Edward H. Egelman

Egelman, E. H. (2024). The myth of high-resolution liquid phase biological electron microscopy. PROTEIN SCIENCE, 33(8). doi:10.1002/pro.5125

Liu, J., Eastep, G. N., Cvirkaite-Krupovic, V., Rich-New, S. T., Kreutzberger, M. A. B., Egelman, E. H., . . . Wang, F. (2024). Two distinct archaeal type IV pili structures formed by proteins with identical sequence. NATURE COMMUNICATIONS, 15(1). doi:10.1038/s41467-024-45062-z

Yu, L. T., Kreutzberger, M. A. B., Hancu, M. C., Bui, T. H., Farsheed, A. C., Egelman, E. H., & Hartgerink, J. D. (2024). Beyond the Triple Helix: Exploration of the Hierarchical Assembly Space of Collagen-like Peptides.. bioRxiv. doi:10.1101/2024.05.14.594194

Treuner-Lange, A., Zheng, W., Viljoen, A., Lindow, S., Herfurth, M., Dufrene, Y. F., . . . Hultgren, S. (2024). Tight- packing of large pilin subunits provides distinct structural and mechanical properties for the Myxococcus xanthus type IVa pilus. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 121(17). doi:10.1073/pnas.2321989121

Sonani, R. R., Esteves, N. C., Scharf, B. E., & Egelman, E. H. (2024). Cryo-EM structure of flagellotropic bacteriophage Chi. STRUCTURE, 32(7). doi:10.1016/j.str.2024.03.011

Niedzialkowska, E., Runyan, L. A., Kudryashova, E., Egelman, E. H., & Kudryashov, D. S. (2024). Stabilization of F-actin by Salmonella effector SipA resembles the structural effects of inorganic phosphate and phalloidin. STRUCTURE, 32(6). doi:10.1016/j.str.2024.02.022

Egelman, E. H. (2024). Helical reconstruction, again. CURRENT OPINION IN STRUCTURAL BIOLOGY, 85. doi:10.1016/j.sbi.2024.102788

Deshmukh, A. P., Zheng, W., Chuang, C., Bailey, A. D., Williams, J. A., Sletten, E. M., . . . Caram, J. R. (2024). Near-atomic-resolution structure of J-aggregated helical light-harvesting nanotubes. NATURE CHEMISTRY, 16(5). doi:10.1038/s41557-023-01432-6

Sonani, R. R., Bianco, S., Dietrich, B., Doutch, J., Draper, E. R., Adams, D. J., & Egelman, E. H. (2024). Atomic structures of naphthalene dipeptide micelles unravel mechanisms of assembly and gelation. CELL REPORTS PHYSICAL SCIENCE, 5(2). doi:10.1016/j.xcrp.2024.101812

Sonani, R. R., Palmer, L. K., Esteves, N. C., Horton, A. A., Sebastian, A. L., Kelly, R. J., . . . Egelman, E. H. (2024). An extensive disulfide bond network prevents tail contraction in Agrobacteriumtumefaciens phage Milano. NATURE COMMUNICATIONS, 15(1). doi:10.1038/s41467-024-44959-z

Niedzialkowska, E., Runyan, L. A., Kudryashova, E., Egelman, E. H., & Kudryashov, D. S. (2023). Stabilization of F-actin by Salmonella effector SipA resembles the structural effects of inorganic phosphate and phalloidin.. bioRxiv. doi:10.1101/2023.12.26.573373

Pang, X., Zhang, Y., Park, K., Liao, Z., Li, J., Xu, J., . . . Sun, F. (2023). Structural elucidation of how ARF small GTPases induce membrane tubulation for vesicle fission.. bioRxiv. doi:10.1101/2023.12.19.572083

Beltran, L., Torsilieri, H., Patkowski, J. B., Yang, J. E., Casanova, J., Costa, T. R. D., . . . Egelman, E. H. (2024). The mating pilus of E. coli pED208 acts as a conduit for ssDNA during horizontal gene transfer. MBIO, 15(1). doi:10.1128/mbio.02857-23

Sonani, R. R., Sanchez, J. C., Baumgardt, J. K., Kundra, S., Wright, E. R., Craig, L., & Egelman, E. H. (2023). Tad and toxin- coregulated pilus structures reveal unexpected diversity in bacterial type IV pili. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 120(49). doi:10.1073/pnas.2316668120

Sonani, R. R., Esteves, N. C., Horton, A. A., Kelly, R. J., Sebastian, A. L., Wang, F., . . . Egelman, E. H. (2023). Neck and capsid architecture of the robust Agrobacterium phage Milano. COMMUNICATIONS BIOLOGY, 6(1). doi:10.1038/s42003-023-05292-1

Liu, J., Eastep, G. N., Cvirkaite-Krupovic, V., Rich-New, S. T., Kreutzberger, M. A. B., Egelman, E. H., . . . Wang, F. (2023). Two dramatically distinct archaeal type IV pili structures formed by the same pilin.. bioRxiv. doi:10.1101/2023.08.07.552285

Kreutzberger, M. A. B., Cvirkaite-Krupovic, V., Liu, Y., Baquero, D. P., Liu, J., Sonani, R. R., . . . Egelman, E. H. (2023). The evolution of archaeal flagellar filaments. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 120(28). doi:10.1073/pnas.2304256120

Thairatana, S., Doran, M., Sonani, R. R., Egelman, E. H., & Bullitt, E. (2023). New Morphologies of Hib Adhesion Pili.. Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada, 29(29 Suppl 1), 937. doi:10.1093/micmic/ozad067.466

Wang, F., Craig, L., Liu, X., Rensing, C., & Egelman, E. H. (2023). Models are useful until high-resolution structures are available: (Trends in Microbiology 31(6), 550-551; 2023).. Trends in microbiology, 31(7), 765. doi:10.1016/j.tim.2023.04.005

