2015 2014 2013 2012 2011 2010 2009 2008 2007
2006 2005 2004 2003 2002 2001 2000 1999 1998
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1988 1986 1985 1984 1983 1982 1981 1980 1979



245. Egelman, E.H. (2020). Cryo-EM: Ice is nice, but good ice can be hard to find. Biophysical Journal 118, 1238-9. 

246. Wang, F., Baquero, D.P., Su, Z., Osinski, T., Prangishvili, D., Egelman, E.H.*, Krupovic, M.* (*=corresponding authors) (2020). Structure of a filamentous virus uncovers familial ties within the archaeal virosphere. Virus Evolution 6, DOI:10.1093/ve/veaa023. 

247. Gunn, K.H., Roberts, B.S., Wang, F., Strauss, J.D., Borgnia, M.J., Egelman, E.H., and Neher, S.B. (2020). The structure of helical lipoprotein lipase reveals an unexpected twist in lipase storage. Proc. Natl. Acad. Sci. U.S.A. 117, 10254-10264. 

248. Chen, Y.X., Ing, N.L., Wang, F., Xu, D., Sloan, N.B., Lam, N.T., Winter, D.L., Egelman, E.H., Hochbaum, A.I., Clark, D.S., Glover, D.J. (2020). Structural Determination of a Filamentous Chaperone to Fabricate Electronically Conductive Metalloprotein Nanowires. ACS Nano 14, 6559-6569. 

249. Feng, Z., Wang, H., Wang, F., Oh, Y., Berciu, C., Cui, Q.*, Egelman, E.H.* and Xu, B.* (*=corresponding authors) (2020). Artificial intracellular filaments. Cell Reports Physical Science 1(7). 

250. Schwebach, C.L., Kudryashova, E., Zheng, W., Orchard, M., Smith, H., Runyan, L.A., Egelman, E.H., Kudryashov, D.H. (2020). Osteogenesis imperfecta mutations in plastin 3 lead to impaired calcium regulation of actin bundling. Bone Research, 8:21. 

251. Kreutzberger, M.A.B., Ewing, C., Poly, F., Wang, F. and Egelman, E.H. (2020). Atomic structure of the Campylobacter jejuni flagellar filament reveals how ? Proteobacteria escaped Toll-like receptor 5 surveillance. Proc. Natl. Acad. Sci. U.S.A. 117, 16985-16991. 

252. Wang, F., Baquero, D.P., Su, Z., Beltran, L., Prangishvili, D., Krupovic, M. and Egelman, E.H. (2020). The structures of two archaeal type IV pili illuminate evolutionary relationships. Nature Communications 11, 3424. 

253. Wang, F., Baquero, D.P., Beltran, L., Su, Z., Osinski, T., Zheng, W., Prangishvili, D., Krupovic, M. and Egelman, E.H. (2020). Structures of filamentous viruses infecting hyperthermophilic archaea explain DNA stabilization in extreme environments. Proc. Natl. Acad. Sci. U.S.A. 117, 19643-19652. 

254. Zheng, W., Pena, A., Low, W.W., Wong, J.L.C, Frankel, G. and Egelman, E.H. (2020). Cryo-EM structure of the pKpQIL conjugative pili from carbapenem-resistant Klebsiella pneumoniae. Structure, in press.  


235. Rico, A.L., Zheng, W., Petiot, N., Egelman, E.H. and Francetic, O. (2019). “Functional reconstitution of the type Iva pilus assembly system from enterohaemorrhagic Escherichia coli.” Molecular Microbiology 111:732-749.

236. Shen, C., Lu, A., Xie, W.J., Ruan, J., Negro, R., Egelman, E.H., Fu, T.M., and Wu, H. (2019). Molecular mechanism for NLRP6 inflammasome assembly and activation. Proc. Natl. Acad. Sci. U.S.A. 116:2052-2057.

237. Wang, F., Gu, Y., O’Brien, J.P., Yi, S.M., Yalcin, S.E., Srikanth, V., Shen, C., Vu, D., Ing, N.L., Hochbaum, A.I.*, Egelman, E.H.* and Malvankar, N.S.* (*=corresponding authors) (2019). Structure of Microbial Nanowires Reveals Stacked Hemes that Transport Electrons over Micrometers. Cell 177, 361-369.

238. Wang, F., Cvirkaite-Krupovic, V., Kreutzberger, M.A,B., Su, Z., de Oliveira, G.A.P., Osinski, T., Sherman, N., DiMaio, F., Wall, J.S., Prangishvili, D., Krupovic, M. and Egelman, E.H. (2019). “An extensively glycosylated archaeal pilus survives extreme conditions.” Nature Microbiology 4, 1401-1410.

239. Bardiaux, B., de Amorim, G.C., Luna Rico, A., Zheng, W., Guilvout, I., Jollivet, C., Nilges, M., Egelman, E.H., Izadi-Pruneyre, N., and Francetic, O. (2019). Structure and Assembly of the Enterohemorrhagic Escherichia coli Type 4 Pilus. Structure 27, 1082-1093.

240. Demircioglu, F.E., Zheng, W., McQuown, A.J., Maier, N., Watson, N., Cheeseman, I.M., Denic, V., Egelman, E.H. and Schwartz, T.U. (2019). The AAA+ ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn. Nature Communications 10, 3262.

241. Hughes, S.A., Wang, F., Wang, S., Kreutzberger, M.A.B., Osinski, T., Orlova, A., Wall, J.S., Zuo, X., Egelman, E.H. and Conticello, V. (2019). Ambidextrous Helical Nanotubes from Self-Assembly of Designed Helical Hairpin Motifs. Proc. Natl. Acad. Sci. U.S.A. 116, 14456-14464.

242. Egelman, E.H. (2019). Hooked on Motility. Nature Structural and Molecular Biology 26, 848-849.

243. Wang, F., Liu, Y., Su, Z., Osinski, T., de Oliveira, G.A.P., Conway, J.F., Schouten, S., Krupovic, M., Prangishvili, D. and Egelman, E.H. (2019). A Novel Packing for A-form DNA in an Icosahedral Virus. Proc. Natl. Acad. Sci. U.S.A. 116, 22591-22597.

244. Zheng, W., Andersson, M., Mortezaei, N., Bullitt, E. and Egelman, E. (2019). Cryo-EM structure of the CFA/I pilus rod. IUCrJ 6, 815-821.



231. Spaulding, C.N., Schreiber, H.L.t., Zheng, W., Dodson, K.W., Hazen, J.E., Conover, M.S., Wang, F., Svenmarker, P., Luna-Rico, A., Francetic, O., Andersson, M., Hultgren, S. and Egelman, E.H. (2018). “Functional role of the type 1 pilus rod structure in mediating host-pathogen interactions.” eLife 7:e31662.

232. Danino, D. and Egelman, E.H. (2018). “Direct Imaging and Computational Cryo-Electron Microscopy of Ribbons and Nanotubes”, Current Opinion in Colloid & Interface Science 34, 100-113.

233. Liu, Y., Osinski, T., Wang, F., Krupovic, M., Schouten, S., Kasson, P., Prangishvili, D. and Egelman, E.H. (2018). “Structural conservation in a membrane-enveloped filamentous virus infecting a hyperthermophilic acidophile”, Nature Communications 9:3360.

234. Matyszewski, M., Zheng, W., Lueck, J., Antiochos, B., Egelman, E.H., and Sohn, J. (2018). “Cryo-EM structure of the NLRC4(CARD) filament provides insights into how symmetric and asymmetric supramolecular structures drive inflammasome assembly.” J Biol Chem. 293, 20240-20248.



222. Kasson, P., DiMaio, F., Yu, X., Lucas-Staat, S., Krupovic, M., Schouten, S., Prangishvili, D. and Egelman, E.H. (2017). “Model for a novel membrane envelope in a filamentous hyperthermophilic virus”, eLife 6:e26268.

223. Egelman, E.H. (2017). “Cryo-EM of Bacterial Pili and Archaeal Flagellar Filaments”, Current Opinion in Structural Biology 46, 31-37.

224. Frenz, B., Walls, A.C., Egelman, E.H., Veesler, D. and DiMaio, F. (2017). “RosettaES: a sampling strategy enabling automated interpretation of difficult cryo-EM maps”, Nature Methods 14, 797-800.

