Structural assembly of the bacterial essential interactome
Open accessPublished version of a preprint
Abstract
The study of protein interactions in living organisms is fundamental for understanding biological processes and central metabolic pathways. Yet, our knowledge of the bacterial interactome remains limited. Here, we combined gene deletion mutant analysis with deep-learning protein folding using AlphaFold2 to predict the core bacterial essential interactome. We predicted and modeled 1402 interactions between essential proteins in bacteria and generated 146 high-accuracy models. Our analysis reveals previously unknown details about the assembly mechanisms of these complexes, highlighting the importance of specific structural features in their stability and function. Our work provides a framework for predicting the essential interactomes of bacteria and highlight the potential of deep-learning algorithms in advancing our understanding of the complex biology of living organisms. Also, the results presented here offer a promising approach to identify novel antibiotic targets.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
Szklarczyk, D., Gable, A. L., Nastou, K. C., Lyon, D., Kirsch, R., Pyysalo, S., Doncheva, N. T., Legeay, M., Fang, T., Bork, P., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkaa1074 · Cited by 8,056 · see citing works
Construction of Escherichia coli K‐12 in‐frame, single‐gene knockout mutants: the Keio collection
Baba, T., Ara, T., Hasegawa, M., Takai, Y., Okumura, Y., Baba, M., Datsenko, K. A., Tomita, M., Wanner, B. L., & Mori, H. (2006) · Molecular Systems Biology · doi:10.1038/msb4100050 · Cited by 7,858 · see citing works
Accurate prediction of protein structures and interactions using a 3-track network
Baek, M., DiMaio, F., Anishchenko, I., Dauparas, J., Ovchinnikov, S., Lee, G. R., Wang, J., Cong, Q., Kinch, L. N., Schaeffer, R. D., et al. (2021) · doi:10.1101/2021.06.14.448402 · Cited by 5,542 · see citing works
Protein complex prediction with AlphaFold-Multimer
Evans, R., O’Neill, M., Pritzel, A., Antropova, N., Senior, A., Green, T., Žídek, A., Bates, R., Blackwell, S., Yim, J., et al. (2021) · doi:10.1101/2021.10.04.463034 · Cited by 3,808 · see citing works
Improved prediction of protein-protein interactions using AlphaFold2
Bryant, P., Pozzati, G., & Elofsson, A. (2021) · doi:10.1101/2021.09.15.460468 · Cited by 1,025 · see citing works
An ordered, nonredundant library of Pseudomonas aeruginosa strain PA14 transposon insertion mutants
Liberati, N. T., Urbach, J. M., Miyata, S., Lee, D. G., Drenkard, E., Wu, G., Villanueva, J. M., Wei, T., & Ausubel, F. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511100103 · Cited by 971 · see citing works
Protein-Protein Interaction Detection: Methods and Analysis
Rao, V. S., Srinivas, K., Sujini, G. N., & Kumar, G. N. S. (2014) · International Journal of Proteomics · doi:10.1155/2014/147648 · Cited by 811 · see citing works
Experimental Determination and System Level Analysis of Essential Genes in Escherichia coli MG1655
Gerdes, S., Scholle, M., Campbell, J., Balázsi, G., Ravasz, E., Daugherty, M., Somera, A., Kyrpides, N., Anderson, I., Gelfand, M., et al. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.19.5673-5684.2003 · Cited by 788 · see citing works
Biosynthesis and Export of Bacterial Lipopolysaccharides
Whitfield, C., & Trent, M. S. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060713-035600 · Cited by 716 · see citing works
