{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,14]],"date-time":"2026-07-14T15:06:08Z","timestamp":1784041568086,"version":"3.55.0"},"reference-count":97,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T00:00:00Z","timestamp":1779321600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"},{"start":{"date-parts":[[2026,7,14]],"date-time":"2026-07-14T00:00:00Z","timestamp":1783987200000},"content-version":"vor","delay-in-days":54,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"}],"funder":[{"DOI":"10.13039\/501100009469","name":"Conseil R\u00e9gional du Centre-Val de Loire","doi-asserted-by":"publisher","award":["2017 119977"],"award-info":[{"award-number":["2017 119977"]}],"id":[{"id":"10.13039\/501100009469","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["BMC Genomics"],"DOI":"10.1186\/s12864-026-12918-1","type":"journal-article","created":{"date-parts":[[2026,5,20]],"date-time":"2026-05-20T23:12:33Z","timestamp":1779318753000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Dynamic proteomics of Nasonia vitripennis pupal development reveals testis-specific regulation of new proteins (orphans) likely related to exo-\u03b1-sialidases"],"prefix":"10.1186","volume":"27","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7339-9185","authenticated-orcid":false,"given":"Charlotte","family":"L\u00e9cureuil","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8749-5557","authenticated-orcid":false,"given":"Christine","family":"Almunia","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vanessa","family":"Gu\u00e9rin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1589-445X","authenticated-orcid":false,"given":"Jean","family":"Armengaud","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0574-3650","authenticated-orcid":false,"given":"Thierry","family":"Moreau","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6923-6220","authenticated-orcid":false,"given":"Sophie","family":"Fouch\u00e9court","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,5,21]]},"reference":[{"key":"12918_CR1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1260419","volume":"347","author":"M Uhl\u00e9n","year":"2015","unstructured":"Uhl\u00e9n M, Fagerberg L, Hallstr\u00f6m BM, Lindskog C, Oksvold P, Mardinoglu A, et al. Tissue-based map of the human proteome. Science. 2015;347:1260419. https:\/\/doi.org\/10.1126\/science.1260419.","journal-title":"Science"},{"key":"12918_CR2","doi-asserted-by":"publisher","first-page":"4215","DOI":"10.1021\/acs.jproteome.9b00351","volume":"18","author":"C Pineau","year":"2019","unstructured":"Pineau C, Hikmet F, Zhang C, Oksvold P, Chen S, Fagerberg L, et al. Cell type-specific expression of testis elevated genes based on transcriptomics and antibody-based proteomics. J Proteome Res. 2019;18:4215\u201330. https:\/\/doi.org\/10.1021\/acs.jproteome.9b00351.","journal-title":"J Proteome Res"},{"key":"12918_CR3","doi-asserted-by":"publisher","first-page":"397","DOI":"10.1074\/mcp.M113.035600","volume":"13","author":"L Fagerberg","year":"2014","unstructured":"Fagerberg L, Hallstr\u00f6m BM, Oksvold P, Kampf C, Djureinovic D, Odeberg J, et al. Analysis of the human tissue-specific expression by genome-wide integration of transcriptomics and antibody-based proteomics. Mol Cell Proteomics. 2014;13:397\u2013406. https:\/\/doi.org\/10.1074\/mcp.M113.035600.","journal-title":"Mol Cell Proteomics"},{"key":"12918_CR4","doi-asserted-by":"publisher","DOI":"10.1016\/j.mcpro.2022.100408","volume":"21","author":"T Lu","year":"2022","unstructured":"Lu T, Qian L, Xie Y, Zhang Q, Liu W, Ge W, et al. Tissue-characteristic expression of mouse proteome. Mol Cell Proteomics. 2022;21:100408. https:\/\/doi.org\/10.1016\/j.mcpro.2022.100408.","journal-title":"Mol Cell Proteomics"},{"key":"12918_CR5","doi-asserted-by":"publisher","DOI":"10.1186\/s12864-018-4931-3","volume":"19","author":"SH Hong","year":"2018","unstructured":"Hong SH, Kwon JT, Kim J, Jeong J, Kim J, Lee S, et al. Profiling of testis-specific long noncoding RNAs in mice. BMC Genomics. 2018;19:539. https:\/\/doi.org\/10.1186\/s12864-018-4931-3.","journal-title":"BMC Genomics"},{"key":"12918_CR6","doi-asserted-by":"publisher","first-page":"445","DOI":"10.1152\/physiolgenomics.00151.2023","volume":"56","author":"B Pi\u00e9gu","year":"2024","unstructured":"Pi\u00e9gu B, Lefort G, Douet C, Milhes M, Jacques A, Lareyre J-J, et al. A first complete catalog of highly expressed genes in eight chicken tissues reveals uncharacterized gene families specific for the chicken testis. Physiol Genomics. 2024;56:445\u201356. https:\/\/doi.org\/10.1152\/physiolgenomics.00151.2023.","journal-title":"Physiol Genomics"},{"key":"12918_CR7","doi-asserted-by":"publisher","first-page":"2312","DOI":"10.1093\/humrep\/dead170","volume":"38","author":"J Castillo","year":"2023","unstructured":"Castillo J, De La Iglesia A, Leiva M, Jodar M, Oliva R. Proteomics of human spermatozoa. Hum Reprod. 2023;38:2312\u201320. https:\/\/doi.org\/10.1093\/humrep\/dead170.","journal-title":"Hum Reprod"},{"key":"12918_CR8","doi-asserted-by":"publisher","DOI":"10.3390\/ani15040484","volume":"15","author":"P Pinto-Pinho","year":"2025","unstructured":"Pinto-Pinho P, Quelhas J, Impens F, Dufour S, Van Haver D, Lopes G, et al. The surface proteome of bovine unsexed and sexed spermatozoa. Animals. 