A conserved fertilization complex bridges sperm and egg in vertebrates
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Abstract
ABSTRACT Fertilization, the fusion of sperm and egg, is essential for sexual reproduction. While several proteins have been demonstrated to be essential for the binding and fusion of gametes in vertebrates, the molecular mechanisms driving this key process are poorly understood. Here, we performed a protein interaction screen using AlphaFold-Multimer to uncover protein-protein interactions in fertilization. This screen resulted in the prediction of a trimeric complex composed of the essential fertilization factors Izumo1 and Spaca6, and Tmem81, a protein previously not implicated in fertilization. We show that Tmem81 is a conserved, testis-expressed transmembrane protein that is evolutionarily related to Izumo1 and Spaca6 and is essential for male fertility in fish and mice. Consistent with trimer formation in vivo , zebrafish izumo1 -/- , spaca6 -/- , and tmem81 -/- mutants exhibit the same sperm-egg binding defect and show co-depletion of all three proteins in sperm. Moreover, we provide experimental evidence that Izumo1, Spaca6, and Tmem81 interact in zebrafish sperm. Strikingly, the Izumo1-Spaca6 interaction is predicted to form a cleft that serves as a binding site for Bouncer, the only identified egg protein essential for fertilization in zebrafish. Together, these results provide compelling evidence for a conserved sperm factor complex in vertebrates that forms a specific interface for the sperm-egg interaction required for successful fertilization.
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AlphaFold-Multimer is being used to uncover protein-protein interactions on the scale of pathways and organisms.
“AF-M is being used to uncover PPIs on the scale of pathways and organisms15–24.”
From Predictomes, a classifier-curated database of AlphaFold-modeled protein-protein interactions (2025) · cites this paper as [24]
Cites
Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
Altschul, S. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.17.3389 · Cited by 73,302 · see citing works
Fiji: an open-source platform for biological-image analysis
Schindelin, J., Arganda-Carreras, I., Frise, E., Kaynig, V., Longair, M., Pietzsch, T., Preibisch, S., Rueden, C., Saalfeld, S., Schmid, B., et al. (2012) · Nature Methods · doi:10.1038/nmeth.2019 · Cited by 66,890 · see citing works
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
ModelFinder: fast model selection for accurate phylogenetic estimates
Kalyaanamoorthy, S., Minh, B. Q., Wong, T. K. F., von Haeseler, A., & Jermiin, L. S. (2017) · Nature Methods · doi:10.1038/nmeth.4285 · Cited by 18,449 · see citing works
IQ-TREE 2: New Models and Efficient Methods for Phylogenetic Inference in the Genomic Era
Minh, B. Q., Schmidt, H. A., Chernomor, O., Schrempf, D., Woodhams, M. D., von Haeseler, A., & Lanfear, R. (2020) · Molecular Biology and Evolution · doi:10.1093/molbev/msaa015 · Cited by 16,873 · see citing works
Accurate structure prediction of biomolecular interactions with AlphaFold 3
Abramson, J., Adler, J., Dunger, J., Evans, R., Green, T., Pritzel, A., Ronneberger, O., Willmore, L., Ballard, A. J., Bambrick, J., et al. (2024) · Nature · doi:10.1038/s41586-024-07487-w · Cited by 15,861 · see citing works
Smyth, G. K. (2004) · Statistical Applications in Genetics and Molecular Biology · doi:10.2202/1544-6115.1027 · Cited by 11,829 · see citing works
UFBoot2: Improving the Ultrafast Bootstrap Approximation
Hoang, D. T., Chernomor, O., von Haeseler, A., Minh, B. Q., & Vinh, L. S. (2018) · Molecular Biology and Evolution · doi:10.1093/molbev/msx281 · Cited by 10,881 · see citing works
Jalview Version 2—a multiple sequence alignment editor and analysis workbench
Waterhouse, A. M., Procter, J. B., Martin, D. M. A., Clamp, M. E., & Barton, G. J. (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp033 · Cited by 10,011 · see citing works
Interactive Tree Of Life (iTOL) v5: an online tool for phylogenetic tree display and annotation
Letunic, I., & Bork, P. (2021) · Nucleic Acids Res. · doi:10.1093/nar/gkab301 · Cited by 9,899 · see citing works
ColabFold - Making protein folding accessible to all
Mirdita, M., Schütze, K., Moriwaki, Y., Heo, L., Ovchinnikov, S., & Steinegger, M. (2021) · doi:10.1101/2021.08.15.456425 · Cited by 9,391 · see citing works
UCSF ChimeraX : Structure visualization for researchers, educators, and developers
Pettersen, E. F., Goddard, T. D., Huang, C. C., Meng, E. C., Couch, G. S., Croll, T. I., Morris, J. H., & Ferrin, T. E. (2020) · Protein Science · doi:10.1002/pro.3943 · Cited by 9,327 · see citing works
Universal sample preparation method for proteome analysis
Wiśniewski, J. R., Zougman, A., Nagaraj, N., & Mann, M. (2009) · Nature Methods · doi:10.1038/nmeth.1322 · Cited by 8,352 · see citing works
Ohno, S. (1970) · doi:10.1007/978-3-642-86659-3 · Cited by 7,833 · see citing works
Pfam: The protein families database in 2021
Mistry, J., Chuguransky, S., Williams, L., Qureshi, M., Salazar, G. A., Sonnhammer, E. L. L., Tosatto, S. C. E., Paladin, L., Raj, S., Richardson, L. J., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkaa913 · Cited by 7,452 · see citing works
Global quantification of mammalian gene expression control
Schwanhäusser, B., Busse, D., Li, N., Dittmar, G., Schuchhardt, J., Wolf, J., Chen, W., & Selbach, M. (2011) · Nature · doi:10.1038/nature10098 · Cited by 6,566 · see citing works
UniProt: the universal protein knowledgebase in 2021
The UniProt Consortium, Bateman, A., Martin, M.-J., Orchard, S., Magrane, M., Agivetova, R., Ahmad, S., Alpi, E., Bowler-Barnett, E. H., Britto, R., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkaa1100 · Cited by 6,372 · see citing works
