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

Structural basis for the final steps of human 40S ribosome maturation

Ameismeier, M., Zemp, I., van den Heuvel, J., Thoms, M., Berninghausen, O., Kutay, U., & Beckmann, R. (2020) · Nature · doi:10.1038/s41586-020-2929-x · Cited by 95

Recessive coding and regulatory mutations in FBLIM1 underlie the pathogenesis of chronic recurrent multifocal osteomyelitis (CRMO)

Cox, A., Darbro, B. W., Laxer, R. M., Velez, G., Bing, X., Finer, A. L., Erives, A. J., Mahajan, V. B., Bassuk, A. G., & Ferguson, P. J. (2017) · PLoS ONE · doi:10.1371/journal.pone.0169687 · Cited by 95

Analysis of aquaporins in Brassicaceae species reveals high-level of conservation and dynamic role against biotic and abiotic stress in canola

Sonah, H., Deshmukh, R. K., Labbé, C., & Bélanger, R. R. (2017) · Scientific Reports · doi:10.1038/s41598-017-02877-9 · Cited by 94

Structure of a eukaryotic cytoplasmic pre‐40S ribosomal subunit

Scaiola, A., Peña, C., Weisser, M. B., Boehringer, D., Leibundgut, M., Klingauf‐Nerurkar, P., Gerhardy, S., Panse, V. G., & Ban, N. (2018) · The EMBO Journal · doi:10.15252/embj.201798499 · Cited by 97

Cultivation and Genomic Analysis of “Candidatus Nitrosocaldus islandicus,” an Obligately Thermophilic, Ammonia-Oxidizing Thaumarchaeon from a Hot Spring Biofilm in Graendalur Valley, Iceland

Daebeler, A., Herbold, C. W., Vierheilig, J., Sedlacek, C. J., Pjevac, P., Albertsen, M., Kirkegaard, R. H., de la Torre, J. R., Daims, H., & Wagner, M. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.00193 · Cited by 96

Induction of antibacterial proteins and peptides in the coprophilous mushroom Coprinopsis cinerea in response to bacteria

Kombrink, A., Tayyrov, A., Essig, A., Stöckli, M., Micheller, S., Hintze, J., van Heuvel, Y., Dürig, N., Lin, C., Kallio, P. T., et al. (2018) · The ISME Journal · doi:10.1038/s41396-018-0293-8 · Cited by 94

Pectin Demethylesterification Generates Platforms that Anchor Peroxidases to Remodel Plant Cell Wall Domains

Francoz, E., Ranocha, P., Ru, A. L., Martinez, Y., Fourquaux, I., Jauneau, A., Dunand, C., & Burlat, V. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.11.016 · Cited by 94

Heterozygous Variants in KMT2E Cause a Spectrum of Neurodevelopmental Disorders and Epilepsy

O’Donnell‐Luria, A., Pais, L. S., Faùndes, V., Wood, J. C., Sveden, A., Luria, V. A., Jamra, R. A., Accogli, A., Amburgey, K., Anderlid, B. M., et al. (2019) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2019.03.021 · Cited by 91

Interconversion between Anticipatory and Active GID E3 Ubiquitin Ligase Conformations via Metabolically Driven Substrate Receptor Assembly

Qiao, S., Langlois, C., Chrustowicz, J., Sherpa, D., Karayel, Ö., Hansen, F. M., Beier, V., von Gronau, S., Bollschweiler, D., Schäfer, T., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.10.009 · Cited by 93

Assembly of the algal CO 2 -fixing organelle, the pyrenoid, is guided by a Rubisco-binding motif

Meyer, M. T., Itakura, A. K., Patena, W., Wang, L., He, S., Emrich‐Mills, T. Z., Lau, C. S., Yates, G., Mackinder, L. C. M., & Jonikas, M. C. (2020) · Science Advances · doi:10.1126/sciadv.abd2408 · Cited by 92

Protein Structure Prediction: Conventional and Deep Learning Perspectives

Jisna, V. A., & Jayaraj, P. B. (2021) · The Protein Journal · doi:10.1007/s10930-021-10003-y · Cited by 102

