Dr. Z. (Tzviya) Zeev Ben Mordehai

David de Wiedgebouw
Universiteitsweg 99
Kamer 2.66
3584 CG Utrecht

Dr. Z. (Tzviya) Zeev Ben Mordehai

Universitair hoofddocent
Structural Biochemistry
030 253 3178
z.zeev@uu.nl

Publicaties

2024

Wetenschappelijke publicaties

Mocking, J., & Zeev-Ben-Mordehai, T. (2024). Towards deciphering the molecular architecture of the human sperm connecting piece. Human Reproduction, 39(Supplement_1), I235-I235. Article deae108.469. https://doi.org/10.1093/humrep/deae108.469
Pascha, M. N., Ballegeer, M., Roelofs, M. C., Meuris, L., Albulescu, I. C., van Kuppeveld, F. J. M., Hurdiss, D. L., Bosch, B. J., Zeev-Ben-Mordehai, T., Saelens, X., & de Haan, C. A. M. (2024). Nanoparticle display of neuraminidase elicits enhanced antibody responses and protection against influenza A virus challenge. npj Vaccines, 9(1), Article 97. https://doi.org/10.1038/s41541-024-00891-3
Pascha, M. N., Ballegeer, M., Roelofs, M. C., Meuris, L., Albulescu, I. C., Kuppeveld, F. J. M. V., Hurdiss, D. L., Bosch, B.-J., Zeev-Ben-Mordehai, T., Saelens, X., & Haan, C. A. M. D. (2024). Nanoparticle display of neuraminidase elicits enhanced antibody responses and protection against influenza A virus challenge in mice. Research Square. https://doi.org/10.21203/rs.3.rs-3579434/v1
https://dspace.library.uu.nl/bitstream/handle/1874/436082/748a8378-0382-43eb-8ee8-d7467ff4d5a6.pdf?sequence=1

2023

Wetenschappelijke publicaties

Wang, Z., He, M., He, H., Kilby, K., Antueno, R. D., Castle, E., McMullen, N., Qian, Z., Zeev-Ben-Mordehai, T., Duncan, R., & Pan, C. (2023). Nonenveloped Avian Reoviruses Released with Small Extracellular Vesicles Are Highly Infectious. Viruses, 15(7). https://doi.org/10.3390/v15071610
https://dspace.library.uu.nl/bitstream/handle/1874/435781/viruses-15-01610.pdf?sequence=1
Leung, M. R., Zeng, J., Wang, X., Roelofs, M. C., Huang, W., Zenezini Chiozzi, R., Hevler, J. F., Heck, A. J. R., Dutcher, S. K., Brown, A., Zhang, R., & Zeev-Ben-Mordehai, T. (2023). Structural specializations of the sperm tail. Cell, 186(13), 2880-2896.e17. https://doi.org/10.1016/j.cell.2023.05.026
https://dspace.library.uu.nl/bitstream/handle/1874/434165/1-s2.0-S0092867423005767-main.pdf?sequence=1

2022

Wetenschappelijke publicaties

Leung, M. R., Roelofs, M. C., Chiozzi, R. Z., Hevler, J. F., Heck, A. J. R., & Zeev-Ben-Mordehai, T. (2022). Unraveling the intricate microtubule inner protein networks that reinforce mammalian sperm flagella. bioRxiv. https://doi.org/10.1101/2022.09.29.510157
Leung, M. R., Zenezini-Chiozzi, R., Hevler, J., Ravi, R. T., Heck, A. J. R., & Zeev-Ben-Mordehai, T. (2022). The remarkable sperm mitochondrial sheath: insights from cryo-electron tomography. Biophysical Journal, 121(3), 4a. Article Supplement 1. https://doi.org/10.1016/j.bpj.2021.11.2684
Judernatz, J. H., Roelofs, M. C., & Zeev-Ben-Mordehai, T. (2022). Cellular Cryo-Electron Tomography. In R. A. Bradshaw, G. W. Hart, & P. D. Stahl (Eds.), Encyclopedia of Cell Biology: Volume 1-6, Second Edition (Vol. 2, pp. 4-15). Elsevier. https://doi.org/10.1016/B978-0-12-821618-7.00112-7
Hurdiss, D. L., El Kazzi, P., Bauer, L., Papageorgiou, N., Ferron, F. P., Donselaar, T., Van Vliet, A. L. W., Shamorkina, T. M., Snijder, J., Canard, B., Decroly, E., Brancale, A., Zeev-Ben-Mordehai, T., Förster, F., Van Kuppeveld, F. J. M., & Coutard, B. (2022). Fluoxetine targets an allosteric site in the enterovirus 2C AAA+ ATPase and stabilizes a ring-shaped hexameric complex. Science advances, 8(1), 1-12. Article abj7615. https://doi.org/10.1126/sciadv.abj7615

