Y.-J., Yang, J.-Y., Liao, S., Chan, D. C., et al. (2017) · Nature · doi:10.1038/nature21077 · Cited by 326

53BP1 cooperation with the REV7–shieldin complex underpins DNA structure-specific NHEJ

Ghezraoui, H., Oliveira, C., Becker, J. R., Bilham, K., Moralli, D., Anzilotti, C., Fischer, R., Deobagkar‐Lele, M., Sanchiz-Calvo, M., Fueyo‐Marcos, E., et al. (2018) · Nature · doi:10.1038/s41586-018-0362-1 · Cited by 331

Hybrid assembly of an agricultural slurry virome reveals a diverse and stable community with the potential to alter the metabolism and virulence of veterinary pathogens

Cook, R., Hooton, S., Trivedi, U. H., King, L., Dodd, C. E. R., Hobman, J. L., Stekel, D. J., Jones, M. A., & Millard, A. D. (2021) · Microbiome · doi:10.1186/s40168-021-01010-3 · Cited by 320

Cryo-EM structure of SARS-CoV-2 ORF3a in lipid nanodiscs

Kern, D. M., Sorum, B., Mali, S. S., Hoel, C., Sridharan, S., Remis, J. P., Toso, D. B., Kotecha, A., Bautista, D. M., & Brohawn, S. G. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00619-0 · Cited by 324

Systematic exploration of Escherichia coli phage–host interactions with the BASEL phage collection

Maffei, E., Shaidullina, A., Burkolter, M., Heyer, Y., Estermann, F., Druelle, V., Sauer, P., Willi, L., Michaelis, S., Hilbi, H., et al. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001424 · Cited by 298

Epitope-based vaccine design: a comprehensive overview of bioinformatics approaches

Parvizpour, S., Pourseif, M. M., Razmara, J., Rafi, M. A., & Omidi, Y. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.03.006 · Cited by 311

Variation of a major facilitator superfamily gene contributes to differential cadmium accumulation between rice subspecies

Yan, H., Xu, W., Xie, J., Gao, Y., Wu, L., Sun, L., Lu, F., Chen, X., Zhang, T., Dai, C., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10544-y · Cited by 305

Structure of the T4 baseplate and its function in triggering sheath contraction

Taylor, N. M. I., Prokhorov, N. S., Guerrero-Ferreira, R., Shneider, M. M., Browning, C., Goldie, K. N., Stahlberg, H., & Leiman, P. G. (2016) · Nature · doi:10.1038/nature17971 · Cited by 310

Cryo-EM Reveals How Human Cytoplasmic Dynein Is Auto-inhibited and Activated

Zhang, K., Foster, H. E., Rondelet, A., Lacey, S. E., Bahi‐Buisson, N., Bird, A. W., & Carter, A. P. (2017) · Cell · doi:10.1016/j.cell.2017.05.025 · Cited by 297

Methanogenesis in oxygenated soils is a substantial fraction of wetland methane emissions

Angle, J., Morin, T., Solden, L., Narrowe, A. B., Smith, G., Borton, M., Rey-Sánchez, C., Daly, R., Mirfenderesgi, G., Hoyt, D., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01753-4 · Cited by 272

The AlphaFold Database of Protein Structures: A Biologist’s Guide

David, A., Islam, S., Tankhilevich, E., & Sternberg, M. J. E. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167336 · Cited by 268

Cryptic inoviruses revealed as pervasive in bacteria and archaea across Earth’s biomes

Roux, S., Krupovìč, M., Daly, R. A., Borges, A. L., Nayfach, S., Schulz, F., Sharrar, A. M., Carnevali, P. B. M., Cheng, J., Ivanova, N., et al. (2019) · Nature Microbiology · doi:10.1038/s41564-019-0510-x · Cited by 291

An atlas of β-glucuronidases in the human intestinal microbiome

Pollet, R. M., D'Agostino, E. H., Walton, W. G., Xu, Y., Little, M. S., Biernat, K. A., Pellock, S. J., Patterson, L. M., Creekmore, B. C., Isenberg, H. N., et al. (2017) · Structure · doi:10.1016/j.str.2017.05.003 · Cited by 289

A repeat protein links Rubisco to form the eukaryotic carbon-concentrating organelle

Mackinder, L. C. M., Meyer, M. T., Mettler‐Altmann, T., Chen, V. K., Mitchell, M. C., Caspari, O. D., Rosenzweig, E. S. F., Pallesen, L. J., Reeves, G., Itakura, A. K., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1522866113 · Cited by 290

Optimized fragmentation schemes and data analysis strategies for proteome-wide cross-link identification

Liu, F., Lössl, P., Scheltema, R. A., Viner, R., & Heck, A. J. R. (2017) · Nature Communications · doi:10.1038/ncomms15473 · Cited by 285

Cryo-EM shows how dynactin recruits two dyneins for faster movement

Urnavicius, L., Lau, C. K., Elshenawy, M. M., Morales‐Ríos, E., Motz, C., Yıldız, A., & Carter, A. P. (2018) · Nature · doi:10.1038/nature25462 · Cited by 277

Prophage-mediated defence against viral attack and viral counter-defence

Dedrick, R. M., Jacobs‐Sera, D., Guerrero-Bustamante, C. A., Garlena, R. A., Mavrich, T. N., Pope, W. H., Reyes, J. C. C., Russell, D. A., Adair, T. L., Alvey, R. M., et al. (2017) · Nature Microbiology · doi:10.1038/nmicrobiol.2016.251 · Cited by 277

Type VI secretion and anti-host effectors

Hachani, A., Wood, T. E., & Filloux, A. (2015) · Current Opinion in Microbiology · doi:10.1016/j.mib.2015.11.006 · Cited by 270

The Pseudomonas putida T6SS is a plant warden against phytopathogens

Bernal, P., Allsopp, L. P., Filloux, A., & Llamas, M. A. (2017) · The ISME Journal · doi:10.1038/ismej.2016.169 · Cited by 270

Evidence for an Ancestral Association of Human Coronavirus 229E with Bats

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SASBDB: Towards an automatically curated and validated repository for biological scattering data

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