Structural diversity and clustering of bacterial flagellar outer domains

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

<i>Coot</i> : model-building tools for molecular graphics

Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571 · see citing works

Inference of macromolecular assemblies from crystalline state.

Krissinel, E., & Henrick, K. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.05.022 · Cited by 10,189 · 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

AlphaFold Protein Structure Database: massively expanding the structural coverage of protein-sequence space with high-accuracy models

Varadi, M., Anyango, S., Deshpande, M., Nair, S., Natassia, C., Yordanova, G., Yuan, D., Stroe, O., Wood, G., Laydon, A., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkab1061 · Cited by 7,850 · 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

Pfam: The protein families database in 2021

Mistry, J., Chuguransky, S., Williams, L., Qureshi, M., Salazar, G. A., Sonnhammer, E. L. L., Tosatto, S. C. E., Paladin, L., Raj, S., Richardson, L. J., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkaa913 · Cited by 7,452 · see citing works

CTFFIND4: Fast and accurate defocus estimation from electron micrographs

Rohou, A. L., & Grigorieff, N. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.08.008 · Cited by 4,926 · 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

MolProbity: More and better reference data for improved all‐atom structure validation

Williams, C. J., Headd, J. J., Moriarty, N. W., Prisant, M. G., Videau, L. L., Deis, L. N., Verma, V., Keedy, D. A., Hintze, B. J., Chen, V. B., et al. (2018) · Protein Science · doi:10.1002/pro.3330 · Cited by 4,599 · 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

Fast and accurate protein structure search with Foldseek

van Kempen, M., Kim, S. S., Tumescheit, C., Mirdita, M., Lee, J., Gilchrist, C. L. M., Söding, J., & Steinegger, M. (2022) · doi:10.1101/2022.02.07.479398 · Cited by 2,598 · see citing works

Fast and accurate protein structure search with Foldseek

van Kempen, M., Kim, S. S., Tumescheit, C., Mirdita, M., Lee, J., Gilchrist, C. L. M., Söding, J., & Steinegger, M. (2024) · Nature Biotechnology · doi:10.1038/s41587-023-01773-0 · Cited by 2,596 · see citing works

Computing Communities in Large Networks Using Random Walks

Pons, P., & Matthieu Latapy, B. (2005) · Lecture notes in computer science · doi:10.1007/11569596_31 · Cited by 2,147 · see citing works

The Resolution Revolution

Kühlbrandt, W. (2014) · Science · doi:10.1126/science.1251652 · Cited by 1,325 · see citing works

How Bacteria Assemble Flagella

Macnab, R. M. (2003) · Annual Review of Microbiology · doi:10.1146/annurev.micro.57.030502.090832 · Cited by 1,043 · see citing works

Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy

Yonekura, K., Maki-Yonekura, S., & Namba, K. (2003) · Nature · doi:10.1038/nature01830 · Cited by 764 · see citing works

TAM Receptor Tyrosine Kinases: Biologic Functions, Signaling, and Potential Therapeutic Targeting in Human Cancer

Linger, R. M. A., Keating, A. K., Earp, H. S., & Graham, D. K. (2008) · Advances in cancer research · doi:10.1016/s0065-230x(08)00002-x · Cited by 750 · see citing works

New tools for the analysis and validation of cryo-EM maps and atomic models

Afonine, P. V., Klaholz, B. P., Moriarty, N. W., Poon, B. K., Sobolev, O. V., Terwilliger, T. C., Adams, P. D., & Urzhumtsev, A. (2018) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798318009324 · Cited by 719 · see citing works

DALI shines a light on remote homologs: One hundred discoveries

Holm, L., Laiho, A., Törönen, P., & Salgado, M. G. (2022) · Protein Science · doi:10.1002/pro.4519 · Cited by 685 · see citing works

The Immunoglobulin Fold

Peer Bork, B., Holm, L., & Sander, C. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1582 · Cited by 676 · see citing works

Life in the human stomach: persistence strategies of the bacterial pathogen Helicobacter pylori

Salama, N. R., Hartung, M. L., & Mueller, A. (2013) · Nature Reviews Microbiology · doi:10.1038/nrmicro3016 · Cited by 668 · see citing works