Baquero, D. P., Cvirkaite-Krupovic, V., Hu, S. S., Fields, J. L., Liu, X., Rensing, C., . . . Wang, F. (2023). Extracellular cytochrome nanowires appear to be ubiquitous in prokaryotes. CELL, 186(13), 2853-+. doi:10.1016/j.cell.2023.05.012

Guo, J., Wang, F., Huang, Y., He, H., Tan, W., Yi, M., . . . Xu, B. (2023). Cell spheroid creation by transcytotic intercellular gelation. NATURE NANOTECHNOLOGY, 18(9). doi:10.1038/s41565-023-01401-7

Nedeljkovic, M., Kreutzberger, M. A. B., Postel, S., Bonsor, D., Xing, Y., Jacob, N., . . . Sundberg, E. J. (2023). An unbroken network of interactions connecting flagellin domains is required for motility in viscous environments. PLOS PATHOGENS, 19(5). doi:10.1371/journal.ppat.1010979

Wang, F., Craig, L., Liu, X., Rensing, C., & Egelman, E. H. (2023). Models are useful until high-resolution structures are available. TRENDS IN MICROBIOLOGY, 31(6), 550-551. doi:10.1016/j.tim.2023.03.007

Yu, L. T., Hancu, M. C., Kreutzberger, M. A. B., Henrickson, A., Demeler, B., Egelman, E. H., & Hartgerink, J. D. (2023). Hollow Octadecameric Self-Assembly of Collagen-like Peptides. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY. doi:10.1021/jacs.2c12931

Beltran, L. C., Cvirkaite-Krupovic, V., Miller, J., Wang, F., Kreutzberger, M. A. B., Patkowski, J. B., . . . Krupovic, M. (2023). Archaeal DNA-import apparatus is homologous to bacterial conjugation machinery. NATURE COMMUNICATIONS, 14(1). doi:10.1038/s41467-023-36349-8

Egelman, E. H. (2023). Mutate or die: Atomic structures explain bacterial SOS induction. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 120(5). doi:10.1073/pnas.2221605120

Wang, F., Craig, L., Liu, X., Rensing, C., & Egelman, E. H. (2023). Microbial nanowires: type IV pili or cytochrome filaments?. TRENDS IN MICROBIOLOGY, 31(4), 384-392. doi:10.1016/j.tim.2022.11.004

Wang, F., Chan, C. H., Suciu, V., Mustafa, K., Ammend, M., Si, D., . . . Bond, D. R. (2022). Structure of Geobacter OmcZ filaments suggests extracellular cytochrome polymers evolved independently multiple times. ELIFE, 11. doi:10.7554/eLife.81551

Kreutzberger, M. A. B., Sonani, R. R., Liu, J., Chatterjee, S., Wang, F., Sebastian, A. L., . . . Egelman, E. H. (2022). Convergent evolution in the supercoiling of prokaryotic flagellar filaments. CELL, 185(19), 3487-+. doi:10.1016/j.cell.2022.08.009

Lin, Z., Beltran, L. C., De los Santos, Z. A., Li, Y., Adel, T., Fagan, J. A., . . . Zheng, M. (2022). DNA-guided lattice remodeling of carbon nanotubes. SCIENCE, 377(6605), 535-+. doi:10.1126/science.abo4628

Yi, M., Wang, F., Tan, W., Hsieh, J. -T., Egelman, E. H., & Xu, B. (2022). Enzyme Responsive Rigid-Rod Aromatics Target "Undruggable" Phosphatases to Kill Cancer Cells in a Mimetic Bone Microenvironment. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY. doi:10.1021/jacs.2c05491

Wang, F., Mustafa, K., Suciu, V., Joshi, K., Chan, C. H., Choi, S., . . . Bond, D. R. (2022). Cryo-EM structure of an extracellular Geobacter OmcE cytochrome filament reveals tetrahaem packing. NATURE MICROBIOLOGY, 7(8), 1291-+. doi:10.1038/s41564-022-01159-z

Chang, L., Wang, F., Connolly, K., Meng, H., Su, Z., Cvirkaite-Krupovic, V., . . . Si, D. (2022). DeepTracer-ID: De novo protein identification from cryo-EM maps. BIOPHYSICAL JOURNAL, 121(15), 2840-2848. doi:10.1016/j.bpj.2022.06.025

Dong, S., Zheng, W., Pinkerton, N., Hansen, J., Tikunova, S. B., Davis, J. P., . . . Kudryashov, D. S. (2022). Photorhabdus luminescens TccC3 Toxin Targets the Dynamic Population of F-Actin and Impairs Cell Cortex Integrity. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 23(13). doi:10.3390/ijms23137026

Wang, F., Cvirkaite-Krupovic, V., Krupovic, M., & Egelman, E. H. (2022). Archaeal bundling pili of Pyrobaculum calidifontis reveal similarities between archaeal and bacterial biofilms. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 119(26). doi:10.1073/pnas.2207037119

Low, W. W., Wong, J. L. C., Beltran, L. C., Seddon, C., David, S., Kwong, H. -S., . . . Frankel, G. (2022). Mating pair stabilization mediates bacterial conjugation species specificity. NATURE MICROBIOLOGY, 7(7), 1016-+. doi:10.1038/s41564-022-01146-4

Schwebach, C. L., Kudryashova, E., Agrawal, R., Zheng, W., Egelman, E. H., & Kudryashov, D. S. (2022). Allosteric regulation controls actin-bundling properties of human plastins. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 29(6), 519-+. doi:10.1038/s41594-022-00771-1

Kreutzberger, M. A. B., Wang, S., Beltran, L. C., Tuachi, A., Zuo, X., Egelman, E. H., & Conticello, V. P. (2022). Phenol-soluble modulins PSMα3 and PSMβ2 form nanotubes that are cross-α amyloids. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 119(20). doi:10.1073/pnas.2121586119