A structural biology community assessment of AlphaFold2 applications
Akdel, M., Pires, D. E. V., Pardo, E. P., Jänes, J., Zalevsky, A. O., Mészáros, B., Bryant, P., Good, L. L., Laskowski, R. A., Pozzati, G., et al. (2022) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00849-w · Cited by 675 · see citing works
Topoisomerase Inhibitors: Fluoroquinolone Mechanisms of Action and ResistancePreprint
Hooper, D. C., & Jacoby, G. A. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a025320 · Cited by 574 · see citing works
FreeSASA: An open source C library for solvent accessible surface area calculations
Mitternacht, S. (2016) · F1000Research · doi:10.12688/f1000research.7931.1 · Cited by 560 · see citing works
Acetyl-coenzyme A carboxylase: crucial metabolic enzyme and attractive target for drug discovery
Tong, L. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5121-4 · Cited by 519 · see citing works
DockQ: A Quality Measure for Protein-Protein Docking Models
Basu, S., & Wallner, B. (2016) · PLOS ONE · doi:10.1371/journal.pone.0161879 · Cited by 460 · see citing works
Protein export through the bacterial Sec pathway
Tsirigotaki, A., De Geyter, J., Šoštaric´, N., Economou, A., & Karamanou, S. (2017) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2016.161 · Cited by 447 · see citing works
Ji, Y., Zhang, B., Van, S. F., Horn, Warren, P. V., Woodnutt, G., Burnham, M. K. R., & Rosenberg, M. J. (2001) · Science · doi:10.1126/science.1063566 · Cited by 414 · see citing works
Lipopolysaccharide transport and assembly at the outer membrane: the PEZ model
Okuda, S., Sherman, D. J., Silhavy, T. J., Ruiz, N., & Kahne, D. E. (2016) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2016.25 · Cited by 382 · see citing works
Stoichiometry and Architecture of Active DNA Replication Machinery in Escherichia coli
Reyes‐Lamothe, R., Sherratt, D. J., & Leake, M. C. (2010) · Science · doi:10.1126/science.1185757 · Cited by 381 · see citing works
How Many Genes Can Make a Cell: The Minimal-Gene-Set Concept
Koonin, E. V. (2000) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev.genom.1.1.99 · Cited by 336 · see citing works
The Essential Genome of Escherichia coli K-12
Goodall, E. C. A., Robinson, A., Johnston, I. G., Jabbari, S., Turner, K. A., Cunningham, A. F., Lund, P. A., Cole, J. A., & Henderson, I. R. (2018) · mBio · doi:10.1128/mbio.02096-17 · Cited by 324 · see citing works
Chaudhuri, R. R., Allen, A. G., Owen, P., Shalom, G., Stone, K. M., Harrison, M., Burgis, T. A., Lockyer, M. J., Garcı́a-Lara, J., Foster, S. J., et al. (2009) · BMC Genomics · doi:10.1186/1471-2164-10-291 · Cited by 309 · see citing works
Current understanding of fatty acid biosynthesis and the acyl carrier protein
Chan, D. I., & Vogel, H. J. (2010) · Biochemical Journal · doi:10.1042/bj20100462 · Cited by 303 · see citing works
High‐throughput CRISPRi phenotyping identifies new essential genes in Streptococcus pneumoniae
Liu, X., Gallay, C., Kjos, M., Domenech, A., Slager, J., van Kessel, S. P., Knoops, K., Sorg, R. A., Zhang, J., & Veening, J. (2017) · Molecular Systems Biology · doi:10.15252/msb.20167449 · Cited by 273 · see citing works
Genome-Scale Identification of Resistance Functions in Pseudomonas aeruginosa Using Tn-seq
Gallagher, L. A., Shendure, J., & Manoil, C. (2011) · mBio · doi:10.1128/mbio.00315-10 · Cited by 253 · see citing works
du Plessis, D. J. F., Nouwen, N. P., & Driessen, A. J. M. (2010) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2010.08.016 · Cited by 253 · see citing works