Evasion of Toll-like receptor 5 by flagellated bacteria

Andersen‐Nissen, E., Smith, K. D., Strobe, K. L., Barrett, S. L. R., Cookson, B. T., Logan, S. M., & Aderem, A. A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502040102 · Cited by 657 · see citing works

WD40 proteins propel cellular networks

Stirnimann, C. U., Petsalaki, E., Russell, R. B., & Müller, C. W. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.003 · Cited by 629 · 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) · Apollo (University of Cambridge) · doi:10.17863/cam.57077 · Cited by 617 · see citing works

Structural Basis of TLR5-Flagellin Recognition and Signaling

Yoon, S., Kurnasov, O. V., Natarajan, V., Hong, M., Gudkov, A. V., Osterman, A. L., & Wilson, I. A. (2012) · Science · doi:10.1126/science.1215584 · Cited by 582 · see citing works

US-align: universal structure alignments of proteins, nucleic acids, and macromolecular complexes

Zhang, C., Shine, M., Pyle, A. M., & Zhang, Y. (2022) · Nature Methods · doi:10.1038/s41592-022-01585-1 · Cited by 511 · see citing works

Flagellar Motility Is Critical for Listeria monocytogenes Biofilm Formation

Lemon, K. P., Higgins, D. E., & Kolter, R. (2007) · Journal of Bacteriology · doi:10.1128/jb.01967-06 · Cited by 464 · see citing works

GENETICS AND BIOGENESIS OF BACTERIAL FLAGELLA

Macnab, R. M. (1992) · Annual Review of Genetics · doi:10.1146/annurev.ge.26.120192.001023 · Cited by 459 · see citing works

A robust algorithm for the reconstruction of helical filaments using single-particle methods

Egelman, E. H. (2000) · Ultramicroscopy · doi:10.1016/s0304-3991(00)00062-0 · Cited by 446 · see citing works

The Immunoglobulin Fold Structural Classification, Sequence Patterns and Common Core

Peer Bork, B., Holm, L. U., & Sander, C. (1994) · Journal of Molecular Biology · doi:10.1016/s0022-2836(84)71582-8 · Cited by 420 · see citing works

Multiple functions of flagellar motility and chemotaxis in bacterial physiology

Colin, R., Ni, B., Laganenka, L., & Sourjik, V. (2021) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuab038 · Cited by 378 · see citing works

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

Afonine, P. V., Poon, B. K., Read, R. J., Sobolev, O. V., Terwilliger, T. C., Urzhumtsev, A., & Adams, P. D. (2018) · eScholarship (California Digital Library) · Cited by 374 · see citing works

How good are predictions of protein secondary structure?

Kabsch, W., & Sander, C. (1983) · FEBS Letters · doi:10.1016/0014-5793(82)80597-8 · Cited by 372 · see citing works

Clustering predicted structures at the scale of the known protein universe

Barrio-Hernandez, I., Yeo, J., Jänes, J., Mirdita, M., Gilchrist, C. L. M., Wein, T., Varadi, M., Velankar, S., Beltrao, P., & Steinegger, M. (2023) · Nature · doi:10.1038/s41586-023-06510-w · Cited by 362 · see citing works

Classification of Alcaligenes faecalis-like isolates from the environment and human clinical samples as Ralstonia gilardii sp. nov.

Coenye, T., Falsen, E., Vancanneyt, M., Hoste, B., Govan, J. R. W., Kersters, K., & Vandamme, P. A. R. (1999) · INTERNATIONAL JOURNAL OF SYSTEMATIC AND EVOLUTIONARY MICROBIOLOGY · doi:10.1099/00207713-49-2-405 · Cited by 322 · see citing works

Stenotrophomonas maltophilia as an Emerging Ubiquitous Pathogen: Looking Beyond Contemporary Antibiotic Therapy

Adegoke, A. A., Stenström, T. A., & Okoh, A. I. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.02276 · Cited by 302 · see citing works