225. Zheng, W., Wang, F., Taylor, N.M.I., Guerrero-Ferreira, R.C., Leiman, P.G. and Egelman, E.H. (2017). “Refined cryo-EM structure of the T4 tail tube: exploring the lowest dose limit”, Structure 25, 1436-1441.

226. Ve, T., Vajjhala, P.R., Hedger, A., Croll, T., DiMaio, F., Horsefield, S., Yu, X., Lavrencic, P., Hassan, Z., Morgan, G.P., Mansell, A., Mobli, M., O’Carroll, A., Chauvin, B., Gambin, Y., Sierecki, E., Landsberg, M.J., Stacey, K.J., Egelman, E.H.* and Kobe, B.* (*=corresponding authors) (2017). “Structural basis of TIR-domain assembly formation in MAL- and MyD88-dependent TLR4 signaling", Nature Structural and Molecular Biology 24, 743-751.

227. Wang, F., Coureuil, M., Osinski, T., Orlova, A., Altindal, T., Gesbert, G., Nassif, X., Egelman, E.H.* and Craig, L.* (*=corresponding authors) (2017). “Cryo-electron microscopy reconstructions of the Pseudomonas aeruginosa and Neisseria gonorrhoeae Type IV pili at sub-nanometer resolution”, Structure 25, 1423-1435 (cover article).

228. Lopez-Castilla, A., Thomassin, J.L., Bardiaux, B., Zheng, W., Nivaskumar, M., Yu, X., Nilges, M., Egelman, E.H., Izadi-Pruneyre, N. and Francetic, O. (2017). “Structure of the calcium dependent Type 2 secretion pseudopilus”, Nature Microbiology DOI:10.1038/s41564-017-0041-2.

229. Wang, F., Burrage, A.M., Postel, S., Clark, R.E., Orlova, A., Sundberg, E.J., Kearns, D.B. and Egelman, E.H. (2017). “A Structural Model of Flagellar Filament Switching Across Multiple Bacterial Species”, Nature Communications 8, 960.

230. Avery, A.W., Fealey, M.E., Wang, F., Orlova, A., Thompson, A.R., Thomas, D.D., Hays, T.S. and Egelman, E.H. (2017). “Structural basis for high-affinity actin binding revealed by a β-III-spectrin missense mutation”, Nature Communications 8, 1350.


213. Hospenthal, M.K., Redzej, A., Dodson, K., Ukleja, M., Frenz, B., Rodrigues, C., Hultgren, S.J., DiMaio, F., Egelman, E.H.* and Waksman, G.* (*=corresponding authors) (2016). “Structure of a Chaperone-Usher pilus reveals the molecular basis of rod uncoiling”, Cell 164: 269-278.

214. Gurung, R., Yadav, R., Brungardt, J.G., Orlova, A., Egelman, E.H. and Beck, M.R. (2016). “Actin Polymerization is Stimulated by Actin Crosslinking Protein Palladin”, Biochemical Journal 473, 383-396.

215. Egelman, E.H. (2016). “The Current Revolution in Cryo-EM”, Biophysical Journal 110, 1008-1012.

216. Subramaniam, S., Earl, L.A., Falconieri, V., Milne, J.L.S. and Egelman, E.H. (2016). “Resolution Advances in Cryo-EM Enable Application to Drug Discovery”, Current Opinion in Structural Biology 41, 194-202.

217. Braun, T., Vos, M., Kalisman, N., Sherman, N.E., Rachel, R., Wirth, R., Schröder, G.F. and Egelman, E.H. (2016). “Archaeal Flagellin Combines a Bacterial Type IV Pilin Domain with an Immunoglobulin-like Domain”, P.N.A.S. 113, 10352-7.

218. Costa, T.R.D., Ilangovan, A., Ukleja, M., Redzej, A., Santini, J.M., Smith, T.K., Egelman, E.H.* and Waksman, G.* (*=corresponding authors) (2016). “Structure of the bacterial sex F pilus reveals an assembly of a stoichiometric protein-phospholipid complex”, Cell 166, 1436-1444.

219. Kolappan, S., Coureuil, M., Yu, X., Nassif, X., Egelman, E.H.* and Craig, L.* (*=corresponding authors) (2016). “Structure of the Neisseria meningitides Type IV Pilus”, Nature Communications 7, 13015.

220. Fu, T.M., Li, Y., Lu, A., Li, Z., Vajjhala, P.R., Cruz, A.C., Srivastava, D.B., DiMaio, F., Penczek, P.A., Siegel, R.M., Stacey, K.J., Egelman, E.H. and 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, 236-50.

221. 221. Postel, S., Deredge, D., Bonsor, D.A., Yu, X., Diedrichs, K., Helmsing, S., Vromen, A., Hust, M., Egelman, E.H., Beckett, D., Wintrode, P.L. and Sundberg, E.J. (2016) “Bacterial flagellar capping proteins adopts diverse oligomeric states”, eLife 5 DOI:10.7554/eLife.18857.


200. DiMaio, F.S., Li, X., Brunner, M., Xu, C., Conticello, V., Egelman, E.H., Marlovits, T., Cheng, Y., and Baker, D. (2015) “Atomic accuracy models from 4.5 Å cryo-electron microscopy data with density-guided iterative local rebuilding and refinement. Nature Methods 12, 361-5.

201. Egelman, E.H., Xu, C., DiMaio, F., Magnotti, E., Modlin, C., Yu, X., Wright, E., Baker, D. and Conticello, V.P. (2015). “Structural Plasticity of Helical Nanotubes Based on Coiled-Coil Assemblies”. Structure 23, 280-9.

202. Galkin, V.E., Orlova, A., Vos, M.R., Schröder, G.F. and Egelman, E.H. (2015). “Near-Atomic Resolution for One State of F-Actin”. Structure 23, 173-182.

203. Kudryashev, M.W., R.; Brackmann, M.; Scherer, S.; Maier, T.; Baker, D.; DiMaio, F.; Stahlberg, H.; Egelman, E.H.*; Basler, M.* (2015) *co-corresponding authors. “The Structure of the Type VI Secretion System Contractile Sheath”. Cell 160, 952-62.

204. Wang, R.Y., Kudryashev, M., Li, X., Egelman, E.H., Basler, M., Cheng, Y., Baker, D. and DiMaio, F. (2015). “De novo  protein structure determination from near-atomic resolution cryo-EM maps”. Nature Methods 12, 335-8.

205. Lu, A., Li, Y., Yin, Q., Ruan, J., Yu, X., Egelman, E. and Wu, H. (2015). “Plasticity in PYD assembly revealed by cryo-EM structure of the PYD filament of AIM2”, Cell Discovery 1, 15013.

206. DiMaio, F., Yu, X., Rensen, E., Krupovic, M., Prangishvili, D. and Egelman, E.H. (2015). “A Virus that Infects a Hyperthermophile Encapsidates A-Form DNA”, Science 348, 914-917.

PDF: http://www.sciencemag.org/cgi/rapidpdf/348/6237/914?ijkey=a8xnYfZlwWb8U&keytype=ref&siteid=sci

207. Egelman, E.H. (2015). "Three-dimensional reconstruction of helical polymers", Archives of Biochemistry and Biophysics 581, 54-8.

208. Taylor, M.R.G., Špírek, M., Chaurasiya, K.R., Ward, J.D., Carzaniga, R., Yu, X., Egelman, E.H., Collinson, L.M., Rueda, D., Krejčí, L. and Boulton, S.J. (2015). “Rad51 paralogs remodel pre-synaptic Rad51 filaments to stimulate homologous recombination”, Cell 162, 271-286.

209. DiMaio, F., Chen, C.C., Yu, X., Frenz, B., Hsu, Y.H., Lin, N.S. and Egelman, E.H. (2015). “The molecular basis for flexibility in the flexible filamentous plant viruses”, Nature Structural and Molecular Biology 22, 642-644 (cover article).

210. Braun, T., Orlova, A., Valegård, K., Lindås, A.C., Schröder, G.F. and Egelman, E.H. (2015). “An Archaeal Actin from a Hyperthermophile Forms a Single-Stranded Filament”, Proc. Natl. Acad. Sciences USA 112, 9340-9345 (profiled in a PNAS Commentary).