Protein interaction networks revealed by proteome coevolution
Cong, Q., Anishchenko, I., Ovchinnikov, S., & Baker, D. (2019) · Science · doi:10.1126/science.aaw6718 · Cited by 241 · see citing works
Genome-wide identification of Acinetobacter baumannii genes necessary for persistence in the lung
Wang, N., Ozer, E. A., Mandel, M. J., & Hauser, A. R. (2014) · mBio · doi:10.1128/mbio.01163-14 · Cited by 234 · see citing works
The binary protein-protein interaction landscape of Escherichia coli
Rajagopala, S. V., Sikorski, P., Kumar, A., Mosca, R., Vlasblom, J., Arnold, R., Franca-Koh, J., Pakala, S. B., Phanse, S., Ceol, A., et al. (2014) · Nature Biotechnology · doi:10.1038/nbt.2831 · Cited by 233 · see citing works
Evaluation of AlphaFold-Multimer prediction on multi-chain protein complexes
Zhu, W., Shenoy, A., Kundrotas, P., & Elofsson, A. (2023) · Bioinformatics · doi:10.1093/bioinformatics/btad424 · Cited by 202 · see citing works
Defining the core essential genome of Pseudomonas aeruginosa
Poulsen, B. E., Yang, R., Clatworthy, A. E., White, T. L., Osmulski, S. J., Li, L., Peñaranda, C., Lander, E. S., Noam Shoresh, F., & Hung, D. T. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1900570116 · Cited by 197 · see citing works
Phosphatidic acid synthesis in bacteria
Yao, J., & Rock, C. O. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2012.08.018 · Cited by 195 · see citing works
High-throughput analysis of gene essentiality and sporulation in Clostridium difficile
Dembek, M., Barquist, L., Boinett, C. J., Cain, A. K., Mayho, M., Lawley, T. D., Fairweather, N. F., & Fagan, R. P. (2015) · mBio · doi:10.1128/mbio.02383-14 · Cited by 185 · see citing works
Structural basis of lipopolysaccharide extraction by the LptB2FGC complex
Li, Y., Orlando, B. J., & Liao, M. (2019) · Nature · doi:10.1038/s41586-019-1025-6 · Cited by 166 · see citing works
Cooperativity of peptidoglycan synthases active in bacterial cell elongation
Banzhaf, M., van Saparoea, H. B. V. D. B., Terrak, M., Fraipont, C., Egan, A. J. F., Philippe, J., Zapun, A., Breukink, E. J., Nguyen‐Distèche, M., den Blaauwen, T., et al. (2012) · Molecular Microbiology · doi:10.1111/j.1365-2958.2012.08103.x · Cited by 164 · see citing works
Suits, M. D. L., Sperandeo, P., Dehò, G., Polissi, A., & Jia, Z. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.04.045 · Cited by 164 · see citing works
DNA replication fidelity in Escherichia coli : a multi-DNA polymerase affair
Fijałkowska, I. J., Schaaper, R. M., & Jonczyk, P. (2012) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2012.00338.x · Cited by 162 · see citing works
Crystal structures of bacterial lipoprotein localization factors, LolA and LolB
Takeda, K., Miyatake, H., Yokota, N., Matsuyama, S., Tokuda, H., & Miki, K. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg324 · Cited by 148 · see citing works
Septum Enlightenment: Assembly of Bacterial Division Proteins
Vicente, M., Rico, A. I., Martínez‐Arteaga, R., & Mingorance, J. (2005) · Journal of Bacteriology · doi:10.1128/jb.188.1.19-27.2006 · Cited by 144 · see citing works
The protein-conducting channel SecYEG
Veenendaal, A. K. J., van der Does, C., & Driessen, A. J. M. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.02.009 · Cited by 135 · see citing works
Yao, J., & Rock, C. O. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.r114.636241 · Cited by 131 · see citing works
The bacterial cell cycle, chromosome inheritance and cell growth.