The immunoglobulin fold family: sequence analysis and 3D structure comparisons

Halaby, D., Poupon, A., & Mornon, J. (1999) · Protein Engineering Design and Selection · doi:10.1093/protein/12.7.563 · Cited by 249 · see citing works

Prokaryotic motility structures

Bardy, S. L., Ng, S. Y. M., & Jarrell, K. F. (2003) · Microbiology · doi:10.1099/mic.0.25948-0 · Cited by 218 · see citing works

How antibodies fold

Feige, M. J., Hendershot, L. M., & Buchner, J. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.11.005 · Cited by 196 · see citing works

Host Protein Binding and Adhesive Properties of H6 and H7 Flagella of Attaching and Effacing Escherichia coli

Erdem, A. L., Avelino, F., Xicohtencatl‐Cortés, J., & Girón, J. A. (2007) · Journal of Bacteriology · doi:10.1128/jb.00464-07 · Cited by 174 · see citing works

De novo protein design by citizen scientists

Koepnick, B., Flatten, J., Husain, T., Ford, A., Silva, D., Bick, M. J., Bauer, A., Liu, G., Ishida, Y., Boykov, A., et al. (2019) · Nature · doi:10.1038/s41586-019-1274-4 · Cited by 160 · see citing works

Variation in bacterial flagellins: from sequence to structure

Beatson, S. A., Minamino, T., & Pallen, M. J. (2006) · Trends in Microbiology · doi:10.1016/j.tim.2006.02.008 · Cited by 157 · see citing works

The Current Revolution in Cryo-EM

Egelman, E. H. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2016.02.001 · Cited by 141 · see citing works

Flagellin of EnteropathogenicEscherichia coliStimulates Interleukin-8 Production in T84 Cells

Zhou, X., Girón, J. A., Torres, A. G., Crawford, J. A., Negrete, E., Vogel, S. N., & Kaper, J. B. (2003) · Infection and Immunity · doi:10.1128/iai.71.4.2120-2129.2003 · Cited by 137 · see citing works

Methylation of Salmonella Typhimurium flagella promotes bacterial adhesion and host cell invasion

Horstmann, J., Lunelli, M., Cazzola, H., Heidemann, J., Kühne, C., Steffen, P., Szefs, S., Rossi, C., Lokareddy, R. K., Wang, C., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15738-3 · Cited by 131 · see citing works

Reconstruction of Helical Filaments and Tubes

Egelman, E. H. (2010) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(10)82006-3 · Cited by 128 · see citing works

Conformational change of flagellin for polymorphic supercoiling of the flagellar filament

Maki-Yonekura, S., Yonekura, K., & Namba, K. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1774 · Cited by 123 · see citing works

A structural model of flagellar filament switching across multiple bacterial species

Wang, F., Burrage, A. M., Postel, S., Clark, R. E., Orlova, A., Sundberg, E. J., Kearns, D. B., & Egelman, E. H. (2017) · Nature Communications · doi:10.1038/s41467-017-01075-5 · Cited by 117 · see citing works

Silent recognition of flagellins from human gut commensal bacteria by Toll-like receptor 5

(2023) · doi:10.1126/sciimmunol.abq7001 · Cited by 117 · see citing works

Cryo-EM structure of an extracellular Geobacter OmcE cytochrome filament reveals tetrahaem packing

Wang, F., Mustafa, K. M., Suciu, V., Joshi, K., Chan, C. H., Choi, S., Su, Z., Si, D., Hochbaum, A. I., Egelman, E. H., et al. (2022) · Nature Microbiology · doi:10.1038/s41564-022-01159-z · Cited by 112 · see citing works

Cryoelectron Microscopy Reconstructions of the Pseudomonas aeruginosa and Neisseria gonorrhoeae Type IV Pili at Sub-nanometer Resolution

Wang, F., Coureuil, M., Osinski, T., Orlova, A., Altindal, T., Gesbert, G., Nassif, X., Egelman, E. H., & Craig, L. (2017) · Structure · doi:10.1016/j.str.2017.07.016 · Cited by 111 · see citing works

Flagellar energy costs across the tree of life

Schavemaker, P. E., & Lynch, M. (2022) · eLife · doi:10.7554/elife.77266 · Cited by 95 · see citing works

