Cryo-EM structure of native honey bee vitellogenin
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Abstract
Vitellogenin (Vg) is the main yolk precursor lipoprotein in almost all egg-laying animals. In addition, along its evolutionary history, Vg has developed a range of new functions in different taxa. In the honey bee, Vg has functions related to immunity, antioxidant protection, social behavior and longevity. However, the molecular mechanisms underlying Vg functionalities are still poorly understood. Here, we report the cryo-EM structure of full-length honey bee Vg, one-step purified directly from hemolymph. The structure provides structural insights into the overall domain architecture, including the lipid binding cavity and the previously uncharacterized von Willebrand factor type D domain. A domain of unknown function has been identified as a C-terminal cystine knot domain based on structural homology. Information about post-translational modifications, cleavage products, metal and lipid binding allow an improved understanding of the mechanisms underlying the range of Vg functionalities. The findings have numerous implications for the structure-function relationship of vitellogenins of other species as well as members of the same protein superfamily, which share the same structural elements.
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Cites
UCSF Chimera—A visualization system for exploratory research and analysis
Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 45,260 · 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
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. D. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 27,510 · 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 · cited 1× · see citing works
“AI-based structure prediction for vitellogenins will become even more relevant after the advent of AlphaFold 3 55 , given its reported ability to predict proteinstructures with non-protein ligands such as metal ions, lipids and covalent glycosylation.”
<i>MolProbity</i> : all-atom structure validation for macromolecular crystallography
Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909042073 · Cited by 14,115 · 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
cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
Punjani, A., Rubinstein, J. L., Fleet, D. J., & Brubaker, M. A. (2017) · Nature Methods · doi:10.1038/nmeth.4169 · Cited by 9,168 · see citing works
MAFFT online service: multiple sequence alignment, interactive sequence choice and visualization
Katoh, K., Rozewicki, J., & Yamada, K. D. (2019) · Briefings in Bioinformatics · doi:10.1093/bib/bbx108 · Cited by 8,909 · see citing works
Liebschner, D. C., Afonine, P. V., Baker, M. L., Bunkòczi, G., Chen, V. B., Croll, T. I., Hintze, B. J., Hung, L., Jain, S., McCoy, A. J., et al. (2019) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798319011471 · Cited by 6,709 · see citing works
ASSEMBLY OF ASPARAGINE-LINKED OLIGOSACCHARIDES
Kornfeld, R., & Kornfeld, S. A. (1985) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.54.070185.003215 · Cited by 4,863 · 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
Potter, S. C., Luciani, A., Eddy, S. R., Park, Y., Lopez, R., & Finn, R. D. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky448 · Cited by 2,607 · see citing works
Fast and accurate protein structure search with Foldseek
van Kempen, M., Kim, S. S., Tumescheit, C., Mirdita, M., Lee, J., Gilchrist, C. L. M., Söding, J., & Steinegger, M. (2022) · doi:10.1101/2022.02.07.479398 · Cited by 2,598 · see citing works
Fast and accurate protein structure search with Foldseek
van Kempen, M., Kim, S. S., Tumescheit, C., Mirdita, M., Lee, J., Gilchrist, C. L. M., Söding, J., & Steinegger, M. (2024) · Nature Biotechnology · doi:10.1038/s41587-023-01773-0 · Cited by 2,596 · see citing works
CASTp 3.0: computed atlas of surface topography of proteins
Tian, W., Chen, C., Lei, X., Zhao, J., & Liang, J. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky473 · Cited by 2,389 · see citing works
CASTp: Computed Atlas of Surface Topography of proteins
Binkowski, T. A. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg512 · Cited by 1,673 · see citing works
Valdar, W. S. J. (2002) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10146 · Cited by 633 · see citing works
The Gene vitellogenin Has Multiple Coordinating Effects on Social Organization
Nelson, C. M., Ihle, K. E., Fondrk, M. K., Page, R. E., & Amdam, G. V. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050062 · Cited by 525 · see citing works