Reyes-Lamothe, R., & Sherratt, D. J. (2019) · Nature Reviews Microbiology · doi:10.1038/s41579-019-0212-7 · Cited by 131 · see citing works
Sjodt, M., Rohs, P. D. A., Gilman, M. S. A., Erlandson, S. C., Zheng, S., Green, A. G., Brock, K. P., Taguchi, A., Kahne, D. E., Walker, S., et al. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0687-z · Cited by 130 · see citing works
Rohs, P. D. A., Buss, J. A., Sim, S. I., Squyres, G. R., Srisuknimit, V., Smith, M. D., Cho, H., Sjodt, M., Kruse, A. C., Garner, E. C., et al. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007726 · Cited by 129 · see citing works
Bacterial lipoproteins; biogenesis, sorting and quality control
Narita, S., & Tokuda, H. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.11.009 · Cited by 128 · see citing works
The DnaA Cycle in Escherichia coli: Activation, Function and Inactivation of the Initiator Protein
Katayama, T., Kasho, K., & Kawakami, H. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.02496 · Cited by 125 · see citing works
Redefining the essential trafficking pathway for outer membrane lipoproteins
Grabowicz, M., & Silhavy, T. J. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1702248114 · Cited by 123 · see citing works
The functional proteome landscape of Escherichia coli
Mateus, A., Hevler, J. F., Bobonis, J., Kurzawa, N., Shah, M., Mitosch, K., Goemans, C., Helm, D., Stein, F., Typas, A., et al. (2020) · Nature · doi:10.1038/s41586-020-3002-5 · Cited by 114 · see citing works
Bacterial cell division at a glance
Mahone, C. R., & Goley, E. D. (2020) · Journal of Cell Science · doi:10.1242/jcs.237057 · Cited by 111 · see citing works
Essential genes in Bacillus subtilis : a re-evaluation after ten years
Commichau, F. M., Pietack, N., & Stülke, J. (2013) · Molecular BioSystems · doi:10.1039/c3mb25595f · Cited by 108 · see citing works
van der Ploeg, R., Verheul, J., Vischer, N. O. E., Alexeeva, S., Hoogendoorn, E., Postma, M., Banzhaf, M., Vollmer, W., & den Blaauwen, T. (2013) · Molecular Microbiology · doi:10.1111/mmi.12150 · Cited by 104 · see citing works
Transport of lipopolysaccharide to the Gram-negative bacterial cell surface
Putker, F., Bos, M. P., & Tommassen, J. (2015) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuv026 · Cited by 104 · see citing works
Guharoy, M., & Chakrabarti, P. (2010) · BMC Bioinformatics · doi:10.1186/1471-2105-11-286 · Cited by 102 · see citing works
Protein Diffusion in the Periplasm of E. coli under Osmotic Stress
Sochacki, K. A., Shkel, I. A., Record, M. T., & Weisshaar, J. C. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2010.11.044 · Cited by 101 · see citing works
Protein interactions: is seeing believing?
MACKAY, J., SUNDE, M., LOWRY, J., CROSSLEY, M., & MATTHEWS, J. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.09.006 · Cited by 100 · see citing works
Do the divisome and elongasome share a common evolutionary past?