Cold acclimation and prospects for cold-resilient crops

Juurakko, C. L., diCenzo, G. C., & Walker, V. K. (2021) · Plant Stress · doi:10.1016/j.stress.2021.100028 · Cited by 97

Processing of NODULE INCEPTION controls the transition to nitrogen fixation in root nodules

Feng, J., Lee, T. H., Schiessl, K., & Oldroyd, G. E. D. (2021) · Science · doi:10.1126/science.abg2804 · Cited by 94

Structures of Tetrahymena ’s respiratory chain reveal the diversity of eukaryotic core metabolism

Zhou, L., Maldonado, M., Padavannil, A., Guo, F., & Letts, J. A. (2022) · Science · doi:10.1126/science.abn7747 · Cited by 94

Orange carotenoid protein burrows into the phycobilisome to provide photoprotection

Harris, D., Tal, O., Jallet, D., Wilson, A., Kirilovsky, D. L., & Adir, N. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1523680113 · Cited by 93

The vacuolar-ATPase complex and assembly factors, TMEM199 and CCDC115, control HIF1α prolyl hydroxylation by regulating cellular iron levels

Miles, A. L., Burr, S. P., Grice, G. L., & Nathan, J. A. (2017) · eLife · doi:10.7554/elife.22693 · Cited by 95

Novel Microbial Diversity and Functional Potential in the Marine Mammal Oral Microbiome

Dudek, N. K., Sun, C. L., Burstein, D. E., Kantor, R. S., Goltsman, D. S. A., Bik, E. M., Thomas, B. C., Banfield, J. F., & Relman, D. A. (2017) · Current Biology · doi:10.1016/j.cub.2017.10.040 · Cited by 91

Structural insight into mitochondrial β-barrel outer membrane protein biogenesis

Diederichs, K. A., Ni, X., Rollauer, S. E., Botos, I., Tan, X.-F., King, M. S., Kunji, E. R. S., Jiang, J., & Buchanan, S. K. (2020) · Nature Communications · doi:10.1038/s41467-020-17144-1 · Cited by 96

The Type IX Secretion System: Advances in Structure, Function and Organisation

Gorasia, D. G., Veith, P. D., & Reynolds, E. C. (2020) · Microorganisms · doi:10.3390/microorganisms8081173 · Cited by 93

The role of VvMYBA2r and VvMYBA2w alleles of the MYBA2 locus in the regulation of anthocyanin biosynthesis for molecular breeding of grape (Vitis spp.) skin coloration

Jiu, S., Guan, L., Leng, X., Zhang, K., Haider, M. S., Yu, X., Zhu, X., Zheng, T., Ge, M., Wang, C., et al. (2021) · Plant Biotechnology Journal · doi:10.1111/pbi.13543 · Cited by 93

Virome composition in marine fish revealed by meta-transcriptomics

Geoghegan, J. L., Giallonardo, F. D., Wille, M., Ortiz-Báez, A. S., Costa, V. A., Ghaly, T. M., Mifsud, J. C. O., Turnbull, O. M. H., Bellwood, D. R., Williamson, J. E., et al. (2021) · Virus Evolution · doi:10.1093/ve/veab005 · Cited by 102

Synaptotagmins at the endoplasmic reticulum–plasma membrane contact sites maintain diacylglycerol homeostasis during abiotic stress

Ruiz‐López, N., Pérez‐Sancho, J., del Valle, A. E., Haslam, R. P., Vanneste, S., Catalá, R., Perea-Resa, C., Damme, D. V., García‐Hernández, S., Albert, A., et al. (2021) · The Plant Cell · doi:10.1093/plcell/koab122 · Cited by 91

Commensal segmented filamentous bacteria-derived retinoic acid primes host defense to intestinal infection

Woo, V., Eshleman, E. M., Hashimoto‐Hill, S., Whitt, J., Wu, S.-E., Engleman, L., Rice, T., Karns, R. A., Qualls, J. E., Haslam, D. B., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.09.010 · Cited by 94