2021

Wetenschappelijke publicaties

Leung, M. R., Chiozzi, R. Z., Roelofs, M. C., Hevler, J. F., Ravi, R. T., Maitan, P., Zhang, M., Henning, H., Bromfield, E. G., Howes, S. C., Gadella, B. M., Heck, A. J. R., & Zeev-Ben-Mordehai, T. (2021). In-cell structures of a conserved supramolecular array at the mitochondria-cytoskeleton interface in mammalian sperm. (pp. 1-17). bioRxiv. https://doi.org/10.1101/2021.02.16.431372
Leung, M. R., Ravi, R. T., Gadella, B. M., & Zeev-Ben-Mordehai, T. (2021). Membrane Remodeling and Matrix Dispersal Intermediates During Mammalian Acrosomal Exocytosis. Frontiers in Cell and Developmental Biology, 9, 1-13. Article 765673. https://doi.org/10.3389/fcell.2021.765673
Maitan, P. P., Bromfield, E. G., Hoogendijk, R., Leung, M. R., Zeev-Ben-Mordehai, T., van de Lest, C. H., Jansen, J. W. A., Leemans, B., Guimarães, J. D., Stout, T. A. E., Gadella, B. M., & Henning, H. (2021). Bicarbonate-Stimulated Membrane Reorganization in Stallion Spermatozoa. Frontiers in Cell and Developmental Biology, 9, 1-17. Article 772254. https://doi.org/10.3389/fcell.2021.772254
Leung, M. R., Zenezini Chiozzi, R., Roelofs, M. C., Hevler, J. F., Ravi, R. T., Maitan, P., Zhang, M., Henning, H., Bromfield, E. G., Howes, S. C., Gadella, B. M., Heck, A. J. R., & Zeev-Ben-Mordehai, T. (2021). In-cell structures of conserved supramolecular protein arrays at the mitochondria-cytoskeleton interface in mammalian sperm. Proceedings of the National Academy of Sciences of the United States of America, 118(45), 1-10. Article e2110996118. https://doi.org/10.1073/pnas.2110996118
Khanal, S., Leung, M. R., Royfman, A., Fishman, E. L., Saltzman, B., Bloomfield-Gadêlha, H., Zeev-Ben-Mordehai, T., & Avidor-Reiss, T. (2021). A dynamic basal complex modulates mammalian sperm movement. Nature Communications, 12(1), 1-11. Article 3808. https://doi.org/10.1038/s41467-021-24011-0
Leung, M. R., Roelofs, M. C., Ravi, R. T., Maitan, P., Henning, H., Zhang, M., Bromfield, E. G., Howes, S. C., Gadella, B. M., Bloomfield-Gadêlha, H., & Zeev-Ben-Mordehai, T. (2021). The multi-scale architecture of mammalian sperm flagella and implications for ciliary motility. EMBO Journal, 40(7), 1-17. Article e107410. https://doi.org/10.15252/embj.2020107410
Leung, M. R., & Zeev-Ben-Mordehai, T. (2021). Cryo-electron microscopy of cholinesterases, present and future. Journal of Neurochemistry, 158(6), 1236-1243. https://doi.org/10.1111/jnc.15245

2020

Wetenschappelijke publicaties

Ravi, R. T., Leung, M. R., & Zeev-Ben-Mordehai, T. (2020). Looking back and looking forward: contributions of electron microscopy to the structural cell biology of gametes and fertilization. Biology Open, 10(9), Article 200186. https://doi.org/10.1098/rsob.200186
Toker, L., Silman, I., Zeev-Ben-Mordehai, T., Sussman, J. L., Schopfer, L. M., & Lockridge, O. (2020). Polyproline-rich peptides associated with Torpedo californica acetylcholinesterase tetramers. Chemico-Biological Interactions, 319, Article 109007. https://doi.org/10.1016/j.cbi.2020.109007