Database resources of the National Center for Biotechnology Information
Agarwala, R., Barrett, T., Beck, J., Benson, D., Bollin, C., Bolton, E. E., Bourexis, D., Brister, J., Bryant, S. H., Canese, K., et al. (2017) · Nucleic Acids Res. · doi:10.1093/nar/gkx1095 · Cited by 6,277 · see citing works
Self-citationCox, J., Hein, M. Y., Luber, C. A., Paron, I., Nagaraj, N., & Mann, M. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.031591 · Cited by 5,180 · see citing works
MMseqs2 enables sensitive protein sequence searching for the analysis of massive data sets
Steinegger, M., & Söding, J. (2017) · Nature Biotechnology · doi:10.1038/nbt.3988 · Cited by 4,840 · see citing works
Skyline: an open source document editor for creating and analyzing targeted proteomics experiments
MacLean, B., Tomazela, D. M., Shulman, N., Chambers, M., Finney, G. L., Frewen, B., Kern, R., Tabb, D. L., Liebler, D. C., & MacCoss, M. J. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btq054 · Cited by 4,697 · see citing works
Protein complex prediction with AlphaFold-Multimer
Evans, R., O’Neill, M., Pritzel, A., Antropova, N., Senior, A., Green, T., Žídek, A., Bates, R., Blackwell, S., Yim, J., et al. (2021) · doi:10.1101/2021.10.04.463034 · Cited by 3,808 · see citing works
Recent developments in the MAFFT multiple sequence alignment program
Katoh, K., & Toh, H. (2008) · Briefings Bioinform. · doi:10.1093/bib/bbn013 · Cited by 3,707 · see citing works
ilastik: interactive machine learning for (bio)image analysis
Berg, S., Kutra, D., Kroeger, T., Straehle, C., Kausler, B. X., Haubold, C., Schiegg, M., Aleš, J., Beier, T., Rudy, M., et al. (2019) · Nature Methods · doi:10.1038/s41592-019-0582-9 · Cited by 3,277 · see citing works
Improvements to the APBS biomolecular solvation software suite
Jurrus, E. R., Engel, D. W., Star, K. T., Monson, K., Brandi, J., Felberg, L. E., Brookes, D. H., Wilson, L., Chen, J., Liles, K., et al. (2017) · Protein Science · doi:10.1002/pro.3280 · Cited by 2,451 · see citing works
Semi-supervised learning for peptide identification from shotgun proteomics datasets
Käll, L., Canterbury, J. D., Weston, J., Noble, W. S., & MacCoss, M. J. (2007) · Nature Methods · doi:10.1038/nmeth1113 · Cited by 2,424 · see citing works
Not So Different After All: A Comparison of Methods for Detecting Amino Acid Sites Under Selection
Pond, S. L. K., & Frost, S. D. W. (2005) · Molecular Biology and Evolution · doi:10.1093/molbev/msi105 · Cited by 2,320 · see citing works
Insect decline in the Anthropocene: Death by a thousand cuts
Wagner, D. L., Grames, E. M., Forister, M. L., Berenbaum, M. R., & Stopak, D. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2023989118 · Cited by 1,960 · see citing works
FUBAR: A Fast, Unconstrained Bayesian AppRoximation for Inferring Selection
Murrell, B., Moola, S., Mabona, A., Weighill, T., Sheward, D. J., Pond, S. L. K., & Scheffler, K. (2013) · Molecular Biology and Evolution · doi:10.1093/molbev/mst030 · Cited by 1,368 · see citing works
Peterson, A. C., Russell, J. D., Bailey, D. J., Westphall, M. S., & Coon, J. J. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o112.020131 · Cited by 1,288 · see citing works
A Human Interactome in Three Quantitative Dimensions Organized by Stoichiometries and Abundances
Hein, M. Y., Hubner, N. C., Poser, I., Cox, J., Nagaraj, N., Toyoda, Y., Gak, I. A., Weisswange, I., Mansfeld, J., Buchholz, F., et al. (2015) · Cell · doi:10.1016/j.cell.2015.09.053 · Cited by 1,270 · see citing works
Yang, B.-J., Han, X., Yin, L.-L., Xing, M., Xu, Z. H., & Xue, H. (2016) · Nature Communications · doi:10.1038/ncomms11388 · Cited by 1,210 · see citing works
Ilastik: Interactive learning and segmentation toolkit
Sommer, C., Straehle, C., Köthe, U., & Hamprecht, F. A. (2011) · IEEE International Symposium on Biomedical Imaging (ISBI) · doi:10.1109/isbi.2011.5872394 · Cited by 1,145 · see citing works
Quorum sensing triggers the stochastic escape of individual cells from Pseudomonas putida biofilms
Cárcamo‐Oyarce, G., Lumjiaktase, P., Kümmerli, R., & Eberl, L. (2015) · Nature Communications · doi:10.1038/ncomms6945 · Cited by 959 · see citing works
Universal and Confident Phosphorylation Site Localization Using phosphoRS
Taus, T., Köcher, T., Pichler, P., Paschke, C., Schmidt, A., Henrich, C., & Mechtler, K. (2011) · Journal of Proteome Research · doi:10.1021/pr200611n · Cited by 875 · see citing works
Gagnon, J. A., Valen, E., Thyme, S. B., Huang, P., Ahkmetova, L., Pauli, A., Montague, T. G., Zimmerman, S., Richter, C., & Schier, A. F. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098186 · Cited by 861 · see citing works
Self-citationThe immunoglobulin superfamily protein Izumo is required for sperm to fuse with eggs
Inoue, N., Ikawa, M., Isotani, A., & Okabe, M. (2005) · Nature · doi:10.1038/nature03362 · Cited by 832 · see citing works
Self-citationHyPhy 2.5—A Customizable Platform for Evolutionary Hypothesis Testing Using Phylogenies
Pond, S. L. K., Poon, A. F. Y., Velazquez, R., Weaver, S., Hepler, N. L., Murrell, B., Shank, S. D., Magalis, B. R., Bouvier, D., Nekrutenko, A., et al. (2019) · Molecular Biology and Evolution · doi:10.1093/molbev/msz197 · Cited by 724 · see citing works
Requirement of CD9 on the Egg Plasma Membrane for Fertilization
Miyado, K., Yamada, G., Yamada, S., Hasuwa, H., Nakamura, Y., Ryu, F., Suzuki, K., Kosai, K.-I., Inoue, K., Ogura, A., et al. (2000) · Science · doi:10.1126/science.287.5451.321 · Cited by 686 · see citing works
Juno is the egg Izumo receptor and is essential for mammalian fertilization
Bianchi, E., Doe, B., Goulding, D., & Wright, G. J. (2014) · Nature · doi:10.1038/nature13203 · Cited by 674 · see citing works
