The SMC-family Wadjet complex protects bacteria from plasmid transformation by recognition and cleavage of closed-circular DNA

Fiji: an open-source platform for biological-image analysis

Schindelin, J., Arganda-Carreras, I., Frise, E., Kaynig, V., Longair, M., Pietzsch, T., Preibisch, S., Rueden, C., Saalfeld, S., Schmid, B., et al. (2012) · Nature Methods · doi:10.1038/nmeth.2019 · Cited by 66,890 · see citing works

UCSF Chimera—A visualization system for exploratory research and analysis

Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 45,260 · see citing works

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

Features and development of Coot

Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. D. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 27,510 · see citing works

ColabFold - Making protein folding accessible to all

Mirdita, M., Schütze, K., Moriwaki, Y., Heo, L., Ovchinnikov, S., & Steinegger, M. (2021) · doi:10.1101/2021.08.15.456425 · Cited by 9,391 · see citing works

UCSF ChimeraX : Structure visualization for researchers, educators, and developers

Pettersen, E. F., Goddard, T. D., Huang, C. C., Meng, E. C., Couch, G. S., Croll, T. I., Morris, J. H., & Ferrin, T. E. (2020) · Protein Science · doi:10.1002/pro.3943 · Cited by 9,327 · see citing works

cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination

Punjani, A., Rubinstein, J. L., Fleet, D. J., & Brubaker, M. A. (2017) · Nature Methods · doi:10.1038/nmeth.4169 · Cited by 9,168 · see citing works

MotionCor2 - anisotropic correction of beam-induced motion for improved cryo-electron microscopy

Zheng, S., Palovcak, E. J., Armache, J., Verba, K., Cheng, Y.-F., & Agard, D. (2017) · Nature Methods · doi:10.1038/nmeth.4193 · Cited by 7,678 · see citing works

Comparison of multiple Amber force fields and development of improved protein backbone parameters

Horn̆ák, V., Abel, R., Okur, A., Strockbine, B., Roitberg, A. E., & Simmerling, C. L. (2006) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21123 · Cited by 6,903 · see citing works

The PRIDE database resources in 2022: a hub for mass spectrometry-based proteomics evidences

Perez-Riverol, Y., Bai, J., Bandla, C., García-Seisdedos, D., Hewapathirana, S., Kamatchinathan, S., Kundu, D. J., Prakash, A., Frericks-Zipper, A., Eisenacher, M., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkab1038 · Cited by 6,125 · see citing works

MMseqs2 enables sensitive protein sequence searching for the analysis of massive data sets

Steinegger, M., & Söding, J. (2017) · Nature Biotechnology · doi:10.1038/nbt.3988 · Cited by 4,840 · see citing works

A cross-platform toolkit for mass spectrometry and proteomics

Chambers, M., MacLean, B., Burke, R., Amodei, D., Ruderman, D., Neumann, S., Gatto, L., Fischer, B., Pratt, B. S., Egertson, J. D., et al. (2012) · Nature Biotechnology · doi:10.1038/nbt.2377 · Cited by 4,038 · see citing works

Real-space refinement in PHENIX for cryo-EM and crystallography

Afonine, P., Poon, B., Read, R. J., Sobolev, O., Terwilliger, T., Urzhumtsev, A., & Adams, P. (2018) · bioRxiv · doi:10.1107/s2059798318006551 · Cited by 3,057 · see citing works

ISOLDE: a physically realistic environment for model building into low-resolution electron-density maps

Croll, T. (2018) · Acta Crystallographica Section D: Structural Biology · doi:10.1107/s2059798318002425 · Cited by 1,934 · see citing works

Meiosis-Specific DNA Double-Strand Breaks Are Catalyzed by Spo11, a Member of a Widely Conserved Protein Family

Keeney, S., Giroux, C. N., & Kleckner, N. E. (1997) · Cell · doi:10.1016/s0092-8674(00)81876-0 · Cited by 1,824 · see citing works

Positive-unlabeled convolutional neural networks for particle picking in cryo-electron micrographs

Bepler, T., Morin, A., Rapp, M., Brasch, J., Shapiro, L., Noble, A., & Berger, B. (2018) · Nature Methods · doi:10.1038/s41592-019-0575-8 · Cited by 1,455 · see citing works

DeepEMhancer: a deep learning solution for cryo-EM volume post-processing

Sánchez-García, R., Gómez-Blanco, J., Cuervo, A., Carazo, J., Sorzano, C. O., & Vargas, J. (2020) · Communications Biology · doi:10.1038/s42003-021-02399-1 · Cited by 1,341 · see citing works

Isolation and characterization of efficient plasmid transformation mutants of <i>Mycobacterium smegmatis</i>

Snapper, S. B., Melton, R. E., Mustafa, S., Kieser, T., & Jr, W. R. J. (1990) · Molecular Microbiology · doi:10.1111/j.1365-2958.1990.tb02040.x · Cited by 1,237 · 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

An atypical topoisomerase II from archaea with implications for meiotic recombination

Bergerat, A., de Massy, B., Gadelle, D., Varoutas, P.-C., Nicolas, A. G., & Forterre, P. (1997) · Nature · doi:10.1038/386414a0 · Cited by 948 · see citing works

DNA loop extrusion by human cohesin

Davidson, I. F., Bauer, B., Goetz, D., Tang, W., Wutz, G., & Peters, J.-M. (2019) · Science · doi:10.1126/science.aaz3418 · Cited by 863 · see citing works

Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency

Kapust, R. B., Tőzsér, J., Fox, J. D., Anderson, D. E., Cherry, S., Copeland, T. D., & Waugh, D. S. (2001) · Protein Engineering Design and Selection · doi:10.1093/protein/14.12.993 · Cited by 860 · see citing works

Real-time imaging of DNA loop extrusion by condensin

Ganji, M., Shaltiel, I. A., Bisht, S., Kim, E., Kalichava, A., Haering, C. H., & Dekker, C. (2018) · Science · doi:10.1126/science.aar7831 · Cited by 793 · see citing works