Adaptation of adherent-invasive E. coli to gut environment: Impact on flagellum expression and bacterial colonization ability

Sevrin, G., Massier, S., Chassaing, B., Agus, A., Delmas, J., Denizot, J., Billard, E., & Barnich, N. (2018) · Gut Microbes · doi:10.1080/19490976.2017.1421886 · Cited by 91 · see citing works

Methods to Evaluate Bacterial Motility and Its Role in Bacterial–Host Interactions

Palma, V., Gutiérrez, M. S., Vargas, O., Parthasarathy, R., & Navarrete, P. (2022) · Microorganisms · doi:10.3390/microorganisms10030563 · Cited by 91 · see citing works

Characterization of Flagella Produced by Clinical Strains ofStenotrophomonas maltophilia

de Oliveira-Garcia, D., DallʼAgnol, M., Rosales, M., Azzuz, A. C. G. S., Martinez, M. B., & Girón, J. A. (2002) · Emerging infectious diseases · doi:10.3201/eid0809.010535 · Cited by 90 · see citing works

Crystal structure of FliC flagellin from Pseudomonas aeruginosa and its implication in TLR5 binding and formation of the flagellar filament

Song, W. S., & Yoon, S. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.01.008 · Cited by 80 · see citing works

Cryo-EM of Helical Polymers

Wang, F., Gnewou, O. M., Solemanifar, A., Conticello, V. P., & Egelman, E. H. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00753 · Cited by 78 · see citing works

Flagellar filament structure and cell motility of Salmonella typhimurium mutants lacking part of the outer domain of flagellin

Yoshioka, K., Aizawa, S., & Yamaguchi, S. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.4.1090-1093.1995 · Cited by 71 · see citing works

Development of Competence for Genetic Transformation of Streptococcus mutans in a Chemically Defined Medium

Desai, K. B., Mashburn‐Warren, L., Federle, M. J., & Morrison, D. A. (2012) · Journal of Bacteriology · doi:10.1128/jb.00337-12 · Cited by 69 · see citing works

Pathogenicity and virulence of Burkholderia pseudomallei

Bzdyl, N. M., Moran, C. L., Bendo, J. B., & Sarkar‐Tyson, M. (2022) · Virulence · doi:10.1080/21505594.2022.2139063 · Cited by 65 · see citing works

Bacterial chemotaxis in human diseases

Zhou, B., Szymanski, C. M., & Baylink, A. (2022) · Trends in Microbiology · doi:10.1016/j.tim.2022.10.007 · Cited by 65 · see citing works

Structural and Functional Comparison of Salmonella Flagellar Filaments Composed of FljB and FliC

Yamaguchi, T., Toma, S., Terahara, N., Miyata, T., Ashihara, M., Minamino, T., Namba, K., & Kato, T. (2020) · Biomolecules · doi:10.3390/biom10020246 · Cited by 65 · see citing works

Control of Bacterial Motility by Environmental Factors in Polarly Flagellated and Peritrichous Bacteria Isolated from Lake Baikal

Soutourina, O. A., Semenova, E. A., Parfenova, V. V., Danchin, A., & Bertin, P. (2001) · Applied and Environmental Microbiology · doi:10.1128/aem.67.9.3852-3859.2001 · Cited by 63 · see citing works

Discovery of a proteolytic flagellin family in diverse bacterial phyla that assembles enzymatically active flagella

Eckhard, U., Bandukwala, H., Mansfield, M. J., Marino, G., Cheng, J., Wallace, I., Holyoak, T., Charles, T. C., Austin, J. W., Overall, C. M., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00599-0 · Cited by 59 · see citing works

Convergent evolution in the supercoiling of prokaryotic flagellar filaments

Kreutzberger, M. A. B., Sonani, R. R., Liu, J., Chatterjee, S., Wang, F., Sebastian, A. L., Biswas, P. P., Ewing, C. P., Zheng, W., Poly, F., et al. (2022) · Cell · doi:10.1016/j.cell.2022.08.009 · Cited by 57 · see citing works

Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium

Neuhaus, A., Selvaraj, M., Salzer, R., Langer, J. D., Kruse, K., Kirchner, L., Sanders, K., Daum, B., Averhoff, B., & Gold, V. A. M. (2020) · Nature Communications · doi:10.1038/s41467-020-15650-w · Cited by 57 · see citing works

An extensively glycosylated archaeal pilus survives extreme conditions

Wang, F., Cvirkaitė‐Krupovič, V., Kreutzberger, M. A. B., Su, Z., de Oliveira, G. A. P., Osinski, T., Sherman, N. E., DiMaio, F., Wall, J. S., Prangishvili, D. A., et al. (2019) · Nature Microbiology · doi:10.1038/s41564-019-0458-x · Cited by 53 · see citing works

A Deletion Variant Study of the Functional Role of the Salmonella Flagellin Hypervariable Domain Region in Motility

Malapaka, R. R. V., Adebayo, L. O., & Tripp, B. C. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.10.054 · Cited by 53 · see citing works

Atomic structure of the Campylobacter jejuni flagellar filament reveals how ε Proteobacteria escaped Toll-like receptor 5 surveillance

Kreutzberger, M. A. B., Ewing, C. P., Poly, F., Wang, F., & Egelman, E. H. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2010996117 · Cited by 49 · see citing works

The structures of two archaeal type IV pili illuminate evolutionary relationships

Wang, F., Baquero, D. P., Su, Z., Beltrán, L. C., Prangishvili, D. A., Krupovìč, M., & Egelman, E. H. (2020) · Nature Communications · doi:10.1038/s41467-020-17268-4 · Cited by 48 · see citing works

A Phase Variant of Azospirillum lipoferum Lacks a Polar Flagellum and Constitutively Expresses Mechanosensing Lateral Flagella

Alexandre, G. M., Rohr, R., & Bally, R. (1999) · Applied and Environmental Microbiology · doi:10.1128/aem.65.10.4701-4704.1999 · Cited by 39 · see citing works

Flagellin outer domain dimerization modulates motility in pathogenic and soil bacteria from viscous environments

Kreutzberger, M. A. B., Sobe, R. C., Sauder, A. B., Chatterjee, S., Peña, A., Wang, F., Girón, J. A., Kiessling, V., Costa, T. R. D., Conticello, V. P., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-29069-y · Cited by 39 · see citing works

Sequence- and Structure-Based Immunoreactive Epitope Discovery for Burkholderia pseudomallei Flagellin

Nithichanon, A., Rinchai, D., Gori, A., Lassaux, P., Peri, C., Conchillo‐Solé, O., Ferrer‐Navarro, M., Gourlay, L. J., Nardini, M., Vilà, J., et al. (2015) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0003917 · Cited by 38 · see citing works

Geovibrio thiophilus sp. nov., a novel sulfur-reducing bacterium belonging to the phylum Deferribacteres

Janssen, P. H., Liesack, W., & Schink, B. (2002) · INTERNATIONAL JOURNAL OF SYSTEMATIC AND EVOLUTIONARY MICROBIOLOGY · doi:10.1099/00207713-52-4-1341 · Cited by 29 · see citing works

Tad and toxin-coregulated pilus structures reveal unexpected diversity in bacterial type IV pili

Sonani, R. R., Sanchez, J. C., Baumgardt, J. K., Kundra, S., Wright, E., Craig, L., & Egelman, E. H. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2316668120 · Cited by 28 · see citing works

Crystal Structure of a Novel Bacterial Cell-Surface Flagellin Binding to a Polysaccharide,

Maruyama, Y., Momma, M., Mikami, B., Hashimoto, W., & Murata, K. (2008) · Biochemistry · doi:10.1021/bi701872x · Cited by 26 · see citing works

Discovery and Characterization of a Myxobacterial Lanthipeptide with Unique Biosynthetic Features and Anti-inflammatory Activity

Wang, X., Chen, X., Wang, Z.-J., Zhuang, M., Zhong, L., Fu, C., Garcia, R., Müller, R., Zhang, Y., Yan, J., et al. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c06014 · Cited by 25 · see citing works

Helicobacter pylori flagellin: TLR5 evasion and fusion-based conversion into a TLR5 agonist