Self-citationMolecular characteristics of insect vitellogenins and vitellogenin receptors
Sappington, T. W., & Raikhel, A. S. (1998) · Insect Biochemistry and Molecular Biology · doi:10.1016/s0965-1748(97)00110-0 · Cited by 523 · see citing works
Molecular characteristics of insect vitellogenins
Tufail, M., & Takeda, M. (2008) · Journal of Insect Physiology · doi:10.1016/j.jinsphys.2008.08.007 · Cited by 483 · see citing works
von Willebrand factor, Jedi knight of the bloodstream
Springer, T. A. (2014) · Blood · doi:10.1182/blood-2014-05-378638 · Cited by 462 · see citing works
Social exploitation of vitellogenin
Amdam, G. V., Norberg, K., Hagen, A. R., & Omholt, S. W. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0333979100 · Cited by 403 · see citing works
Self-citationPrivateer: software for the conformational validation of carbohydrate structures
Agirre, J., Iglesias‐Fernández, J., Rovira, C., Davies, G. J., Wilson, K. S., & Cowtan, K. D. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3115 · Cited by 373 · see citing works
Vitellogenin regulates hormonal dynamics in the worker caste of a eusocial insect
Guidugli, K. R., do Nascimento, A. M., Amdam, G. V., Barchuk, A. R., Omholt, S. W., Simões, Z. L. P., & Hartfelder, K. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.07.085 · Cited by 330 · see citing works
Self-citationThe evolution of egg yolk proteins
Byrne, B. M., Gruber, M., & Ab, G. (1989) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(89)90005-9 · Cited by 323 · see citing works
The hive bee to forager transition in honeybee colonies: the double repressor hypothesis
Amdam, G. V., & Omholt, S. W. (2003) · Journal of Theoretical Biology · doi:10.1016/s0022-5193(03)00121-8 · Cited by 290 · see citing works
Self-citationTransfer of Immunity from Mother to Offspring Is Mediated via Egg-Yolk Protein Vitellogenin
Salmela, H., Amdam, G. V., & Freitak, D. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1005015 · Cited by 264 · see citing works
Self-citationRaikhel, A. S., Kokoza, V. A., Zhu, J., Martı́n, D., Wang, S., Li, C., Sun, G., Ahmed, A., Dittmer, N. T., & Attardo, G. M. (2002) · Insect Biochemistry and Molecular Biology · doi:10.1016/s0965-1748(02)00090-5 · Cited by 258 · see citing works
Finding one's way in proteomics: a protein species nomenclature
Schlüter, H., Apweiler, R., Holzhütter, H., & Jungblut, P. (2009) · Chemistry Central Journal · doi:10.1186/1752-153x-3-11 · Cited by 254 · see citing works
CURRENT TOPICS IN DEVELOPMENTAL BIOLOGY, VOL. 61
Maden, M. (2004) · Cited by 203 · see citing works
Vitellogenin Functions as a Multivalent Pattern Recognition Receptor with an Opsonic Activity
Li, Z., Zhang, S., & Liu, Q. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001940 · Cited by 173 · see citing works
Molecular diversity and evolution of the large lipid transfer protein superfamily
Smolenaars, M. M. W., Madsen, O., Rodenburg, K. W., & HORST, D. J. V. D. (2006) · Journal of Lipid Research · doi:10.1194/jlr.r600028-jlr200 · Cited by 172 · see citing works
The structural basis of lipid interactions in lipovitellin, a soluble lipoprotein
Anderson, T. A., Levitt, D., & Banaszak, L. J. (1998) · Structure · doi:10.1016/s0969-2126(98)00091-4 · Cited by 155 · see citing works
Antônio, D. S. M., Guidugli-Lazzarini, K. R., do Nascimento, A. M., Simões, Z. L. P., & Hartfelder, K. (2008) · Die Naturwissenschaften · doi:10.1007/s00114-008-0413-9 · Cited by 149 · see citing works
Li, A., Sadasivam, M., & Ding, J. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m205067200 · Cited by 141 · see citing works
Vitellogenin is a novel player in defense reactions
Shi, X., Zhang, S., & PANG, Q. (2005) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2005.09.005 · Cited by 138 · see citing works
Assembly Mechanism of Mucin and von Willebrand Factor Polymers
Javitt, G., Khmelnitsky, L., Albert, L., Bigman, L. S., Elad, N., Morgenstern, D., Ilani, T., Levy, Y., Diskin, R., & Fass, D. (2020) · Cell · doi:10.1016/j.cell.2020.09.021 · Cited by 137 · see citing works
Salmela, H., Münch, D., Baumann, A., Zhong, S., Halskau, Ø., Krogsgaard, M., & Amdam, G. V. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.465021 · Cited by 131 · see citing works
Self-citation‘The entire protein universe’: AI predicts shape of nearly every known protein
Callaway, E. (2022) · Nature · doi:10.1038/d41586-022-02083-2 · Cited by 113 · cited 1× · see citing works
“The relevance of Vg as a target for AI-based technologies to predict protein structures is highlighted by an article where it was used to exemplify the upcoming revolution in structural biology 68 .”