211. Morrone, S.R., Matyszewski, M., Yu, X., Delannoy, M., Egelman, E.H. and Sohn, J. (2015). “Assembly-driven activation of the AIM2 foreign dsDNA-sensor provides a polymerization template for downstream ASC”. Nature Communications 6, 7827.

212. Sborgi, L., Ravotti, F., Dandey, V.P., Dick, M.S., Mazur, A., Reckel, S., Chami, M., Scherer, S., Huber, M., Böckmann, A., Egelman, E.H., Stahlberg, H., Broz, P., Meier, B.H.,
Hiller, S. (2015). “Structure and assembly of the mouse ASC inflammasome by combined NMR spectroscopy and cryo-electron microscopy”, Proc. Natl. Acad. Sciences USA 112:13237-42.


193. Lu, A., Magupalli, V.G., Ruan, J., Yin, Q., Atianand, K., Vos, M., Schröder, G.F., Fitzgerald, K.A., Wu, H., and Egelman, E.H. (2014). “Unified Polymerization Mechanism for the Assembly of ASC‐dependent  Inflammasomes”. Cell 156, 1193-1206.

194. Nivaskumar, M., Bouvier, G., Campos, M., Nadeau, N., Yu, X., Egelman, E.H., Nilges, M., and 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, 685-696.

195. Thompson, P.M., Tolbert, C.E., Shen, K., Kota, P., Palmer, S.M., Plevock, K.M., Orlova, A., Galkin, V.E., Burridge, K., Egelman, E.H., Dokholyan, N.V., Superfine, R., and Campbell, S.L. (2014). “Identification of an Actin Binding Surface on Vinculin that Mediates Mechanical Cell and Focal Adhesion Properties”. Structure 22, 697-706.

196. Wu, B., Peisley, A., Tetrault, D., Li, Z., Egelman, E.H., Magor, K.E., Walz, T., Penczek, P.A. and Hur, S. (2014). “Molecular imprinting as a signal activation mechanism of the viral RNA sensor RIG-I”. Molecular Cell 55, 511-523.

197. Kostan, J., Salzer, U., Orlova, A., Törö, I., Hodnik, V., Senju, Y., Zou, J., Schreiner, C., Steiner, J., Meriläinen, J., Nikki, M., Virtanen, I., Carugo, O., Rappsilber, J., Lappalainen, P., Lehto, V., Anderluh, G., Egelman, E.H. and Djinović-Carugo, K. (2014). “Direct Interaction of Actin Filaments with F-BAR Protein Pacsin2”. EMBO Reports 15, 1154-62.

198. Pang, X., Fan, J., Zhang, Y., Zhang, K., Gao, B., Ma, J., Li, J., Deng, Y., Zhou, Q., Egelman, E.H., Hsu, V.W., and Sun, F. (2014). “A PH domain in ACAP1 possesses key features of the BAR domain in promoting membrane curvature”. Developmental Cell 31, 73-86.

199. Egelman, E.H. (2014). “Ambiguities in helical reconstruction”. eLife 3:e04969 doi:10.7554/eLife.04969.


190. Galkin, V.E., Kolappan, S., Ng, D., Zong, Z., Li, J., Yu, X., Egelman, E.H., and Craig, L. (2013). “Structure of the Cs1 Pilus of Enterotoxigenic Escherichia coli Reveals Structural Polymorphism.” J. Bacteriol. 195, 1360-1370.

191. Schroeter, M.M., Orlova, A., Egelman, E.H., Beall, B. and Chalovich, J.M. (2013), “Organization of F-Actin by Fesselin (avian smooth muscle synaptopodin 2)”, Biochemistry 52, 4955-61.

192. Qiao, Q, Yang, C., Zheng, C., Fontán, L., David, L., Yu, X., Bracken, C., Rosen, M., Melnick, A., Egelman, E.H. and Wu, H. (2013). “Structural Architecture of the CARMA1/Bcl10/MALT1 Signalosome: Nucleation Induced Filamentous Assembly.” Molecular Cell 51, 766-779.



181. Galkin, V.E., Orlova, A. and Egelman, E.H. (2012). “Actin Filaments as Tension Sensors”, Current Biology 22, R96-R101.

182. Li, J., Egelman, E.H. and Craig, L. (2012). “Structure of the Vibrio cholerae Type IVb pilus and stability comparison with the Neisseria gonorrhoeae Type IVa pilus”, J. Mol. Biol. 418, 47-64.

183. Behrmann, E., Tao, G., Stokes, D.L., Egelman, E.H., Raunser, S. and Penczek, P.A. (2012). “Real-space processing of helical filaments in SPARX”, J. Struct. Biol. 177, 302-313.

184. Henderson, R., Sali, A., Baker, M.L., Carragher, B., Devkota, B., Downing, K.H., Egelman, E.H., Feng, Z., Frank, J., Grigorieff, N., Jiang, W., Ludtke, S.J., Medalia, O., Penczek, P.A., Rosenthal, P.B., Rossmann, M.G., Schmid, M.F., Schroder, G.F., Steven, A.C., Stokes, D.L., Westbrook, J.D., Wriggers, W., Yang, H., Young ,J., Berman, H.M., Chiu, W., Kleywegt, G.J., and Lawson, C.L. (2012). “Outcome of the first electron microscopy validation task force meeting”, Structure 20, 205-214.

185. Yu, X., Goforth, C., Meyer, C., Rachel, R., Wirth, R., Schröder, G. and Egelman, E.H. (2012). “Filaments from Ignicoccus hospitalis Show Diversity of Packing in Proteins Containing N-terminal Type IV Pilin Helices”, J. Mol. Biol. 422, 274-281.

186. 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, 5628-5637.

187. Galkin, V.E., Orlova, A. and Egelman, E.H. (2012). “Are ParM filaments polar or bipolar?”, J. Mol. Biol. 423, 482-485.

188. Berke, I.C., Yu, X., Modis, Y. and Egelman, E.H. (2012). “MDA5 assembles into a polar helical filament”, Proc. Natl. Acad. Sci. U.S.A. 109, 18437-18441.

189. Henche, A.L., Ghosh, A., Yu, X., Jeske, T., Egelman, E., and Albers, S.V. (2012). “Structure and function of the adhesive type IV pilus of Sulfolobus acidocaldarius.” Environ. Microbiol. 14, 3188-3202.



175. Gajewski, S., Webb, M.R., Galkin, V.E., Egelman, E.H., Kreuzer, K.N. and White, S.W. (2011), “Crystal structure of the phage T4 recombinase UvsX and its functional interaction with the T4 SF2 helicase UvsW”, J. Mol. Biol. 405, 65-76.

176. Galkin,V.E., Britt,R.L., Bane,L.B., Yu,X., Cox,M.M., and 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". J. Mol. Biol. 408, 815-824.

177. Patel,G., Johnson,D.S., Sun,B., Pandey,M., Yu,X., Egelman,E.H., Wang,M.D., and Patel,S.S. (2011). "The A257T linker region mutant of T7 helicase-primase protein is defective in DNA loading and rescued by T7 DNA polymerase". J. Biol. Chem. 286, 20490-20499.

178. Egelman, E.H. (2011). "Intelligent Design". Encyclopedia of Genetics, Second Edition. S. Maloy and K. Hughes, Eds. Academic Press (in press).

179. Orlova, A., Galkin, V.E., Jeffries, C.M.J., Egelman, E.H. and Trewhella, J. (2011). "The N-terminal Domains of Myosin Binding Protein C Can Bind Polymorphically to F-actin". J. Mol. Biol. 412, 379-386.

180. Galkin, V.E., Orlova, A., Kudryashov, D., Solodukhin, A., Reisler, E., Schröder, G.N. and Egelman, E.H. (2011). Remodeling of Actin Filaments by ADF/Cofilin Proteins”, Proc. Natl. Acad. Sci. U.S.A. 108, 20568-20572.


165. Egelman, E.H. (2010), “Reducing Irreducible Complexity: Divergence of Quaternary Structure and Function in Macromolecular Assemblies”, Current Opinion in Cell Biology 22, 68-74.

166. Galkin, V.E.,  Schmied, W.H., Schraidt, O., Marlovits, T.C. and Egelman, E.H. (2010), “The Structure of the Salmonella typhimurium Type III Secretion System Needle Shows Divergence from the Flagellar System”, J. Mol. Biol. 396, 1392-1397.