Wang, F., Cvirkaite-Krupovic, V., Vos, M., Beltran, L. C., Kreutzberger, M. A. B., Winter, J. -M., . . . Egelman, E. H. (2022). Spindle-shaped archaeal viruses evolved from rod-shaped ancestors to package a larger genome. CELL, 185(8), 1297-+. doi:10.1016/j.cell.2022.02.019

Kreutzberger, M. A. B., Sobe, R. C., Sauder, A. B., Chatterjee, S., Pena, A., Wang, F., . . . Egelman, E. H. (2022). Flagellin outer domain dimerization modulates motility in pathogenic and soil bacteria from viscous environments. NATURE COMMUNICATIONS, 13(1). doi:10.1038/s41467-022-29069-y

Wang, F., Gnewou, O., Solemanifar, A., Conticello, V. P., & Egelman, E. H. (2022). Cryo-EM of Helical Polymers. CHEMICAL REVIEWS, 122(17), 14055-14065. doi:10.1021/acs.chemrev.1c00753

Pieri, L., Wang, F., Arteni, A. -A., Vos, M., Winter, J. -M., Le Du, M. -H., . . . Paternostre, M. (2022). Atomic structure of Lanreotide nanotubes revealed by cryo-EM. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 119(4). doi:10.1073/pnas.2120346119

Wang, F., Cvirkaite-Krupovic, V., Krupovic, M., & Egelman, E. H. (2022). Archaeal bundling pili of Pyrobaculum calidifontis reveal similarities between archaeal and bacterial biofilms (vol 119, e2207037119, 2022). PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 119(44). doi:10.1073/pnas.2216660119

Wang, F., Gnewou, O., Wang, S., Osinski, T., Zuo, X., Egelman, E. H., & Conticello, V. P. (2021). Deterministic chaos in the self-assembly of β sheet nanotubes from an amphipathic oligopeptide. MATTER, 4(10), 3217-3231. doi:10.1016/j.matt.2021.06.037

Krupovic, M., Kuhn, J. H., Wang, F., Baquero, D. P., V. Dolja, V., Egelman, E. H., . . . V. Koonin, E. (2021). Adnaviria: a New Realm for Archaeal Filamentous Viruses with Linear A-Form Double-Stranded DNA Genomes. JOURNAL OF VIROLOGY, 95(15). doi:10.1128/JVI.00673-21

Matyszewski, M., Zheng, W., Lueck, J., Mazanek, Z., Mohideen, N., Lau, A. Y., . . . Sohn, J. (2021). Distinct axial and lateral interactions within homologous filaments dictate the signaling specificity and order of the AIM2-ASC inflammasome. NATURE COMMUNICATIONS, 12(1). doi:10.1038/s41467-021-23045-8

Egelman, E. H., & Wang, F. (2021). Cryo-EM is a powerful tool, but helical applications can have pitfalls. SOFT MATTER, 17(12), 3291-3293. doi:10.1039/d1sm00282a

Wang, F., Gnewou, O., Modlin, C., Beltran, L. C., Xu, C., Su, Z., . . . Conticello, V. P. (2021). Structural analysis of cross α-helical nanotubes provides insight into the designability of filamentous peptide nanomaterials. NATURE COMMUNICATIONS, 12(1). doi:10.1038/s41467-020-20689-w

Zheng, W., Pena, A., Ilangovan, A., Clark, J. N. -B., Frankel, G., Egelman, E. H., & Costa, T. R. D. (2021). Cryoelectron-microscopy structure of the enteropathogenic Escherichia coli type III secretion system EspA filament. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 118(2). doi:10.1073/pnas.2022826118

Zheng, W., Pena, A., Low, W. W., Wong, J. L. C., Frankel, G., & Egelman, E. H. (2020). Cryoelectron-Microscopic Structure of the pKpQIL Conjugative Pili from Carbapenem-Resistant Klebsiella pneumoniae. STRUCTURE, 28(12), 1321-+. doi:10.1016/j.str.2020.08.010

Wang, F., Baquero, D. P., Beltran, L. C., Su, Z., Osinski, T., Zheng, W., . . . Egelman, E. H. (2020). Structures of filamentous viruses infecting hyperthermophilic archaea explain DNA stabilization in extreme environments. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 117(33), 19643-19652. doi:10.1073/pnas.2011125117

Wang, F., Baquero, D. P., Su, Z., Beltran, L. C., Prangishvili, D., Krupovic, M., & Egelman, E. H. (2020). The structures of two archaeal type IV pili illuminate evolutionary relationships. NATURE COMMUNICATIONS, 11(1). doi:10.1038/s41467-020-17268-4

Kreutzberger, M. A. B., Ewing, C., Poly, F., Wang, F., & Egelman, E. H. (2020). Atomic structure of the Campylobacter jejuni flagellar filament reveals how ε Proteobacteria escaped Toll-like receptor 5 surveillance. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 117(29), 16985-16991. doi:10.1073/pnas.2010996117

Feng, Z., Wang, H., Wang, F., Oh, Y., Berciu, C., Cui, Q., . . . Xu, B. (2020). Artificial Intracellular Filaments. CELL REPORTS PHYSICAL SCIENCE, 1(7). doi:10.1016/j.xcrp.2020.100085

Schwebach, C. L., Kudryashova, E., Zheng, W., Orchard, M., Smith, H., Runyan, L. A., . . . Kudryashov, D. S. (2020). Osteogenesis imperfecta mutations in plastin 3 lead to impaired calcium regulation of actin bundling.. Bone research, 8(1), 21. doi:10.1038/s41413-020-0095-2

Chen, Y. X., Ing, N. L., Wang, F., Xu, D., Sloan, N. B., Lam, N. T., . . . Glover, D. J. (2020). Structural Determination of a Filamentous Chaperone to Fabricate Electronically Conductive Metalloprotein Nanowires. ACS NANO, 14(6), 6559-6569. doi:10.1021/acsnano.9b09405