Severely Reduced Female Fertility in CD9-Deficient Mice
Naour, F. L., Rubinstein, E., Jasmin, C., Prenant, M., & Boucheix, C. (2000) · Science · doi:10.1126/science.287.5451.319 · Cited by 645 · see citing works
Valdar, W. S. J. (2002) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10146 · Cited by 633 · see citing works
RevTrans: multiple alignment of coding DNA from aligned amino acid sequences
Wernersson, R. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg609 · Cited by 516 · see citing works
The gamete fusion process is defective in eggs of Cd9-deficient mice
Kaji, K., Oda, S., Shikano, T., Ohnuki, T., Uematsu, Y., Sakagami, J., Tada, N., Miyazaki, S., & Kudō, A. (2000) · Nature Genetics · doi:10.1038/73502 · Cited by 490 · see citing works
MS Amanda, a Universal Identification Algorithm Optimized for High Accuracy Tandem Mass Spectra
Dorfer, V., Pichler, P., Stranzl, T., Stadlmann, J., Taus, T., Winkler, S., & Mechtler, K. (2014) · Journal of Proteome Research · doi:10.1021/pr500202e · Cited by 477 · see citing works
Reduced fertility of female mice lacking CD81
Rubinstein, E., Ziyyat, A., Prenant, M., Wróbel, E., Wolf, J., Levy, S., Naour, F. L., & Boucheix, C. (2005) · Developmental Biology · doi:10.1016/j.ydbio.2005.11.031 · Cited by 220 · see citing works
SARS-CoV-2 requires cholesterol for viral entry and pathological syncytia formation
Sanders, D. W., Jumper, C. C., Ackerman, P. J., Bracha, D., Donlic, A., Kim, H., Kenney, D., Castello-Serrano, I., Suzuki, S., Tamura, T., et al. (2021) · eLife · doi:10.7554/elife.65962 · Cited by 215 · see citing works
Organization, evolution and functions of the human and mouse Ly6/uPAR family genes
Loughner, C. L., Bruford, E. A., McAndrews-Hill, M., Delp, E. E., Swamynathan, S., & Swamynathan, S. K. (2016) · Human Genomics · doi:10.1186/s40246-016-0074-2 · Cited by 192 · see citing works
Visualization of the moment of mouse sperm–egg fusion and dynamic localization of IZUMO1
Satouh, Y., Inoue, N., Ikawa, M., & Okabe, M. (2012) · Journal of Cell Science · doi:10.1242/jcs.100867 · Cited by 183 · see citing works
Self-citationMolecular architecture of the human sperm IZUMO1 and egg JUNO fertilization complex
Aydin, H., Sultana, A., Li, S., Thavalingam, A., & Lee, J. E. (2016) · Nature · doi:10.1038/nature18595 · Cited by 179 · see citing works
Self-citationSperm proteins SOF1, TMEM95, and SPACA6 are required for sperm−oocyte fusion in mice
Noda, T., Lu, Y., Fujihara, Y., Oura, S., Koyano, T., Kobayashi, S., Matzuk, M. M., & Ikawa, M. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1922650117 · Cited by 173 · see citing works
Self-citationStructure of IZUMO1–JUNO reveals sperm–oocyte recognition during mammalian fertilization
Ohto, U., Ishida, H., Krayukhina, E., Uchiyama, S., Inoue, N., & Shimizu, T. (2016) · Nature · doi:10.1038/nature18596 · Cited by 155 · see citing works
Measuring Protein‐Protein and Protein‐Nucleic Acid Interactions by Biolayer Interferometry
Sultana, A., & Lee, J. E. (2015) · Current Protocols in Protein Science · doi:10.1002/0471140864.ps1925s79 · Cited by 144 · see citing works
Self-citationIzumo is part of a multiprotein family whose members form large complexes on mammalian sperm
Ellerman, D. A., Pei, J., Gupta, S., Snell, W. J., Myles, D., & Primakoff, P. (2009) · Molecular Reproduction and Development · doi:10.1002/mrd.21092 · Cited by 143 · see citing works
Molecular dissection of IZUMO1, a sperm protein essential for sperm-egg fusion
Inoue, N., Hamada, D., Kamikubo, H., Hirata, K., Kataoka, M., Yamamoto, M., Ikawa, M., Okabe, M., & Hagihara, Y. (2013) · Development · doi:10.1242/dev.094854 · Cited by 127 · see citing works
Self-citationTMEM95 is a sperm membrane protein essential for mammalian fertilization
Lamas‐Toranzo, I., Hamze, J. G., Bianchi, E., Fernández-Fuertes, B., Pérez‐Cerezales, S., Laguna‐Barraza, R., Fernández‐González, R., Lonergan, P., Gutiérrez‐Adán, A., Wright, G. J., et al. (2020) · eLife · doi:10.7554/elife.53913 · Cited by 115 · see citing works
2013 IEEE International Symposium on Biomedical Imaging: From Nano to Macro
(2012) · IEEE Pulse · doi:10.1109/mpul.2012.2210847 · Cited by 114 · see citing works
Oocyte-triggered dimerization of sperm IZUMO1 promotes sperm–egg fusion in mice
Inoue, N., Hagihara, Y., Wright, D., Suzuki, T., & Wada, I. (2015) · Nature Communications · doi:10.1038/ncomms9858 · Cited by 110 · see citing works
Fujihara, Y., Lu, Y., Noda, T., Oji, A., Larasati, T., Kojima‐Kita, K., Yu, Z., Matzuk, R. M., Matzuk, M. M., & Ikawa, M. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1917060117 · Cited by 110 · see citing works
Self-citationShetty, J., Wolkowicz, M. J., Digilio, L. C., Klotz, K. L., Jayes, F. L., Diekman, A. B., Westbrook, V. A., Farris, E. M., Hao, Z., Coonrod, S. A., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301713200 · Cited by 108 · see citing works
Pausch, H., Kölle, S., Wurmser, C., Schwarzenbacher, H., Emmerling, R., Jansen, S., Trottmann, M., Fuerst, C., Götz, K., & Fries, R. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004044 · Cited by 104 · see citing works
Membrane protein isolation and structure determination in cell-derived membrane vesicles
Tao, X., Zhao, C., & MacKinnon, R. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2302325120 · Cited by 103 · see citing works
apQuant: Accurate Label-Free Quantification by Quality Filtering
Doblmann, J., Dusberger, F., Imre, R., Hudecz, O., Stanek, F., Mechtler, K., & Dürnberger, G. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00113 · Cited by 102 · see citing works
Lorenzetti, D., Poirier, C., Zhao, M., Overbeek, P. A., Harrison, W. R., & Bishop, C. E. (2013) · Mammalian Genome · doi:10.1007/s00335-013-9491-x · Cited by 96 · see citing works