Purification and characterization of honey bee vitellogenin
Wheeler, D. E., & Kawooya, J. K. (1990) · Archives of Insect Biochemistry and Physiology · doi:10.1002/arch.940140405 · Cited by 109 · see citing works
Vitellogenin-6 Is a Major Carbonylated Protein in Aged Nematode, Caenorhabditis elegans
Nakamura, A., Yasuda, K., Adachi, H., Sakurai, Y., Ishii, N., & Goto, S. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1549 · Cited by 99 · see citing works
Lipid−Protein Interactions in Lipovitellin,
Thompson, J. R., & Banaszak, L. J. (2002) · Biochemistry · doi:10.1021/bi025674w · Cited by 98 · see citing works
Hemagglutinating and antibacterial activities of vitellogenin
Zhang, S., Sun, Y., Pang, Q., & Shi, X. (2005) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2004.10.008 · Cited by 89 · see citing works
Dong, X., Leksa, N. C., Chhabra, E. S., Arndt, J. W., Lü, Q., Knockenhauer, K. E., Peters, R., & Springer, T. A. (2019) · Blood · doi:10.1182/blood-2018-10-876300 · Cited by 86 · see citing works
Kohlmeier, P., Feldmeyer, B., & Foitzik, S. (2018) · PLoS Biology · doi:10.1371/journal.pbio.2005747 · Cited by 85 · see citing works
Vitellogenesis and Yolk Proteins, Fish
Sullivan, C. V., & Yılmaz, Ö. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-809633-8.20567-0 · Cited by 85 · see citing works
Vitellogenin and Lipovitellin: Zinc Proteins of Xenopus laevis Oocytes
Montorzi, M., Falchuk, K. H., & Vallée, B. L. (1995) · Biochemistry · doi:10.1021/bi00034a018 · Cited by 81 · see citing works
Li, Z., Zhang, S., Zhang, J., Liu, M., & Liu, Z. (2009) · Molecular Immunology · doi:10.1016/j.molimm.2009.08.006 · Cited by 79 · see citing works
Plasma zinc as an index of vitellogenin production and reproductive status in the domestic fowl
Mitchell, M. A., & Carlisle, A. J. (1991) · Comparative Biochemistry and Physiology Part A Physiology · doi:10.1016/0300-9629(91)90396-t · Cited by 78 · see citing works
The crystal structure of human microsomal triglyceride transfer protein
Biterova, E. I., Isupov, M. N., Keegan, R. M., Lebedev, A. A., Sohail, A. A., Liaqat, I., Alanen, H. I., & Ruddock, L. W. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1903029116 · Cited by 76 · see citing works
Cabrera, J. A. G., Munro, E. S., Monte, M. M., Fourrier, M. C. S., Whitelaw, J., Smail, D. A., & Ellis, A. E. (2010) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2010.04.010 · Cited by 75 · see citing works
Characterization of a pattern recognition molecule vitellogenin from carp (Cyprinus carpio)
Liu, Q., Zhang, S., Li, Z., & Gao, C.-R. (2008) · Immunobiology · doi:10.1016/j.imbio.2008.10.003 · Cited by 74 · see citing works
Highly reinforced structure of a C-terminal dimerization domain in von Willebrand factor
Zhou, Y., & Springer, T. A. (2014) · Blood · doi:10.1182/blood-2013-11-523639 · Cited by 71 · see citing works
Vitellogenin is an acute phase protein with bacterial-binding and inhibiting activities
Tong, Z., Li, L., Pawar, R., & Zhang, S. (2009) · Immunobiology · doi:10.1016/j.imbio.2009.10.001 · Cited by 70 · see citing works
Intestinal mucin is a chaperone of multivalent copper
Reznik, N., Gallo, A. D., Rush, K. W., Javitt, G., Fridmann‐Sirkis, Y., Ilani, T., Nairner, N. A., Fishilevich, S., Gokhman, D., Chacón, K. N., et al. (2022) · Cell · doi:10.1016/j.cell.2022.09.021 · Cited by 69 · see citing works
Vertebrate and Invertebrate Respiratory Proteins, Lipoproteins and other Body Fluid Proteins
Hoeger, U., & Harris, J. (2020) · Subcellular Biochemistry · doi:10.1007/978-3-030-41769-7 · Cited by 67 · see citing works
Tegoni, M., Spinelli, S., Verhoeyen, M. E., Davis, P. J., & Cambillau, C. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2845 · Cited by 63 · see citing works