Human cohesin compacts DNA by loop extrusion

Kim, Y., Shi, Z., Zhang, H., Finkelstein, I. J., & Yu, H. (2019) · Science · doi:10.1126/science.aaz4475 · Cited by 701 · see citing works

DNA Modification and Restriction

Arber, W., & Linn, S. (1969) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.38.070169.002343 · Cited by 649 · see citing works

Diverse enzymatic activities mediate antiviral immunity in prokaryotes

Gao, L. A., Altae-Tran, H., Böhning, F., Makarova, K. S., Segel, M., Schmid-Burgk, J. L., Koob, J. G., Wolf, Y. I., Koonin, E. V., & Zhang, F. (2020) · Science · doi:10.1126/science.aba0372 · Cited by 612 · see citing works

Data Conversion with ProteoWizard msConvert

Adusumilli, R., & Mallick, P. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6747-6_23 · Cited by 609 · see citing works

The phage abortive infection system, ToxIN, functions as a protein–RNA toxin–antitoxin pair

Fineran, P. C., Blower, T. R., Foulds, I. J., Humphreys, D. P., Lilley, K. S., & Salmond, G. P. C. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808832106 · Cited by 574 · see citing works

The phage‐host arms race: Shaping the evolution of microbes

Stern, A., & Sorek, R. (2010) · BioEssays · doi:10.1002/bies.201000071 · Cited by 527 · see citing works

Genome folding through loop extrusion by SMC complexes

Davidson, I. F., & Peters, J. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00349-7 · Cited by 507 · see citing works

The Evolution and Ecology of Bacterial Warfare

Granato, E. T., Meiller-Legrand, T. A., & Foster, K. R. (2019) · Current Biology · doi:10.1016/j.cub.2019.04.024 · Cited by 496 · see citing works

An expanding arsenal of immune systems that protect bacteria from phages

(2022) · doi:10.1101/2022.05.11.491447 · Cited by 428 · see citing works

An expanded arsenal of immune systems that protect bacteria from phages

Millman, A., Melamed, S., Leavitt, A., Doron, S., Bernheim, A., Hör, J., Garb, J., Bechon, N., Brandis, A., Lopatina, A., et al. (2022) · Cell Host &amp; Microbe · doi:10.1016/j.chom.2022.09.017 · Cited by 428 · see citing works

Bacterial Retrons Function In Anti-Phage Defense

Millman, A., Bernheim, A. G., Stokar-Avihail, A., Fedorenko, T., Voichek, M., Leavitt, A., Oppenheimer‐Shaanan, Y., & Sorek, R. (2020) · Cell · doi:10.1016/j.cell.2020.09.065 · Cited by 406 · see citing works

The new gene mukB codes for a 177 kd protein with coiled‐coil domains involved in chromosome partitioning of E. coli.

Niki, H., Jaffé, A., Imamura, R., Ogura, T., & Hiraga, S. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07935.x · Cited by 405 · see citing works

Toprim--a conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins

Aravind, L. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.18.4205 · Cited by 401 · see citing works

DNA Modification and Restriction

Arber, W. (1974) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(08)60204-4 · Cited by 391 · see citing works

Structural Probing of a Protein Phosphatase 2A Network by Chemical Cross-Linking and Mass Spectrometry

Herzog, F., Kahraman, A., Boehringer, D., Mak, R., Bracher, A., Walzthoeni, T., Leitner, A., Beck, M., Hartl, F. U., Ban, N., et al. (2012) · Science · doi:10.1126/science.1221483 · Cited by 372 · see citing works

Multiscale Structuring of the E. coli Chromosome by Nucleoid-Associated and Condensin Proteins

Lioy, V. S., Cournac, A., Marbouty, M., Duigou, S., Mozziconacci, J., Espéli, O., Boccard, F., & Koszul, R. (2018) · Cell · doi:10.1016/j.cell.2017.12.027 · Cited by 343 · see citing works

Organization of Chromosomal DNA by SMC Complexes

Yatskevich, S., Rhodes, J., & Nasmyth, K. (2019) · Annual Review of Genetics · doi:10.1146/annurev-genet-112618-043633 · Cited by 337 · see citing works

Compaction and segregation of sister chromatids via active loop extrusion

Goloborodko, A. A., Imakaev, M., Marko, J. F., & Mirny, L. A. (2016) · eLife · doi:10.7554/elife.14864 · Cited by 317 · see citing works

Lysine-specific chemical cross-linking of protein complexes and identification of cross-linking sites using LC-MS/MS and the xQuest/xProphet software pipeline

Leitner, A., Walzthoeni, T., & Aebersold, R. H. (2013) · Nature Protocols · doi:10.1038/nprot.2013.168 · Cited by 275 · see citing works

In vivo Architecture and Action of Bacterial Structural Maintenance of Chromosome Proteins

Badrinarayanan, A., Reyes-Lamothe, R., Uphoff, S., Leake, M. C., & Sherratt, D. (2012) · Science · doi:10.1126/science.1227126 · Cited by 246 · see citing works

Bacterial chromosome organization and segregation

Badrinarayanan, A., Le, T., & Laub, M. (2015) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100814-125211 · Cited by 206 · see citing works

Structure and function of an archaeal topoisomerase VI subunit with homology to the meiotic recombination factor Spo11

Nichols, M. D., DeAngelis, K. M., Keck, J. L., & Berger, J. M. (1999) · The EMBO Journal · doi:10.1093/emboj/18.21.6177 · Cited by 200 · see citing works

Structure and Mechanism of a Cyclic Trinucleotide-Activated Bacterial Endonuclease Mediating Bacteriophage Immunity

Lau, R., Ye, Q., Birkholz, E. A., Berg, K. R., Patel, L., Mathews, I. T., Watrous, J. D., Ego, K. M., Whiteley, A. T., Lowey, B., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2019.12.010 · Cited by 199 · see citing works

Cryo-EM structure of the human cohesin-NIPBL-DNA complex

Shi, Z.-B., Gao, H.-S., Bai, X.-C., & Yu, H.-T. (2020) · Science · doi:10.1126/science.abb0981 · Cited by 196 · see citing works

Xlink Analyzer: Software for analysis and visualization of cross-linking data in the context of three-dimensional structures

Kosiński, J., von Appen, A., Ori‬‬, A., Karius, K., Müller, C. W., & Beck, M. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.01.014 · Cited by 163 · see citing works

MukB colocalizes with the oriC region and is required for organization of the two Escherichia coli chromosome arms into separate cell halves

Danilova, O., Reyes‐Lamothe, R., Pinskaya, M., Sherratt, D. J., & Possoz, C. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05881.x · Cited by 158 · see citing works

Structural studies of a bacterial condensin complex reveal ATP-dependent disruption of intersubunit interactions.