Szwedziak, P., & Löwe, J. (2013) · Current Opinion in Microbiology · doi:10.1016/j.mib.2013.09.003 · Cited by 95 · see citing works
A new platform for ultra-high density Staphylococcus aureus transposon libraries
Santiago, M., Matano, L. M., Moussa, S. H., Gilmore, M. S., Walker, S., & Meredith, T. C. (2015) · BMC Genomics · doi:10.1186/s12864-015-1361-3 · Cited by 93 · see citing works
Mahalakshmi, S., Sunayana, M. R., SaiSree, L., & Reddy, M. (2013) · Molecular Microbiology · doi:10.1111/mmi.12452 · Cited by 91 · see citing works
LptE binds to and alters the physical state of LPS to catalyze its assembly at the cell surface
Malojcic, G., Andres, D., Grabowicz, M., George, A. H., Ruiz, N., Silhavy, T. J., & Kahne, D. E. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402746111 · Cited by 90 · see citing works
Oswald, J., Njenga, R., Natriashvili, A., Sarmah, P., & Koch, H.-G. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.664241 · Cited by 88 · see citing works
Kaplan, E., Greene, N. P., Crow, A., & Koronakis, V. E. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1806822115 · Cited by 84 · see citing works
Advances in bacterial pathways for the biosynthesis of ubiquinone
Abby, S. S., Kazemzadeh, K., Vragniau, C., Pélosi, L., & Pierrel, F. (2020) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2020.148259 · Cited by 83 · see citing works
Chasing acyl carrier protein through a catalytic cycle of lipid A production
Masoudi, A., Raetz, C. R. H., Zhou, P., & Pemble, C. W., IV (2013) · Nature · doi:10.1038/nature12679 · Cited by 82 · see citing works
Comprehensive Arrayed Transposon Mutant Library of Klebsiella pneumoniae Outbreak Strain KPNIH1
Ramage, B., Erolin, R., Held, K. G., Gasper, J. S., Weiss, E. J., Brittnacher, M. J., Gallagher, L. A., & Manoil, C. (2017) · Journal of Bacteriology · doi:10.1128/jb.00352-17 · Cited by 82 · see citing works
Control of Initiation of DNA Replication in Bacillus subtilis and Escherichia coli
Jameson, K. H., & Wilkinson, A. J. (2017) · Genes · doi:10.3390/genes8010022 · Cited by 76 · see citing works
Structure of the substrate-engaged SecA-SecY protein translocation machine
Ma, C., Wu, X., Sun, D., Park, E., Catipovic, M. A., Rapoport, T. A., Gao, N., & Li, L. (2019) · Nature Communications · doi:10.1038/s41467-019-10918-2 · Cited by 74 · see citing works
Centrality in the host–pathogen interactome is associated with pathogen fitness during infection
Asensio, N. C., Giner, E. M., de Groot, N. S., & Torrent, M. (2017) · Nature Communications · doi:10.1038/ncomms14092 · Cited by 70 · see citing works
The Biotinyl Domain of Escherichia coli Acetyl-CoA Carboxylase
Cronan, J. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106353200 · Cited by 68 · see citing works
Bai, J., Dai, Y., Farinha, A., Tang, A. Y., Syal, S., Vargas-Cuebas, G. G., Surujon, D., Isberg, R. R., van Opijnen, T., & Geisinger, E. (2021) · Journal of Bacteriology · doi:10.1128/jb.00565-20 · Cited by 65 · see citing works
Concentration‐dependent oligomerization and oligomeric arrangement of LptA
Merten, J. A., Schultz, K. M., & Klug, C. S. (2011) · Protein Science · doi:10.1002/pro.2004 · Cited by 63 · see citing works
Roles of FtsEX in cell division
Pichoff, S., Du, S., & Lutkenhaus, J. (2019) · Research in Microbiology · doi:10.1016/j.resmic.2019.07.003 · Cited by 59 · see citing works
Olsen, L. R., Vetting, M. W., & Roderick, S. L. (2007) · Protein Science · doi:10.1110/ps.072779707 · Cited by 59 · see citing works
A central cavity within the holo-translocon suggests a mechanism for membrane protein insertion
Botte, M., Zaccai, N. R., Nijeholt, J. A. L. A., Martin, R., Knoops, K., Pápai, G., Zou, J., Deniaud, A., Karuppasamy, M., Jiang, Q., et al. (2016) · Scientific Reports · doi:10.1038/srep38399 · Cited by 59 · see citing works
A Soluble Metabolon Synthesizes the Isoprenoid Lipid Ubiquinone
Chehade, M. H., Pélosi, L., Fyfe, C. D., Loiseau, L., Rascalou, B., Brugière, S., Kazemzadeh, K., Vo, C.-D.-T., Ciccone, L., Aussel, L., et al. (2018) · Cell chemical biology · doi:10.1016/j.chembiol.2018.12.001 · Cited by 56 · see citing works
Protein‐protein interactions as antibiotic targets: A medicinal chemistry perspective
Cossar, P. J., Lewis, P. J., & McCluskey, A. (2020) · Medicinal Research Reviews · doi:10.1002/med.21519 · Cited by 55 · see citing works
Structural and dynamical rationale for fatty acid unsaturation in Escherichia coli
Dodge, G. J., Patel, A., Jaremko, K. L., McCammon, J. A., Smith, J. L., & Burkart, M. D. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1818686116 · Cited by 53 · see citing works
Badshah, S. L., & Ullah, A. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.04.059 · Cited by 52 · see citing works
MreC and MreD balance the interaction between the elongasome proteins PBP2 and RodA
Liu, X.-L., Biboy, J., Consoli, E., Vollmer, W., & den Blaauwen, T. (2019) · bioRxiv · doi:10.1371/journal.pgen.1009276 · Cited by 52 · see citing works
Inter-membrane association of the Sec and BAM translocons for bacterial outer-membrane biogenesis.