Sun, C., Hu, L., Liu, S., Gao, Z., & Zhang, S. (2013) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2013.07.005 · Cited by 62 · see citing works
Studies on vitellogenin from the tobacco hornworm, Manduca sexta
Osir, E. O., Wells, M. A., & Law, J. H. (1986) · Archives of Insect Biochemistry and Physiology · doi:10.1002/arch.940030302 · Cited by 60 · see citing works
Wu, B., Liu, Z., Zhou, L., Ji, G., & Yang, A. (2014) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2014.12.004 · Cited by 59 · see citing works
Tufail, M., & Takeda, M. (2002) · Insect Biochemistry and Molecular Biology · doi:10.1016/s0965-1748(02)00067-x · Cited by 58 · see citing works
The kinetics of zinc and cadmium in the haemolymph of the shore crab Carcinus maenas (L.)
Martin, D. J., & Rainbow, P. S. (1998) · Aquatic Toxicology · doi:10.1016/s0166-445x(97)00048-9 · Cited by 54 · see citing works
Intestinal Gel-Forming Mucins Polymerize by Disulfide-Mediated Dimerization of D3 Domains
Javitt, G., Calvo, M. L. G., Albert, L., Reznik, N., Ilani, T., Diskin, R., & Fass, D. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.07.018 · Cited by 51 · see citing works
Identification of Posttranslational Modifications (PTMs) of Proteins by Mass Spectrometry
Aslebagh, R., Wormwood, K. L., Channaveerappa, D., Wetie, A. G. N., Woods, A. G., & Darie, C. C. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-15950-4_11 · Cited by 50 · see citing works
Glycosylation Changes in Prostate Cancer Progression
Butler, W., & Huang, J. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.809170 · Cited by 46 · see citing works
Furukawa, K., & Kobata, A. (1992) · Current Opinion in Biotechnology · doi:10.1016/0958-1669(92)90085-w · Cited by 44 · see citing works
Vitellogenin gene family in vertebrates: evolution and functions
Carducci, F., Biscotti, M. A., & Canapa, A. (2019) · The European Zoological Journal · doi:10.1080/24750263.2019.1631398 · Cited by 42 · see citing works
Deconstructing honeybee vitellogenin: novel 40 kDa fragment assigned to its N terminus
Salmela, H., Halskau, Ø., Skjærven, L., Smedal, B., & Amdam, G. V. (2011) · Journal of Experimental Biology · doi:10.1242/jeb.048314 · Cited by 42 · see citing works
Self-citationRakhshandehroo, M., Gijzel, S. M. W., Siersbæk, R., Broekema, M. F., de Haar, C. G., Schipper, H. S., Boes, M. L., Mandrup, S., & Kalkhoven, E. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.551242 · Cited by 39 · see citing works
Roth, Z., Weil, S., Aflalo, E. D., Manor, R., Sagi, A., & Khalaila, I. (2013) · ChemBioChem · doi:10.1002/cbic.201300152 · Cited by 39 · see citing works
Zhang, Q., Lu, Y., Zheng, H., Liu, H., & Li, S. (2016) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2016.01.001 · Cited by 38 · see citing works
Ando, S., & Yanagida, K. (1999) · Comparative Biochemistry and Physiology Part C Pharmacology Toxicology and Endocrinology · doi:10.1016/s0742-8413(98)10137-8 · Cited by 34 · see citing works
Salmela, H., Underhaug, J., Wolschin, F., Amdam, G. V., & Halskau, Ø. (2012) · Journal of Experimental Biology · doi:10.1242/jeb.065623 · Cited by 30 · see citing works
Self-citationVitellogenin mediates phagocytosis through interaction with FcγR
Liu, M., Pan, J., Ji, H., Zhao, B., & Zhang, S. (2011) · Molecular Immunology · doi:10.1016/j.molimm.2011.08.011 · Cited by 30 · see citing works
Du, X., Wang, X., Wang, S., Zhou, Y., Zhang, Y., & Zhang, S. (2016) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2016.10.006 · Cited by 28 · see citing works
High-resolution structural-omics of human liver enzymes
Su, C., Lyu, M., Zhang, Z., Miyagi, M., Huang, W., Taylor, D. J., & Yu, E. W. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112609 · Cited by 25 · see citing works