Gunn, K. H., Roberts, B. S., Wang, F., Strauss, J. D., Borgnia, M. J., Egelman, E. H., & Neher, S. B. (2020). The structure of helical lipoprotein lipase reveals an unexpected twist in lipase storage. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 117(19), 10254-10264. doi:10.1073/pnas.1916555117

Egelman, E. H. (2020). Cryo-EM: Ice Is Nice, but Good Ice Can Be Hard to Find. BIOPHYSICAL JOURNAL, 118(6), 1238-1239. doi:10.1016/j.bpj.2020.01.026

Schwebach, C. L., Kudryashova, E., Zheng, W., Orchard, M., Smith, H., Runyan, L. A., . . . Kudryashov, D. S. (2020). Osteogenesis imperfecta mutations in plastin 3 lead to impaired calcium regulation of actin bundling. BONE RESEARCH, 8(1). doi:10.1038/s41413-020-0095-2

Wang, F., Baquero, D. P., Su, Z., Osinski, T., Prangishvili, D., Egelman, E. H., & Krupovic, M. (2020). Structure of a filamentous virus uncovers familial ties within the archaeal virosphere. VIRUS EVOLUTION, 6(1). doi:10.1093/ve/veaa023

Wang, F., Liu, Y., Su, Z., Osinski, T., de Oliveira, G. A. P., Conway, J. F., . . . Egelman, E. H. (2019). A packing for A-form DNA in an icosahedral virus. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 116(45), 22591-22597. doi:10.1073/pnas.1908242116

Egelman, E. H. (2019). Hooked on motility. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 26(10), 848-849. doi:10.1038/s41594-019-0302-2

Demircioglu, F. E., Zheng, W., McQuown, A. J., Maier, N. K., Watson, N., Cheeseman, I. M., . . . Schwartz, T. U. (2019). The AAA plus ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn. NATURE COMMUNICATIONS, 10. doi:10.1038/s41467-019-11194-w

Zheng, W., Andersson, M., Mortezaei, N., Bullitt, E., & Egelman, E. (2019). Cryo-EM structure of the CFA/I pilus rod. IUCRJ, 6, 815-821. doi:10.1107/S2052252519007966

Hughes, S. A., Wang, F., Wang, S., Kreutzberger, M. A. B., Osinski, T., Orlova, A., . . . Conticello, V. P. (2019). Ambidextrous helical nanotubes from self-assembly of designed helical hairpin motifs. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 116(29), 14456-14464. doi:10.1073/pnas.1903910116

Wang, F., Cvirkaite-Krupovic, V., Kreutzberger, M. A. B., Su, Z., de Oliveira, G. A. P., Osinski, T., . . . Egelman, E. H. (2019). An extensively glycosylated archaeal pilus survives extreme conditions. NATURE MICROBIOLOGY, 4(8), 1401-1410. doi:10.1038/s41564-019-0458-x

Bardiaux, B., de Amorim, G. C., Rico, A. L., Zheng, W., Guilvout, I., Jollivet, C., . . . Francetic, O. (2019). Structure and Assembly of the Enterohemorrhagic Escherichia coli Type 4 Pilus. STRUCTURE, 27(7), 1082-+. doi:10.1016/j.str.2019.03.021

Wang, F., Gu, Y., O'Brien, J. P., Yi, S. M., Yalcin, S. E., Srikanth, V., . . . Malvankar, N. S. (2019). Structure of Microbial Nanowires Reveals Stacked Hemes that Transport Electrons over Micrometers. CELL, 177(2), 361-+. doi:10.1016/j.cell.2019.03.029

Shen, C., Lu, A., Xie, W. J., Ruan, J., Negro, R., Egelman, E. H., . . . Wu, H. (2019). Molecular mechanism for NLRP6 inflammasome assembly and activation. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 116(6), 2052-2057. doi:10.1073/pnas.1817221116

Rico, A. L., Zheng, W., Petiot, N., Egelman, E. H., & Francetic, O. (2019). Functional reconstitution of the type IVa pilus assembly system from enterohaemorrhagic Escherichia coli. MOLECULAR MICROBIOLOGY, 111(3), 732-749. doi:10.1111/mmi.14188

Matyszewski, M., Zheng, W., Lueck, J., Antiochos, B., Egelman, E. H., & Sohn, J. (2018). Cryo-EM structure of the NLRC4^CARD filament provides insights into how symmetric and asymmetric supramolecular structures drive inflammasome assembly. JOURNAL OF BIOLOGICAL CHEMISTRY, 293(52), 20240-20248. doi:10.1074/jbc.RA118.006050

Liu, Y., Osinski, T., Wang, F., Krupovic, M., Schouten, S., Kasson, P., . . . Egelman, E. H. (2018). Structural conservation in a membrane-enveloped filamentous virus infecting a hyperthermophilic acidophile. NATURE COMMUNICATIONS, 9. doi:10.1038/s41467-018-05684-6

Spaulding, C., Schreiber, H. L., Zheng, W., Dodson, K. W., Hazen, J. E., Conover, M., . . . Egelman, E. H. (2018). Functional role of the type 1 pilus rod structure in mediating host-pathogen interactions. ELIFE, 7. doi:10.7554/eLife.31662

Danino, D., & Egelman, E. (2018). MICROSCOPY METHODS: YOU CAN OBSERVE A LOT BY WATCHING. CURRENT OPINION IN COLLOID & INTERFACE SCIENCE, 34, A1-A3. doi:10.1016/j.cocis.2018.06.003

Danino, D., & Egelman, E. H. (2018). Direct imaging and computational cryo-electron microscopy of ribbons and nanotubes. CURRENT OPINION IN COLLOID & INTERFACE SCIENCE, 34, 100-113. doi:10.1016/j.cocis.2018.05.002