Alvira, S., Watkins, D. W., Troman, L. A., Allen, W. J., Lorriman, J. S., Degliesposti, G., Cohen, E. J., Beeby, M., Daum, B., Gold, V. A., et al. (2020) · eLife · doi:10.7554/elife.60669 · Cited by 51 · see citing works
Altered Regulation of Escherichia coli Biotin Biosynthesis in BirA Superrepressor Mutant Strains
Chakravartty, V., & Cronan, J. E. (2011) · Journal of Bacteriology · doi:10.1128/jb.06549-11 · Cited by 49 · see citing works
Xu, Z., & Dixon, N. E. (2018) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.09.006 · Cited by 48 · see citing works
Complex Formation and Regulation of Escherichia coli Acetyl-CoA Carboxylase
Broussard, T. C., Price, A. E., Laborde, S. M., & Waldrop, G. L. (2013) · Biochemistry · doi:10.1021/bi4000707 · Cited by 46 · see citing works
Cronan, J. E. (2021) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00032-21 · Cited by 45 · see citing works
Hicks, G., & Jia, Z. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092680 · Cited by 39 · see citing works
Dong, C., Jin, Y.-T., Hua, H., Wen, Q., Luo, S., Zheng, W., & Guo, F. (2018) · Briefings in Bioinformatics · doi:10.1093/bib/bby116 · Cited by 36 · see citing works
Convergent allostery in ribonucleotide reductase
Thomas, W. C., Brooks, F. P., Burnim, A. A., Bacik, J. P., Stubbe, J., Kaelber, J. T., Chen, J. Z., & Ando, N. (2019) · Nature Communications · doi:10.1038/s41467-019-10568-4 · Cited by 36 · see citing works
Carro, L. (2018) · Beilstein Journal of Organic Chemistry · doi:10.3762/bjoc.14.267 · Cited by 35 · see citing works
Hayashi, Y., Tsurumizu, R., Tsukahara, J., Takeda, K., Narita, S., Mori, M., Miki, K., & Tokuda, H. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.539270 · Cited by 35 · see citing works
LptA Assembles into Rod-Like Oligomers Involving Disorder-to-Order Transitions
Santambrogio, C., Sperandeo, P., Villa, R., Sobott, F., Polissi, A., & Grandori, R. (2013) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-013-0687-9 · Cited by 33 · see citing works
Driving forces of translocation through bacterial translocon SecYEG.