2025;15:484. https:\/\/doi.org\/10.3390\/ani15040484.","journal-title":"Animals"},{"key":"12918_CR9","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-024-63410-3","volume":"14","author":"C Hern\u00e1ndez-Avil\u00e9s","year":"2024","unstructured":"Hern\u00e1ndez-Avil\u00e9s C, Ram\u00edrez-Ag\u00e1mez L, Weintraub ST, Scoggin CF, Davis BW, Raudsepp T, et al. Proteomic analysis of sperm from fertile stallions and subfertile stallions due to impaired acrosomal exocytosis. Sci Rep. 2024;14:12446. https:\/\/doi.org\/10.1038\/s41598-024-63410-3.","journal-title":"Sci Rep"},{"key":"12918_CR10","doi-asserted-by":"publisher","DOI":"10.1016\/j.ejcb.2023.151296","volume":"102","author":"T Ot\u010den\u00e1\u0161kov\u00e1","year":"2023","unstructured":"Ot\u010den\u00e1\u0161kov\u00e1 T, Mac\u00ed\u010dkov\u00e1 E, Vondr\u00e1kov\u00e1 J, Frol\u00edkov\u00e1 M, Komrskova K, Stopkov\u00e1 R, et al. Proteomic analysis of the mouse sperm acrosome - towards an understanding of an organelle with diverse functionality. Eur J Cell Biol. 2023;102:151296. https:\/\/doi.org\/10.1016\/j.ejcb.2023.151296.","journal-title":"Eur J Cell Biol"},{"key":"12918_CR11","doi-asserted-by":"publisher","DOI":"10.1002\/pmic.202400075","volume":"25","author":"M Arad","year":"2025","unstructured":"Arad M, Ku K, Frey C, Hare R, McAfee A, Ghafourifar G, et al. What proteomics has taught us about honey bee (Apis mellifera) health and disease. Proteomics. 2025;25:2400075. https:\/\/doi.org\/10.1002\/pmic.202400075.","journal-title":"Proteomics"},{"key":"12918_CR12","doi-asserted-by":"publisher","first-page":"137","DOI":"10.1093\/molehr\/gan002","volume":"14","author":"E Bonilla","year":"2008","unstructured":"Bonilla E, Xu EY. Identification and characterization of novel mammalian spermatogenic genes conserved from fly to human. Mol Hum Reprod. 2008;14:137\u201342. https:\/\/doi.org\/10.1093\/molehr\/gan002.","journal-title":"Mol Hum Reprod"},{"key":"12918_CR13","doi-asserted-by":"publisher","first-page":"841","DOI":"10.2741\/e145","volume":"2","author":"EB Rodgers-Melnick","year":"2010","unstructured":"Rodgers-Melnick EB, Naz RK. Male-biased genes of Drosophila melanogaster that are conserved in mammalian testis. Front Biosci (Elite Ed). 2010;2:841\u20138. https:\/\/doi.org\/10.2741\/e145.","journal-title":"Front Biosci (Elite Ed)"},{"key":"12918_CR14","doi-asserted-by":"publisher","DOI":"10.1186\/s12862-021-01825-6","volume":"21","author":"C L\u00e9cureuil","year":"2021","unstructured":"L\u00e9cureuil C, Fouch\u00e9court S, Eliautout R, Gu\u00e9rin V, Hidalgo K, Neutre D, et al. A comparative genomic approach using mouse and fruit fly data to discover genes involved in testis function in hymenopterans with a focus on Nasonia vitripennis. BMC Ecol Evo. 2021;21:90. https:\/\/doi.org\/10.1186\/s12862-021-01825-6.","journal-title":"BMC Ecol Evo"},{"key":"12918_CR15","doi-asserted-by":"publisher","DOI":"10.1186\/s12862-019-1462-8","volume":"19","author":"S Fouch\u00e9court","year":"2019","unstructured":"Fouch\u00e9court S, Picolo F, Elis S, L\u00e9cureuil C, Th\u00e9lie A, Govoroun M, et al. An evolutionary approach to recover genes predominantly expressed in the testes of the zebrafish, chicken and mouse. BMC Evol Biol. 2019;19:137. https:\/\/doi.org\/10.1186\/s12862-019-1462-8.","journal-title":"BMC Evol Biol"},{"key":"12918_CR16","doi-asserted-by":"publisher","first-page":"179","DOI":"10.3109\/19396368.2012.691943","volume":"58","author":"S Chocu","year":"2012","unstructured":"Chocu S, Calvel P, Rolland AD, Pineau C. Spermatogenesis in mammals: proteomic insights. Syst Biol Reprod Med. 2012;58:179\u201390. https:\/\/doi.org\/10.3109\/19396368.2012.691943.","journal-title":"Syst Biol Reprod Med"},{"key":"12918_CR17","doi-asserted-by":"publisher","first-page":"404","DOI":"10.1016\/j.cbd.2006.10.002","volume":"1","author":"M Paz","year":"2006","unstructured":"Paz M, Mor\u00edn M, Del Mazo J. Proteome profile changes during mouse testis development. Comp Biochem Physiol D Genomics Proteomics. 2006;1:404\u201315. https:\/\/doi.org\/10.1016\/j.cbd.2006.10.002.","journal-title":"Comp Biochem Physiol D Genomics Proteomics"},{"key":"12918_CR18","doi-asserted-by":"publisher","first-page":"103","DOI":"10.1016\/j.ejcb.2019.01.001","volume":"98","author":"SMK G\u00e4rtner","year":"2019","unstructured":"G\u00e4rtner SMK, Hundertmark T, Nolte H, Theofel I, Eren-Ghiani Z, Tetzner C, et al. Stage-specific testes proteomics of Drosophila melanogaster identifies essential proteins for male fertility. Eur J Cell Biol. 2019;98:103\u201315. https:\/\/doi.org\/10.1016\/j.ejcb.2019.01.001.","journal-title":"Eur J Cell Biol"},{"key":"12918_CR19","doi-asserted-by":"publisher","first-page":"93","DOI":"10.1016\/j.anireprosci.2017.12.012","volume":"189","author":"Z Lu","year":"2018","unstructured":"Lu Z, Ma Y, Zhang Q, Zhao X, Zhang Y, Zhang L. Proteomic analyses of ram (Ovis aries) testis during different developmental stages. Anim Reprod Sci. 2018;189:93\u2013102. https:\/\/doi.org\/10.1016\/j.anireprosci.2017.12.012.","journal-title":"Anim Reprod Sci"},{"key":"12918_CR20","doi-asserted-by":"publisher","first-page":"209","DOI":"10.1146\/annurev.ento.53.103106.093441","volume":"53","author":"GE Heimpel","year":"2007","unstructured":"Heimpel GE, de Boer JG. Sex determination in the Hymenoptera. Annu Rev Entomol. 