Woo, J.-S., Lim, J.-H., Shin, H.-C., Suh, M., Ku, B., Lee, K.-H., Joo, K., Robinson, H., Lee, J., Park, S.-Y., et al. (2009) · Cell · doi:10.1016/j.cell.2008.10.050 · Cited by 147 · see citing works

The Smc5/6 Complex: New and Old Functions of the Enigmatic Long-Distance Relative

Aragón, L. (2018) · Annual Review of Genetics · doi:10.1146/annurev-genet-120417-031353 · Cited by 147 · see citing works

Rad50-CARD9 interactions link cytosolic DNA sensing to IL-1β production

Roth, S., Rottach, A., Lotz-Havla, A. S., Laux, V., Muschaweckh, A., Gersting, S. W., Muntau, A. C., Hopfner, K., Jin, L., Vanness, K., et al. (2014) · Nature Immunology · doi:10.1038/ni.2888 · Cited by 138 · see citing works

The Smc5/6 complex is a DNA loop-extruding motor

Pradhan, B., Kanno, T., Igarashi, M. U., Loke, M. S., Baaske, M. D., Wong, J. S. K., Jeppsson, K. E., Björkegren, C., & Kim, E. (2023) · Nature · doi:10.1038/s41586-023-05963-3 · Cited by 136 · see citing works

Two defence systems eliminate plasmids from seventh pandemic Vibrio cholerae

Jaskólska, M., Adams, D. W., & Blokesch, M. (2022) · Nature · doi:10.1038/s41586-022-04546-y · Cited by 134 · see citing works

<i>xVis</i>: a web server for the schematic visualization and interpretation of crosslink-derived spatial restraints

Grimm, M., Zimniak, T., Kahraman, A., & Herzog, F. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv463 · Cited by 121 · see citing works

A hold-and-feed mechanism drives directional DNA loop extrusion by condensin

Shaltiel, I. A., Datta, S., Lecomte, L., Hassler, M., Kschonsak, M., Bravo, S., Stober, C., Ormanns, J., Eustermann, S., & Haering, C. H. (2022) · Science · doi:10.1126/science.abm4012 · Cited by 112 · see citing works

Holoenzyme assembly and ATP-mediated conformational dynamics of topoisomerase VI

Corbett, K. D., Benedetti, P., & Berger, J. M. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1264 · Cited by 104 · see citing works

Organization of the Escherichia coli Chromosome by a MukBEF Axial Core

Mäkelä, J., & Sherratt, D. (2020) · Molecules and Cells · doi:10.1016/j.molcel.2020.02.003 · Cited by 90 · see citing works

A new family of bacterial condensins

Petrushenko, Z. M., She, W., & Rybenkov, V. V. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07763.x · Cited by 83 · see citing works

Chromosome organization by a conserved condensin-ParB system in the actinobacterium Corynebacterium glutamicum

Böhm, K., Giacomelli, G., Schmidt, A., Imhof, A., Koszul, R., Marbouty, M., & Bramkamp, M. (2019) · Nature Communications · doi:10.1038/s41467-020-15238-4 · Cited by 75 · see citing works

Cryo-EM structure of MukBEF reveals DNA loop entrapment at chromosomal unloading sites

Bürmann, F., Funke, L. F. H., Chin, J. W., & Löwe, J. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.10.011 · Cited by 74 · see citing works

Crystal Structure of an Intact Type II DNA Topoisomerase: Insights into DNA Transfer Mechanisms

Graille, M., Cladière, L., Christiane, D. D., Lecointe, F., Gadelle, D., Quevillon‐Chéruel, S., Vachette, P., Forterre, P., & TILBEURGH, H. V. (2008) · Structure · doi:10.1016/j.str.2007.12.020 · Cited by 73 · see citing works

The MukF subunit of Escherichia coli condensin: architecture and functional relationship to kleisins

Fennell-Fezzie, R., Gradia, S., Akey, D. L., & Berger, J. M. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600680 · Cited by 70 · see citing works

Structural characterization of Class 2 OLD family nucleases supports a two-metal catalysis mechanism for cleavage

Schiltz, C. J., Lee, A., Partlow, E. A., Hosford, C. J., & Chappie, J. S. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz703 · Cited by 66 · see citing works

Noncanonical SMC protein in <i>Mycobacterium smegmatis</i> restricts maintenance of <i>Mycobacterium fortuitum</i> plasmids

Panas, M. W., Jain, P., Yang, H., Mitra, S., Biswas, D., Wattam, A. R., Letvin, N. L., & Jacobs, W. R. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1414207111 · Cited by 62 · see citing works

Cargo Genes of Tn 7 -Like Transposons Comprise an Enormous Diversity of Defense Systems, Mobile Genetic Elements, and Antibiotic Resistance Genes

Benler, S., Faure, G., Tran, H.-A., Shmakov, S., Zheng, F., & Koonin, E. (2021) · mBio · doi:10.1128/mbio.02938-21 · Cited by 61 · see citing works

Distinct Activities of Bacterial Condensins for Chromosome Management in Pseudomonas aeruginosa