Sperm SPACA6 protein is required for mammalian Sperm-Egg Adhesion/Fusion
Barbaux, S., Ialy‐Radio, C., Chalbi, M., Dybal, E., Homps-Legrand, M., Cruzeiro, M. D., Vaiman, D., Wolf, J., & Ziyyat, A. (2020) · Scientific Reports · doi:10.1038/s41598-020-62091-y · Cited by 94 · see citing works
Mache, C., Schulze, J., Holland, G., Bourquain, D. R., Gensch, J.-M., Oh, D., Nitsche, A., Dürrwald, R., Laue, M. M., & Wolff, T. (2022) · Communications Biology · doi:10.1038/s42003-022-04068-3 · Cited by 94 · see citing works
Structural and functional insights into IZUMO1 recognition by JUNO in mammalian fertilization
Kato, K., Satouh, Y., Nishimasu, H., Kurabayashi, A., Morita, J., Fujihara, Y., Oji, A., Ishitani, R., Ikawa, M., & Nureki, O. (2016) · Nature Communications · doi:10.1038/ncomms12198 · Cited by 90 · see citing works
Self-citationEvolutionarily conserved sperm factors, DCST1 and DCST2, are required for gamete fusion
Inoue, N., Hagihara, Y., & Wada, I. (2021) · eLife · doi:10.7554/elife.66313 · Cited by 89 · see citing works
Sperm Meets Egg: The Genetics of Mammalian Fertilization
Bianchi, E., & Wright, G. J. (2016) · Annual Review of Genetics · doi:10.1146/annurev-genet-121415-121834 · Cited by 88 · see citing works
Molnar, J. L., Pierce, S. E., Bhullar, B.-A. S., Turner, A. H., & Hutchinson, J. R. (2015) · Royal Society Open Science · doi:10.1098/rsos.150439 · Cited by 86 · see citing works
The Ly6/uPAR protein Bouncer is necessary and sufficient for species-specific fertilization
Herberg, S., Gert, K. R., Schleiffer, A., & Pauli, A. (2018) · Science · doi:10.1126/science.aat7113 · Cited by 83 · see citing works
Self-citationSperm–egg interaction and fertilization: past, present, and future
Okabe, M. (2018) · Biology of Reproduction · doi:10.1093/biolre/ioy028 · Cited by 82 · see citing works
Quality Control of Protein Complex Assembly by a Transmembrane Recognition Factor
Natarajan, N., Foresti, O., Wendrich, K., Stein, A., & Carvalho, P. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.10.003 · Cited by 76 · see citing works
Muller, E. M., & van Woesik, R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0110759 · Cited by 68 · see citing works
The Fertilization Enigma: How Sperm and Egg Fuse
Deneke, V. E., & Pauli, A. (2021) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-120219-021751 · Cited by 65 · see citing works
Self-citationSperm membrane proteins DCST1 and DCST2 are required for sperm-egg interaction in mice and fish
Noda, T., Blaha, A., Fujihara, Y., Gert, K. R., Emori, C., Deneke, V. E., Oura, S., Panser, K., Lu, Y., Berent, S., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-03289-w · Cited by 65 · see citing works
Self-citationIzumo1 and Juno: the evolutionary origins and coevolution of essential sperm–egg binding partners
Grayson, P. (2015) · Royal Society Open Science · doi:10.1098/rsos.150296 · Cited by 64 · see citing works
The SERK3 elongated allele defines a role for BIR ectodomains in brassinosteroid signalling
Hohmann, U., Nicolet, J., Moretti, A., Hothorn, L. A., & Hothorn, M. (2018) · Nature Plants · doi:10.1038/s41477-018-0150-9 · Cited by 64 · see citing works
Fujihara, Y., Herberg, S., Blaha, A., Panser, K., Kobayashi, K., Larasati, T., Novatchkova, M., Theussl, H., Olszanska, O., Ikawa, M., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2108777118 · Cited by 55 · see citing works
Self-citationProtein degradation corrects for imbalanced subunit stoichiometry in OST complex assembly
Mueller, S., Wåhlander, Å., Selevsek, N., Otto, C., Ngwa, E. M., Poljak, K., Frey, A. D., Aebi, M., & Gauss, R. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-03-0168 · Cited by 54 · see citing works
The structure of sperm Izumo1 reveals unexpected similarities with Plasmodium invasion proteins
Nishimura, K., Han, L., Bianchi, E., Wright, G. J., de Sanctis, D., & Jovine, L. (2016) · Current Biology · doi:10.1016/j.cub.2016.06.028 · Cited by 47 · see citing works
A novel function for the sperm adhesion protein IZUMO1 in cell–cell fusion
Brukman, N. G., Nakajima, K. P., Valansi, C., Flyak, K., Li, X., Higashiyama, T., & Podbilewicz, B. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202207147 · Cited by 43 · see citing works
The molecular complexity of fertilization: Introducing the concept of a fertilization synapse
Krauchunas, A. R., Marcello, M. R., & Singson, A. W. (2016) · Molecular Reproduction and Development · doi:10.1002/mrd.22634 · Cited by 39 · see citing works
Fernández-Fuertes, B., Laguna‐Barraza, R., Fernández‐González, R., Gutiérrez‐Adán, A., Blanco, A., O’Doherty, A., Fenza, M. D., Kelly, A. K., Kölle, S., & Lonergan, P. (2017) · Biology of Reproduction · doi:10.1093/biolre/iox065 · Cited by 39 · see citing works
Deep learning insights into the architecture of the mammalian egg-sperm fusion synapse
Elofsson, A., Han, L., Bianchi, E., Wright, G. J., & Jovine, L. (2024) · eLife · doi:10.7554/elife.93131 · Cited by 36 · see citing works
Quality Control of a Cytoplasmic Protein Complex
Scazzari, M., Amm, I., & Wolf, D. H. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.596064 · Cited by 27 · see citing works
Human sperm TMEM95 binds eggs and facilitates membrane fusion
Tang, S., Lu, Y., Skinner, W. M., Sanyal, M., Lishko, P. V., Ikawa, M., & Kim, P. S. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2207805119 · Cited by 26 · see citing works
Self-citationSperm IZUMO1 Is Required for Binding Preceding Fusion With Oolemma in Mice and Rats
Matsumura, T., Noda, T., Satouh, Y., Morohoshi, A., Yuri, S., Ogawa, M., Lu, Y., Isotani, A., & Ikawa, M. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.810118 · Cited by 25 · see citing works