Knyazev, D. G., Kuttner, R., Zimmermann, M., Sobakinskaya, E., & Pohl, P. (2018) · The Journal of Membrane Biology · doi:10.1007/s00232-017-0012-9 · Cited by 33 · see citing works
Elucidation of transient protein-protein interactions within carrier protein-dependent biosynthesis
Bartholow, T. G., Sztain, T., Patel, A., Lee, D. J., Young, M. A., Abagyan, R. A., & Burkart, M. D. (2021) · Communications Biology · doi:10.1038/s42003-021-01838-3 · Cited by 29 · see citing works
Structural basis of lipoprotein recognition by the bacterial Lol trafficking chaperone LolA
Kaplan, E., Greene, N. P., Jepson, A. E., & Koronakis, V. E. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2208662119 · Cited by 28 · see citing works
A Dynamic Network of Proteins Facilitate Cell Envelope Biogenesis in Gram-Negative Bacteria
Graham, C. L., Newman, H., Gillett, F. N., Smart, K., Briggs, N. S., Banzhaf, M., & Roper, D. I. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222312831 · Cited by 27 · see citing works
Bacteria use structural imperfect mimicry to hijack the host interactome
de Groot, N. S., & Torrent, M. (2020) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1008395 · Cited by 21 · see citing works
FabG: from a core to circumstantial catalyst
Shanbhag, A. P. (2019) · Biotechnology Letters · doi:10.1007/s10529-019-02678-2 · Cited by 20 · see citing works
Borrego, J. G., & Torrent, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911489 · Cited by 12 · see citing works
Steudle, A., Spann, D., Pross, E. K., Shanmugam, S. K., Dalbey, R., & Kühn, A. (2021) · Scientific Reports · doi:10.1038/s41598-021-83224-x · Cited by 10 · see citing works
HPIPred: Host–pathogen interactome prediction with phenotypic scoring
Rendón, J. M., Rios, R. R., & Torrent, M. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.11.026 · Cited by 10 · see citing works
A Novel Computational Approach for Identifying Essential Proteins From Multiplex Biological Networks
Zhao, B., Hu, S., Liu, X., Xiong, H., Han, X., Zhang, Z., Li, X., & Wang, L. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.00343 · Cited by 10 · see citing works
Launay, R., Teppa, E., Martins, C., Abby, S. S., Pierrel, F., André, I., & Esque, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231810323 · Cited by 9 · see citing works
Craven, S. J., Condon, S. G. F., & Senes, A. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.10.30.514410 · Cited by 9 · see citing works
van Teeseling, M. C. F. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.732031 · Cited by 8 · see citing works
Mslar: Microbial synthetic lethal and rescue database
Zhu, S.-B., Jiang, Q.-H., Chen, Z., Zhou, X. Y., Jin, Y.-T., Deng, Z., & Guo, F. (2023) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1011218 · Cited by 2 · see citing works
Flagged first, then by citations
2 of the 108 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Borrego, J. G., & Torrent, M. (2025) · Journal of Cheminformatics · doi:10.1186/s13321-025-01067-4 · Cited by 20 · see citing works
Structural Insights into the Lipopolysaccharide Transport (Lpt) System as a Novel Antibiotic Target
Yoon, Y., & Song, S. (2024) · The Journal of Microbiology · doi:10.1007/s12275-024-00137-w · Cited by 15 · see citing works
The ubiquitin ligase SINA3 and the transcription factor WOX14 regulate tomato growth and development
Yuan, Y., Li, H., Lu, H., Xia, C., Ramirez, C., Gao, M., Zhang, C., & Xiao, F. (2025) · The Plant Cell · doi:10.1093/plcell/koaf096 · Cited by 10 · see citing works
Mitochondrial Sorting and Assembly Machinery: Chaperoning a Moonlighting Role?