2018

Wetenschappelijke publicaties

Leung, M. R., van Bezouwen, L. S., Schopfer, L. M., Sussman, J. L., Silman, I., Lockridge, O., & Zeev-Ben-Mordehai, T. (2018). Cryo-EM structure of the native butyrylcholinesterase tetramer reveals a dimer of dimers stabilized by a superhelical assembly. Proceedings of the National Academy of Sciences of the United States of America, 115(52), 13270-13275. https://doi.org/10.1073/pnas.1817009115
Chorev, D. S., Baker, L. A., Wu, D., Beilsten-Edmands, V., Rouse, S. L., Zeev-Ben-Mordehai, T., Jiko, C., Samsudin, F., Gerle, C., Khalid, S., Stewart, A. G., Matthews, S. J., Grünewald, K., & Robinson, C. V. (2018). Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry. Science, 362(6416), 829-834. https://doi.org/10.1126/science.aau0976
Zeng, X., Leung, M. R., Zeev-ben-mordehai, T., & Xu, M. (2018). A convolutional autoencoder approach for mining features in cellular electron cryo-tomograms and weakly supervised coarse segmentation. Journal of Structural Biology, 202(2), 150-160. https://doi.org/10.1016/j.jsb.2017.12.015

2017

Wetenschappelijke publicaties

Xu, M., Chai, X., Muthakana, H., Liang, X., Yang, G., Zeev-Ben-Mordehai, T., & Xing, E. P. (2017). Deep learning-based subdivision approach for large scale macromolecules structure recovery from electron cryo tomograms. Bioinformatics, 33(14), I13-I22. https://doi.org/10.1093/bioinformatics/btx230

2016

Wetenschappelijke publicaties

Zeev-Ben-Mordehai, T., Vasishtan, D., Duran, A. H., Vollmer, B., White, P., Pandurangan, A. P., Siebert, C. A., Topf, M., & Gruenewald, K. (2016). Two distinct trimeric conformations of natively membrane-anchored full-length herpes simplex virus 1 glycoprotein B. Proceedings of the National Academy of Sciences of the United States of America, 113(15), 4176-4181. https://doi.org/10.1073/pnas.1523234113

2015

Wetenschappelijke publicaties

Hagen, C., Dent, K. C., Zeev-Ben-Mordehai, T., Grange, M., Bosse, J. B., Whittle, C., Klupp, B. G., Siebert, C. A., Vasishtan, D., Baeuerlein, F. J. B., Cheleski, J., Werner, S., Guttmann, P., Rehbein, S., Henzler, K., Demmerle, J., Adler, B., Koszinowski, U., Schermelleh, L., ... Gruenewald, K. (2015). Structural Basis of Vesicle Formation at the Inner Nuclear Membrane. Cell, 163(7), 1692-1701. https://doi.org/10.1016/j.cell.2015.11.029
Zeev-Ben-Mordehai, T., Weberruss, M., Lorenz, M., Cheleski, J., Hellberg, T., Whittle, C., El Omari, K., Vasishtan, D., Dent, K. C., Harlos, K., Franzke, K., Hagen, C., Klupp, B. G., Antonin, W., Mettenleiter, T. C., & Gruenewald, K. (2015). Crystal Structure of the Herpesvirus Nuclear Egress Complex Provides Insights into Inner Nuclear Membrane Remodeling. Cell Reports, 13(12), 2645-2652. https://doi.org/10.1016/j.celrep.2015.11.008

2014

Wetenschappelijke publicaties

Zeev-Ben-Mordehai, T., Vasishtan, D., Siebert, C. A., & Gruenewald, K. (2014). The full-length cell-cell fusogen EFF-1 is monomeric and upright on the membrane. Nature Communications, 5, Article 3912. https://doi.org/10.1038/ncomms4912
Zeev-Ben-Mordehai, T., Hagen, C., & Gruenewald, K. (2014). A cool hybrid approach to the herpesvirus 'life' cycle. Current Opinion in Virology, 5, 42-49. https://doi.org/10.1016/j.coviro.2014.01.008
Zeev-Ben-Mordehai, T., Vasishtan, D., Siebert, C. A., Whittle, C., & Gruenewald, K. (2014). Extracellular Vesicles: A Platform for the Structure Determination of Membrane Proteins by Cryo-EM. Structure with Folding & design, 22(11), 1687-1692. https://doi.org/10.1016/j.str.2014.09.005

2013

Wetenschappelijke publicaties

Maurer, U. E., Zeev-Ben-Mordehai, T., Pandurangan, A. P., Cairns, T. M., Hannah, B. P., Whitbeck, J. C., Eisenberg, R. J., Cohen, G. H., Topf, M., Huiskonen, J. T., & Gruenewald, K. (2013). The Structure of Herpesvirus Fusion Glycoprotein B-Bilayer Complex Reveals the Protein-Membrane and Lateral Protein-Protein Interaction. Structure with Folding & design, 21(8), 1396-1405. https://doi.org/10.1016/j.str.2013.05.018