Avery, A. W., Fealey, M. E., Wang, F., Orlova, A., Thompson, A. R., Thomas, D. D., . . . Egelman, E. H. (2017). Structural basis for high-affinity actin binding revealed by a β-III-spectrin SCA5 missense mutation. NATURE COMMUNICATIONS, 8. doi:10.1038/s41467-017-01367-w

Wang, F., Burrage, A. M., Postel, S., Clark, R. E., Orlova, A., Sundberg, E. J., . . . Egelman, E. H. (2017). A structural model of flagellar filament switching across multiple bacterial species. NATURE COMMUNICATIONS, 8. doi:10.1038/s41467-017-01075-5

Lopez-Castilla, A., Thomassin, J. -L., Bardiaux, B., Zheng, W., Nivaskumar, M., Yu, X., . . . Francetic, O. (2017). Structure of the calcium-dependent type 2 secretion pseudopilus. NATURE MICROBIOLOGY, 2(12), 1686-1695. doi:10.1038/s41564-017-0041-2

Wang, F., Coureuil, M., Osinski, T., Orlova, A., Altindal, T., Gesbert, G., . . . Craig, L. (2017). Cryoelectron Microscopy Reconstructions of the Pseudomonas aeruginosa and Neisseria gonorrhoeae Type IV Pili at Sub-nanometer Resolution. STRUCTURE, 25(9), 1423-+. doi:10.1016/j.str.2017.07.016

Ve, T., Vajjhala, P. R., Hedger, A., Croll, T., DiMaio, F., Horsefield, S., . . . Kobe, B. (2017). Structural basis of TIR-domain-assembly formation in MAL- and MyD88-dependent TLR4 signaling. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 24(9), 743-+. doi:10.1038/nsmb.3444

Zheng, W., Wang, F., Taylor, N. M. I., Guerrero-Ferreira, R. C., Leiman, P. G., & Egelman, E. H. (2017). Refined Cryo-EM Structure of the T4 Tail Tube: Exploring the Lowest Dose Limit. STRUCTURE, 25(9), 1436-+. doi:10.1016/j.str.2017.06.017

Kasson, P., DiMaio, F., Yu, X., Lucas-Staat, S., Krupovic, M., Schouten, S., . . . Egelman, E. H. (2017). Model for a novel membrane envelope in a filamentous hyperthermophilic virus. ELIFE, 6. doi:10.7554/eLife.26268

Frenz, B., Walls, A. C., Egelman, E. H., Veesler, D., & DiMaio, F. (2017). RosettaES: a sampling strategy enabling automated interpretation of difficult cryo-EM maps. NATURE METHODS, 14(8), 797-+. doi:10.1038/NMETH.4340

Egelman, E. H. (2017). Cryo-EM of bacterial pili and archaeal flagellar filaments. CURRENT OPINION IN STRUCTURAL BIOLOGY, 46, 31-37. doi:10.1016/j.sbi.2017.05.012

Fu, T. -M., Li, Y., Lu, A., Li, Z., Vajjhala, P. R., Cruz, A. C., . . . Wu, H. (2016). Cryo-EM Structure of Caspase-8 Tandem DED Filament Reveals Assembly and Regulation Mechanisms of the Death-Inducing Signaling Complex. MOLECULAR CELL, 64(2), 236-250. doi:10.1016/j.molcel.2016.09.009

Kolappan, S., Coureuil, M., Yu, X., Nassif, X., Egelman, E. H., & Craig, L. (2016). Structure of the Neisseria meningitidis Type IV pilus. NATURE COMMUNICATIONS, 7. doi:10.1038/ncomms13015

Postel, S., Deredge, D., Bonsor, D. A., Yu, X., Diederichs, K., Helmsing, S., . . . Sundberg, E. J. (2016). Bacterial flagellar capping proteins adopt diverse oligomeric states. ELIFE, 5. doi:10.7554/eLife.18857

Costa, T. R. D., Ilangovan, A., Ukleja, M., Redzej, A., Santini, J. M., Smith, T. K., . . . Waksman, G. (2016). Structure of the Bacterial Sex F Pilus Reveals an Assembly of a Stoichiometric Protein-Phospholipid Complex. CELL, 166(6), 1436-+. doi:10.1016/j.cell.2016.08.025

Braun, T., Vos, M. R., Kalisman, N., Sherman, N. E., Rachel, R., Wirth, R., . . . Egelman, E. H. (2016). Archaeal flagellin combines a bacterial type IV pilin domain with an Ig-like domain. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 113(37), 10352-10357. doi:10.1073/pnas.1607756113

Subramaniam, S., Earl, L. A., Falconieri, V., Milne, J. L. S., & Egelman, E. H. (2016). Resolution advances in cryo-EM enable application to drug discovery. CURRENT OPINION IN STRUCTURAL BIOLOGY, 41, 194-202. doi:10.1016/j.sbi.2016.07.009

Egelman, E. H. (2016). The Current Revolution in Cryo-EM. BIOPHYSICAL JOURNAL, 110(5), 1008-1012. doi:10.1016/j.bpj.2016.02.001

Egelman, E. H., & Engel, A. (2016). Biophysical Journal Special Issue: Focus on Cryo-EM. BIOPHYSICAL JOURNAL, 110(4), E01. doi:10.1016/j.bpj.2016.01.025

Hospenthal, M. K., Redzej, A., Dodson, K., Ukleja, M., Frenz, B., Rodrigues, C., . . . Waksman, G. (2016). Structure of a Chaperone-Usher Pilus Reveals the Molecular Basis of Rod Uncoiling. CELL, 164(1-2), 269-278. doi:10.1016/j.cell.2015.11.049

Gurung, R., Yadav, R., Brungardt, J. G., Orlova, A., Egelman, E. H., & Beck, M. R. (2016). Actin polymerization is stimulated by actin cross-linking protein palladin. BIOCHEMICAL JOURNAL, 473, 383-396. doi:10.1042/BJ20151050