2007;53:209\u201330. https:\/\/doi.org\/10.1146\/annurev.ento.53.103106.093441.","journal-title":"Annu Rev Entomol"},{"key":"12918_CR21","doi-asserted-by":"publisher","first-page":"10","DOI":"10.1016\/j.jinsphys.2016.06.002","volume":"91\u201392","author":"M Chirault","year":"2016","unstructured":"Chirault M, Van de Zande L, Hidalgo K, Chevrier C, Bressac C, L\u00e9cureuil C. The spatio-temporal partitioning of sperm by males of the prospermatogenic parasitoid Nasonia vitripennis is in line with its gregarious lifestyle. J Insect Physiol. 2016;91\u201392:10\u20137. https:\/\/doi.org\/10.1016\/j.jinsphys.2016.06.002.","journal-title":"J Insect Physiol"},{"key":"12918_CR22","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-019-48332-9","volume":"9","author":"PM Ferree","year":"2019","unstructured":"Ferree PM, Aldrich JC, Jing XA, Norwood CT, Van Schaick MR, Cheema MS, et al. Spermatogenesis in haploid males of the jewel wasp Nasonia vitripennis. Sci Rep. 2019;9:9. https:\/\/doi.org\/10.1038\/s41598-019-48332-9.","journal-title":"Sci Rep"},{"key":"12918_CR23","first-page":"483","volume":"69","author":"MI Pennypacker","year":"1958","unstructured":"Pennypacker MI. The chromosomes of the parasitic wasp, Mormoniellavitripennis. I. In spermatogenesis of haploid and diploid males. Arch Biol (Liege). 1958;69:483\u201395.","journal-title":"Arch Biol (Liege)"},{"key":"12918_CR24","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1093\/oxfordjournals.jhered.a107631","volume":"59","author":"PW Whiting","year":"1968","unstructured":"Whiting PW. The chromosomes of Mormoniella. J Hered. 1968;59:19\u201322. https:\/\/doi.org\/10.1093\/oxfordjournals.jhered.a107631.","journal-title":"J Hered"},{"key":"12918_CR25","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pgen.1008518","volume":"16","author":"A Rago","year":"2020","unstructured":"Rago A, Werren JH, Colbourne JK. Sex biased expression and co-expression networks in development, using the hymenopteran Nasonia vitripennis. PLoS Genet. 2020;16:e1008518. https:\/\/doi.org\/10.1371\/journal.pgen.1008518.","journal-title":"PLoS Genet"},{"key":"12918_CR26","doi-asserted-by":"publisher","first-page":"2647","DOI":"10.1534\/g3.115.021386","volume":"5","author":"PM Ferree","year":"2015","unstructured":"Ferree PM, Fang C, Mastrodimos M, Hay BA, Amrhein H, Akbari OS. Identification of genes uniquely expressed in the germ-line tissues of the jewel wasp Nasonia vitripennis. G3 Bethesda. 2015;5:2647\u201353. https:\/\/doi.org\/10.1534\/g3.115.021386.","journal-title":"G3 Bethesda"},{"key":"12918_CR27","doi-asserted-by":"publisher","first-page":"1597","DOI":"10.1534\/g3.113.007583","volume":"3","author":"OS Akbari","year":"2013","unstructured":"Akbari OS, Antoshechkin I, Hay BA, Ferree PM. Transcriptome profiling of Nasonia vitripennis testis reveals novel transcripts expressed from the selfish B chromosome, paternal sex ratio. G3 Bethesda. 2013;3:1597\u2013605. https:\/\/doi.org\/10.1534\/g3.113.007583.","journal-title":"G3 Bethesda"},{"key":"12918_CR28","doi-asserted-by":"publisher","first-page":"5","DOI":"10.1016\/j.jprot.2014.01.007","volume":"105","author":"J Armengaud","year":"2014","unstructured":"Armengaud J, Trapp J, Pible O, Geffard O, Chaumot A, Hartmann EM. Non-model organisms, a species endangered by proteogenomics. J Proteomics. 2014;105:5\u201318. https:\/\/doi.org\/10.1016\/j.jprot.2014.01.007.","journal-title":"J Proteomics"},{"key":"12918_CR29","doi-asserted-by":"publisher","DOI":"10.1016\/j.jprot.2025.105441","volume":"316","author":"J Armengaud","year":"2025","unstructured":"Armengaud J, Cardon T, Cristobal S, Matallana-Surget S, Bertile F. Novel model organisms and proteomics for a better biological understanding. J Proteomics. 2025;316:105441. https:\/\/doi.org\/10.1016\/j.jprot.2025.105441.","journal-title":"J Proteomics"},{"key":"12918_CR30","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0120656","volume":"10","author":"M Chirault","year":"2015","unstructured":"Chirault M, Lucas C, Goubault M, Chevrier C, Bressac C, L\u00e9cureuil C. A combined approach to heat stress effect on male fertility in Nasonia vitripennis: From the physiological consequences on spermatogenesis to the reproductive adjustment of females mated with stressed males. PLoS ONE. 2015;10:e0120656. https:\/\/doi.org\/10.1371\/journal.pone.0120656.","journal-title":"PLoS ONE"},{"key":"12918_CR31","doi-asserted-by":"publisher","unstructured":"Hartmann EM, Allain F, Gaillard J-C, Pible O, Armengaud J. Taking the Shortcut for High-Throughput Shotgun Proteomic Analysis of Bacteria. In: Vergunst AC, O\u2019Callaghan D, editors. Host-Bacteria Interactions. New York, NY: Springer New York; 2014. p. 275\u201385. https:\/\/doi.org\/10.1007\/978-1-4939-1261-2_16.","DOI":"10.1007\/978-1-4939-1261-2_16"},{"key":"12918_CR32","doi-asserted-by":"publisher","first-page":"1555","DOI":"10.1080\/17435390.2016.1244299","volume":"10","author":"G Klein","year":"2016","unstructured":"Klein G, Math\u00e9 C, Biola-Clier M, Devineau S, Drouineau E, Hatem E, et al. RNA-binding proteins are a major target of silica nanoparticles in cell extracts. Nanotoxicology. 