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 · see citing works

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 · see citing works

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 6,951 · see citing works

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 6,093 · see citing works

Protein secondary structure prediction based on position-specific scoring matrices.

Jones, D. C. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3091 · Cited by 5,741 · see citing works

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 · see citing works

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 3,915 · see citing works

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 · see citing works

Protein homology detection by HMM–HMM comparison

Söding, J. (2004) · Bioinformatics · doi:10.1093/bioinformatics/bti125 · Cited by 2,381 · see citing works

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 · see citing works

Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life

Ward, J. J., Sodhi, J. S., McGuffin, L. J., Buxton, B. F., & Jones, D. T. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.002 · Cited by 2,010 · see citing works

Template-based protein structure modeling using the RaptorX web server

Källberg, M., Wang, H., Wang, S., Peng, J., Wang, Z., Lu, H. J., & Xu, J. (2012) · Nature Protocols · doi:10.1038/nprot.2012.085 · Cited by 1,576 · see citing works

CDD: conserved domains and protein three-dimensional structure

Marchler‐Bauer, A., Zheng, C., Chitsaz, F., Derbyshire, M. K., Geer, L. Y., Geer, R. C., Gonzales, N. R., Gwadz, M., Hurwitz, D. I., Lanczycki, C. J., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1243 · Cited by 872 · see citing works

Improving the Assessment of the Outcome of Nonsynonymous SNVs with a Consensus Deleteriousness Score, Condel

González-Pérez, A., & López-Bigas, N. (2011) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2011.03.004 · Cited by 765 · see citing works

Predicting functionally important residues from sequence conservation

Capra, J. A., & Singh, M. (2007) · Bioinformatics · doi:10.1093/bioinformatics/btm270 · Cited by 693 · see citing works

Critical assessment of methods of protein structure prediction (CASP) — round x

Moult, J., Fidelis, K. A., Kryshtafovych, A., Schwede, T. F., & Tramontano, A. L. (2013) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24452 · Cited by 673 · see citing works

3DLigandSite: predicting ligand-binding sites using similar structures

Wass, M. N., Kelley, L. A., & Sternberg, M. J. E. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq406 · Cited by 629 · see citing works

The Catalytic Site Atlas: a resource of catalytic sites and residues identified in enzymes using structural data

Porter, C. T. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkh028 · Cited by 605 · see citing works

The structure of the protein universe and genome evolution

Koonin, E. V., Wolf, Y. I., & Karev, G. P. (2002) · Nature · doi:10.1038/nature01256 · Cited by 553 · see citing works

Cyclic coordinate descent: A robotics algorithm for protein loop closure

Canutescu, A. A., & Dunbrack, R. L. (2003) · Protein Science · doi:10.1110/ps.0242703 · Cited by 527 · see citing works

Structure prediction for CASP8 with all‐atom refinement using Rosetta

Raman, S., Vernon, R. M., Thompson, J., Tyka, M. D., Sadreyev, R. I., Pei, J., Kim, D. E., Kellogg, E. H., DiMaio, F., Lange, O. F., et al. (2009) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22540 · Cited by 511 · see citing works

Improving the accuracy of transmembrane protein topology prediction using evolutionary information

Jones, D. T. (2007) · Bioinformatics · doi:10.1093/bioinformatics/btl677 · Cited by 420 · see citing works

MaxSub: an automated measure for the assessment of protein structure prediction quality

Siew, N., Elofsson, A., Rychlewski, L., & Fischer, D. (2000) · Bioinformatics · doi:10.1093/bioinformatics/16.9.776 · Cited by 401 · see citing works

Fast procedure for reconstruction of full‐atom protein models from reduced representations

Rotkiewicz, P., & Skolnick, J. (2008) · Journal of Computational Chemistry · doi:10.1002/jcc.20906 · Cited by 395 · see citing works

pGenTHREADER and pDomTHREADER: new methods for improved protein fold recognition and superfamily discrimination

Lobley, A., Sadowski, M. I., & Jones, D. T. (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp302 · Cited by 302 · see citing works

fpocket: online tools for protein ensemble pocket detection and tracking

Schmidtke, P., Guilloux, V. L., Maupetit, J., & Tufféry, P. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq383 · Cited by 292 · see citing works

SuSPect: Enhanced Prediction of Single Amino Acid Variant (SAV) Phenotype Using Network Features

Yates, C. M., Filippis, I., Kelley, L. A., & Sternberg, M. J. E. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.04.026 · Cited by 246 · see citing works