Self-citationThe Sperm Protein Spaca6 is Essential for Fertilization in Zebrafish
Binner, M. I., Kogan, A., Panser, K., Schleiffer, A., Deneke, V. E., & Pauli, A. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.806982 · Cited by 25 · see citing works
Self-citationSPACA6 ectodomain structure reveals a conserved superfamily of gamete fusion-associated proteins
Vance, T. D. R., Yip, P., Jiménez, E., Li, S., Gawol, D., Byrnes, J., Usón, I., Ziyyat, A., & Lee, J. E. (2022) · Communications Biology · doi:10.1038/s42003-022-03883-y · Cited by 23 · see citing works
Self-citationA molecular switch orchestrates the nuclear export of human messenger RNAPreprint
Hohmann, U., Graf, M., Schellhaas, U., Pacheco-Fiallos, B., Fin, L., Riabov-Bassat, D., Pühringer, T., Szalay, M.-F., Tirián, L., Handler, D., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.24.586400 · Cited by 23 · see citing works
Self-citationEukaryotic fertilization and gamete fusion at a glance
Lu, Y., & Ikawa, M. (2022) · Journal of Cell Science · doi:10.1242/jcs.260296 · Cited by 21 · see citing works
Self-citationRivera, A., & Swanson, W. J. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.827454 · Cited by 18 · see citing works
Divergent molecular signatures in fish Bouncer proteins define cross-fertilization boundaries
Gert, K. R. B., Panser, K., Surm, J., Steinmetz, B. S., Schleiffer, A., Jovine, L., Moran, Y., Kondrashov, F., & Pauli, A. (2023) · Nature Communications · doi:10.1038/s41467-023-39317-4 · Cited by 15 · see citing works
Self-citationReciprocal zebrafish-medaka hybrids reveal maternal control of zygotic genome activation timingPreprint
Gert, K. R., Schulze, G., Novatchkova, M., Panser, K., Cabrera-Quio, L. E., Koller, A., Guo, Y., Cairns, B. R., Valen, E., & Pauli, A. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.11.03.467109 · Cited by 10 · see citing works
Self-citationSpermatogenic cell-specific SPACA4 is essential for efficient sperm-zona pellucida binding in vitro
Chen, L., Song, J., Zhang, J., Luo, Z., Chen, X., Zhou, C., & Shen, X. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1204017 · Cited by 7 · see citing works
Author response: SARS-CoV-2 requires cholesterol for viral entry and pathological syncytia formation
Sanders, D. W., Jumper, C. C., Ackerman, P. J., Bracha, D., Donlic, A., Kim, H., Kenney, D., Castello-Serrano, I., Suzuki, S., Tamura, T., et al. (2021) · eLife · doi:10.7554/elife.65962.sa2 · Cited by 4 · see citing works
Deep learning insights into the architecture of the mammalian egg-sperm fusion synapse
Elofsson, A., Han, L., Bianchi, E., Wright, G. J., & Jovine, L. (2023) · doi:10.1101/2023.07.27.550195 · Cited by 3 · see citing works
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Predictomes, a classifier-curated database of AlphaFold-modeled protein-protein interactions
Schmid, E. W., & Walter, J. C. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.01.034 · Cited by 120 · see citing works
“AF-M AF-M is being used to uncover PPIs on the scale of pathways and organisms 15–24 .”
AlphaFold 3: an unprecedent opportunity for fundamental research and drug development
Fang, Z., Ran, H., Zhang, Y., Chen, C., Ping, L., Zhang, X., & Wu, M. (2025) · Precision Clinical Medicine · doi:10.1093/pcmedi/pbaf015 · Cited by 59 · see citing works
Deep learning insights into the architecture of the mammalian egg-sperm fusion synapse
Elofsson, A., Han, L., Bianchi, E., Wright, G. J., & Jovine, L. (2024) · eLife · doi:10.7554/elife.93131 · Cited by 36 · see citing works
Sperm Membrane Stability: In-Depth Analysis from Structural Basis to Functional Regulation
Xue, S.-H., Xu, B., Yan, X., Zhang, J., & Su, R. (2025) · Veterinary Sciences · doi:10.3390/vetsci12070658 · Cited by 21 · see citing works
CASP16 Protein Monomer Structure Prediction Assessment
Yuan, R., Zhang, J., Kryshtafovych, A., Schaeffer, R. D., Zhou, J., Cong, Q., & Grishin, N. V. (2025) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.70031 · Cited by 19 · see citing works
Recent progress and future challenges in structure-based protein-protein interaction prediction
Yuan, R., Zhang, J., Zhou, J., & Cong, Q. (2025) · Molecular Therapy · doi:10.1016/j.ymthe.2025.04.003 · Cited by 20 · see citing works
Bianchi, E., Jiménez‐Movilla, M., Cots, P., Viola, C., & Wright, G. J. (2024) · Science Advances · doi:10.1126/sciadv.adk6352 · Cited by 13 · see citing works
Ogawa, Y., Lu, Y., Kiyozumi, D., Chang, H., & Ikawa, M. (2023) · Andrology · doi:10.1111/andr.13564 · Cited by 9 · see citing works
Self-citationNew Insights and Implications of Cell–Cell Interactions in Developmental Biology
Wu, G., Liang, Y., Xi, Q., & Zuo, Y. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26093997 · Cited by 8 · see citing works
AlphaFold is five years old — these charts show how it revolutionized science
Callaway, E. (2025) · Nature · doi:10.1038/d41586-025-03886-9 · Cited by 8 · see citing works
Deep learning insights into the architecture of the mammalian egg-sperm fusion synapse
Elofsson, A., Han, L., Bianchi, E., Wright, G. J., & Jovine, L. (2024) · eLife · doi:10.7554/elife.93131.3 · Cited by 8 · see citing works
Noncanonical phagocytosis-like SEAL establishes mammalian fertilization
Inoue, N., Saitô, T., & Wada, I. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115463 · Cited by 7 · see citing works
Proteome-wide in silico screening for human protein-protein interactionsPreprint
Schmid, E. W., Zhu, H., Ryu, E., Lim, Y., Smogorzewska, A., Brown, A., & Walter, J. C. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.10.687652 · Cited by 12 · see citing works
Sperm induction of somatic cell-cell fusion as a novel functional test
Brukman, N. G., Valansi, C., & Podbilewicz, B. (2024) · eLife · doi:10.7554/elife.94228 · Cited by 6 · see citing works