Kim, J.-H., Namgung, B., Jeon, Y. J., Song, W. S., Lee, J., Kang, S. G., & Yoon, S. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.09.179 · Cited by 24 · see citing works

Analysis of a flagellar filament cap mutant reveals that HtrA serine protease degrades unfolded flagellin protein in the periplasm of Borrelia burgdorferi

Zhang, K., Qin, Z., Chang, Y., Liu, J., Malkowski, M. G., Shipa, S., Li, L., Qiu, W., Zhang, J., & Li, C. (2019) · Molecular Microbiology · doi:10.1111/mmi.14243 · Cited by 24 · see citing works

Helical Perturbations of the Flagellar Filament:Rhizobium lupiniH13–3 at 13 Å Resolution

Cohen-Krausz, S., & Trachtenberg, S. (1998) · Journal of Structural Biology · doi:10.1006/jsbi.1998.4001 · Cited by 24 · see citing works

Two distinct archaeal type IV pili structures formed by proteins with identical sequence

Liu, J., Eastep, G. N., Cvirkaitė‐Krupovič, V., Rich-New, S. T., Kreutzberger, M. A. B., Egelman, E. H., Krupovìč, M., & Wang, F. (2024) · Nature Communications · doi:10.1038/s41467-024-45062-z · Cited by 23 · see citing works

Comparative Genomics Reveals a Well-Conserved Intrinsic Resistome in the Emerging Multidrug-Resistant Pathogen Cupriavidus gilardii

Ruiz, C., McCarley, A., Espejo, M. L., Cooper, K. K., & Harmon, D. E. (2019) · mSphere · doi:10.1128/msphere.00631-19 · Cited by 20 · see citing works

Non-helical perturbations of the flagellar filament: Salmonella typhimurium SJW117 at 9.6 Å resolution

Trachtenberg, S., DeRosier, D. J., Zemlin, F., & Beckmann, E. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1537 · Cited by 20 · see citing works

The catalytic mechanism and unique low pH optimum ofCaldicellulosiruptor besciifamily 3 pectate lyase

Alahuhta, M., Taylor, L. E., Brunecky, R., Sammond, D. W., Michener, W. E., Adams, M. W. W., Himmel, M. E., Bomble, Y. J., & Lunin, V. V. (2015) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s1399004715013760 · Cited by 15 · see citing works

An unbroken network of interactions connecting flagellin domains is required for motility in viscous environments

Nedeljković, M., Kreutzberger, M. A. B., Postel, S., Bonsor, D., Xing, Y., Jacob, N., Schuler, W. J., Egelman, E. H., & Sundberg, E. J. (2023) · PLOS Pathogens · doi:10.1371/journal.ppat.1010979 · Cited by 13 · see citing works

The structure of the helically perturbed flagellar filament of Pseudomonas rhodos: implications for the absence of the outer domain in other complex flagellins and for the flexibility of the radial spokes

Cohen-Krausz, S., & Trachtenberg, S. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03466.x · Cited by 12 · see citing works

Characterization of the relationship between polar and lateral flagellar structural genes in the deep-sea bacterium Shewanella piezotolerans WP3

Jian, H., Wang, H., Zeng, X., Xiong, L., Wang, F., & Xiao, X. (2016) · Scientific Reports · doi:10.1038/srep39758 · Cited by 10 · see citing works

Infection caused by Cupriavidus gilardii in a convalescent COVID-19 patient

Fang, X., Lu, K., Sun, S., Zhang, H., Yu, X., & Han, W. (2023) · International Journal of Infectious Diseases · doi:10.1016/j.ijid.2023.07.015 · Cited by 9 · see citing works

Glycyl aminopeptidase (Sphingomonas)

Byun, T. S., & Blinkovsky, A. M. (2004) · Handbook of Proteolytic Enzymes · doi:10.1016/b978-0-12-079611-3.50132-4 · Cited by 3 · see citing works

Trustworthiness in action

Miguel, J., Caballé, S., & Xhafa, F. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-804535-0.00007-1 · Cited by 3 · see citing works