Sborgi, L., Ravotti, F., Dandey, V. P., Dick, M. S., Mazur, A., Reckel, S., . . . Hiller, S. (2015). Structure and assembly of the mouse ASC inflammasome by combined NMR spectroscopy and cryo-electron microscopy. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 112(43), 13237-13242. doi:10.1073/pnas.1507579112

Morrone, S. R., Matyszewski, M., Yu, X., Delannoy, M., Egelman, E. H., & Sohn, J. (2015). Assembly-driven activation of the AIM2 foreign-dsDNA sensor provides a polymerization template for downstream ASC. NATURE COMMUNICATIONS, 6. doi:10.1038/ncomms8827

Taylor, M. R. G., Spirek, M., Chaurasiya, K. R., Ward, J. D., Carzaniga, R., Yu, X., . . . Boulton, S. J. (2015). Rad51 Paralogs Remodel Pre-synaptic Rad51 Filaments to Stimulate Homologous Recombination. CELL, 162(2), 271-286. doi:10.1016/j.cell.2015.06.015

DiMaio, F., Chen, C. -C., Yu, X., Frenz, B., Hsu, Y. -H., Lin, N. -S., & Egelman, E. H. (2015). The molecular basis for flexibility in the flexible filamentous plant viruses. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 22(8), 642-644. doi:10.1038/nsmb.3054

Braun, T., Orlova, A., Valegard, K., Lindas, A. -C., Schroeder, G. F., & Egelman, E. H. (2015). Archaeal actin from a hyperthermophile forms a single-stranded filament. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 112(30), 9340-9345. doi:10.1073/pnas.1509069112

DiMaio, F., Yu, X., Rensen, E., Krupovic, M., Prangishvili, D., & Egelman, E. H. (2015). A virus that infects a hyperthermophile encapsidates A-form DNA. SCIENCE, 348(6237), 914-917. doi:10.1126/science.aaa4181

Egelman, E. H. (2015). Three-dimensional reconstruction of helical polymers. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 581, 54-58. doi:10.1016/j.abb.2015.04.004

Loew, L., Beckett, D., Egelman, E. H., & Scarlata, S. (2015). Reproducibility of Research in Biophysics. BIOPHYSICAL JOURNAL, 108(7), E01. doi:10.1016/j.bpj.2015.03.002

Kudryashev, M., Wang, R. Y. -R., Brackmann, M., Scherer, S., Maier, T., Baker, D., . . . Basler, M. (2015). Structure of the Type VI Secretion System Contractile Sheath. CELL, 160(5), 952-962. doi:10.1016/j.cell.2015.01.037

DiMaio, F., Song, Y., Li, X., Brunner, M. J., Xu, C., Conticello, V., . . . Baker, D. (2015). Atomic-accuracy models from 4.5-Å cryo-electron microscopy data with density-guided iterative local refinement. NATURE METHODS, 12(4), 361-U129. doi:10.1038/NMETH.3286

Wang, R. Y. -R., Kudryashev, M., Li, X., Egelman, E. H., Basler, M., Cheng, Y., . . . DiMaio, F. (2015). De novo protein structure determination from near-atomic-resolution cryo-EM maps. NATURE METHODS, 12(4), 335-U84. doi:10.1038/NMETH.3287

Egelman, E. H., Xu, C., DiMaio, F., Magnotti, E., Modlin, C., Yu, X., . . . Conticello, V. P. (2015). Structural Plasticity of Helical Nanotubes Based on Coiled-Coil Assemblies. STRUCTURE, 23(2), 280-289. doi:10.1016/j.str.2014.12.008

Lu, A., Li, Y., Yin, Q., Ruan, J., Yu, X., Egelman, E., & Wu, H. (2015). Plasticity in PYD assembly revealed by cryo-EM structure of the PYD filament of AIM2. CELL DISCOVERY, 1. doi:10.1038/celldisc.2015.13

Galkin, V. E., Orlova, A., Vos, M. R., Schroeder, G. F., & Egelman, E. H. (2015). Near-Atomic Resolution for One State of F-Actin. STRUCTURE, 23(1), 173-182. doi:10.1016/j.str.2014.11.006

Egelman, E. H. (2014). Ambiguities in helical reconstruction. ELIFE, 3. doi:10.7554/eLife.04969

Pang, X., Fan, J., Zhang, Y., Zhang, K., Gao, B., Ma, J., . . . Sun, F. (2014). A PH Domain in ACAP1 Possesses Key Features of the BAR Domain in Promoting Membrane Curvature. DEVELOPMENTAL CELL, 31(1), 73-86. doi:10.1016/j.devcel.2014.08.020

Kostan, J., Salzer, U., Orlova, A., Toeroe, I., Hodnik, V., Senju, Y., . . . Djinovic-Carugo, K. (2014). Direct interaction of actin filaments with F-BAR protein pacsin2. EMBO REPORTS, 15(11), 1154-1162. doi:10.15252/embr.201439267

Wu, B., Peisley, A., Tetrault, D., Li, Z., Egelman, E. H., Magor, K. E., . . . Hur, S. (2014). Molecular Imprinting as a Signal-Activation Mechanism of the Viral RNA Sensor RIG-I. MOLECULAR CELL, 55(4), 511-523. doi:10.1016/j.molcel.2014.06.010

Nivaskumar, M., Bouvier, G., Campos, M., Nadeau, N., Yu, X., Egelman, E. H., . . . Francetic, O. (2014). Distinct Docking and Stabilization Steps of the Pseudopilus Conformational Transition Path Suggest Rotational Assembly of Type IV Pilus-like Fibers. STRUCTURE, 22(5), 685-696. doi:10.1016/j.str.2014.03.001