2016;10:1555\u201364. https:\/\/doi.org\/10.1080\/17435390.2016.1244299.","journal-title":"Nanotoxicology"},{"key":"12918_CR33","doi-asserted-by":"publisher","first-page":"2996","DOI":"10.1111\/1462-2920.14975","volume":"22","author":"D Gouveia","year":"2020","unstructured":"Gouveia D, Grenga L, Pible O, Armengaud J. Quick microbial molecular phenotyping by differential shotgun proteomics. Environ Microbiol. 2020;22:2996\u20133004. https:\/\/doi.org\/10.1111\/1462-2920.14975.","journal-title":"Environ Microbiol"},{"key":"12918_CR34","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1093\/nar\/28.1.235","volume":"28","author":"HM Berman","year":"2000","unstructured":"Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H. The Protein Data Bank. Nucleic Acids Res. 2000;28:235\u201342. https:\/\/doi.org\/10.1093\/nar\/28.1.235.","journal-title":"Nucleic Acids Res"},{"key":"12918_CR35","doi-asserted-by":"publisher","first-page":"129","DOI":"10.1002\/pro.3289","volume":"27","author":"RA Laskowski","year":"2018","unstructured":"Laskowski RA, Jab\u0142o\u0144ska J, Pravda L, Va\u0159ekov\u00e1 RS, Thornton JM. PDBsum: Structural summaries of PDB entries. Protein Sci. 2018;27:129\u201334. https:\/\/doi.org\/10.1002\/pro.3289.","journal-title":"Protein Sci"},{"key":"12918_CR36","doi-asserted-by":"publisher","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","volume":"596","author":"J Jumper","year":"2021","unstructured":"Jumper J, Evans R, Pritzel A, Green T, Figurnov M, Ronneberger O, et al. Highly accurate protein structure prediction with AlphaFold. Nature. 2021;596:583\u20139. https:\/\/doi.org\/10.1038\/s41586-021-03819-2.","journal-title":"Nature"},{"key":"12918_CR37","doi-asserted-by":"publisher","first-page":"D368","DOI":"10.1093\/nar\/gkad1011","volume":"52","author":"M Varadi","year":"2024","unstructured":"Varadi M, Bertoni D, Magana P, Paramval U, Pidruchna I, Radhakrishnan M, et al. AlphaFold protein structure database in 2024: providing structure coverage for over 214 million protein sequences. Nucleic Acids Res. 2024;52:D368\u201375. https:\/\/doi.org\/10.1093\/nar\/gkad1011.","journal-title":"Nucleic Acids Res"},{"key":"12918_CR38","doi-asserted-by":"publisher","first-page":"D439","DOI":"10.1093\/nar\/gkab1061","volume":"50","author":"M Varadi","year":"2022","unstructured":"Varadi M, Anyango S, Deshpande M, Nair S, Natassia C, Yordanova G, et al. AlphaFold protein structure database: massively expanding the structural coverage of protein-sequence space with high-accuracy models. Nucleic Acids Res. 2022;50:D439\u201344. https:\/\/doi.org\/10.1093\/nar\/gkab1061.","journal-title":"Nucleic Acids Res"},{"key":"12918_CR39","doi-asserted-by":"publisher","first-page":"590","DOI":"10.1038\/s41586-021-03828-1","volume":"596","author":"K Tunyasuvunakool","year":"2021","unstructured":"Tunyasuvunakool K, Adler J, Wu Z, Green T, Zielinski M, \u017d\u00eddek A, et al. Highly accurate protein structure prediction for the human proteome. Nature. 2021;596:590\u20136. https:\/\/doi.org\/10.1038\/s41586-021-03828-1.","journal-title":"Nature"},{"key":"12918_CR40","doi-asserted-by":"publisher","first-page":"637","DOI":"10.1038\/s41586-023-06510-w","volume":"622","author":"I Barrio-Hernandez","year":"2023","unstructured":"Barrio-Hernandez I, Yeo J, J\u00e4nes J, Mirdita M, Gilchrist CLM, Wein T, et al. Clustering predicted structures at the scale of the known protein universe. Nature. 2023;622:637\u201345. https:\/\/doi.org\/10.1038\/s41586-023-06510-w.","journal-title":"Nature"},{"key":"12918_CR41","doi-asserted-by":"publisher","first-page":"243","DOI":"10.1038\/s41587-023-01773-0","volume":"42","author":"M van Kempen","year":"2024","unstructured":"van Kempen M, Kim SS, Tumescheit C, Mirdita M, Lee J, Gilchrist CLM, et al. Fast and accurate protein structure search with Foldseek. Nat Biotechnol. 2024;42:243\u20136. https:\/\/doi.org\/10.1038\/s41587-023-01773-0.","journal-title":"Nat Biotechnol"},{"key":"12918_CR42","doi-asserted-by":"publisher","first-page":"889","DOI":"10.1093\/bioinformatics\/btq066","volume":"26","author":"J Xu","year":"2010","unstructured":"Xu J, Zhang Y. How significant is a protein structure similarity with TM-score = 0.5? Bioinformatics. 2010;26:889\u201395. https:\/\/doi.org\/10.1093\/bioinformatics\/btq066.","journal-title":"Bioinformatics"},{"key":"12918_CR43","doi-asserted-by":"publisher","DOI":"10.1002\/pro.4792","volume":"32","author":"EC Meng","year":"2023","unstructured":"Meng EC, Goddard TD, Pettersen EF, Couch GS, Pearson ZJ, Morris JH, et al. UCSF ChimeraX: tools for structure building and analysis. Protein Sci. 2023;32:e4792. https:\/\/doi.org\/10.1002\/pro.4792.","journal-title":"Protein Sci"},{"key":"12918_CR44","doi-asserted-by":"publisher","first-page":"2307","DOI":"10.1093\/molbev\/msx168","volume":"34","author":"TC Levin","year":"2017","unstructured":"Levin TC, Malik HS. Rapidly evolving Toll-3\/4 genes encode male-specific toll-like receptors in Drosophila. Mol Biol Evol. 2017;34:2307\u201323. https:\/\/doi.org\/10.1093\/molbev\/msx168.","journal-title":"Mol Biol Evol"},{"key":"12918_CR45","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.75761","volume":"11","author":"NR Braffman","year":"2022","unstructured":"Braffman NR, Ruskoski TB, Davis KM, Glasser NR, Johnson C, Okafor CD, et al. Structural basis for an unprecedented enzymatic alkylation in cylindrocyclophane biosynthesis. Elife. 