Ravi, R., Routray, D., & Mahalakshmi, R. (2025) · Biochemistry · doi:10.1021/acs.biochem.4c00727 · Cited by 7 · see citing works
Sakaguchi, T., Irifune, Y., Kamada, R., & Sakaguchi, K. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26199326 · Cited by 3 · see citing works
Rapid Proteome‐Wide Discovery of Protein–Protein Interactions With ppIRIS
Piochi, L. F., Tang, D., Malmström, J. A., Karami, Y., & Khakzad, H. (2026) · Advanced Science · doi:10.1002/advs.202521310 · Cited by 3 · see citing works
Liu, C., Duan, B., Chen, P., Jiang, Q., Wang, Y., Lu, L., Chen, Y., Hu, C., Zhang, L., & Guo, A. (2026) · eLife · doi:10.7554/elife.107677.4 · Cited by 3 · see citing works
Zhang, R., Zhu, X., Dong, L., Guo, C., & Shu, Y. (2026) · Plant Cell & Environment · doi:10.1111/pce.70408 · Cited by 2 · see citing works
Chen, L., Duan, B., Chen, P., Jiang, Q., Wang, Y., Lu, L., Chen, Y., Hu, C., Zhang, L., & Guo, A. (2025) · eLife · doi:10.7554/elife.107677 · Cited by 2 · see citing works
Chen, L., Duan, B., Chen, P., Jiang, Q., Wang, Y., Lu, L., Chen, Y., Hu, C., Zhang, L., & Guo, A. (2025) · eLife · doi:10.7554/elife.107677.1 · Cited by 2 · see citing works
Chen, L., Duan, B., Chen, P., Jiang, Q., Wang, Y., Lu, L., Chen, Y., Hu, C., Zhang, L., & Guo, A. (2026) · eLife · doi:10.7554/elife.107677.2 · Cited by 1 · see citing works
Saha, C. K., Roghanian, M., Häußler, S., & Guy, L. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.23.634437
Chen, L., Duan, B., Chen, P., Jiang, Q., Wang, Y., Lu, L., Chen, Y., Hu, C., Zhang, L., & Guo, A. (2026) · eLife · doi:10.7554/elife.107677.2.sa0
Chen, L., Duan, B., Chen, P., Jiang, Q., Wang, Y., Lu, L., Chen, Y., Hu, C., Zhang, L., & Guo, A. (2026) · eLife · doi:10.7554/elife.107677.3.sa0
Chen, L., Duan, B., Chen, P., Jiang, Q., Wang, Y., Lu, L., Chen, Y., Hu, C., Zhang, L., & Guo, A. (2026) · eLife · doi:10.7554/elife.107677.3
Zhang, R., Zhu, X., Xue, Y. J., Tang, X., Yao, Y., Cao, D., He, W., Guo, C., Liu, X. Y., & Shu, Y. (2026) · Journal of Agriculture and Food Research · doi:10.1016/j.jafr.2026.103139
Oka, G. U., Adan, W. C. D. S., Calomeno, C. V. A. Q., & de Souza, R. F. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.08.23.746524
- Authors
- Gómez Borrego, J., & Torrent Burgas, M.
- Affiliations
- Systems Biology of Infection Lab, Department of Biochemistry and Molecular Biology, Biosciences Faculty, Universitat Autònoma de Barcelona
- Venue
- eLife
- Publisher
- eLife Sciences Publications, Ltd
- Published
- 2024-01-16
- Volume
- 13
- ISSN
- 2050-084X (ISSN-L)
- PMC
- PMC10863985
- OpenAlex
- W4390909534
- Cited by
- 16
- References
- 108
- Citations by year
- 2026: 7 · 2025: 7 · 2024: 2
- FWCI
- 2.17
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- eLife (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Ministerio de Ciencia e Innovación (PDC2021-121544-I00, PID2020-114627RB-I00)
- European Society of Clinical Microbiology and Infectious Diseases (ESCMID2022)
- Generalitat de Catalunya (Joan Oró Fellowship 2023 FI-100278)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bioinformatics and Genomic Networks
- Keywords
- essential proteins, protein-protein interaction, protein complex formation, deletion mutants, AlphaFold2, protein structure prediction, antibiotic targets, protein stability
- MeSH terms
- Bacteria, Proteins, Computational Biology, Protein Interaction Mapping, Metabolic Networks and Pathways
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 ›
Are you an author, or do you see a problem with this page? Request a review