Large language models improve annotation of prokaryotic viral proteins

Flamholz, Z. N., Biller, S. J., & Kelly, L. (2024) · Nature Microbiology · doi:10.1038/s41564-023-01584-8 · Cited by 92

The Acinetobacter baumannii Mla system and glycerophospholipid transport to the outer membrane

Kamischke, C., Fan, J., Bergeron, J. R. C., Kulasekara, H. D., Dalebroux, Z. D., Burrell, A. L., Kollman, J. M., & Miller, S. I. (2019) · eLife · doi:10.7554/elife.40171 · Cited by 96

Drop-in biofuel production using fatty acid photodecarboxylase from Chlorella variabilis in the oleaginous yeast Yarrowia lipolytica

Bruder, S., Moldenhauer, E. J., Lemke, R. D., Ledesma‐Amaro, R., & Kabisch, J. (2019) · Biotechnology for Biofuels · doi:10.1186/s13068-019-1542-4 · Cited by 92

LAG3 ectodomain structure reveals functional interfaces for ligand and antibody recognition

Ming, Q., Celias, D. P., Wu, C., Cole, A. R., Singh, S., Mason, C. C., Dong, S., Tran, T. H., Amarasinghe, G. K., Ruffell, B., et al. (2022) · Nature Immunology · doi:10.1038/s41590-022-01238-7 · Cited by 92

Genome-Wide Identification and Comprehensive Expression Profiling of Ribosomal Protein Small Subunit (RPS) Genes and their Comparative Analysis with the Large Subunit (RPL) Genes in Rice

Saha, A., Das, S., Moin, M., Dutta, M., Bakshi, A., Madhav, M. S., & Kirti, P. B. (2017) · Frontiers in Plant Science · doi:10.3389/fpls.2017.01553 · Cited by 91

Structure of the human plasma membrane Ca2+-ATPase 1 in complex with its obligatory subunit neuroplastin

Gong, D., Chi, X., Ren, K., Huang, G., Zhou, G., Yan, N., Lei, J., & Zhou, Q. (2018) · Nature Communications · doi:10.1038/s41467-018-06075-7 · Cited by 91

Relatives of rubella virus in diverse mammals

Bennett, A. J., Paskey, A. C., Ebinger, A., Pfaff, F., Priemer, G., Höper, D. W., Breithaupt, A., Heuser, E., Ulrich, R. G., Kuhn, J. H., et al. (2020) · Nature · doi:10.1038/s41586-020-2812-9 · Cited by 91

Systematic prediction of genes functionally associated with bacterial retrons and classification of the encoded tripartite systems

Mestre, M. R., González-Delgado, A., Gutierrez-Rus, L. I., Martínez‐Abarca, F., & Toro, N. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa1149 · Cited by 87

Mutational insights into the envelope protein of SARS-CoV-2

Rahman, M. S., Hoque, M. N., Islam, M. R., Islam, I., Mishu, I. D., Rahaman, M. M., Sultana, M., & Hossain, M. A. (2020) · Gene Reports · doi:10.1016/j.genrep.2020.100997 · Cited by 91

Machine learning aided construction of the quorum sensing communication network for human gut microbiota

Wu, S., Feng, J., Liu, C., Wu, H., Qiu, Z., Ge, J., Sun, S., Hong, X., Li, Y., Wang, X., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30741-6 · Cited by 92

Effector Identification in Plant Pathogens

Lovelace, A. H., Dorhmi, S., Hulin, M. T., Li, Y., Mansfıeld, J. W., & Ma, W. (2023) · Phytopathology · doi:10.1094/phyto-09-22-0337-kd · Cited by 100

The source of high signal cooperativity in bacterial chemosensory arrays

Piñas, G. E., Frank, V., Vaknin, A., & Parkinson, J. S. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1600216113 · Cited by 91

Structural and functional insights into IZUMO1 recognition by JUNO in mammalian fertilization