A new method for rearing genetically manipulated honey bee workers
Aase, A. L. T. O., Amdam, G. V., Hagen, A. R., & Omholt, S. W. (2005) · Apidologie · doi:10.1051/apido:2005003 · Cited by 24 · see citing works
Self-citationNuclear translocation of vitellogenin in the honey bee (Apis mellifera)
Salmela, H., Harwood, G. P., Münch, D., Elsik, C. G., Herrero‐Galán, E., Vartiainen, M. K., & Amdam, G. V. (2022) · Apidologie · doi:10.1007/s13592-022-00914-9 · Cited by 23 · see citing works
Self-citationVitellogenin2: spermatozoon specificity and immunoprotection in mud crabs
Yang, Y., Zheng, B., Bao, C., Huang, H., & Ye, H. (2016) · Reproduction · doi:10.1530/rep-16-0188 · Cited by 22 · see citing works
Structure prediction of honey bee vitellogenin: a multi‐domain protein important for insect immunity
Leipart, V., Montserrat‐Canals, M., Cunha, E. S., Luecke, H., Herrero‐Galán, E., Halskau, Ø., & Amdam, G. V. (2021) · FEBS Open Bio · doi:10.1002/2211-5463.13316 · Cited by 21 · see citing works
Self-citationDrosophila melanogaster Models of Galactosemia
Daenzer, J. M. I., & Fridovich‐Keil, J. L. (2016) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2016.07.009 · Cited by 16 · see citing works
Auld, D. S., Falchuk, K. H., Zhang, K., Montorzi, M., & Vallée, B. L. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.8.3227 · Cited by 15 · see citing works
Leipart, V., Ludvigsen, J., Kent, M., Sandve, S. R., To, T., Árnyasi, M., Kreibich, C. D., Dahle, B., & Amdam, G. V. (2022) · Protein Science · doi:10.1002/pro.4369 · Cited by 11 · see citing works
Self-citationHow Honey Bee Vitellogenin Holds Lipid Cargo: A Role for the C-Terminal
Leipart, V., Halskau, Ø., & Amdam, G. V. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.865194 · Cited by 9 · see citing works
Self-citationLeipart, V., Enger, Ø., Turcu, D. C., Dobrovolska, O., Drabløs, F., Halskau, Ø., & Amdam, G. V. (2022) · Insect Molecular Biology · doi:10.1111/imb.12807 · Cited by 8 · see citing works
Self-citationCampanella, C., Caputo, M., Vaccaro, M. C., Marco, N. D., Tretola, L., Romano, M., Prisco, M., Camardella, L., Flagiello, A., Carotenuto, R., et al. (2011) · Molecular Reproduction and Development · doi:10.1002/mrd.21282 · Cited by 7 · see citing works
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- Authors
- Montserrat-Canals, M., Schnelle, K., Leipart, V., Halskau, Ø., Amdam, G. V., Moeller, A., Cunha, E. S., & Luecke, H.
- Affiliations
- Osnabrück University (DE)
- Norwegian University of Life Sciences (NO)
- University of Bergen (NO)
- University of California, Irvine (US)
- Corresponding author
- Luecke, Hartmut
- ORCID
- Venue
- Nature Communications
- Published
- 2025-07-01
- Volume
- 16
- Issue
- 1
- Pages
- 5736-5736
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC12214520
- OpenAlex
- W4411886911
- Cited by
- 7
- References
- 85
- Citations by year
- 2026: 4 · 2025: 3
- FWCI
- 2.10
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Nature Communications (publishedVersion, cc-by-nc-nd)
- Research Square (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Union's Horizon Europe Research and Innovation Programme
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Keywords
- vitellogenin, Apis mellifera, protein structure, hemolymph, post-translational modification, structure-function relationship, protein superfamilies
- MeSH terms
- Protein Domains, Amino Acid Sequence, Animals, Bees, Hemolymph, Models, Molecular, Vitellogenins, Insect Proteins, Cryoelectron Microscopy
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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