Lu, Y., Ikawa, M., & Tang, S. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2425952122 · Cited by 5 · see citing works
Self-citationMolecular interplay between sperm and oocyte: a narrative review
Chang, H., Gierke, T. R., Tang, S., & Lu, Y. (2026) · Human Reproduction Update · doi:10.1093/humupd/dmag008 · Cited by 5 · see citing works
Self-citationGao, Y., Wang, H., Zhou, J., & Yang, Y. (2025) · Current Research in Structural Biology · doi:10.1016/j.crstbi.2024.100163 · Cited by 5 · see citing works
The rise of AlphaFold in drug design
Stecuła, A., Paul, R., Litchfield, K., Dalton, S. E., Low, C. M. R., Reis, C. R., & Congreve, M. (2025) · Progress in medicinal chemistry · doi:10.1016/bs.pmch.2025.09.002 · Cited by 4 · see citing works
Deep learning insights into the architecture of the mammalian egg-sperm fusion synapse
Elofsson, A., Han, L., Bianchi, E., Wright, G. J., & Jovine, L. (2023) · doi:10.1101/2023.07.27.550195 · Cited by 3 · see citing works
Immunolocalization and proteomic analyses of IZUMO1 in porcine spermatozoa
Hernández-Falcó, M., Sáez‐Espinosa, P., López-Botella, A., Robles‐Gómez, L., García‐Vázquez, F. A., Izquierdo-Rico, M. J., Llamas‐López, P. J., & Gómez‐Torres, M. J. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1576881 · Cited by 3 · see citing works
Advances in Contraceptive Vaccine Development: A Comprehensive Review
Gao, W., Shen, X., Li, P., Xiao, C., & Wang, Y. (2025) · Vaccines · doi:10.3390/vaccines13070692 · Cited by 3 · see citing works
Mouse genome engineering uncovers 18 genes dispensable for male reproduction
Chang, H., Lu, Y., Yamamoto, K., Sun, J., Shimada, K., Hiradate, Y., Fujihara, Y., & Ikawa, M. (2025) · Andrology · doi:10.1111/andr.70088 · Cited by 3 · see citing works
Self-citationvon Wiegen, N., Behl, C., & Körschgen, H. (2025) · iScience · doi:10.1016/j.isci.2025.112976 · Cited by 3 · see citing works
Anderson, S. M., Choi, J., Cushman, E. M., Leander, M., Raman, S., & Senes, A. (2025) · PNAS Nexus · doi:10.1093/pnasnexus/pgaf305 · Cited by 3 · see citing works
Sawada, H., Saitô, T., Shimada, Y., & Nishimura, H. (2025) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2025.01.010 · Cited by 3 · see citing works
Electrostatic changes enabled the diversification of an exocyst subunit via protein complex escapePreprint
la Concepción, J. C. D., Duvergé, H., Kim, Y., Julian, J., Xu, H. D., Ikene, S. A., Bianchi, A. T. J., Grujic, N., Papareddy, R. K., Grishkovskaya, I., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.26.609756 · Cited by 3 · see citing works
Conservation and divergence of the molecular regulators of the vertebrate fertilization synapse
Blaha, A., Schleiffer, A., & Pauli, A. (2025) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2025.102352 · Cited by 2 · see citing works
Self-citationPredicting Protein Function in the AI and Big Data Era
Percudani, R., & Rito, C. D. (2025) · Biochemistry · doi:10.1021/acs.biochem.5c00186 · Cited by 3 · see citing works
Torra‐Massana, M., Morse, B., Miguel-Escalada, I., Guillén, J. J., Rodríguez-Aranda, A., Popovic, M., & Sakkas, D. (2025) · Human Reproduction · doi:10.1093/humrep/deaf152 · Cited by 2 · see citing works
Qiu, Y., Shimada, K., & Ikawa, M. (2025) · Andrology · doi:10.1111/andr.70144 · Cited by 2 · see citing works
Self-citationThe Xenopus Oocyte System: Molecular Dynamics of Maturation, Fertilization, and Post-Ovulatory Fate
Sato, K.-I. (2025) · Biomolecules · doi:10.3390/biom16010022 · Cited by 2 · see citing works
Zhang, R., Zhu, X., Dong, L., Guo, C., & Shu, Y. (2026) · Plant Cell & Environment · doi:10.1111/pce.70408 · Cited by 2 · see citing works
Need for speed: advances in the era of high throughput interaction proteomics
Frommelt, F., Uliana, F., Aebersold, R. H., & Fossati, A. (2026) · Molecular Omics · doi:10.1093/molecular-omics/aaiag012 · Cited by 2 · see citing works
Membrane Fusions During Mammalian Fertilization
Gierke, T. R., Liu, P., Lu, Y., & Tang, S. (2026) · Advances in experimental medicine and biology · doi:10.1007/978-3-032-22637-2_4 · Cited by 2 · see citing works
Self-citationStructure and inhibition of the sperm TMEM95–FIMP complex in mammalian fertilizationPreprint
Liu, P., Castelino, R. E., Gierke, T. R., Wood, A. J., Lu, Y., & Tang, S. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.14.724122 · Cited by 2 · see citing works
Self-citationElango, J. N., Shin, I. H., Gurjar, A., & Krauchunas, A. R. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.14.723898 · Cited by 2 · see citing works
Electrostatic changes enabled the diversification of an exocyst subunit via protein complex escape
la Concepción, J. C. D., Duvergé, H., Kim, Y., Julian, J., Xu, H. D., Watt, M., Ikene, S. A., Bianchi, A., Grujic, N., Papareddy, R. K., et al. (2025) · Nature Plants · doi:10.1038/s41477-025-02135-1 · Cited by 1 · see citing works
Nisio, V. D., Šutovský, P., Antonouli, S., Messini, C. I., Chatzimeletiou, K., Kokkali, G., & Anifandis, G. (2026) · Systems Biology in Reproductive Medicine · doi:10.1080/19396368.2026.2618253 · Cited by 1 · see citing works
AlphaFold 3-powered discovery of phage proteins that inhibit bacterial transcription initiation
Yuan, L., Liu, Q., Xiao, X., Xu, L., Liang, L., Guo, Y., Yao, Y., Wang, H., Feng, Y., Hua, X., et al. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.117082 · Cited by 1 · see citing works
Spermatozoa lacking TEX51 display hypofertility and defects in morphology
Dupuis, S., Beulze, M. L., Vance, T. D. R., Pierre, R., Lee, J. E., Ziyyat, A., & Barbaux, S. (2025) · Communications Biology · doi:10.1038/s42003-025-08937-5 · Cited by 1 · see citing works
Self-citationSperm, eggs, pollen, and gelato, oh my!