2022;11:e75761. https:\/\/doi.org\/10.7554\/eLife.75761.","journal-title":"Elife"},{"key":"12918_CR46","doi-asserted-by":"publisher","first-page":"5180","DOI":"10.1021\/pr4004773","volume":"12","author":"R Zareie","year":"2013","unstructured":"Zareie R, Eubel H, Millar AH, Baer B. Long-term survival of high quality sperm: insights into the sperm proteome of the honeybee Apis mellifera. J Proteome Res. 2013;12:5180\u20138. https:\/\/doi.org\/10.1021\/pr4004773.","journal-title":"J Proteome Res"},{"key":"12918_CR47","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0125068","volume":"10","author":"V Gorshkov","year":"2015","unstructured":"Gorshkov V, Blenau W, Koeniger G, R\u00f6mpp A, Vilcinskas A, Spengler B. Protein and peptide composition of male accessory glands of Apis mellifera drones investigated by mass spectrometry. PLoS ONE. 2015;10:e0125068. https:\/\/doi.org\/10.1371\/journal.pone.0125068.","journal-title":"PLoS ONE"},{"key":"12918_CR48","doi-asserted-by":"publisher","first-page":"541","DOI":"10.1111\/j.1365-2583.2006.00674.x","volume":"15","author":"AM Collins","year":"2006","unstructured":"Collins AM, Caperna TJ, Williams V, Garrett WM, Evans JD. Proteomic analyses of male contributions to honey bee sperm storage and mating. Insect Mol Biol. 2006;15:541\u20139. https:\/\/doi.org\/10.1111\/j.1365-2583.2006.00674.x.","journal-title":"Insect Mol Biol"},{"key":"12918_CR49","doi-asserted-by":"publisher","first-page":"2085","DOI":"10.1002\/pmic.200800708","volume":"9","author":"B Baer","year":"2009","unstructured":"Baer B, Heazlewood JL, Taylor NL, Eubel H, Millar AH. The seminal fluid proteome of the honeybee Apis mellifera. Proteomics. 2009;9:2085\u201397. https:\/\/doi.org\/10.1002\/pmic.200800708.","journal-title":"Proteomics"},{"key":"12918_CR50","doi-asserted-by":"publisher","first-page":"28","DOI":"10.1016\/j.jprot.2012.11.023","volume":"79","author":"CJ Martyniuk","year":"2013","unstructured":"Martyniuk CJ, Alvarez S. Proteome analysis of the fathead minnow (Pimephales promelas) reproductive testes. J Proteomics. 2013;79:28\u201342. https:\/\/doi.org\/10.1016\/j.jprot.2012.11.023.","journal-title":"J Proteomics"},{"key":"12918_CR51","doi-asserted-by":"publisher","first-page":"826","DOI":"10.1111\/andr.13314","volume":"11","author":"K Nozawa","year":"2023","unstructured":"Nozawa K, Garcia TX, Kent K, Leng M, Jain A, Malovannaya A, et al. Testis-specific serine kinase 3 is required for sperm morphogenesis and male fertility. Andrology. 2023;11:826\u201339. https:\/\/doi.org\/10.1111\/andr.13314.","journal-title":"Andrology"},{"key":"12918_CR52","doi-asserted-by":"publisher","first-page":"1267","DOI":"10.1093\/genetics\/155.3.1267","volume":"155","author":"S Orgad","year":"2000","unstructured":"Orgad S, Rosenfeld G, Greenspan RJ, Segal D. Courtless, the Drosophila UBC7 homolog, is involved in male courtship behavior and spermatogenesis. Genetics. 2000;155:1267\u201380. https:\/\/doi.org\/10.1093\/genetics\/155.3.1267.","journal-title":"Genetics"},{"key":"12918_CR53","doi-asserted-by":"publisher","DOI":"10.1126\/science.abd4914","volume":"371","author":"S Gadadhar","year":"2021","unstructured":"Gadadhar S, Alvarez Viar G, Hansen JN, Gong A, Kostarev A, Ialy-Radio C, et al. Tubulin glycylation controls axonemal dynein activity, flagellar beat, and male fertility. Science. 2021;371:eabd4914. https:\/\/doi.org\/10.1126\/science.abd4914.","journal-title":"Science"},{"key":"12918_CR54","doi-asserted-by":"publisher","first-page":"1076","DOI":"10.1016\/j.cell.2009.05.020","volume":"137","author":"K Rogowski","year":"2009","unstructured":"Rogowski K, Juge F, van Dijk J, Wloga D, Strub J-M, Levilliers N, et al. Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation. Cell. 2009;137:1076\u201387. https:\/\/doi.org\/10.1016\/j.cell.2009.05.020.","journal-title":"Cell"},{"key":"12918_CR55","doi-asserted-by":"publisher","first-page":"1097","DOI":"10.1002\/prot.26496","volume":"91","author":"J Liu","year":"2023","unstructured":"Liu J, Yuan R, Shao W, Wang J, Silman I, Sussman JL. Do \u201cnewly born\u201d orphan proteins resemble \u201cnever born\u201d proteins? A study using three deep learning algorithms. Proteins. 2023;91:1097\u2013115. https:\/\/doi.org\/10.1002\/prot.26496.","journal-title":"Proteins"},{"key":"12918_CR56","doi-asserted-by":"publisher","first-page":"295","DOI":"10.1038\/s41588-024-02059-0","volume":"57","author":"S Xia","year":"2025","unstructured":"Xia S, Chen J, Arsala D, Emerson JJ, Long M. Functional innovation through new genes as a general evolutionary process. Nat Genet. 