Isolation and characterization of fMGyn-Pae01, a phiKZ-like jumbo phage infecting Pseudomonas aeruginosa

Ranta, K., Skurnik, M., & Kiljunen, S. (2025) · Virology Journal · doi:10.1186/s12985-025-02679-w · Cited by 12 · see citing works

Flagellin: A crucial virulence factor coordinating bacterial pathogenesis and host immune responses

Xia, P., Lian, S., Liu, J., Ji, X., Zhao, T., Yang, C., Meng, X., Duan, Q., & Zhu, G. (2025) · Animals and zoonoses. · doi:10.1016/j.azn.2025.09.001 · Cited by 9 · see citing works

Balancing harm and harmony: Evolutionary dynamics between gut microbiota-derived flagellin and TLR5-mediated host immunity and metabolism

Seo, B., & Lim, M. Y. (2025) · Virulence · doi:10.1080/21505594.2025.2512035 · Cited by 8 · see citing works

Transcription Regulation of Flagellins: A Structural Perspective

Sheenu, & Jain, D. (2025) · Biochemistry · doi:10.1021/acs.biochem.4c00791 · Cited by 7 · see citing works

CryoEM-enabled visual proteomics reveals de novo structures of oligomeric protein complexes

Shen, Y., Maggiolo, A. O., Zhang, T., & Warmack, R. A. (2025) · Structure · doi:10.1016/j.str.2025.06.007 · Cited by 4 · see citing works

Rescue of bacterial motility using two- and three-species FliC chimeras

Scadden, J., Ridone, P., Pandit, D., Sowa, Y., & Baker, M. A. B. (2025) · Journal of Bacteriology · doi:10.1128/jb.00517-24 · Cited by 4 · see citing works

Cryo-EM reconstruction of helical polymers: Beyond the simple cases

Kreutzberger, M. A. B., Sonani, R. R., & Egelman, E. H. (2024) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583524000155 · Cited by 4 · see citing works

Structural basis for curvature generation and functional specialization in spirochete flagella

Troman, L. A., Paul, B., Kim, J., Fenno, J. C., Goetting‐Minesky, M. P., Reynolds, E. C., Banfield, J. F., Veith, P. D., & Ghosal, D. (2026) · Nature Communications · doi:10.1038/s41467-026-78968-x · Cited by 2 · see citing works

Validation of helical symmetry parameters in the EMDB

Li, D., Pérez, M., Zhang, X., Li, J., & Jiang, W. (2025) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798325007260 · Cited by 1 · see citing works

Flagellin beyond motility: exploiting flagellar filaments in biotechnology

Pandit, D., Scadden, J., & Baker, M. A. B. (2026) · Trends in biotechnology · doi:10.1016/j.tibtech.2026.05.007 · Cited by 1 · see citing works

From Swimming to Sensing: The Multifunctional Flagella of Helicobacter

Fong, J. C. N., Huang, E. H. L., Ponce, A. I., Liu, X., & Ottemann, K. M. (2026) · Annual Review of Microbiology · doi:10.1146/annurev-micro-042924-021000 · Cited by 1 · see citing works

Distinct flagellins differentially fine tune biofilm initiation via flagellar stator-associated proteinsPreprint

Liu, X., Eastep, G. N., Torres-Mejia, N., Zia, A., Ottemann, K. M., & Wang, F. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.30.697036 · Cited by 1 · see citing works

Análisis comparativo de la conservación y variabilidad de la secuencia de flagelina en bacterias gramnegativas de interés clínico

Tapia, N. G. F., & Pilco, J. A. O. (2025) · Esprint Investigación · doi:10.61347/ei.v4i3.203

The regulation of AsfR on tmRNA expression mediates bacterial motility and virulence in Aeromonas veronii

Chang, H., Tong, Y., Gao, S., Jiang, X., Ma, X., Li, H., Tang, Y., Li, J., Tang, H., Lin, M., et al. (2025) · Virulence · doi:10.1080/21505594.2025.2602247

DNAJB13 polymorphisms and association with idiopathic asthenozoospermia in Sichuan, China