Lioy, V. S., Junier, I., Lagage, V., Vallet-Gély, I., & Boccard, F. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108344 · Cited by 58 · see citing works

Clamping of DNA shuts the condensin neck gate

Lee, B.-G., Rhodes, J., & Löwe, J. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2120006119 · Cited by 49 · see citing works

SMC complexes organize the bacterial chromosome by lengthwise compaction

Mäkelä, J., & Sherratt, D. J. (2020) · Current Genetics · doi:10.1007/s00294-020-01076-w · Cited by 39 · see citing works

Engineering a Minimal Cloning Vector from a pUC18 Plasmid Backbone with an Extended Multiple Cloning Site

Staal, J., Alci, K., Schamphelaire, W. D., Vanhoucke, M., & Beyaert, R. (2019) · BioTechniques · doi:10.2144/btn-2019-0014 · Cited by 24 · see citing works

Dynamic architecture of the Escherichia coli structural maintenance of chromosomes (SMC) complex, MukBEF

Rajasekar, K. V., Baker, R., Fisher, G. L. M., Bolla, J. R., Mäkelä, J., Tang, M., Zawadzka, K., Koczy, O., Wagner, F., Robinson, C. V., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz696 · Cited by 20 · see citing works

Alternating Dynamics of oriC , SMC, and MksBEF in Segregation of Pseudomonas aeruginosa Chromosome

Zhao, H., Bhowmik, B. K., Petrushenko, Z. M., & Rybenkov, V. V. (2020) · mSphere · doi:10.1128/msphere.00238-20 · Cited by 13 · see citing works

The highly diverse antiphage defence systems of bacteria

Georjon, H., & Bernheim, A. G. (2023) · Nature Reviews Microbiology · doi:10.1038/s41579-023-00934-x · Cited by 516 · see citing works

Mycobacterium smegmatis: The Vanguard of Mycobacterial Research

Sparks, I. L., Derbyshire, K. M., Jacobs, W. R., & Morita, Y. S. (2023) · Journal of Bacteriology · doi:10.1128/jb.00337-22 · Cited by 149 · see citing works

Genome control by SMC complexes

Hoencamp, C., & Rowland, B. D. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00609-8 · Cited by 138 · see citing works

A host of armor: Prokaryotic immune strategies against mobile genetic elements

Mayo-Muñoz, D., Pinilla‐Redondo, R., Birkholz, N., & Fineran, P. C. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112672 · Cited by 99 · see citing works

A Comprehensive Resource for Exploring Antiphage Defense: DefenseFinder Webservice,Wiki and Databases

Tesson, F., Planel, R., Egorov, A. A., Georjon, H., Vaysset, H., Brancotte, B., Néron, B., Mordret, E., Atkinson, G. C., Bernheim, A., et al. (2024) · Peer Community Journal · doi:10.24072/pcjournal.470 · Cited by 120 · see citing works

How do interactions between mobile genetic elements affect horizontal gene transfer?

Horne, T., Orr, V. T., & Hall, J. P. J. (2023) · Current Opinion in Microbiology · doi:10.1016/j.mib.2023.102282 · Cited by 98 · see citing works

Evolution of triclosan resistance modulates bacterial permissiveness to multidrug resistance plasmids and phages

Yang, Q., Ma, X., Li, M., Zhao, M., Zeng, L., He, M., Deng, H., Liao, H., Rensing, C., Friman, V., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-48006-9 · Cited by 80 · see citing works

A virally encoded tRNA neutralizes the PARIS antiviral defence system

Burman, N., Belukhina, S., Depardieu, F., Wilkinson, R. A., Skutel, M. A., Santiago‐Frangos, A., Graham, A. B., Livenskyi, A., Chechenina, A., Morozova, N. E., et al. (2024) · Nature · doi:10.1038/s41586-024-07874-3 · Cited by 88 · see citing works

Prokaryotic Gabija complex senses and executes nucleotide depletion and DNA cleavage for antiviral defense

Cheng, R., Huang, F., Lu, X., Yan, Y., Yu, B., Wang, X., & Zhu, B. (2023) · Cell Host & Microbe · doi:10.1016/j.chom.2023.06.014 · Cited by 69 · see citing works

Architecture and activation mechanism of the bacterial PARIS defence system

Deep, A., Liang, Q., Enüstün, E., Pogliano, J., & Corbett, K. D. (2024) · Nature · doi:10.1038/s41586-024-07772-8 · Cited by 68 · see citing works

DNA end sensing and cleavage by the Shedu anti-phage defense system

Loeff, L., Walter, A., Rosalen, G. T., & Jinek, M. (2025) · Cell · doi:10.1016/j.cell.2024.11.030 · Cited by 56 · see citing works

Improved Multimer Prediction using Massive Sampling with AlphaFold in CASP15

Wallner, B. (2023) · doi:10.22541/au.168170986.60158084/v1 · Cited by 53 · see citing works

DNA-measuring Wadjet SMC ATPases restrict smaller circular plasmids by DNA cleavage

Liu, H. W., Roisné-Hamelin, F., Beckert, B., Li, Y., Myasnikov, A., & Gruber, S. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.11.015 · Cited by 53 · see citing works

Improved multimer prediction using massive sampling with <scp>AlphaFold</scp> in <scp>CASP15</scp>

Wallner, B. (2023) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.26562 · Cited by 53 · see citing works

The impact of <scp>AI</scp> ‐based modeling on the accuracy of protein assembly prediction: Insights from <scp>CASP15</scp>

Ozden, B., Kryshtafovych, A., & Karaca, E. (2023) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.26598 · Cited by 51 · see citing works

Unraveling the role of mobile genetic elements in antibiotic resistance transmission and defense strategies in bacteria

Kumavath, R., Gupta, P., Tatta, E. R., Mohan, M. S., Salim, S. A., & Busi, S. (2025) · Frontiers in Systems Biology · doi:10.3389/fsysb.2025.1557413 · Cited by 55 · see citing works

Multiple enzymatic activities of a Sir2-HerA system cooperate for anti-phage defense