167. Hui, M.P.,  Galkin, V.E.,  Yu, X.,  Stasiak, A.Z.,  Stasiak, A.,  Waldor, M.K. and Egelman, E.H. (2010), “ParA2, a Vibrio cholerae chromosome partitioning protein, forms left-handed helical filaments on DNA”, Proc. Natl. Acad. Sci. U.S.A. 107, 4590-4595.

168. Galkin, V.E., Orlova, A., Salmazo, A., Djinovic-Carugo, K. and Egelman, E.H. (2010), “Opening of tandem calponin homology domains regulates their affinity for F-actin”, Nature Structural and Molecular Biology 17, 614-616.

169. Grintsevich, E.E., Galkin, V.E., Orlova, A., Ytterberg, A.J., Mikati, M.M., Kudryashov, D.S., Loo, J.A., Egelman, E.H. and Reisler, E. (2010), “Mapping of drebrin binding site on F-actin”, J. Mol. Biol. 398, 542-554.

170. Egelman, E.H. (2010), “Reconstruction of Helical Filaments and Tubes”, Methods in Enzymology 482, 167-183.

171. Yu, X. and Egelman, E.H. (2010), “Helical filaments of human Dmc1 protein on single-stranded DNA: a cautionary tale”, J. Mol. Biol.401, 544-551.

172. Parent, K.N., Sinkovits, R.S.,  Suhanovsky, M.M., Teschke, C.M., Egelman, E.H. and  Baker, T.S. (2010),  “Cryo-reconstructions of P22 polyheads suggest that phage assembly is nucleated by trimeric interactions among coat proteins”, Physical Biology 7, 045004.

173. Galkin, V.E., Orlova, A., Schröder, G.N. and Egelman, E.H. (2010), “Structural polymorphism in F-actin”, Nature Structural and Molecular Biology 17, 1318-1323.

174. Dray, E., Etchin, J.,  Wiese, C., Saro, D.,  Williams, G.J., Hammel, M., Yu, X., Galkin, V.E., Liu, D., Tsai, M.S., Sy, S.M., Schild, D., Egelman, E., Chen, J. and Sung, P. (2010) “Enhancement of RAD51 recombinase activity by the tumor suppressor PALB2”, Nature Structural and Molecular Biology 17, 1255-1259.


157. Wang, Y.A., Yu, X., Silverman, P.M., Harris, R.L. and Egelman, E.H. (2009), “The Structure of F-Pili”, J. Mol. Biol. 385, 22-29.

158. Galkin, V., Yu, X., Bielnicki, J., Ndjonka, D., Bell, C.E. and Egelman, E.H. (2009), “Cleavage of Bacteriophage λ cI Repressor Involves the RecA C-terminal Domain”, J. Mol. Biol. 385, 779-787.

159. Zhang, X.P., Galkin, V.E., Yu, X., Egelman, E.H. and Heyer, W.D. (2009), “Loop 2 in S. cerevisiae Rad51 protein regulates filament formation and ATPase activity”, Nucleic Acids Research 37, 158-171.

160. Makhov, A.M., Sen, A., Simon, M.N., Griffith, J.D. and Egelman, E.H. (2009), “The bipolar filaments formed by Herpes simplex virus type 1 SSB/recombination protein (ICP8) suggest a mechanism for DNA annealing”, J. Mol. Biol. 386, 273-279.

161. Egelman, E.H. and Amos, L.A. (2009), “Electron microscopy of helical filaments: rediscovering buried treasures in negative stain”, BioEssays 31, 909-911.

162. Lucarelli, D., Wang, Y.A., Galkin, V.E., Yu, X., Wigley, D.B. and Egelman, E.H. (2009), “The RecB nuclease domain binds to RecA-DNA filaments: Implications for filament loading”, J. Mol. Biol. 391, 269-274.

163. Galkin, V.E., Orlova, A., Rivera, C., Mullins, R.D. and Egelman, E.H. (2009), "Structural polymorphism of the ParM filament and dynamic instability". Structure 17, 1253-1264.

164. Egelman, E.H. (2009), “Divergence of the Flagellar Hook and Filament”, Structure 17, 1425-1426.


145. Galkin, V.E., Orlova, A., Brieher, W., Kueh, H.Y., Mitchison, T.J. and Egelman, E.H. (2008), “Coronin-1A Stabilizes F-Actin by Bridging Adjacent Actin Protomers and Stapling Opposite Strands of the Actin Filament”, J. Mol. Biol. 376, 607-613.

146. Huang, R.H.,  Wang, Y., Roth, R.,  Yu, X., Purvis, A.R., Heuser, J.E., Egelman, E.H. and Sadler, J.E. (2008), "Assembly of Weibel-Palade Body-like Tubules from N-Terminal Domains of von Willebrand Factor", Proc. Natl. Acad. Sci. U.S.A. 105, 482-487.

147. Galkin, V.E., Orlova, A., Cherepanova, O., Lebart, M.C. and Egelman, E.H. (2008), “High Resolution Cryo-EM Structure of the F-Actin-Fimbrin/Plastin ABD2 Complex”, Proc. Natl. Acad. Sci. U.S.A. 105, 1494-1498.

148. Shvetsov, A., Galkin, V.E., Orlova, A., Phillips, M., Bergeron, S.E., Rubenstein, P.A., Egelman, E.H., and Reisler, E. (2008), “Actin Hydrophobic Loop 262-274 and Filament Nucleation and Elongation”,  J. Mol. Biol. 375, 793-801.

149. Frost, A., Perera, R., Roux, A., Spasov, K., Destaing, O., Egelman, E.H., De Camilli, P. and Unger, V.M. (2008), “Structural Basis of Membrane Invagination by F-BAR Domains”, Cell 132, 807-817.

150. Galkin, V.E., Yu, X., Bielnicki, J., Heuser, J., Ewing, C.P., Guerry, P. and Egelman, E.H. (2008), “Divergence of Quaternary Structures among Bacterial Flagellar Filaments”, Science 320, 382-385. Full Text: http://www.sciencemag.org/cgi/content/full/320/5874/382?ijkey=yeFpcCKkG4J4E&keytype=ref&siteid=sci

151. Wang, Y.A., Yu, X., Ng, S.Y., Jarrell, K.F. and Egelman, E.H. (2008), “The Structure of an Archaeal Pilus”, J. Mol. Biol.381, 456-466.

152. Ghazi-Tabatabai,  S., Saksena, S., Short,  J.M., Pobbati, A.V., Veprintsev, D.B., Crowther, R.A.,  Emr, S.D. Egelman, E.H. and Williams, R.L. (2008),  “Structure and disassembly of filaments formed by the ESCRT-III subunit Vps24”, Structure 16, 1345-1356.

153. Sheridan, S.D., Yu, X., Roth, R., Heuser, J.E., Sehorn, M.G., Sung, P., Egelman, E.H., and Bishop, D.K. (2008), “A comparative analysis of Dmc1 and Rad51 nucleoprotein filaments”, Nucleic Acids Res. 36, 4057-4066.

154.  Egelman, E.H. (2008), “Helicity in electron microscopy images – a comment on Wang et al.”, BioEssays 30, 791-792.

155. Ploquin, M., Bransi, A., Paquet, E.R., Stasiak, A.Z., Stasiak, A., Yu, X., Cieslinska, A.M., Egelman, E.H., Moineau, S., Masson, J.Y. (2008), “Functional and Structural Basis for a Bacteriophage Homolog of Human RAD52”, Current Biology 18, 1142-1146.

156. Egelman, E.H. (2008), “Problems in Fitting High Resolution Structures into Electron Microscopic Reconstructions”, HFSP Journal 2, 324-331.


135.  Egelman, E. H. (2007), “The Iterative Helical Real Space Reconstruction Method: Surmounting the Problems Posed by Real Polymers”, J. Structural Biology 157, 83-94.

136.  Benchaar, S.A., Xie, Y., Phillips, M., Loo, R.R., Galkin, V.E., Orlova, A., Thevis, M., Muhlrad, A., Almo, S.C., Loo, J.A., Egelman, E.H. and Reisler, E. (2007), “Mapping the Interaction of Cofilin with Subdomain 2 on Actin”, Biochemistry 46, 225-233.