Kato, K., Satouh, Y., Nishimasu, H., Kurabayashi, A., Morita, J., Fujihara, Y., Oji, A., Ishitani, R., Ikawa, M., & Nureki, O. (2016) · Nature Communications · doi:10.1038/ncomms12198 · Cited by 90

Gram-negative synthase-dependent exopolysaccharide biosynthetic machines

Low, K. E., & Howell, P. L. (2018) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.05.001 · Cited by 90

Isobutanol production freed from biological limits using synthetic biochemistry

Sherkhanov, S., Korman, T. P., Chan, S., Faham, S., Liu, H., Sawaya, M. R., Hsu, W.-T., Vikram, E. P., Cheng, T., & Bowie, J. U. (2020) · Nature Communications · doi:10.1038/s41467-020-18124-1 · Cited by 93

Inactivation of rice starch branching enzyme IIb triggers broad and unexpected changes in metabolism by transcriptional reprogramming

Baysal, C., He, W., Drapal, M., Villorbina, G., Medina, V., Capell, T., Khush, G. S., Zhu, C., Fraser, P. D., & Christou, P. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2014860117 · Cited by 90

Structural analysis of RIG-I-like receptors reveals ancient rules of engagement between diverse RNA helicases and TRIM ubiquitin ligases

Kato, K., Ahmad, S., Zhu, Z., Young, J. M., Mu, X. N., Park, S., Malik, H. S., & Hur, S. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.11.047 · Cited by 89

The American lobster genome reveals insights on longevity, neural, and immune adaptations

Polinski, J. M., Zimin, A. V., Clark, K. F., Kohn, A. B., Sadowski, N., Timp, W., Ptitsyn, A. A., Khanna, P., Romanova, D. Y., Williams, P., et al. (2021) · Science Advances · doi:10.1126/sciadv.abe8290 · Cited by 93

Phage defence by deaminase-mediated depletion of deoxynucleotides in bacteria

Hsueh, B. Y., Severin, G. B., Elg, C. A., Waldron, E. J., Kant, A., Wessel, A. J., Dover, J. A., Rhoades, C. R., Ridenhour, B. J., Parent, K. N., et al. (2022) · Nature Microbiology · doi:10.1038/s41564-022-01162-4 · Cited by 90

Emergence of mmpT5 Variants during Bedaquiline Treatment of Mycobacterium intracellulare Lung Disease

Alexander, D. C., Vasireddy, R., Vasireddy, S., Philley, J. V., Brown‐Elliott, B. A., Perry, B. J., Griffith, D. E., Benwill, J. L., Cameron, A. D. S., & Wallace, R. J. (2016) · Journal of Clinical Microbiology · doi:10.1128/jcm.02087-16 · Cited by 93

Recurrent Germline DLST Mutations in Individuals with Multiple Pheochromocytomas and Paragangliomas

Remacha, L., Pirman, D. A., Mahoney, C. E., Coloma, J., Calsina, B., Currás-Freixes, M., Letón, R., Torres‐Pérez, R., Richter, S., Pita, G., et al. (2019) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2019.02.017 · Cited by 88

HvWRKY23 regulates flavonoid glycoside and hydroxycinnamic acid amide biosynthetic genes in barley to combat Fusarium head blight

Karre, S., Kumar, A., Yogendra, K. N., Kage, U., Kushalappa, A. C., & Charron, J. (2019) · Plant Molecular Biology · doi:10.1007/s11103-019-00882-2 · Cited by 89

Compartmentalized biosynthesis of mycophenolic acid

Zhang, W., Du, L., Qu, Z., Zhang, X., Li, F., Li, Z. A., Qi, F., Wang, X., Jiang, Y., Men, P., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1821932116 · Cited by 89

Novel hepatitis D-like agents in vertebrates and invertebrates

Chang, W.-S., Pettersson, J. H. ‐., Lay, C. L., Shī, M., Lo, N. C., Wille, M., Eden, J., & Holmes, E. C. (2019) · Virus Evolution · doi:10.1093/ve/vez021 · Cited by 89