Tang, D., Chen, Y., Chen, H., Jia, T., Chen, Q., & Yu, Y. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.11.010 · Cited by 45 · see citing works

Evolution and ecology of anti-defence systems in phages and plasmids

Niault, T., van Houte, S., Westra, E. R., & Swarts, D. C. (2025) · Current Biology · doi:10.1016/j.cub.2024.11.033 · Cited by 48 · see citing works

A unified model for cohesin function in sister chromatid cohesion and chromatin loop formation

Uhlmann, F. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.02.005 · Cited by 44 · see citing works

Defence systems and horizontal gene transfer in bacteria

Kogay, R., Wolf, Y. I., & Koonin, E. V. (2024) · Environmental Microbiology · doi:10.1111/1462-2920.16630 · Cited by 43 · see citing works

Conserved domains can be found across distinct phage defence systems

Mariano, G., & Blower, T. R. (2023) · Molecular Microbiology · doi:10.1111/mmi.15047 · Cited by 40 · see citing works

The extended mobility of plasmids

Garcillán-Barcia, M. P., de la Cruz, F., & Rocha, E. P. C. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf652 · Cited by 39 · see citing works

Molecular mechanism of plasmid elimination by the DdmDE defense system

(2024) · doi:10.1126/science.adq0534 · Cited by 38 · see citing works

Loop-extrusion-mediated plasmid DNA cleavage by the bacterial SMC Wadjet complex

Pradhan, B., Deep, A., König, J., Baaske, M. D., Corbett, K. D., & Kim, E. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.11.002 · Cited by 35 · see citing works

Structural biology of SMC complexes across the tree of life

Burmann, F., & Löwe, J. (2023) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2023.102598 · Cited by 29 · see citing works

Assessment of the assessment—All about complexes

Studer, G., Tauriello, G., & Schwede, T. F. (2023) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26612 · Cited by 31 · see citing works

Structural basis for plasmid restriction by SMC JET nuclease

Roisné-Hamelin, F., Liu, H. W., Taschner, M., Li, Y., & Gruber, S. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.01.009 · Cited by 34 · see citing works

The MksG nuclease is the executing part of the bacterial plasmid defense system MksBEFG

Weiß, M., Giacomelli, G., Assaya, M. B., Grundt, F., Haouz, A., Peng, F., Petrella, S., Wehenkel, A. M., & Bramkamp, M. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad130 · Cited by 37 · see citing works

Multi-layered genome defences in bacteria

Agapov, A., Baker, K. S., Bedekar, P., Bhatia, R. P., Blower, T. R., Brockhurst, M. A., Brown, C., Chong, C. E., Fothergill, J. L., Graham, S., et al. (2024) · Current Opinion in Microbiology · doi:10.1016/j.mib.2024.102436 · Cited by 33 · see citing works

SMC-based immunity against extrachromosomal DNA elements

Liu, H. W., Roisné-Hamelin, F., & Gruber, S. (2023) · Biochemical Society Transactions · doi:10.1042/bst20221395 · Cited by 31 · see citing works

Phage selection drives resistance–virulence trade-offs in Ralstonia solanacearum plant-pathogenic bacterium irrespective of the growth temperature

Wang, J., Wang, X., Yang, K., Lu, C., Fields, B., Xu, Y., Shen, Q., Wei, Z., & Friman, V. (2023) · Evolution Letters · doi:10.1093/evlett/qrad056 · Cited by 28 · see citing works

DNA glycosylases provide antiviral defence in prokaryotes

Hossain, A. A., Pigli, Y. Z., Baca, C. F., Heissel, S., Thomas, A., Libis, V. K., Burian, J., Chappie, J. S., Brady, S. F., Rice, P. A., et al. (2024) · Nature · doi:10.1038/s41586-024-07329-9 · Cited by 27 · see citing works

Everything OLD is new again: How structural, functional, and bioinformatic advances have redefined a neglected nuclease family

Dot, E. W. I., Thomason, L. C., & Chappie, J. S. (2023) · Molecular Microbiology · doi:10.1111/mmi.15074 · Cited by 27 · see citing works

The SMC5/6 complex: folding chromosomes back into shape when genomes take a break

Roy, S., Adhikary, H., & D’Amours, D. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae103 · Cited by 24 · see citing works

Correlation of Pseudomonas aeruginosa Phage Resistance with the Numbers and Types of Antiphage Systems

Burke, K. A., Urick, C. D., Mzhavia, N., Nikolich, M. P., & Filippov, A. A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031424 · Cited by 24 · see citing works

Genomic characterization of the antiviral arsenal of Actinobacteria

Georjon, H., Tesson, F., Shomar, H., & Bernheim, A. G. (2023) · Microbiology · doi:10.1099/mic.0.001374 · Cited by 21 · see citing works

A synthetic biology approach to assemble and reboot clinically relevant Pseudomonas aeruginosa tailed phages

Ipoutcha, T., Racharaks, R., Huttelmaier, S., Wilson, C., Ozer, E. A., & Hartmann, E. M. (2024) · Microbiology Spectrum · doi:10.1128/spectrum.02897-23 · Cited by 20 · see citing works

DdmABC-dependent death triggered by viral palindromic DNA sequences

Robins, W. P., Meader, B. T., Toska, J., & Mekalanos, J. J. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114450 · Cited by 20 · see citing works

Toward Microbiome Engineering: Expanding the Repertoire of Genetically Tractable Members of the Human Gut Microbiome

Marsh, J. W., Kirk, C., & Ley, R. E. (2023) · Annual Review of Microbiology · doi:10.1146/annurev-micro-032421-112304 · Cited by 19 · see citing works

Using Cupriavidus necator H16 to Provide a Roadmap for Increasing Electroporation Efficiency in Nonmodel Bacteria

Vajente, M., Clerici, R., Ballerstedt, H., Blank, L. M., & Schmidt, S. (2024) · ACS Synthetic Biology · doi:10.1021/acssynbio.4c00380 · Cited by 18 · see citing works

Insights in bacterial genome folding.