2025;57:295\u2013309. https:\/\/doi.org\/10.1038\/s41588-024-02059-0.","journal-title":"Nat Genet"},{"key":"12918_CR57","doi-asserted-by":"publisher","first-page":"73","DOI":"10.1016\/j.sbi.2014.05.006","volume":"26","author":"S Light","year":"2014","unstructured":"Light S, Basile W, Elofsson A. Orphans and new gene origination, a structural and evolutionary perspective. Curr Opin Struct Biol. 2014;26:73\u201383. https:\/\/doi.org\/10.1016\/j.sbi.2014.05.006.","journal-title":"Curr Opin Struct Biol"},{"key":"12918_CR58","doi-asserted-by":"publisher","DOI":"10.1093\/gbe\/evae176","volume":"16","author":"L Middendorf","year":"2024","unstructured":"Middendorf L, Ravi Iyengar B, Eicholt LA. Sequence, structure, and functional space of Drosophilade novo proteins. Genome Biol Evol. 2024;16:evae176. https:\/\/doi.org\/10.1093\/gbe\/evae176.","journal-title":"Genome Biol Evol"},{"key":"12918_CR59","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pgen.1009787","volume":"17","author":"EL Rivard","year":"2021","unstructured":"Rivard EL, Ludwig AG, Patel PH, Grandchamp A, Arnold SE, Berger A, et al. A putative de novo evolved gene required for spermatid chromatin condensation in Drosophila melanogaster. PLoS Genet. 2021;17:e1009787. https:\/\/doi.org\/10.1371\/journal.pgen.1009787.","journal-title":"PLoS Genet"},{"key":"12918_CR60","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-021-21667-6","volume":"12","author":"A Lange","year":"2021","unstructured":"Lange A, Patel PH, Heames B, Damry AM, Saenger T, Jackson CJ, et al. Structural and functional characterization of a putative de novo gene in Drosophila. Nat Commun. 2021;12:1667. https:\/\/doi.org\/10.1038\/s41467-021-21667-6.","journal-title":"Nat Commun"},{"key":"12918_CR61","doi-asserted-by":"publisher","DOI":"10.1101\/2024.08.08.607187","author":"SY Guay","year":"2024","unstructured":"Guay SY, Patel PH, Thomalla JM, McDermott KL, O\u2019Toole JM, Arnold SE, et al. An orphan gene is essential for efficient sperm entry into eggs in Drosophila melanogaster. 2024. https:\/\/doi.org\/10.1101\/2024.08.08.607187.","journal-title":"An orphan gene is essential for efficient sperm entry into eggs in Drosophila melanogaster"},{"key":"12918_CR62","doi-asserted-by":"publisher","DOI":"10.1038\/s42003-023-04488-9","volume":"6","author":"N Bordin","year":"2023","unstructured":"Bordin N, Sillitoe I, Nallapareddy V, Rauer C, Lam SD, Waman VP, et al. AlphaFold2 reveals commonalities and novelties in protein structure space for 21 model organisms. Commun Biol. 2023;6:160. https:\/\/doi.org\/10.1038\/s42003-023-04488-9.","journal-title":"Commun Biol"},{"key":"12918_CR63","doi-asserted-by":"publisher","first-page":"646","DOI":"10.1038\/s41586-023-06622-3","volume":"622","author":"J Durairaj","year":"2023","unstructured":"Durairaj J, Waterhouse AM, Mets T, Brodiazhenko T, Abdullah M, Studer G, et al. Uncovering new families and folds in the natural protein universe. Nature. 2023;622:646\u201353. https:\/\/doi.org\/10.1038\/s41586-023-06622-3.","journal-title":"Nature"},{"key":"12918_CR64","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-024-45028-1","volume":"15","author":"J Peng","year":"2024","unstructured":"Peng J, Zhao L. The origin and structural evolution of de novo genes in Drosophila. Nat Commun. 2024;15:810. https:\/\/doi.org\/10.1038\/s41467-024-45028-1.","journal-title":"Nat Commun"},{"key":"12918_CR65","doi-asserted-by":"publisher","first-page":"2742","DOI":"10.1093\/bioinformatics\/btac202","volume":"38","author":"T Salda\u00f1o","year":"2022","unstructured":"Salda\u00f1o T, Escobedo N, Marchetti J, Zea DJ, Mac Donagh J, Velez Rueda AJ, et al. Impact of protein conformational diversity on AlphaFold predictions. Bioinformatics. 2022;38:2742\u20138. https:\/\/doi.org\/10.1093\/bioinformatics\/btac202.","journal-title":"Bioinformatics"},{"key":"12918_CR66","doi-asserted-by":"publisher","first-page":"1056","DOI":"10.1038\/s41594-022-00849-w","volume":"29","author":"M Akdel","year":"2022","unstructured":"Akdel M, Pires DEV, Pardo EP, J\u00e4nes J, Zalevsky AO, M\u00e9sz\u00e1ros B, et al. A structural biology community assessment of AlphaFold2 applications. Nat Struct Mol Biol. 2022;29:1056\u201367. https:\/\/doi.org\/10.1038\/s41594-022-00849-w.","journal-title":"Nat Struct Mol Biol"},{"key":"12918_CR67","doi-asserted-by":"publisher","unstructured":"Malhotra Y, John J, Yadav D, Sharma D, Vanshika, Rawal K, et al. Advancements in protein structure prediction: A comparative overview of AlphaFold and its derivatives. Computers in Biology and Medicine. 2025;188:109842. https:\/\/doi.org\/10.1016\/j.compbiomed.2025.109842.","DOI":"10.1016\/j.compbiomed.2025.109842"},{"key":"12918_CR68","doi-asserted-by":"publisher","first-page":"916","DOI":"10.1038\/nchembio.2421","volume":"13","author":"H Nakamura","year":"2017","unstructured":"Nakamura H, Schultz EE, Balskus EP. A new strategy for aromatic ring alkylation in cylindrocyclophane biosynthesis. Nat Chem Biol. 2017;13:916\u201321. https:\/\/doi.org\/10.1038\/nchembio.2421.","journal-title":"Nat Chem Biol"},{"key":"12918_CR69","doi-asserted-by":"publisher","first-page":"2108","DOI":"10.1021\/acscatal.1c04816","volume":"12","author":"H-Q Wang","year":"2022","unstructured":"Wang H-Q, Mou S-B, Xiao W, Zhou H, Hou X-D, Wang S-J, et al. Structural basis for the Friedel\u2013Crafts alkylation in cylindrocyclophane biosynthesis. ACS Catal. 