137. Li, X., Zhang, X.-P., Solinger, J., Kiianitsa, K., Yu, X., Egelman, E.H., Heyer, W.-D. (2007), “Rad51 And Rad54 Atpase Activities Are Both Required To Modulate Rad51-dsDNA Filament Dynamics,” Nucleic Acids Research 35, 4124-4140.

138. Egelman, E.H. (2007), “Prolegomena to Any Future Biophysics (with apologies to I. Kant)”. Biophys. J. 93, E01-E02.

139. Esashi, F., Galkin, V.E., Yu, X., Egelman, E.H., and West, S.C. (2007). Stabilization of RAD51 nucleoprotein filaments by the C-terminal region of BRCA2. Nature Struct. Mol. Biol. 14, 468-474.

140. Petalcorin, M.I., Galkin, V.E., Yu, X., Egelman, E.H., and Boulton, S.J. (2007). Stabilization of RAD-51-DNA filaments via an interaction domain in Caenorhabditis elegans BRCA2. Proc. Natl. Acad. Sci. U. S. A 104, 8299-8304.

141. Egelman, E.H. (2007), “Single-particle reconstruction from EM images of helical filaments”, Current Opinion in Structural Biology 17, 556-561.

142. Orlova, A., Garner, E.C., Galkin, V.E., Heuser, J., Mullins, R.D. and Egelman, E.H. (2007). "The Structure of Bacterial ParM Filaments", Nature Structural and Molecular Biology 14, 921-926.

143. Burgeev, D.V., Yu, X., Egelman, E.H. and Mazin, A.V. (2007), “Novel pro- and anti-recombination activities of the Bloom’s syndrome helicase”, Genes and Dev.21, 3085-3094.

144. Reisler, E. and Egelman, E.H. (2007), “Actin's structure and function: What we still do not understand”, J. Biol. Chem. 282, 36133-7.

128. Cherepanova, O., Orlova, A., Galkin, V.E., vander Ven, P.F.,  Furst, D.O., Jin, J.P., and Egelman, E.H. (2006). “Xin-repeats and Nebulin-like Repeats Bind to F-actin in a Similar Manner”, J. Mol. Biol. 356, 714-723.

129. Kudryashov, D.S., Galkin, V.E., Orlova, A., Phan, M., Egelman, E.H., Reisler, E. (2006), “Cofilin cross-bridges adjacent actin protomers and replaces the longitudinal F-actin interface”, J. Mol. Biol. 358, 785-797.

130. Galkin, V.E., Orlova, A., Fattoum, A., Walsh, M.P. and Egelman, E.H. (2006), “The CH-domain of calponin does not determine the modes of calponin binding to F-actin,” J. Mol. Biol. 359, 478-485.

131. Galkin, V.E., Wu, Y., Zhang, X.P., Qian, X., He, Y., Yu, X., Heyer, W.D., Luo, Y., and Egelman, E.H. (2006), “The Rad51/RadA N-Terminal Domain Activates Nucleoprotein Filament ATPase Activity,” Structure. 14, 983-992.

132. Wang, Y.A., Yu, X., Overman, S.A., Tsuboi, M., Thomas, G.J., Jr., and Egelman, E.H. (2006), “The Structure of a Filamentous Bacteriophage,” J. Mol. Biol. 361, 209-215.

133. Wang, Y.A., Yu, X., Yip, C.K., Strynadka, N.C., and Egelman, E.H. (2006), “Structural Polymorphism in Bacterial EspA Filaments Revealed by Cryo-EM and an Improved Approach to Helical Reconstruction,” Structure 14, 1189-96.

134. Craig, L., Volkmann, N., Arvai, A.S., Pique, M.E., Yeager, M., Egelman, E.H., and Tainer, J.A. (2006), “Type IV Pilus Structure by Cryo-Electron Microscopy and Crystallography: Implications for Pilus Functions in Pathogenicity,” Mol. Cell 23, 651-662.

122. Chen, Y.-J., Yu, X., Kasiviswanathan, R., Shin, J.-H., Kelman, Z. and Egelman, E.H. (2005), “Structural Polymorphism of Methanothermobacter thermautotrophicus MCM”, J. Mol. Biol. 346, 389-394.

123. Galkin, V.E., Orlova, A., Koleske, A.J. and Egelman, E.H. (2005), “The Arg nonreceptor tyrosine kinase modifies F-actin structure”, J. Mol. Biol. 346, 565-575.

124. Trachtenberg, S., Galkin, V.E. and Egelman, E.H. (2005), “Refining the Structure of the Halobacterium salinarum Flagellar Filament Using the Iterative Helical Real Space Reconstruction Method: Insights into Polymorphism”, J. Mol. Biol. 346, 665-676.

125. Galkin, V., Esashi, F., Yu, X., Yang, S., West, S.C. and Egelman, E.H. (2005), “BRCA2 BRC Motifs Bind RAD51-DNA Filaments”, Proc. Natl. Acad. Sci. U.S.A. 102, 8537-8542.

126. Dang, T.X., Farah, S.J., Gast, A., Robertson, C., Carragher, B., Egelman, E. and Wilson-Kubalek, E.M. (2005), “Helical crystallization on lipid nanotubes: streptavidin as a model protein”, J. Struct. Biol. 150, 90-99.

127. Woodhead, J.L., Zhao, F.-Q., Craig, R., Egelman, E.H., Alamo, L. and Padron, R. (2005), “Atomic Model of a Myosin Filament in the Relaxed State”, Nature 436, 1195-1199.


117. Yu, X., VanLoock, M.S., Yang, S., Reese, J.T., and Egelman, E.H. (2004), “What is the Structure of the RecA-DNA Filament?”, Current Protein and Peptide Science 5, 73-79.

118. Chen, Y.-J., Zhang, P., Egelman, E.H. and Hinshaw, J.E. (2004), “Stalk Region of Dynamin Drives the Constriction of Dynamin Tubes,” Nature Structural and Molecular Biology 11, 574-575.

119. Egelman, E.H. (2004), “More Insights into Structural Plasticity of Actin-Binding Proteins,” Structure 12, 909-910.

120. Egelman, E.H. (2004),”Acrosomal Actin: Twists and Turns of a Versatile Filament”, Current Biology 14, R959-961.

121. Orlova, A., Shvetsov, A., Galkin, V.E., Kudryashov, D.S., Rubenstein, P.A., Egelman, E.H. and Reisler, E. (2004), “Actin destabilizing factors disrupt filaments via a time-reversal of polymerization”, Proc. Natl. Acad. Sci. U.S.A. 101, 17664-668.


105. VanLoock, M.S.,  Yu, X., Yang, S., Lai, A.L., Low, C., Campbell, M.J. and Egelman, E.H. (2003), “ATP-Mediated Conformational Changes in the RecA Filament”, Structure 11, 187-196.

106. Galkin, V.E., Orlova, A., Lukoyanova, N., VanLoock, M.S., Hååg, P., Bullard, P., and Egelman, E. H. (2003), “The Location of Ubiquitin in Lethocerus Arthrin,” J. Mol. Biol. 325, 623-628.

107. Egelman, E.H. (2003),  “A Tale of Two Polymers: New Insights into Helical Filaments”, Nature Reviews Mol. Cell Biology 4, 621-630.

108. Cordes, F.S., Komoriya, K., Larquet, E., Yang, S., Egelman, E.H., Blocker, A., and Lea, S.M. (2003), “Helical Structure of the Needle of the Type III Secretion System of Shigella flexneri”, J. Biol. Chem. 278, 17103-17107.

109. Egelman, E.H. (2003), “Actin’s Prokaryotic Homologs”, Current Opinion in Structural Biology 13, 244-248.

110. Egelman,E.H.(2003), “Cell walls, cell shape, and bacterial actin homologs”,  Developmental Cell 5, 4-5.

111. Galkin, V.E., Orlova, A., VanLoock, M.S. and Egelman, E.H. (2003), “Do the Utrophin Tandem Calponin Homology Domains Bind F-Actin in a Compact or Extended Conformation?”, J. Mol. Biol. 331, 967-972.