Yáñez-Cuna, F. O., & Koszul, R. (2023) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2023.102679 · Cited by 12 · see citing works

Genome engineering of the human gut microbiome

Zheng, L., Shen, J., Chen, R., Hu, Y., Zhao, W., Leung, E. L., & Dai, L. (2024) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2024.01.002 · Cited by 17 · see citing works

To split or not to split: CASP15 targets and their processing into tertiary structure evaluation units

Kryshtafovych, A., & Rigden, D. J. (2023) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26533 · Cited by 13 · see citing works

The immune system of prokaryotes: potential applications and implications for gene editing

Liu, S. M., Liu, H., Wang, X., & Shi, L. (2024) · Biotechnology Journal · doi:10.1002/biot.202300352 · Cited by 15 · see citing works

OLD family nuclease function across diverse anti-phage defense systems

Akritidou, K., & Thurtle-Schmidt, B. H. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2023.1268820 · Cited by 13 · see citing works

An enterococcal phage protein inhibits type IV restriction enzymes involved in antiphage defense

Bullen, N. P., Johnson, C. N., Andersen, S. E., Arya, G., Marotta, S. R., Lee, Y.-J., Weigele, P. R., Whitney, J. C., & Duerkop, B. A. (2024) · Nature Communications · doi:10.1038/s41467-024-51346-1 · Cited by 13 · see citing works

Nucleic acid recognition during prokaryotic immunity

Baca, C. F., & Marraffini, L. A. (2025) · Molecular Cell · doi:10.1016/j.molcel.2024.12.007 · Cited by 13 · see citing works

Recent advances and challenges in protein complex model accuracy estimation

Liang, F., Sun, M., Xie, L., Zhao, X., Liu, D., Zhao, K., & Zhang, G. (2024) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2024.04.049 · Cited by 15 · see citing works

Mechanism of DNA capture by the MukBEF SMC complex and its inhibition by a viral DNA mimic

Bürmann, F., Clifton, B., Koekemoer, S., Wilkinson, O. J., Kimanius, D., Dillingham, M. S., & Löwe, J. (2025) · Cell · doi:10.1016/j.cell.2025.02.032 · Cited by 12 · see citing works

Structural basis of antiphage defence by an ATPase-associated reverse transcriptase

George, J. T., Burman, N., Wilkinson, R. A., de Silva, S., McKelvey-Pham, Q., Buyukyoruk, M., Dale, A., Landman, H., Graham, A. B., DeLuca, S. Z., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-63285-6 · Cited by 14 · see citing works

Characterization of the conserved features of the NSE6 subunit of the Physcomitrium patens SMC5 /6 complex

Lelkes, E., Vaculíková, J., Holá, M., Štefanovie, B., Kolesár, P., Vágnerová, R., Tomaštíková, E. D., Pečinka, A., Angelis, K. J., & Palecek, J. J. (2023) · The Plant Journal · doi:10.1111/tpj.16282 · Cited by 11 · see citing works

Architecture and infection-sensing mechanism of the bacterial PARIS defense systemPreprint

Deep, A., Liang, Q., Enüstün, E., Pogliano, J., & Corbett, K. D. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.01.02.573835 · Cited by 11 · see citing works

Viral proteins activate PARIS-mediated tRNA degradation and viral tRNAs rescue infectionPreprint

Burman, N., Belukhina, S., Depardieu, F., Wilkinson, R. A., Skutel, M. A., Santiago‐Frangos, A., Graham, A. B., Livenskyi, A., Chechenina, A., Morozova, N. E., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.01.02.573894 · Cited by 11 · see citing works

Distribution of bacterial DNA repair proteins and their co-occurrence with immune systems

Mutte, S. K., Barendse, P., Ugarte, P. B., & Swarts, D. C. (2025) · Cell Reports · doi:10.1016/j.celrep.2024.115110 · Cited by 10 · see citing works

Structural and functional investigation of GajB protein in Gabija anti-phage defense

Oh, H., Koo, J., An, S. Y., Hong, S.-H., Suh, J., & Bae, E. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad951 · Cited by 10 · see citing works

With a pinch of salt: metagenomic insights into Namib Desert salt pan microbial mats and halites reveal functionally adapted and competitive communities

Martínez-Álvarez, L., Ramond, J., Vikram, S., León‐Sobrino, C., Maggs‐Kölling, G., & Cowan, D. A. (2023) · Applied and Environmental Microbiology · doi:10.1128/aem.00629-23 · Cited by 10 · see citing works

Structural basis of the RNA-mediated Retron-Eco2 oligomerization

Wang, Y., Wang, C., Yin, Y., Cui, Y., Dai, Z., Liu, C., Chen, Y., Guan, Z., & Zou, T. (2025) · Cell Discovery · doi:10.1038/s41421-025-00823-y · Cited by 14 · see citing works

The SMC Hinge is a Selective Gate for Obstacle Bypass

Liu, H. W., Roisné-Hamelin, F., Taschner, M., Collier, J., Srinivasan, M., & Gruber, S. (2025) · Nature Communications · doi:10.1038/s41467-025-65408-5 · Cited by 11 · see citing works

Knowing Our Enemy in the Antimicrobial Resistance Era: Dissecting the Molecular Basis of Bacterial Defense Systems

Martínez, M., Rizzuto, I., & Molina, R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25094929 · Cited by 8 · see citing works

Architecture and mechanism of a dual-enzyme retron system in prokaryotic immunity

Li, X., He, Q., Liu, Y., Liu, B., Liu, Z., Chen, H., Zhang, S., Han, J., Liu, Y., Yang, J., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-67175-9 · Cited by 8 · see citing works

Replisomes restrict SMC translocation in vivo

Liao, Q., Brandão, H. B., Ren, Z., & Wang, X.-D. (2025) · Nature Communications · doi:10.1038/s41467-025-62596-y · Cited by 6 · see citing works

Bacterial WYL domain transcriptional repressors sense single-stranded DNA to control gene expression

Blankenchip, C. L., & Corbett, K. D. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae1101 · Cited by 6 · see citing works

Diverse defense systems and prophages in human-associated Bifidobacterium species reveal coevolutionary “arms race” dynamics

Docherty, J. A. D., Cook, R., Kiu, R., Dyball, X., Brown, T. L., Kujawska, M., Smith, R.-L., Phillips, S., Watt, R., Telatin, A., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116542 · Cited by 6 · see citing works

Genome Analysis of Anti-Phage Defense Systems and Defense Islands in Stenotrophomonas maltophilia: Preservation and Variability

Jdeed, G., Витальевна, М. В., & Викторовна, Т. Н. (2024) · Viruses · doi:10.3390/v16121903 · Cited by 6 · see citing works

The ecology of horizontal gene transfer.