2022;12:2108\u201317. https:\/\/doi.org\/10.1021\/acscatal.1c04816.","journal-title":"ACS Catal"},{"key":"12918_CR70","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.49853","volume":"8","author":"E Afanasieva","year":"2019","unstructured":"Afanasieva E, Chaudhuri I, Martin J, Hertle E, Ursinus A, Alva V, et al. Structural diversity of oligomeric \u03b2-propellers with different numbers of identical blades. Elife. 2019;8:e49853. https:\/\/doi.org\/10.7554\/eLife.49853.","journal-title":"Elife"},{"key":"12918_CR71","doi-asserted-by":"publisher","first-page":"553","DOI":"10.1016\/j.tibs.2011.07.004","volume":"36","author":"CK-M Chen","year":"2011","unstructured":"Chen CK-M, Chan N-L, Wang AH-J. The many blades of the \u03b2-propeller proteins: conserved but versatile. Trends Biochem Sci. 2011;36:553\u201361. https:\/\/doi.org\/10.1016\/j.tibs.2011.07.004.","journal-title":"Trends Biochem Sci"},{"key":"12918_CR72","doi-asserted-by":"publisher","first-page":"48","DOI":"10.1016\/j.sbi.2020.11.009","volume":"68","author":"B Mylemans","year":"2021","unstructured":"Mylemans B, Voet AR, Tame JR. The taming of the screw: the natural and artificial development of \u03b2 -propeller proteins. Curr Opin Struct Biol. 2021;68:48\u201354. https:\/\/doi.org\/10.1016\/j.sbi.2020.11.009.","journal-title":"Curr Opin Struct Biol"},{"key":"12918_CR73","doi-asserted-by":"publisher","first-page":"13574","DOI":"10.1021\/acs.jmedchem.2c01258","volume":"65","author":"JM Keil","year":"2022","unstructured":"Keil JM, Rafn GR, Turan IM, Aljohani MA, Sahebjam-Atabaki R, Sun X-L. Sialidase inhibitors with different mechanisms. J Med Chem. 2022;65:13574\u201393. https:\/\/doi.org\/10.1021\/acs.jmedchem.2c01258.","journal-title":"J Med Chem"},{"key":"12918_CR74","doi-asserted-by":"publisher","DOI":"10.3389\/fmicb.2019.00039","volume":"10","author":"JL McAuley","year":"2019","unstructured":"McAuley JL, Gilbertson BP, Trifkovic S, Brown LE, McKimm-Breschkin JL. Influenza virus neuraminidase structure and functions. Front Microbiol. 2019;10:39. https:\/\/doi.org\/10.3389\/fmicb.2019.00039.","journal-title":"Front Microbiol"},{"key":"12918_CR75","doi-asserted-by":"publisher","first-page":"436","DOI":"10.1016\/j.jmb.2008.09.032","volume":"384","author":"G Xu","year":"2008","unstructured":"Xu G, Potter JA, Russell RJM, Oggioni MR, Andrew PW, Taylor GL. Crystal structure of the NanB sialidase from Streptococcus pneumoniae. J Mol Biol. 2008;384:436\u201349. https:\/\/doi.org\/10.1016\/j.jmb.2008.09.032.","journal-title":"J Mol Biol"},{"key":"12918_CR76","doi-asserted-by":"publisher","first-page":"772","DOI":"10.1107\/S1744309108024044","volume":"64","author":"G Xu","year":"2008","unstructured":"Xu G, Li X, Andrew PW, Taylor GL. Structure of the catalytic domain of Streptococcus pneumoniae sialidase NanA. Acta Crystallogr F Struct Biol Cryst Commun. 2008;64:772\u20135. https:\/\/doi.org\/10.1107\/S1744309108024044.","journal-title":"Acta Crystallogr F Struct Biol Cryst Commun"},{"key":"12918_CR77","doi-asserted-by":"publisher","first-page":"830","DOI":"10.1016\/S0959-440X(96)80014-5","volume":"6","author":"G Taylor","year":"1996","unstructured":"Taylor G. Sialidases: structures, biological significance and therapeutic potential. Curr Opin Struct Biol. 1996;6:830\u20137. https:\/\/doi.org\/10.1016\/S0959-440X(96)80014-5.","journal-title":"Curr Opin Struct Biol"},{"key":"12918_CR78","doi-asserted-by":"publisher","first-page":"9080","DOI":"10.1074\/jbc.M710247200","volume":"283","author":"SL Newstead","year":"2008","unstructured":"Newstead SL, Potter JA, Wilson JC, Xu G, Chien C-H, Watts AG, et al. The structure of Clostridium perfringens NanI sialidase and its catalytic intermediates. J Biol Chem. 2008;283:9080\u20138. https:\/\/doi.org\/10.1074\/jbc.M710247200.","journal-title":"J Biol Chem"},{"key":"12918_CR79","doi-asserted-by":"publisher","first-page":"4149","DOI":"10.1074\/jbc.M510677200","volume":"281","author":"AG Watts","year":"2006","unstructured":"Watts AG, Oppezzo P, Withers SG, Alzari PM, Buschiazzo A. Structural and kinetic analysis of two covalent Sialosyl-Enzyme intermediates on Trypanosoma rangeli sialidase. J Biol Chem. 2006;281:4149\u201355. https:\/\/doi.org\/10.1074\/jbc.M510677200.","journal-title":"J Biol Chem"},{"key":"12918_CR80","doi-asserted-by":"publisher","first-page":"467","DOI":"10.1016\/j.bbrc.2009.01.108","volume":"380","author":"Y-S Hsiao","year":"2009","unstructured":"Hsiao Y-S, Parker D, Ratner AJ, Prince A, Tong L. Crystal structures of respiratory pathogen neuraminidases. Biochem Biophys Res Commun. 2009;380:467\u201371. https:\/\/doi.org\/10.1016\/j.bbrc.2009.01.108.","journal-title":"Biochem Biophys Res Commun"},{"key":"12918_CR81","doi-asserted-by":"publisher","DOI":"10.3390\/pathogens8010039","volume":"8","author":"P Sudhakara","year":"2019","unstructured":"Sudhakara P, Sellamuthu I, Aruni A. Bacterial sialoglycosidases in virulence and pathogenesis. Pathogens. 