Genome-wide survey of the amino acid transporter gene family in wheat (Triticum aestivum L.): Identification, expression analysis and response to abiotic stress

Tian, R., Yang, Y., & Chen, M. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.07.302 · Cited by 89

GID E3 ligase supramolecular chelate assembly configures multipronged ubiquitin targeting of an oligomeric metabolic enzyme

Sherpa, D., Chrustowicz, J., Qiao, S., Langlois, C., Hehl, L. A., Gottemukkala, K. V., Hansen, F. M., Karayel, Ö., von Gronau, S., Prabu, J. R., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.03.025 · Cited by 85

Structures of outer-arm dynein array on microtubule doublet reveal a motor coordination mechanism

Rao, Q., Han, L., Wang, Y., Chai, P., Kuo, Y., Yang, R., Hu, F., Yang, Y., Howard, J., & Zhang, K. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00656-9 · Cited by 84

Unusual Five Copies and Dual Forms of nrdB in “Candidatus Liberibacter asiaticus”: Biological Implications and PCR Detection Application

Zheng, Z., Xu, M., Bao, M., Wu, F., Chen, J., & Deng, X. (2016) · Scientific Reports · doi:10.1038/srep39020 · Cited by 88

Convergent Evolution of Slick Coat in Cattle through Truncation Mutations in the Prolactin Receptor

Porto-Neto, L. R., Bickhart, D. M., Landaeta‐Hernández, A. J., Utsunomiya, Y. T., Pagán, M., Jiménez, E., Hansen, P. J., Dikmen, S., Schroeder, S., Kim, E.-S., et al. (2018) · Frontiers in Genetics · doi:10.3389/fgene.2018.00057 · Cited by 94

Physiological activation and deactivation of soluble guanylate cyclase

Horst, B. G., & Marletta, M. A. (2018) · Nitric Oxide · doi:10.1016/j.niox.2018.04.011 · Cited by 88

Adaptive evolution of distinct prey-specific toxin genes in rear-fanged snake venom

Modahl, C. M., Mrinalini, Frietze, S. E., & Mackessy, S. P. (2018) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.2018.1003 · Cited by 88

CsPrx25, a class III peroxidase in Citrus sinensis, confers resistance to citrus bacterial canker through the maintenance of ROS homeostasis and cell wall lignification

Li, Q., Qin, X., Qi, J., Dou, W., Dunand, C., Chen, S., & He, Y. (2020) · Horticulture Research · doi:10.1038/s41438-020-00415-9 · Cited by 88

A Tad-like apparatus is required for contact-dependent prey killing in predatory social bacteria

Seef, S., Herrou, J., de Boissier, P., My, L., Brasseur, G., Robert, D., Jain, R., Mercier, R., Cascalès, E., Habermann, B. H., et al. (2021) · eLife · doi:10.7554/elife.72409 · Cited by 88

Diverse events have transferred genes for edible seaweed digestion from marine to human gut bacteria

Pudlo, N. A., Pereira, G. V., Parnami, J., Cid, M., Markert, S., Tingley, J. P., Unfried, F., Ali, A. Y., Varghese, N. J., Kim, K. S., et al. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2022.02.001 · Cited by 92

Outer Membrane Proteome of Veillonella parvula: A Diderm Firmicute of the Human Microbiome

Poppleton, D., Duchateau, M., Hourdel, V., Matondo, M., Flechsler, J., Klingl, A., Beloin, C., & Gribaldo, S. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.01215 · Cited by 89

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

De novo variants in CAMK 2A and CAMK 2B cause neurodevelopmental disorders

Akita, T., Aoto, K., Kato, M., Shiina, M., Mutoh, H., Nakashima, M., Kuki, I., Okazaki, S., Magara, S., Shiihara, T., et al. (2018) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.528 · Cited by 87

Structures of DPAGT1 Explain Glycosylation Disease Mechanisms and Advance TB Antibiotic Design

Dong, Y. Y., Wang, H., Pike, A. C. W., Cochrane, S. A., Hamedzadeh, S., Wyszyński, F. J., Bushell, S. R., Royer, S. F., Widdick, D. A., Sajid, A., et al. (2018) · Cell · doi:10.1016/j.cell.2018.10.037 · Cited by 87