Etten, J. V., & Johnson, M. D. (2026) · Trends in Genetics · doi:10.1016/j.tig.2026.02.002 · Cited by 2 · see citing works

Structural Maintenance of Chromosomes Complexes

Jeppsson, K. E. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-4136-1_2 · Cited by 4 · see citing works

4G cloning: rapid gene assembly for expression of multisubunit protein complexes in diverse hosts

Taschner, M., Dickinson, J. B., Roisné-Hamelin, F., & Gruber, S. (2024) · Life Science Alliance · doi:10.26508/lsa.202402899 · Cited by 5 · see citing works

Reduced prevalence of phage defense systems in Pseudomonas aeruginosa strains from cystic fibrosis patients

van den Berg, D. F., & Brouns, S. J. J. (2025) · mBio · doi:10.1128/mbio.03548-24 · Cited by 5 · see citing works

Exploring the eco-evolutionary role of plasmids and defense systems in ‘Fervidacidithiobacillus caldus’ extreme acidophile

Pacheco-Acosta, S., Castro-Toro, G., Rojas-Villalobos, C., Valenzuela, C., Haristoy, J. J., Zapata-Araya, A., Moya-Beltrán, A., Sepúlveda-Rebolledo, P., Pérez‐Rueda, E., Ulloa, R. J., et al. (2025) · Frontiers in Microbiology · doi:10.3389/fmicb.2025.1610279 · Cited by 4 · see citing works

A nuclease domain fused to the Snf2 helicase confers antiphage defence in coral‐associated Halomonas meridiana

Liu, T., Gao, X., Chen, R., Tang, K., Liu, Z., Wang, P., & Wang, X. (2024) · Microbial Biotechnology · doi:10.1111/1751-7915.14524 · Cited by 4 · see citing works

Structure of a type II SMC Wadjet complex from Neobacillus vireti

(2025) · doi:10.1016/j.str.2025.06.004 · Cited by 4 · see citing works

Synthetically designed anti-defense proteins overcome barriers to bacterial transformation and phage infection

Garb, J., Adams, D. W., Yardeni, E. H., Blokesch, M., & Sorek, R. (2026) · Nature Communications · doi:10.1038/s41467-026-74301-8 · Cited by 4 · see citing works

An update on Escalating Drug Resistance among Uropathogenic Bacteria: Challenges in Treatment and Scope for Maneuver

Asim, M., Rizvi, S. A., Ahmed, V., & Haq, Q. M. R. (2026) · Current Microbiology · doi:10.1007/s00284-026-04813-5 · Cited by 3 · see citing works

Structural and bioinformatics analyses identify deoxydinucleotide-specific nucleases and their association with genomic islands in gram-positive bacteria

Mortensen, S., Kuncová, S., Lormand, J. D., Myers, T. M., Kim, S.-K., Lee, V. T., Winkler, W. C., & Sondermann, H. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae1235 · Cited by 2 · see citing works

Bulleidia extructa PP_925: Genome Reduction, Minimalist Metabolism, and Evolutionary Insights into Firmicutes Diversification

Evseev, P., Podoprigora, I., Chaplin, A., Khabadze, Z., Malkov, A. A., Kafarskaia, L. I., Shagin, D., Urban, Y., Borisova, O., & Efimov, B. A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms27010448 · Cited by 2 · see citing works

Supercoiled DNA recognition and cleavage control in topoisomerase VI

Richman, D. E., Wendorff, T. J., Rashid, F., Beck, C., Yan, Q., Johnson, H. R., Eckerty, R. A., Fogg, J. M., Baker, M. L., Zechiedrich, L., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-69491-0 · Cited by 5 · see citing works

Mechanism of DNA entrapment by a loop-extruding Wadjet SMC motor

Roisné-Hamelin, F., Liu, H. W., Marechal, N., Uchikawa, E., Durand, A., & Gruber, S. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.09.015 · Cited by 2 · see citing works

Genetic conflicts in budding yeast: The 2μ plasmid as a model selfish element

Hays, M. (2024) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2024.04.002 · Cited by 2 · see citing works

Defense systems and horizontal gene transfer in bacteriaPreprint

Kogay, R., Wolf, Y. I., & Koonin, E. V. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.02.09.579689 · Cited by 2 · see citing works

Structural basis of antiphage defense by an ATPase-associated reverse transcriptasePreprint

George, J. T., Burman, N., Wilkinson, R. A., de Silva, S., McKelvey-Pham, Q., Buyukyoruk, M., Dale, A., Landman, H., Graham, A. B., DeLuca, S. Z., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.26.645336 · Cited by 2 · see citing works

SMC-like Wadjet system prevents plasmid transfer into Clostridium cellulovorans

Schöllkopf, A. I., Ehrenreich, A., & Liebl, W. (2025) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-025-13551-w · Cited by 1 · see citing works

Abundant bacterial nucleoid-associated protein H-NS limits plasmid transfer through mechanical modification of DNA

Fei, M., Fang, M., Zhou, Q., Chen, Z., Gong, M., Wu, F., Tian, C. F., & Sun, D. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf928 · Cited by 1 · see citing works