Whittington, E., & Ålund, M. (2023) · Molecular Reproduction and Development · doi:10.1002/mrd.23722 · Cited by 1 · see citing works
AlphaFold reveals how sperm and egg hook up in intimate detail
Ledford, H. K. (2024) · Nature · doi:10.1038/d41586-024-03319-z · Cited by 1 · see citing works
Bouncer’s receptor on sperm: Investigating sperm-egg compatibility in fishPreprint
Blaha, A., & Pauli, A. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.13.628393 · Cited by 1 · see citing works
Self-citationThe dramatic impact of the PER-DBT interaction on circadian timekeeping and temperature compensationPreprint
Petersen, E. N., Keefer, E., Ludewig, H., Sullivan, C., Kern, D., & Rosbash, M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.01.636007 · Cited by 1 · see citing works
Pinello, J. F., Ferrino-Iriarte, A., Hussain, H., Legrand, P., Manikumar, S., Demissie, R., Rey, F. A., Snell, W. J., & Baquero, E. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.09.653094 · Cited by 1 · see citing works
Cross-species insemination reveals mouse sperm ability to enter and cross the fish micropylePreprint
Garibova, S., Stickler, E., Ali, F. A., Abdulla, M. A., Sathappan, A., Da'as, S. I., Ghanem, L., Djekidel, M. N., Portman, R., & Avella, M. (2025) · eLife · doi:10.7554/elife.106303 · Cited by 1 · see citing works
Deep learning insights into the architecture of the mammalian egg-sperm fusion synapsePreprint
Elofsson, A., Han, L., Bianchi, E., Wright, G. J., & Jovine, L. (2024) · eLife · doi:10.7554/elife.93131.1
Deep learning insights into the architecture of the mammalian egg-sperm fusion synapsePreprint
Elofsson, A., Han, L., Bianchi, E., Wright, G. J., & Jovine, L. (2024) · eLife · doi:10.7554/elife.93131.2
Protein-mediated cell–cell interactions in multicellular biology
(2024) · Elsevier eBooks · doi:10.1016/b978-0-323-99893-2.00006-3
Fertilization and evolution: AI-powered search finds a missing link in sperm–egg interaction
Huang, X., & Chung, J. (2024) · Current Biology · doi:10.1016/j.cub.2024.10.051
Luo, H., Wang, Y., Huang, J., Miao, B., Zhang, H., Luo, X., You, W., Lu, Y. H., Cai, M., & Ke, C. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.139677
Self-citationKomondor, K. M., & Carlson, A. E. (2025) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2024.12.003
Cross-species insemination reveals mouse sperm ability to enter and cross the fish micropyle
Garibova, S., Stickler, E., Ali, F. A., Abdulla, M. A., Sathappan, A., Da'as, S. I., Ghanem, L., Djekidel, M. N., Portman, R., & Avella, M. (2025) · eLife · doi:10.7554/elife.106303.3
Zhang, W., Sun, Y., Li, X., Yu, D. H., Liu, S., Su, H., & Xing, W. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5364167
Cross-species insemination reveals mouse sperm ability to enter and cross the fish micropylePreprint
Garibova, S., Stickler, E., Ali, F. A., Abdulla, M. A., Sathappan, A., Da'as, S. I., Ghanem, L., Djekidel, M. N., Portman, R., & Avella, M. (2025) · eLife · doi:10.7554/elife.106303.2
Zebrafish Unga Is Required for Genomic Maintenance upon Genotoxic Stress and Male Fertility
Kazzazy, L., Huba, F., Hausz, B. L., Mező, D., Perey‐Simon, V., Jezsó, B., Seddik, A., Marinović, Z., Tóth, J. S., Békési, A., et al. (2025) · Journal of Developmental Biology · doi:10.3390/jdb13030032
Moriwaki, Y., Shiraishi, T., Katsuyama, Y., Matsuda, K., Ose, T., Minami, A., Oikawa, H., Kuzuyama, T., Ishitani, R., & Terada, T. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.26.684697
Role of adjuvants in the efficacy of an IZUMO1-based immunocontraceptive vaccine in mice
Hernandez-Franco, J. F., AbdelKhalek, A., Zhang, L., Ibrahium, O. M. H., Pérez, D. C., Flora, D., Upatising, V., Ostafe, R., & HogenEsch, H. (2025) · Vaccine · doi:10.1016/j.vaccine.2025.128071
Ayoub, N., Pietrancosta, N., Gianetto, Q. G., Karimova, G., Gedeon, A., & Munier‐Lehmann, H. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.149706
Metabolomics Reveals Betaine as a Biomarker for Better Boar Spermatozoa Freezability
Qin, H., Zhao, Y., Wang, T., Gao, R., Yan, L., Yin, Z., Yang, C., & Du, Z. (2026) · Reproduction in Domestic Animals · doi:10.1111/rda.70154
Cots, P., Wang, X., Sanchez-Tudela, M., Siu, K. K. W., Yip, P., Gómez, E., Lee, J. E., Hamze, J. G., & Jiménez‐Movilla, M. (2026) · Human Reproduction Open · doi:10.1093/hropen/hoag010
Self-citationSmall molecule recognition based on molecularly imprinted labels
Chen, Z., wang, Z., Han, H., & Ma, Z. (2026) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2026.140232
How Artificial Intelligence Shapes Science: Evidence from AlphaFoldPreprint
Stein, C., & Hill, R. (2026) · SSRN Electronic Journal · doi:10.2139/ssrn.6395041
Brukman, N. G., Kabha, M., Levi, R., Abbas, R., Baram, S., Beck‐Fruchter, R., & Podbilewicz, B. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.07.723220
The SPARK complex forms the molecular basis of vertebrate fertilizationPreprint