The nuclear actin-containing Arp8 module is a linker DNA sensor driving INO80 chromatin remodeling

Knoll, K. R., Eustermann, S., Niebauer, V., Oberbeckmann, E., Stoehr, G., Schall, K., Tosi, A., Schwarz, M., Buchfellner, A., Korber, P., et al. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0115-8 · Cited by 92

RiCRN1, a Crinkler Effector From the Arbuscular Mycorrhizal Fungus Rhizophagus irregularis, Functions in Arbuscule Development

Voß, S., Betz, R., Heidt, S., Corradi, N., & Requena, N. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.02068 · Cited by 87

The biosynthetic origin of psychoactive kavalactones in kava

Pluskal, T., Torrens-Spence, M. P., Fallon, T. R., Abreu, A. D., Shi, C. H., & Weng, J. (2019) · Nature Plants · doi:10.1038/s41477-019-0474-0 · Cited by 87

Structure and mechanism of mitochondrial proton-translocating transhydrogenase

Kampjut, D., & Sazanov, L. A. (2019) · Nature · doi:10.1038/s41586-019-1519-2 · Cited by 87

Enhanced GROMACS: toward a better numerical simulation framework

Rakhshani, H., Dehghanian, E., & Rahati, A. (2019) · Journal of Molecular Modeling · doi:10.1007/s00894-019-4232-z · Cited by 88

Modular genetic control of social status in a cichlid fish

Alward, B. A., Laud, V. A., Skalnik, C. J., York, R. A., Juntti, S. A., & Fernald, R. D. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2008925117 · Cited by 87

Iron Oxidation by a Fused Cytochrome-Porin Common to Diverse Iron-Oxidizing Bacteria

Keffer, J. L., McAllister, S. M., Garber, A. I., Hallahan, B. J., Sutherland, M. C., Rozovsky, S., & Chan, C. S. (2021) · mBio · doi:10.1128/mbio.01074-21 · Cited by 88

Genomic mechanisms for cold tolerance and production of exopolysaccharides in the Arctic cyanobacterium Phormidesmis priestleyi BC1401

Chrismas, N. A. M., Barker, G., Anesio, A. M., & Sánchez‐Baracaldo, P. (2016) · BMC Genomics · doi:10.1186/s12864-016-2846-4 · Cited by 85

Recognition of EGF-like domains by the Notch-modifying O-fucosyltransferase POFUT1

Li, Z., Han, K., Pak, J. E., Satkunarajah, M., Zhou, D., & Rini, J. M. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2381 · Cited by 85

Cryo-EM Structure of the Exocyst Complex

Mei, K., Li, Y., Wang, S., Shao, G.-C., Wang, J., Ding, Y., Luo, G., Yue, P., Liu, J., Wang, X., et al. (2017) · Worldwide Protein Data Bank · doi:10.2210/pdb5yfp/pdb · Cited by 85

Emerging Microbes & Infections

Yuen, K. (2016) · Cited by 92

TssA forms a gp6‐like ring attached to the type VI secretion sheath

Planamente, S., Salih, O., Manoli, E., Albesa-Jové, D., Freemont, P. S., & Filloux, A. (2016) · The EMBO Journal · doi:10.15252/embj.201694024 · Cited by 86

Mutation in POLR3K causes hypomyelinating leukodystrophy and abnormal ribosomal RNA regulation

Dorboz, I., Dumay‐Odelot, H., Boussaid, K., Bouyacoub, Y., Barreau, P., Samaan, S., Jmel, H., Eymard-Pierre, É., Cancès, C., Bar, C., et al. (2018) · Neurology Genetics · doi:10.1212/nxg.0000000000000289 · Cited by 86

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Folding Membrane Proteins by Deep Transfer Learning

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OCTN: A Small Transporter Subfamily with Great Relevance to Human Pathophysiology, Drug Discovery, and Diagnostics

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