2012

Wetenschappelijke publicaties

Zeev-Ben-Mordehai, T., & Grünewald, K. (2012). Electron cryomicroscopy of large glycoprotein assemblies. In Structural Glycobiology (pp. 47-68). CRC Press. https://doi.org/10.1201/b12965

2011

Wetenschappelijke publicaties

Avinoam, O., Fridman, K., Valansi, C., Abutbul, I., Zeev-Ben-Mordehai, T., Maurer, U. E., Sapir, A., Danino, D., Gruenewald, K., White, J. M., & Podbilewicz, B. (2011). Conserved Eukaryotic Fusogens Can Fuse Viral Envelopes to Cells. Science, 332(6029), 589-592. https://doi.org/10.1126/science.1202333

2010

Wetenschappelijke publicaties

Paz, A., Zeev-Ben-Mordehai, T., Sussman, J. L., & Silman, I. (2010). Purification of Intrinsically Disordered Proteins. In Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation (pp. 695-704). John Wiley and Sons Ltd. https://doi.org/10.1002/9780470602614.ch24

2009

Wetenschappelijke publicaties

Zeev-Ben-Mordehai, T., Paz, A., Peleg, Y., Toker, L., Wolf, S. G., Rydberg, E. H., Sussman, J. L., & Silman, I. (2009). Amalgam, an axon guidance Drosophila adhesion protein belonging to the immunoglobulin superfamily: Over-expression, purification and biophysical characterization. Protein Expression and Purification, 63(2), 147-157. https://doi.org/10.1016/j.pep.2008.09.019
Zeev-Ben-Mordehai, T., Mylonas, E., Paz, A., Peleg, Y., Toker, L., Silman, I., Svergun, D. I., & Sussman, J. L. (2009). The Quaternary Structure of Amalgam, a Drosophila Neuronal Adhesion Protein, Explains Its Dual Adhesion Properties. Biophysical Journal, 97(8), 2316-2326. https://doi.org/10.1016/j.bpj.2009.07.045

2008

Wetenschappelijke publicaties

Paz, A., Zeev-Ben-Mordehai, T., Lundqvist, M., Sherman, E., Mylonas, E., Weiner, L., Haran, G., Svergun, D. I., Mulder, F. A. A., Sussman, J. L., & Silman, I. (2008). Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3. Biophysical Journal, 95(4), 1928-1944. https://doi.org/10.1529/biophysj.107.126995

2006

Wetenschappelijke publicaties

Aricescu, A. R., Assenberg, R., Bill, R. M., Busso, D., Chang, V. T., Davis, S. J., Dubrovsky, A., Gustafsson, L. L., Hedfalk, K., Heinemann, U., Jones, I. M., Ksiazek, D., Lang, C. C., Maskos, K., Messerschmidt, A., Macieira, S., Peleg, Y., Perrakis, A., Poterszman, A., ... Jones, E. Y. (2006). Eukaryotic expression: developments for structural proteomics. Acta Crystallographica Section D: Biological Crystallography, 62, 1114-1124. https://doi.org/10.1107/S0907444906029805

2005

Wetenschappelijke publicaties

Prilusky, J., Felder, CE., Zeev-Ben-Mordehai, T., Rydberg, EH., Man, O., Beckmann, J. S., Silman, I., & Sussman, J. L. (2005). FoldIndex((c)): a simple tool to predict whether a given protein sequence is intrinsically unfolded. Bioinformatics, 21(16), 3435-3438. https://doi.org/10.1093/bioinformatics/bti537

2004

Wetenschappelijke publicaties

Venema, DR., Zeev-Ben-Mordehai, T., & Auld, VJ. (2004). Transient apical polarization of Gliotactin and Coracle is required for parallel alignment of wing hairs in Drosophila. Developmental Biology, 275(2), 301-314. https://doi.org/10.1016/j.ydbio.2004.07.040

2003

Wetenschappelijke publicaties

Zeev-Ben-Mordehai, T., Silman, I., & Sussman, J. L. (2003). Acetylcholinesterase in motion: Visualizing conformational changes in crystal structures by a morphing procedure. Biopolymers, 68(3), 395-406. https://doi.org/10.1002/bip.10287
Zeev-Ben-Mordehai, T., Rydberg, EH., Solomon, A., Toker, L., Auld, VJ., Silman, I., Botti, S., & Sussman, J. L. (2003). The intracellular domain of the Drosophila cholinesterase-like neural adhesion protein, gliotactin, is natively unfolded. Proteins: Structure, Function and Genetics, 53(3), 758-767. https://doi.org/10.1002/prot.10471