Deneke, V. E., Suwita, J. P., Wang, H., Tonai, S., Lu, Y., Panser, K., Schleiffer, A., Hollis, J. A., Novatchkova, M., Duernberger, G., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.13.724128
Self-citationWang, Y., Fan, Z., Chu, X., Zhou, K., Wang, T., Guan, J., Hu, R., Li, A., Li, W., Liu, X., et al. (2026) · Science China Life Sciences · doi:10.1007/s11427-025-3260-6
Self-citationEvolution of an Aurora Kinase A Inhibitor from an Essential tRNA SynthetasePreprint
Ross, J. J., Tikanova, P., Hagmüller, A., Krogull, D., Xiao, K., van Bavel, C., Balla, T., Liao, T., Echano, K. A., Gokcezade, J., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.15.725417
Rat DCST1 and DCST2 are essential for sperm–egg fusion
Nakano, M., Yamaga, K., Uriu, R., Taira, A., MASUDA, K., Araki, K., Isotani, A., Yuri, S., Takeo, T., Ikawa, M., et al. (2026) · Biology of Reproduction · doi:10.1093/biolre/ioag111
Self-citationMoriwaki, Y., Shiraishi, T., Katsuyama, Y., Matsuda, K., Zhang, J., Ose, T., Minami, A., Oikawa, H., Kuzuyama, T., Ishitani, R., et al. (2026) · Computational and Structural Biotechnology Journal · doi:10.34133/csbj.0149 · Cited by 3 · see citing works
Zhang, W., Sun, Y., Li, X., Liu, S., Su, H., & Xing, W. (2026) · Theriogenology · doi:10.1016/j.theriogenology.2026.118029
Fertilization: Loops in a ß-propeller as substrates for evolution of species specificity
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Zhang, R., Zhu, X., Xue, Y. J., Tang, X., Yao, Y., Cao, D., He, W., Guo, C., Liu, X. Y., & Shu, Y. (2026) · Journal of Agriculture and Food Research · doi:10.1016/j.jafr.2026.103139
Girault, M.-S., Dupuis, S., Pierre, R., Gourier, C., Lee, J. E., Barbaux, S., & Ziyyat, A. (2026) · Cell Biochemistry and Function · doi:10.1002/cbf.70265
Self-citationZAN, IZUMO1, and TMEM95 Protein Domains Identify the Physiological Status of the Sperm
Hernández-Falcó, M., Sáez‐Espinosa, P., Romero, A., López-Botella, A., Robles‐Gómez, L., & Gómez‐Torres, M. J. (2026) · Andrology · doi:10.1111/andr.70336
Adhimoolam, S., Prakash, R. L. M., George, N., Siva Ranjani, S., Meena, Y. K., & Udhayan, A. (2026) · Journal of Reproductive Immunology · doi:10.1016/j.jri.2026.104969
Giambó-Falian, I., & Fuentes, R. (2026) · Cells and Development · doi:10.1016/j.cdev.2026.204114
Hatakeyama, S. (2026) · Reproductive Medicine and Biology · doi:10.1002/rmb2.70106
Balestra, A. C., Merolle, M. I., Bergner, T., Tang, M., Robles, N. Y., Ndayiragije, A., Wallbank, B. A., Daniels, A. M., Laue, M. M., Klotz, C., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.10.13.757955
- Authors
- Deneke, V. E., Blaha, A., Lu, Y., Suwita, J. P., Draper, J. M., Phan, C. S., Panser, K., Schleiffer, A., Jacob, L., Humer, T., Stejskal, K., Krssakova, G., Roitinger, E., Handler, D., Kamoshita, M., Vance, T. D. R., Wang, X., Surm, J. M., Moran, Y., Lee, J. E., Ikawa, M., & Pauli, A.
- Affiliations
- Research Institute of Molecular Pathology (AT)
- University of Vienna (AT)
- The University of Osaka Premium Research Institute for Human Metaverse Medicine (JP)
- Institute of Molecular Biotechnology (AT)
- Research Institute for Microbial Diseases, The University of Osaka (JP)
- University of Toronto (CA)
- Hebrew University of Jerusalem (IL)
- Institute of Medical Science, The University of Tokyo (JP)
- Corresponding author
- Deneke, Victoria E.
- Pauli, Andrea
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2024-12
- Volume
- 187
- Issue
- 25
- Pages
- 7066-7078.e22
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W4403479239
- Cited by
- 78
- References
- 101
- Citations by year
- 2026: 27 · 2025: 37 · 2024: 11 · 2023: 3
- FWCI
- 29.58
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Cell (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- Japan Science and Technology Agency (JPMJCR21N1)
- Canadian Institutes of Health Research (PJT-153281)
- Israel Science Foundation (636/21)
- Boehringer Ingelheim Foundation
- Government of Ontario
- Japan Society for the Promotion of Science (JP21H05033, JP23K20043, JP24K02033, JP22K15103)
- Human Frontier Science Program (LT000455/2020-L)
- Ministry of Education, Culture, Sports, Science and Technology
- Boehringer Ingelheim
- Boehringer Ingelheim Fonds
- FFG
- Binational Science Foundation (2020669)
- ERC
- European Research Council (F80)
- Austrian Science Fund (Y 1031-B28)
- Topics
- Health Sciences › Medicine › Reproductive Medicine › Sperm and Testicular Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Reproductive biology and impacts on aquatic species
- Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Reproductive Biology and Fertility
- Keywords
- fertilisation (biology), sperm-egg interaction, IZUMO1, bouncers, JUNO, male fertility, zebrafish, mice, protein complex formation
- MeSH terms
- Animals, Female, Fertilization, Humans, Immunoglobulins, Male, Membrane Proteins, Ovum, Sperm-Ovum Interactions, Spermatozoa, Zebrafish, Zebrafish Proteins, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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