112. VanLoock, M.S., Yu, X. Yang, S., Galkin, V.E., Huang, H., Rajan, S.S., Anderson, W.F., Stohl, E.A., Seifert, H.S. and Egelman, E.H. (2003), “Complexes of RecA with LexA and RecX Differentiate Between Active and Inactive RecA Nucleoprotein Filaments”, J. Mol. Biol. 333, 345-354.

113. Lilic, M., Galkin, V.E., Orlova, A., VanLoock, M.S., Egelman, E.H. and Stebbins, C.E. (2003), “Salmonella SipA Polymerizes Actin by Stapling Filaments with non-Globular Protein Arms”, Science 301, 1918-1921.

114. Yang, S., Yu, X., Galkin, V.E. and Egelman, E.H. (2003), “Issue of Resolution and Polymorphism in Single-Particle Reconstruction”, J. Structural Biology 144, 162-171.

115. Haruta, N., Yu, X., Yang, S., Egelman, E.H. and Cox, M.M. (2003), “A DNA-Pairing Enhanced Conformation of Bacterial RecA Proteins”, J. Biol. Chem. 278, 52710-52723.

116. Galkin, V.E., Orlova, A., VanLoock, M.S., Shvetsov, A., Reisler, E. and Egelman, E.H. (2003), “ADF/Cofilin Use an Intrinsic Mode of F-Actin Instability to Disrupt Actin Filaments,” J. Cell Biol. 163, 1057-1066.

94. Lukoyanova, N., VanLoock, M.S., Orlova, A., Galkin, V.E., Wang, K. and Egelman, E.H. (2002), “Each Actin Subunit Has Three Nebulin-Binding Sites: Implications for Steric Blocking.” Current Biology 12, 383-388.

95. VanLoock, M.S., Alexandrov, A., Yu, X., Cozzarelli, N.R. and Egelman, E.H. (2002), “SV40 Large T-antigen Hexamer Structure: Domain Organization and DNA-Induced Conformational Changes.” Current Biology 12, 472-476.

96. Galkin, V.E., VanLoock, M.S., Orlova, A. and Egelman, E.H. (2002), “A New Internal Mode in F-Actin Helps Explain the Remarkable Evolutionary Conservation of Actin’s Sequence and Structure.” Current Biology 12, 570-575.

97. Galkin, V.E.,  Orlova, A., VanLoock, M.S., Rybakova, I.N., Ervasti, J.M. and Egelman, E.H. (2002), “The Utrophin Actin-Binding Domain Binds F-Actin in Two Different Modes: Implications for the Spectrin Superfamily of Proteins.” J. Cell Biol. 157, 243-251.

98. Chen, Y.J., Yu, X., and Egelman, E.H. (2002), “The Hexameric Ring Structure of the E. coli RuvB Branch Migration Protein.” J. Mol. Biol. 319, 587-591.

99. Galkin, V.E., Orlova, A., VanLoock, M.S., Zhou, D., Galán, J.E. and Egelman, E.H. (2002), “The Bacterial Protein SipA Polymerizes G-Actin and Mimics Muscle Nebulin.” Nature Struct. Biol. 9, 518-521.

100. Mu, X.-O., Egelman, E.H. and Bullitt, E. (2002), “Structure and function of Hib pili from Haemophilus influenzae type b.” J. Bact. 184, 4868-4874.

101. Yu, X., VanLoock, M.S., Poplawski, A., Kelman, Z., Xiang, T., Tye, B.K. and Egelman, E.H. (2002), “The Methanobacterium thermoautotrophicum MCM protein Can Form Heptameric Rings,” EMBO Reports 3,  792-797.

102. Yang, S., Yu, X., VanLoock, M.S., Jezewska, M.J., Bujalowski, W. and Egelman, E.H. (2002), “Flexibility of the Rings: Structural Asymmetry in the DnaB Hexameric Helicase,” J. Mol. Biol. 321, 839-849.

103. Sablin, E.P., Dawson, J.F., VanLoock, M.S., Spudich, J.A., Egelman, E.H., and Fletterick, R.J. (2002), “How Does ATP Hydrolysis Control Actin’s Associations?”, P.N.A.S. 99, 10945-10947.

104. Ayora, S., Missich, R., Mesa, P., Lurz, R., Yang, S., Egelman, E.H., Alonso, J.C. (2002), “Homologous-pairing activity of the Bacillus subtilis bacteriophage SPP1 replication protein G35P”, J. Biol. Chem. 277, 35969-35979.


80. Orlova, A., Prochniewicz, E., Thomas, D.D., Rybakova, I.N., Ervasti, J.M. and Egelman, E.H. (2001). “Binding of dystrophin’s tandem calponin homology domain to F-actin is modulated by actin’s structure.” Biophysical Journal 80, 1926-1931.

81. Galkin, V.E., Orlova, A., Lukoyanova, N., Wriggers, W. and Egelman, E.H. (2001). “ADF Stabilizes an Existing State of F-Actin and Can Change the Tilt of F-Actin Subunits.” J. Cell Biol. 153, 75-86.

82. Egelman, E.H. (2001). “Bacterial Conjugation: Running rings around DNA.” Current Biology 11, R103-R105.

83. Egelman, E.H. (2001). “Pumping DNA”. Nature 409, 573-575.

84. Yu, X., Jacobs, S.A., West, S.C., Ogawa, T. and Egelman, E.H. (2001). “Domain Structure and Dynamics in the Helical Filaments Formed by RecA and Rad51 on DNA”. Proc. Natl. Acad. Sci. U.S.A. 98, 8419-8424.

85. Egelman, E. H. (2001). “Does a Stretched DNA Structure Dictate the Helical Geometry of RecA-like Filaments?”, J. Mol. Biol. 309, 539-542.

86. VanLoock, M.S., Yu, X., Kasai, M. and Egelman, E.H. (2001). “Electron Microscopic Studies of the Translin Octameric Ring.” J. Structural Biology 135, 58-66.

87. Peterson, C., Simon, M., Hodges, J., Mertens, P., Higgins, L., Egelman, E.H. and Anderson, D. (2001). “Composition and Mass of the Bacteriophage Phi29 Prohead and Virion.”  J. Structural Biology 135, 18-25.

88. Orlova, A., Galkin, V.E., VanLoock, M.S., Kim, E., Shvetsov, A., Reisler, E. and Egelman, E.H. (2001), “Probing the Structure of F-Actin: Cross-links Constrain Atomic Models and Modify Actin Dynamics”, J. Mol. Biol. 312, 95-106.

89. VanLoock, M.S.,  Chen, Y.-J., Yu, X., Patel, S.S. and Egelman, Edward H. (2001), “The Primase Active Site is on the Outside of the Hexameric Bacteriophage T7 Gene 4 Helicase-Primase Ring”, J. Mol. Biol. 311, 951-956.

90. Yang, S., VanLoock, M.S., Yu, X. and Egelman, E.H. (2001), “Comparison of Bacteriophage T4 UvsX and Human Rad51 Filaments Suggests that RecA-like Polymers May Have Evolved Independently”, J. Mol. Biol. 312, 1001-1011.

91. Egelman, E.H. (2001), “Actin Allostery Again?”, Nature Structural Biology 8, 735-736.

92. Yang, S., Yu, X., Seitz, E.M., Kowalczykowski, S.C. and Egelman, E.H. (2001), “Archaeal RadA protein binds DNA as both helical filaments and octameric rings.” J. Mol. Biol. 314, 1077-1085.

93. Egelman, E.H. (2001), “Molecular Evolution: Actin’s Long Lost Relative Found.” Current Biology 11, R1022-1024.


74. Stasiak, A.Z., Larquet, E., Stasiak, A., Müller, S., Engel, A., Van Dyck, E., West, S.C. and Egelman, E.H. (2000). “The human Rad52 protein exists as a heptameric ring, with structural homology to hexameric helicases.” Current Biology 10, 337-340.

75. Orlova, A. and Egelman, E.H. (2000). “F-actin retains a memory of angular order.” Biophysical Journal 78, 2180-2185.

76. Yu, X., Horiguchi, T., Shigesada, K, and Egelman, E.H. (2000) “Three-dimensional Reconstruction of transcription Termination Factor rho: Orientation of the N-terminal Domain and Visualization of an RNA-binding site.” J. Mol. Biol. 299, 1279-1287.