Thompson, P. M., Tolbert, C. E., Shen, K., Kota, P., Palmer, S. M., Plevock, K. M., . . . Campbell, S. L. (2014). Identification of an Actin Binding Surface on Vinculin that Mediates Mechanical Cell and Focal Adhesion Properties. STRUCTURE, 22(5), 697-706. doi:10.1016/j.str.2014.03.002

Lu, A., Magupalli, V. G., Ruan, J., Yin, Q., Atianand, M. K., Vos, M. R., . . . Egelman, E. H. (2014). Unified Polymerization Mechanism for the Assembly of ASC-Dependent Inflammasomes. CELL, 156(6), 1193-1206. doi:10.1016/j.cell.2014.02.008

Qiao, Q., Yang, C., Zheng, C., Fontan, L., David, L., Yu, X., . . . Wu, H. (2013). Structural Architecture of the CARMA1/Bcl10/MALT1 Signalosome: Nucleation-Induced Filamentous Assembly. MOLECULAR CELL, 51(6), 766-779. doi:10.1016/j.molcel.2013.08.032

Schroeter, M. M., Orlova, A., Egelman, E. H., Beall, B., & Chalovich, J. M. (2013). Organization of F-Actin by Fesselin (avian smooth muscle synaptopodin 2). BIOCHEMISTRY, 52(29), 4955-4961. doi:10.1021/bi4005254

Galkin, V. E., Orlova, A., Solodukhin, A., Schroeder, G. F., & Egelman, E. H. (2013). Structural Polymorphism of F-Actin is Coupled with its Mechanical Properties. BIOPHYSICAL JOURNAL, 104(2), 644A-645A. doi:10.1016/j.bpj.2012.11.3561

Galkin, V. E., Kolappan, S., Ng, D., Zong, Z., Li, J., Yu, X., . . . Craig, L. (2013). The Structure of the CS1 Pilus of Enterotoxigenic Escherichia coli Reveals Structural Polymorphism. JOURNAL OF BACTERIOLOGY, 195(7), 1360-1370. doi:10.1128/JB.01989-12

Berke, I. C., Yu, X., Modis, Y., & Egelman, E. H. (2012). MDA5 assembles into a polar helical filament on dsRNA. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 109(45), 18437-18441. doi:10.1073/pnas.1212186109

Henche, A. -L., Ghosh, A., Yu, X., Jeske, T., Egelman, E., & Albers, S. -V. (2012). Structure and function of the adhesive type IV pilus of Sulfolobus acidocaldarius. ENVIRONMENTAL MICROBIOLOGY, 14(12), 3188-3202. doi:10.1111/j.1462-2920.2012.02898.x

Galkin, V. E., Orlova, A., & Egelman, E. H. (2012). Are ParM Filaments Polar or Bipolar?. JOURNAL OF MOLECULAR BIOLOGY, 423(4), 482-485. doi:10.1016/j.jmb.2012.08.006

Yu, X., Goforth, C., Meyer, C., Rachel, R., Wirth, R., Schroeder, G. F., & Egelman, E. H. (2012). Filaments from Ignicoccus hospitalis Show Diversity of Packing in Proteins Containing N-Terminal Type IV Pilin Helices. JOURNAL OF MOLECULAR BIOLOGY, 422(2), 274-281. doi:10.1016/j.jmb.2012.05.031

Parent, K. N., Deedas, C. T., Egelman, E. H., Casjens, S. R., Baker, T. S., & Teschke, C. M. (2012). Stepwise molecular display utilizing icosahedral and helical complexes of phage coat and decoration proteins in the development of robust nanoscale display vehicles. BIOMATERIALS, 33(22), 5628-5637. doi:10.1016/j.biomaterials.2012.04.026

Li, J., Egelman, E. H., & Craig, L. (2012). Structure of the Vibrio cholerae Type IVb Pilus and Stability Comparison with the Neisseria gonorrhoeae Type IVa Pilus. JOURNAL OF MOLECULAR BIOLOGY, 418(1-2), 47-64. doi:10.1016/j.jmb.2012.02.017

Henderson, R., Sali, A., Baker, M. L., Carragher, B., Devkota, B., Downing, K. H., . . . Lawson, C. L. (2012). Outcome of the First Electron Microscopy Validation Task Force Meeting. STRUCTURE, 20(2), 205-214. doi:10.1016/j.str.2011.12.014

Galkin, V. E., Orlova, A., & Egelman, E. H. (2012). Actin Filaments as Tension Sensors. CURRENT BIOLOGY, 22(3), R96-R101. doi:10.1016/j.cub.2011.12.010

Behrmann, E., Tao, G., Stokes, D. L., Egelman, E. H., Raunser, S., & Penczek, P. A. (2012). Real-space processing of helical filaments in SPARX. JOURNAL OF STRUCTURAL BIOLOGY, 177(2), 302-313. doi:10.1016/j.jsb.2011.12.020

Orlova, A. A., Solodukhin, A., Kostan, J., Salzer, U., Shreiner, C., Carugo, K., & Egelman, E. H. (2012). Direct binding of BAR-domain protein FAP52 to F-actin.. MOLECULAR BIOLOGY OF THE CELL, 23. Retrieved from https://www.webofscience.com/

Galkin, V. E., Orlova, A., Solodukhin, A., & Egelman, E. (2012). Cofilin uses intrinsic zones of instability within F-actin to disrupt the actin filament.. MOLECULAR BIOLOGY OF THE CELL, 23. Retrieved from https://www.webofscience.com/

Galkin, V. E., Orlova, A., Kudryashov, D., Soloduhin, A., Reisler, E., Schroeder, G. F., & Egelman, E. H. (2012). Remodeling of Actin Filaments by Cofilin. BIOPHYSICAL JOURNAL, 102(3), 238A. doi:10.1016/j.bpj.2011.11.1307

Galkin, V. E., Orlova, A., Kudryashov, D. S., Solodukhin, A., Reisler, E., Schroeder, G. F., & Egelman, E. H. (2011). Remodeling of actin filaments by ADF/cofilin proteins. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 108(51), 20568-20572. doi:10.1073/pnas.1110109108