Improved model quality assessment using ProQ2

Ray, A., Lindahl, E. R., & Wallner, B. (2012) · BMC Bioinformatics · doi:10.1186/1471-2105-13-224 · Cited by 191 · see citing works

GAME: detecting cis-regulatory elements using a genetic algorithm

Wei, Z., & Jensen, S. T. (2006) · Bioinformatics · doi:10.1093/bioinformatics/btl147 · Cited by 96 · see citing works

Protein Folding Requires Crowd Control in a Simulated Cell

Jefferys, B. R., Kelley, L. A., & Sternberg, M. J. E. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.01.074 · Cited by 89 · see citing works

ePlant and the 3D Data Display Initiative: Integrative Systems Biology on the World Wide Web

Fucile, G., Biase, D. D., Nahal-Bose, H. K., La, G., Khodabandeh, S., Chen, Y., Easley, K., Christendat, D., Kelley, L. A., & Provart, N. J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0015237 · Cited by 66 · see citing works

Genome3D: a UK collaborative project to annotate genomic sequences with predicted 3D structures based on SCOP and CATH domains

Lewis, T. E., Sillitoe, I., Andreeva, A. E., Blundell, T. L., Buchan, D. W. A., Chothia, C., Cuff, A. L., Dana, J. M., Filippis, I., Gough, J., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1266 · Cited by 59 · see citing works

PiSite: a database of protein interaction sites using multiple binding states in the PDB

Higurashi, M., Ishida, T., & Kinoshita, K. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn659 · Cited by 58 · see citing works

Residue-rotamer-reduction algorithm for the protein side-chain conformation problem

Xie, W., & Sahinidis, N. V. (2005) · Bioinformatics · doi:10.1093/bioinformatics/bti763 · Cited by 43 · see citing works

Functional assignment of Mycobacterium tuberculosis proteome revealed by genome-scale fold-recognition

Mao, C., Shukla, M. P., Larrouy-Maumus, G. J., Dix, F. L., Kelley, L. A., Sternberg, M. J. E., Sobral, B., & de Carvalho, L. P. S. (2013) · Tuberculosis · doi:10.1016/j.tube.2012.11.008 · Cited by 19 · see citing works

Genome-Wide Protein Structure Prediction

Mukherjee, S., Szilágyi, A., Roy, A., & Zhang, Y. (2010) · Springer eBooks · doi:10.1007/978-1-4419-6889-0_11 · Cited by 8 · see citing works

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 · see citing works

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 · see citing works

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 1,356 · see citing works

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 1,190 · see citing works

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 · see citing works

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

Shaffer, M., Borton, M., McGivern, B. B., Zayed, A., Rosa, S. L. L., Solden, L., Liu, P.-F., Narrowe, A. B., Rodríguez-Ramos, J. A., Bolduc, B., et al. (2020) · bioRxiv · doi:10.1093/nar/gkaa621 · Cited by 1,043 · see citing works

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 1,067 · see citing works

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 · see citing works

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 · see citing works

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 837 · see citing works

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 · see citing works

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 · see citing works

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 761 · see citing works

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 749 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Computational methods in drug discovery

Leelananda, S. P., & Lindert, S. (2016) · Beilstein Journal of Organic Chemistry · doi:10.3762/bjoc.12.267 · Cited by 647 · see citing works

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 614 · see citing works

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 615 · see citing works

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 · see citing works

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 593 · see citing works

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 574 · see citing works

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 · see citing works

Protein Structure and Function Prediction Using I‐TASSER

Yang, J., & Zhang, Y. (2015) · Current Protocols in Bioinformatics · doi:10.1002/0471250953.bi0508s52 · Cited by 553 · see citing works

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 537 · see citing works

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 512 · see citing works

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 512 · see citing works

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 524 · see citing works

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 516 · see citing works

Identification of Novel Mobilized Colistin Resistance Gene <i>mcr-9</i> 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 · see citing works

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 · see citing works

The architecture of respiratory supercomplexes

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

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 498 · see citing works

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 496 · see citing works

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 495 · see citing works

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 484 · see citing works

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 485 · see citing works

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 487 · see citing works

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 481 · see citing works

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 468 · see citing works

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., & Jínek, M. (2017) · Nature · doi:10.1038/nature23467 · Cited by 464 · see citing works

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 · see citing works

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 461 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 369 · see citing works

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 · see citing works

<i>Enterococcus</i> 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 · see citing works

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 367 · see citing works

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

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Architecture of human mTOR complex 1

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