77. Frank, E.G., Cheng, N., Do, C., Cerritelli, M.E., Bruck, I., Goodman,  M.F., Egelman, E.H., Woodgate, R., and Steven, A.C. (2000). “Visualization of two binding sites for the Escherichia coli UmuD'2C complex (DNA pol V) on RecA-ssDNA filaments.” J. Mol. Biol. 297, 585-597.

78. Egelman, E.H. (2000). “A common structural core in proteins active in DNA recombination and replication.” Trends in Biochemical Sciences (TIBS) 25, 180-184.

79. Egelman, E.H. (2000). “A Robust Algorithm for the Reconstruction of Helical Filaments Using Single-Particle Methods.” Ultramicroscopy 85, 225-234.



70. Fouts, E.,  Yu, X., Egelman, E.H. and Botchan,  M. (1999) “Biochemical and Electron Microscopic Image Analysis of the Hexameric E1 Helicase”, J. Biol. Chem., 274, 4447-4458

71. Belmont, L.D., Orlova, A., Drubin, D.G. and Egelman, E.H. (1999) “A Change in Actin Conformation Associated with Filament Instability after Pi Release.” Proc. Natl. Acad. Sci. U.S.A. 96, 29-34.

72. Passy, S. I., Yu, X., Li, Z., Radding, C.M. and Egelman, E.H. (1999) “Rings and Filaments of β Protein from Bacteriophage λ Suggest a New Superfamily of Recombination Proteins.” Proc. Natl. Acad. Sci. U.S.A. 96, 4279-4284.

73. Passy, S.I., Yu, X., Li, Z., Radding, C.M., Masson, J.-Y., West, S.C. And Egelman, E.H. (1999) “Human Dmc1 protein binds DNA as an octameric ring.”  Proc. Natl. Acad. Sci.U.S.A. 96, 10684-10688.

66. Egelman, E.H. (1998) “Tubulin Family: Kinship of Key Proteins Across Phylogenetic Domains,” Current Biology 8, R288-R290.

67. Yu, X., Shibata, T. and Egelman, E.H. (1998) “Identification of a Defined Epitope on the Surface of the Active RecA-DNA Filament Using a Monoclonal Antibody and Three-Dimensional Reconstruction.” J. Mol. Biol. 283, 985-992.

68. Kim, E., Bobkova, E., Miller, C.J., Orlova, A., Hegyi, G., Egelman, E.H., Muhlrad, A. and Reisler, E. (1998) “Intrastrand Cross-linked Actin Between Gln41 and Cys374. II. Inhibition of Motion and Force Generation with Myosin.” Biochemistry 37, 17801-17809.

69. Egelman, E.H. (1998) “Bacterial Helicases.” Journal of Structural Biology 124, 123-128.

59. Orlova, A. and Egelman, E.H. (1997) “Cooperative Rigor Binding of Myosin to Actin is a Function of F-Actin Structure”, J. Mol. Biol. 265, 469-474.

60. Yu, X., West, S.C. and Egelman, E.H. (1997) “Structure and Subunit Composition of the RuvAB-Holliday Junction Complex”, J. Mol. Biol. 266, 217-222.

61. Yu, X. and Egelman, E.H. (1997) “The RecA Hexamer Is a Structural Homologue of Ring Helicases”, Nature Structural Biology 4, 101-104.

62. Orlova, A., Chen, X., Rubenstein, P.A, and Egelman, E.H. (1997) “Modulation of Yeast F-actin Structure by a Mutation in the Nucleotide-Binding Cleft”, J. Mol. Biol. 271, 235-243.

63· Egelman, E.H. (1997) “New Angles on Actin Dynamics”, Structure 5, 1135-37.

64. A. Stasiak, A., West, S.C. and  Egelman, E.H. (1997) “Sickle Cell Anemia Research and a Recombinant DNA Technique (letter)”, Science 277, 460.

65. Egelman, E.H., Orlova, A. and McGough, A. (1997) “Only One F-Actin Model (letter)”, Nature Structural Biology 4, 683-684.

56. Yu, X., Jezewska, M.J., Bujalowski, W. and Egelman, E.H. (1996) “The Hexameric E. coli” DnaB Helicase Can Exist in Different Quaternary States”, J. Mol. Biol. 259, 7-14.

57. Yu, X., Hingorani, M., Patel, S.S. and Egelman, E.H. (1996) “DNA Is Bound Within the Central Hole to One or Two of the Six Subunits of the T7 DNA Helicase”, Nature Struct. Biol. 3, 740-743.

58. Egelman, E.H. (1996) “Homomorphous hexameric helicases: tales from the ring cycle”, Structure 4, 759-762.

48. Egelman, E.H., Yu, X., Wild, R., Hingorani, M.M. and Patel, S.S. (1995) “Bacteriophage T7 Helicase/Primase Proteins Form Rings Around Single-Stranded DNA that Suggest a General Structure for Hexameric Helicases.” Proc. Natl. Acad. Sci. U.S.A. 92, 3869-3873

49. Orlova, A. and Egelman, E.H. (1995) "Structural Dynamics of F-actin. I. Changes in the C-terminus." J. Mol. Biol. 245, 582-597.

50. Orlova, A., Prochniewicz, E. and Egelman, E.H. (1995) "Structural Dynamics of F-actin. II. Cooperativity in Structural Transitions."  J. Mol. Biol. 245, 598-607.

51· Nojima, D., Linck, R. and Egelman, E.H. (1995) "At Least One of the Protofilaments of the Axonemal Doublet Microtubule is Not Made From Tubulin." Current Biology 5, 158-167.

52· Egelman, E.H.  and Orlova, A. (1995) "New Insights Into Actin Filament Dynamics." Current Opinion in Structural Biology 5, 172-180.

53. Egelman, E.H. (1995) “Structural Studies of Tubulin-Based Motility Race Ahead”, Current Biology 5, 1354-1356.

54. Yu, X., Angov, E., Camerini-Otero, R.D. and Egelman, E.H. (1995) “Structural Polymorphism of the RecA Protein from the Thermophilic Bacterium T. Aquaticus”, Biophysical J. 69, 2728-2738.

55. Egelman, E.H. and Orlova, A. (1995) “Allostery, Cooperativity and Different Structural States in F-Actin”, Journal of Structural Biology 115, 159-162.


42. Stasiak, A. and Egelman, E.H.(1994) "Structure and Function of RecA-DNA Complexes." Experientia 50, 192-203.

43. Bednar, J., Furrer, P., Stasiak, A., Dubochet, J., Egelman, E.H. and Bates, A.D. (1994) "The twist, writhe and overall shape of supercoiled DNA change during counterion induced transition from a loosely to a tightly interwound superhelix. Possible implications for DNA structure in vivo." J. Mol. Biol. 235, 825-847.

44. Orlova, A., Yu, X. and Egelman, E.H. (1994) "Three-dimensional Reconstruction of a Co-complex of F-Actin with Antibody Fab Fragments to Actin's Amino Terminus." Biophysical Journal 66, 276-285.

45. Egelman, E.H. (1994) "The Ghost of Ribbons Past." Current Biology 4, 79-81.

46. Stasiak, A., Tsaneva, I., West, S.C., Benson, K., Yu, X. and Egelman, E.H. (1994) "The E. coli RuvB Branch Migration Protein Forms Double Hexameric Rings Around DNA." Proc. Natl. Acad. Sci. U.S.A. 91, 7618-7622.

47. Tsuprun, V., Anderson, D. and Egelman, E.H. (1994) "The Bacteriophage Phi29 Head-Tail Connector Shows 13-Fold Symmetry in Both Hexagonally-Packed Arrays and as Single Particles." Biophysical Journal 66, 2139-2150.


35. Egelman, E.H. and Stasiak, A. (1993) "Electron Microscopy of RecA-DNA Complexes." Micron 24, 309-324.

36. Yu, X. and Egelman, E.H. (1993) "The LexA Repressor Binds within the Deep Helical Groove of the Activated RecA Filament." J.  Mol. Biol. 231, 29-40.

37. Orlova, A. and Egelman, E.H. (1993) "A Conformational Change in the Actin Subunit Can Change the Flexibility of the Actin Filament." J. Mol. Biol. 232, 334-341.

38. Egelman, E.H. (1993) "What do X-ray Crystallographic and Electron Microscopic Structural Studies of the RecA Protein Tell Us About Recombination?", Current Opinion in Structural Biology 3, 189-197.