Orlova, A., Galkin, V. E., Jeffries, C. M. J., Egelman, E. H., & Trewhella, J. (2011). The N-Terminal Domains of Myosin Binding Protein C Can Bind Polymorphically to F-Actin. JOURNAL OF MOLECULAR BIOLOGY, 412(3), 379-386. doi:10.1016/j.jmb.2011.07.056

Patel, G., Johnson, D. S., Sun, B., Pandey, M., Yu, X., Egelman, E. H., . . . Patel, S. S. (2011). A257T Linker Region Mutant of T7 Helicase-Primase Protein Is Defective in DNA Loading and Rescued by T7 DNA Polymerase. JOURNAL OF BIOLOGICAL CHEMISTRY, 286(23), 20490-20499. doi:10.1074/jbc.M110.201657

Galkin, V. E., Britt, R. L., Bane, L. B., Yu, X., Cox, M. M., & Egelman, E. H. (2011). Two Modes of Binding of DinI to RecA Filament Provide a New Insight into the Regulation of SOS Response by DinI Protein. JOURNAL OF MOLECULAR BIOLOGY, 408(5), 815-824. doi:10.1016/j.jmb.2011.03.046

Parent, K. N., Sinkovits, R. S., Suhanovsky, M. M., Teschke, C. M., Egelman, E. H., & Baker, T. S. (2010). Cryo-reconstructions of P22 polyheads suggest that phage assembly is nucleated by trimeric interactions among coat proteins. PHYSICAL BIOLOGY, 7(4). doi:10.1088/1478-3975/7/4/045004

Gajewski, S., Webb, M. R., Galkin, V., Egelman, E. H., Kreuzer, K. N., & White, S. W. (2011). Crystal Structure of the Phage T4 Recombinase UvsX and Its Functional Interaction with the T4 SF2 Helicase UvsW. JOURNAL OF MOLECULAR BIOLOGY, 405(1), 65-76. doi:10.1016/j.jmb.2010.10.004

Galkin, V. E., Orlova, A., Schroeder, G. F., & Egelman, E. H. (2010). Structural polymorphism in F-actin. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 17(11), 1318-U169. doi:10.1038/nsmb.1930

Dray, E., Etchin, J., Wiese, C., Saro, D., Williams, G. J., Hammel, M., . . . Sung, P. (2010). Enhancement of RAD51 recombinase activity by the tumor suppressor PALB2. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 17(10), 1255-+. doi:10.1038/nsmb.1916

Yu, X., & Egelman, E. (2010). The Structure of hDmc1 Filaments and Ambiguities in Helical Reconstruction. Microscopy and Microanalysis, 16(S2), 1088-1089. doi:10.1017/s1431927610056576

Yu, X., & Egelman, E. H. (2010). Helical Filaments of Human Dmc1 Protein on Single-Stranded DNA: A Cautionary Tale. JOURNAL OF MOLECULAR BIOLOGY, 401(3), 544-551. doi:10.1016/j.jmb.2010.06.049

Galkin, V. E., Orlova, A., Salmazo, A., Djinovic-Carugo, K., & Egelman, E. H. (2010). Opening of tandem calponin homology domains regulates their affinity for F-actin. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 17(5), 614-616. doi:10.1038/nsmb.1789

Grintsevich, E. E., Galkin, V. E., Orlova, A., Ytterberg, A. J., Mikati, M. M., Kudryashov, D. S., . . . Reisler, E. (2010). Mapping of Drebrin Binding Site on F-Actin. JOURNAL OF MOLECULAR BIOLOGY, 398(4), 542-554. doi:10.1016/j.jmb.2010.03.039

Ban, N., & Egelman, E. H. (2010). Structure and function of large cellular assemblies. CURRENT OPINION IN STRUCTURAL BIOLOGY, 20(2), 207-209. doi:10.1016/j.sbi.2010.02.003

Hui, M. P., Galkin, V. E., Yu, X., Stasiak, A. Z., Stasiak, A., Waldor, M. K., & Egelman, E. H. (2010). ParA2, a Vibrio cholerae chromosome partitioning protein, forms left-handed helical filaments on DNA. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 107(10), 4590-4595. doi:10.1073/pnas.0913060107

Galkin, V. E., Schmied, W. H., Schraidt, O., Marlovits, T. C., & Egelman, E. H. (2010). The Structure of the Salmonella typhimurium Type III Secretion System Needle Shows Divergence from the Flagellar System. JOURNAL OF MOLECULAR BIOLOGY, 396(5), 1392-1397. doi:10.1016/j.jmb.2010.01.001

Egelman, E. (2010). Actin and Bacterial Actin-Like Proteins: Insights Into Evolution. BIOPHYSICAL JOURNAL, 98(3), 3A-4A. doi:10.1016/j.bpj.2009.12.021

Schroeter, M. M., Orlova, A., Beall, B., Egelman, E. H., & Chalovich, J. M. (2010). Organization of F-Actin by Avian Smooth Muscle Synaptopodin 2 (Fesselin). BIOPHYSICAL JOURNAL, 98(3), 157A. doi:10.1016/j.bpj.2009.12.843

Orlova, A., Galkin, V. E., Jeffries, C. M., Trewhella, J., & Egelman, E. H. (2010). Binding of N-Terminus Fragments of Cardiac Myosin-Binding C-protein to Actin. BIOPHYSICAL JOURNAL, 98(3), 157A. doi:10.1016/j.bpj.2009.12.845

Egelman, E. H. (2010). RECONSTRUCTION OF HELICAL FILAMENTS AND TUBES. METHODS IN ENZYMOLOGY, VOL 482: CRYO-EM, PART B: 3-D RECONSTRUCTION, 482, 167-183. doi:10.1016/S0076-6879(10)82006-3