Antiplasmid systems: a novel strategy to combat antibiotic resistance

Asim, M., Rizvi, S. A., & Haq, Q. M. R. (2025) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkaf472 · Cited by 1 · see citing works

The balance between defence systems and horizontal gene transfer shapes adaptation in clinical strains of Acinetobacter spp

Muthuraman, V., Roy, P., Dean, P., Lopes, B. S., & Shehreen, S. (2026) · Journal of Applied Microbiology · doi:10.1093/jambio/lxag069 · Cited by 1 · see citing works

Insights into the Arms Race between Prokaryotic Hosts and Their Viruses in Mangrove Ecosystem

Gu, C., Gu, J., Li, J., Zou, D., Qi, Y., Xia, R., Zhou, Z., & Li, M. (2026) · Environmental Science & Technology · doi:10.1021/acs.est.5c14802 · Cited by 1 · see citing works

Structural and Functional Features of Bacterial SMC Complexes

Morozova, N. E., Potysyeva, A. S., & Vedyaykin, A. D. (2023) · Tsitologiya · doi:10.31857/s004137712306007x · Cited by 1 · see citing works

Properties of the Ureaplasma parvum structural maintenance of chromosomes protein related to its interaction with DNA

Rumyantseva, N. A., Shutov, V. M., Belenkaia, D. G., Alekseev, A. A., Morozova, N. E., & Vedyaykin, A. D. (2025) · FEMS Microbiology Letters · doi:10.1093/femsle/fnaf010 · Cited by 1 · see citing works

DNA Bioconjugation with Polymer Beads Using SNAP-tag® Technology

Liu, H. W., & Gruber, S. (2025) · Methods in molecular biology · doi:10.1007/978-1-0716-5005-9_6 · Cited by 1 · see citing works

Genomic landscape of antiviral defense systems in prokaryotes and phagesPreprint

Li, J., Gu, J., Xia, R., & Li, M. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.26.620412 · Cited by 1 · see citing works

Barriers to Antimicrobial Resistance Gene Exchange in Methicillin Resistant Staphylococcus aureus Cluster into Transfer IslandsPreprint

Wildfire, J., Maree, M., Mallinson, S. R., Witney, A. A., Knight, G. M., & Lindsay, J. A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.19.694131 · Cited by 1 · see citing works

Disruption of SMC-related genes promotes recombinant cholesterol esterase production in Burkholderia stabilis

Konishi, K., Yasutake, Y., Muramatsu, S., Murata, S., Yoshida, K., Ishiya, K., Aburatani, S., Sakasegawa, S., & Tamura, T. (2022) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-022-12277-3

The Impact of AI-Based Modeling on the Accuracy of Protein Assembly Prediction: Insights from CASP15Preprint

Karaca, E., Ozden, B., & Kryshtafovych, A. (2023) · doi:10.22541/au.168897262.26176460/v1

Properties of the Ureaplasma parvum SMC protein related to its interaction with DNAPreprint

Rumyantseva, N. A., Shutov, V. M., Belenkaia, D. G., Alekseev, A. A., Morozova, N. E., & Vedyaykin, A. D. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.04.14.589448

Organization and Role of Bacterial SMC, MukBEF, MksBEF, Wadjet, and RecN Complexes

Morozova, N. E., Potysyeva, A. S., & Vedyaykin, A. D. (2024) · Cell and Tissue Biology · doi:10.1134/s1990519x23700074

A novel strategy to protect prokaryotic cells from virus infection

Ishino, Y. (2024) · Engineering Microbiology · doi:10.1016/j.engmic.2024.100153

Plasmidome-defensome interactions drive adaptation of ‘ Fervidacidithiobacillus caldus’ in natural and industrial extreme acidic environmentsPreprint

Pacheco-Acosta, S., Castro-Toro, G., Rojas-Villalobos, C., Valenzuela, C., Haristoy, J. J., Zapata-Araya, A., Moya-Beltrán, A., Sepúlveda-Rebolledo, P., Pérez‐Rueda, E., Ulloa, R. J., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.02.646953

Adaptive trade-offs between niche-driven defence system selection and horizontal gene transfer suggests clinical success in Acinetobacter sppPreprint

Muthuraman, V., Roy, P., Dean, P., Lopes, B. S., & Shehreen, S. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.01.668115

Wadjet—Keeping a watchful eye on circular DNA

Corbett, K. D., & Deep, A. (2025) · Structure · doi:10.1016/j.str.2025.08.006 · Cited by 1 · see citing works

MksEF Accessory Proteins Inhibit MksB ATPase Activity and Modulate DNA Substrate Binding

Kumari, P., C, S., Biswas, T., Hegde, V., Appaiah, U., Prasad, M. D., Sharan, K., Patra, D., & Kumar, R. (2025) · Biochemistry · doi:10.1021/acs.biochem.5c00151

Weaving the loops of life: DNA loading by loop-extrusion machines in plasmid defense and genome organization

Bramkamp, M. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.10.014

Loop-extrusion-mediated plasmid DNA cleavage by the bacterial SMC Wadjet complex

Pradhan, B., Deep, A., König, J., Baaske, M. D., Corbett, K. D., & Kim, E. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.11.002 · Cited by 35 · see citing works

DNA-measuring Wadjet SMC ATPases restrict smaller circular plasmids by DNA cleavage

Liu, H. W., Roisné-Hamelin, F., Beckert, B., Li, Y., Myasnikov, A., & Gruber, S. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.11.015 · Cited by 53 · see citing works

Wadjet—Keeping a watchful eye on circular DNA

Corbett, K. D., & Deep, A. (2025) · Structure · doi:10.1016/j.str.2025.08.006 · Cited by 1 · see citing works

Structural basis for plasmid restriction by SMC JET nuclease

Liu, H. W. (2024) · Data Archiving and Networked Services (DANS) · doi:10.17632/htskytjh6v

Wadjet in a eukaryotic system

Bernhard, A. C. (2026) · University of Vienna · doi:10.25365/thesis.81473