He, J., Zhang, Z., Ding, Y., Cheng, C., Li, N., Li, T., Zhao, X., Wang, C., & Ding, X. (2025) · Basic and Clinical Andrology · doi:10.1186/s12610-025-00295-w

Flagellin fusion proteins as self-adjuvanting vaccines for viral infections and cancer

Erridge, C. (2026) · Exploration of Immunology · doi:10.37349/ei.2026.1003234

Discovery and genomics of H2-oxidizing/O2-reducing Deferribacterota ectosymbiotic with protists in the guts of termites and a Cryptocercus cockroach

Maruoka, N., Kudo, R., Igai, K., Shimizu, M., Yuki, M., Ohkuma, M., & Hongoh, Y. (2026) · ISME Communications · doi:10.1093/ismeco/ycag002

Insights into the structure and diversity of the bacterial flagellum from cryo-EM studies

Qin, K., Rando, M. R. I., & Bergeron, J. R. C. (2026) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2026.03.002

Deoxynivalenol-induced intestinal toxicity in piglets is mediated by multi-kingdom microbial dysbiosis and metatranscriptomic reprogramming

Liu, H.-Y., Ogamune, K. J., Hu, P., Zhu, M., Zhu, C., Yuan, P., Yuan, L., Huang, H., Zhang, Y., Ahmed, A. A., et al. (2026) · npj Biofilms and Microbiomes · doi:10.1038/s41522-026-01135-z

Phages Targeting Flagella: Adsorption and Infection Mechanisms of Flagellotropic Phages

Wood, J. A., Esteves, N. C., & Scharf, B. E. (2026) · Annual Review of Virology · doi:10.1146/annurev-virology-100424-123335

Reverse vaccinology and immunoinformatics-driven design of a multiepitope vaccine candidate against Renibacterium salmoninarum

Morales, C., Arriagada, V., Bonilla, E., Prina, B., Godoy, E., Molina-Chavez, B., Osorio, A., Gutiérrez, E., Roa, V., Gómez, L. A., et al. (2026) · Frontiers in Bioinformatics · doi:10.3389/fbinf.2026.1899416

The CUP pilus SMF-1 utilizes a specific antiparallel bundling mechanism to initiate biofilm formation

Fields, J. L., Sebastian, C. C., Zhang, H., Bhaumik, R., Zia, A., Robertson, A. N., Anderson, G. G., Mattoo, S., Wu, H., Kiedrowski, M. R., et al. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.118075

A Specific Ancestral Sequence Reconstruction of Flagellin Can Drive Motility in Salmonella enterica but not Escherichia coliPreprint

Scadden, J., Philip, J. S., Ridone, P., Sowa, Y., & Baker, M. A. B. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.10.20.760431

Flagellin outer domain dimerization modulates motility in pathogenic and soil bacteria from viscous environments

Kreutzberger, M. A. B., Sobe, R. C., Sauder, A. B., Chatterjee, S., Peña, A., Wang, F., Girón, J. A., Kiessling, V., Costa, T. R. D., Conticello, V. P., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-29069-y · Cited by 39 · see citing works

The structure of the helically perturbed flagellar filament of Pseudomonas rhodos: implications for the absence of the outer domain in other complex flagellins and for the flexibility of the radial spokes

Cohen-Krausz, S., & Trachtenberg, S. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03466.x · Cited by 12 · see citing works

Bacterial Flagellar Filament: A Supramolecular Multifunctional Nanostructure

Nedeljković, M., Sastre, D. E., & Sundberg, E. J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147521 · Cited by 109 · see citing works

A structural model of flagellar filament switching across multiple bacterial species

Wang, F., Burrage, A. M., Postel, S., Clark, R. E., Orlova, A., Sundberg, E. J., Kearns, D. B., & Egelman, E. H. (2017) · Nature Communications · doi:10.1038/s41467-017-01075-5 · Cited by 117 · see citing works

Structural diversity of bacterial flagellar motors

Chen, S., Beeby, M., Murphy, G. E., Leadbetter, J. R., Hendrixson, D. R., Briegel, A., Li, Z., Shi, J. R., Tocheva, E. I., Müller, A., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.186 · Cited by 303 · see citing works