39. Ogawa, T., Yu, X., Shinohara, A. and Egelman, E.H. (1993) "Similarity of the Yeast Rad51 Filament to the Bacterial RecA Filament." Science 259, 1896-1899.

40. Yu, X. and Egelman, E.H. (1993) "The DNA Conformation Induced by the Bacteriophage T4 UvsX Protein Appears Identical to the Conformation Induced by the E. coli RecA Protein". J. Mol. Biol. 232, 1-4.

41. Ogawa, T., Shinohara, A., Nabetani, A., Ikeya, T., Yu, X., Egelman, E.H. and Ogawa, H. (1993) "RecA-like Recombination Proteins in Eukaryotes: Functions and Structures of RAD51 Genes." Cold Spring Harbor Symposia on Quantitative Biology 58, 567-576.


29. Yu, X. and Egelman, E.H. (1992) "Direct Visualization of Dynamics and Cooperative Conformational Changes Within RecA Filaments That Appear To Be Associated with the Hydrolysis of ATP-g-S." J. Mol. Biol. 225, 193-216.

30. Yu, X. and Egelman, E.H. (1992) "Structural Data Suggest that the Active and Inactive Forms of the RecA Filament are not Simply Interconvertible." J. Mol. Biol. 227, 334-346.

31. Egelman, E.H. (1992) "Two Key Questions Raised by an Atomic Model for F-actin." Current Opinion in Structural Biology 2, 286-292.

32. Egelman, E.H. and DeRosier, D.J. (1992) "Image Analysis Shows that Variations in Actin Crossover Spacings are Random, Not Compensatory." Biophysical Journal 63, 1299-1305.

33. Orlova, A. and Egelman, E.H. (1992) "The Structural Basis for the Destabilization of F-Actin by Phosphate Release Following ATP Hydrolysis." J. Mol. Biol. 227, 1043-1053.

34. Turnquist, S., Simon, M., Egelman, E.H. and Anderson, D. (1992) "Supercoiled DNA Wraps Around the Bacterio­phage f29 Head-Tail Connector." P.N.A.S. 89, 10479-10483.

26. Egelman, E.H. and DeRosier, D.J. (1991) "Angular Disorder in Actin: Is it Consistent with General Principles of Protein Structure?" Journal of Molecular Biology 217, 405-408.

27. Yu, X. and Egelman, E.H (1991) "Removal of the RecA C-terminus Results in a Conformational Change in the RecA-DNA Filament." Journal of Structural Biology 106, 243-254.

28. Dustin, I., Furrer, P., Stasiak, A., Dubochet, J. Langowski, J. and Egelman, E.H. (1991) "Spatial Visualization of DNA in Solution." Journal of Structural Biology 107, 15-21.

25. Yu, X. and Egelman, E.H. (1990) "Image analysis reveals that the E. coli RecA protein consists of two domains."  Biophysical Journal 57, 555-566.

23. Egelman, E.H., Wu, S.-S., Amrein, A., Portner, A. and Murti, G. (1989). "The Sendai Virus Nucleocapsid Exists in at Least Four Different Helical States." J. Virology 63, 2233-2243.

24. Egelman, E.H. and Yu, X. (1989) "The Location of DNA in RecA-DNA Helical Filaments." Science 245, 404-407.


20. Egelman, E.H. and Stasiak, A. (1988) "Structure of Helical RecA-DNA Complexes.  II. Local Conformational Changes Visualized in Bundles of RecA-ATP-γ-S Filaments."  Journal of Molecular Biology 200, 329-349.

21. Stasiak, A. and Egelman, E.H. (1988) "Visualization of Recombination Reactions." p. 265-307, in Genetic Recombination, R.Kucherlapati and G. Smith, eds., ASM Press.

22. Stasiak, A., Egelman, E.H. and Howard-Flanders, P. (1988) "Structure of Helical RecA-DNA Complexes. III. The Structural Polarity of RecA Filaments and Functional Polarity in the RecA-Mediated Strand Exchange Reaction." Journal of Molecular Biology 202, 659-662.


13. Trinick, J., Cooper, J., Seymour, J. and Egelman, E.H. (1986) "Electron Micros­copy of Frozen Hydrated Actin Filaments". Journal of Microscopy 141, 349-360.

14. Stasiak, A. and Egelman, E.H. (1986) "The Structure and Dynamics of recA Protein ‑ DNA Complexes as Determined by Image Analysis of Electron Micrographs."  Biophysical Journal 49, 5-7.

15. Stasiak, A. and Egelman, E.H. (1986) "RecA‑DNA Helical Complexes in Genetic Recombination." Biochemical Society Transactions 14, 218-220.

16. Egelman, E.H. (1986) "An Algorithm for Straightening Images of Curved Filaments".  Ultramicroscopy 19, 367-374.

17. Egelman, E.H. and Stasiak, A. (1986) "The Structure of Helical RecA-DNA Com­plexes: I. Complexes Formed in the Presence of ATP-gamma-S or ATP." Journal of Molecular Biology 191, 677-697.

18. Stasiak, A. and Egelman, E.H. (1986) "RecA Protein-DNA Interactions in ­Recombination," in: DNA Replication and Recombination, 619-628, T. Kelly and R. McMacken, eds., Alan R. Liss, N.Y.

19. Howard-Flanders, P., West, S.C., Cassuto, E., Hahn, T-R, Egelman, E.H., and Stasiak, A. (1986)  "Structure of recA spiral Filaments and their Role in Homol­ogous Pairing and Strand Exchange in Genetic Recombination." in: DNA Replication and Recombination, 609-617, T. Kelly and R. McMacken, eds., Alan R. Liss, N.Y.


12. Egelman, E.H. (1985) "The Structure of F‑Actin" . The Journal of Muscle Research and Cell Motility 6, 129‑151.

11. Howard‑Flanders, P., West, S.C., Rusche, J.R., and Egelman, E.H. (1984) "Molecular Mechanisms of General Genetic Recombination: The DNA Binding Sites of Rec A Protein". Cold Spring Harbor Symposia on Quantitative Bio­logy XLIX, 571‑580.


7. Tilney, L.G., Egelman, E.H., DeRosier, D.J., and Saunders,J.C. (1983) "Hair Cells, Stereocilia, and Actin Filaments of the Bird Cochlea.II"  Journal of Cell Biology 96, 822‑834.

8. Egelman, E.H., Francis, N., and DeRosier, D.J. (1983) "Helical Disorder and the Filament Structure of F‑Actin are Elucid­ated by the Angle‑layered Aggregate". Journal of Molecular Biology 166, 605‑623.
Appendix: Egelman, E.H. and DeRosier, D.J. (1983) "A Model for F‑Actin Derived from Image Analysis of Isolated Filaments". Journal of Molecular Biology 166, 623‑629.

9. Egelman, E.H. and DeRosier, D.J. (1983) "Structural Studies of F‑Actin"  in Actin: Its Structure and Function in Muscle and Non‑Muscle Cells, p. 17-24, C. dos Remedios and J. Barden, eds., Academic Press, Sydney.

10. Egelman, E.H. and Padron, R. (1983) "X‑Ray Diffraction Evidence that Actin is a 100A Filament". Nature 307, 56‑58.

4. Tilney, L.G., Saunders, J.C., Egelman, E.H., and DeRosier,D.J. (1982) "Changes in the Organization of Actin Filaments in the Stereocilia of Noise Damaged Lizard Cochlea". Hearing Research 7, 181‑197.

5. Egelman, E.H., Francis, N. and DeRosier, D.J. (1982) "F‑Actin: A Helix with a Random Variable Twist". Nature 298, 131‑135

6. Egelman, E.H. and DeRosier, D.J. (1982) "The Fourier Transform of Actin and Other Helical Systems with Cumulative Random Angular Disorder". Acta Crystallographica A38, 796‑799.

3. Egelman, E.H. (1981) "Problem of Light Piping in Immunofluorescence Studies". Nature 294, 674.


2. DeRosier, D.J., Tilney, L.G., and Egelman, E.H. (1980) "Actin in the Inner Ear: The Remarkable Structure of the Stereocilium."  Nature 287, 291‑296.

1. Egelman, E.H. (1979) "Sauce Bearnaise." New England Journal of Medicine 301, 276.