2019;8:39. https:\/\/doi.org\/10.3390\/pathogens8010039.","journal-title":"Pathogens"},{"key":"12918_CR82","doi-asserted-by":"publisher","DOI":"10.1039\/D5CB00170F","author":"EI Alvarado-Melendez","year":"2025","unstructured":"Alvarado-Melendez EI, Ruessink ST, Strijbis K, Wennekes T. Selective labeling and visualization of viral and bacterial neuraminidases using ortho -quinone methide-based probes. RSC Chem Biol. 2025. https:\/\/doi.org\/10.1039\/D5CB00170F.","journal-title":"RSC Chem Biol"},{"key":"12918_CR83","doi-asserted-by":"publisher","unstructured":"Monti E, Miyagi T. Structure and Function of Mammalian Sialidases. In: SialoGlyco Chemistry and Biology I. Berlin, Heidelberg: Springer Berlin Heidelberg; 2012. p. 183\u2013208. https:\/\/doi.org\/10.1007\/128_2012_328.","DOI":"10.1007\/128_2012_328"},{"key":"12918_CR84","doi-asserted-by":"publisher","first-page":"550","DOI":"10.1007\/s13238-018-0597-5","volume":"10","author":"F Li","year":"2019","unstructured":"Li F, Ding J. Sialylation is involved in cell fate decision during development, reprogramming and cancer progression. Protein Cell. 2019;10:550\u201365. https:\/\/doi.org\/10.1007\/s13238-018-0597-5.","journal-title":"Protein Cell"},{"key":"12918_CR85","doi-asserted-by":"publisher","first-page":"29","DOI":"10.1016\/S1096-4959(01)00372-4","volume":"129","author":"KE Achyuthan","year":"2001","unstructured":"Achyuthan KE, Achyuthan AM. Comparative enzymology, biochemistry and pathophysiology of human exo-\u03b1-sialidases (neuraminidases). Comp Biochem Physiol B Biochem Mol Biol. 2001;129:29\u201364. https:\/\/doi.org\/10.1016\/S1096-4959(01)00372-4.","journal-title":"Comp Biochem Physiol B Biochem Mol Biol"},{"key":"12918_CR86","doi-asserted-by":"publisher","first-page":"151","DOI":"10.1515\/BC.2001.023","volume":"382","author":"I Marchal","year":"2001","unstructured":"Marchal I, Jarvis DL, Cacan R, Verbert A. Glycoproteins from insect cells: sialylated or not? Biol Chem. 2001;382:151\u20139. https:\/\/doi.org\/10.1515\/BC.2001.023.","journal-title":"Biol Chem"},{"key":"12918_CR87","doi-asserted-by":"publisher","first-page":"329","DOI":"10.1093\/glycob\/cww128","volume":"27","author":"W Di","year":"2017","unstructured":"Di W, Fujita A, Hamaguchi K, Delannoy P, Sato C, Kitajima K. Diverse subcellular localizations of the insect CMP-sialic acid synthetases. Glycobiology. 2017;27:329\u201341. https:\/\/doi.org\/10.1093\/glycob\/cww128.","journal-title":"Glycobiology"},{"key":"12918_CR88","doi-asserted-by":"publisher","first-page":"4346","DOI":"10.1074\/jbc.M309912200","volume":"279","author":"K Koles","year":"2004","unstructured":"Koles K, Irvine KD, Panin VM. Functional characterization of Drosophila sialyltransferase. J Biol Chem. 2004;279:4346\u201357. https:\/\/doi.org\/10.1074\/jbc.M309912200.","journal-title":"J Biol Chem"},{"key":"12918_CR89","doi-asserted-by":"publisher","first-page":"673","DOI":"10.1126\/science.1585182","volume":"256","author":"J Roth","year":"1992","unstructured":"Roth J, Kempf A, Reuter G, Schauer R, Gehring WJ. Occurrence of sialic acids in Drosophila melanogaster. Science. 1992;256:673\u20135. https:\/\/doi.org\/10.1126\/science.1585182.","journal-title":"Science"},{"key":"12918_CR90","doi-asserted-by":"publisher","first-page":"146","DOI":"10.1021\/bp00020a005","volume":"9","author":"PJ Licari","year":"1993","unstructured":"Licari PJ, Jarvis DL, Bailey JE. Insect cell hosts for baculovirus expression vectors contain endogenous exoglycosidase activity. Biotechnol Prog. 1993;9:146\u201352. https:\/\/doi.org\/10.1021\/bp00020a005.","journal-title":"Biotechnol Prog"},{"key":"12918_CR91","doi-asserted-by":"publisher","first-page":"625","DOI":"10.1093\/glycob\/5.6.625","volume":"5","author":"R Amino","year":"1995","unstructured":"Amino R, Serrano AA, Morita OM, Pereira-Chioccola VL, Schenkman S. A sialidase activity in the midgut of the insect Triatomainfestans is responsible for the low levels of sialic acid in Trypanosomacruzi growing in the insect vector. Glycobiology. 1995;5:625\u201331. https:\/\/doi.org\/10.1093\/glycob\/5.6.625.","journal-title":"Glycobiology"},{"key":"12918_CR92","doi-asserted-by":"publisher","DOI":"10.1155\/2015\/504187","volume":"2015","author":"J Cime-Castillo","year":"2015","unstructured":"Cime-Castillo J, Delannoy P, Mendoza-Hern\u00e1ndez G, Monroy-Mart\u00ednez V, Harduin-Lepers A, Lanz-Mendoza H, et al. Sialic acid expression in the mosquito Aedesaegypti and its possible role in Dengue Virus-vector interactions. Biomed Res Int. 2015;2015:504187. https:\/\/doi.org\/10.1155\/2015\/504187.","journal-title":"Biomed Res Int"},{"key":"12918_CR93","doi-asserted-by":"publisher","first-page":"315","DOI":"10.1016\/S0040-8166(97)80007-9","volume":"29","author":"S Kara\u00e7al\u0131","year":"1997","unstructured":"Kara\u00e7al\u0131 S, K\u0131rm\u0131z\u0131g\u00fcl S, Deveci R, Deveci \u00d6, Onat T, G\u00fcrc\u00fc B. Presence of sialic acid in prothoracic glands of Galleriamellonella (Lepidoptera). Tissue Cell. 1997;29:315\u201321. https:\/\/doi.org\/10.1016\/S0040-8166(97)80007-9.","journal-title":"Tissue Cell"},{"key":"12918_CR94","doi-asserted-by":"publisher","first-page":"123, 1","DOI":"10.1095\/biolreprod.115.137810","volume":"94","author":"X Ma","year":"2016","unstructured":"Ma X, Pan Q, Feng Y, Choudhury BP, Ma Q, Gagneux P, et al. Sialylation facilitates the maturation of mammalian sperm and affects its survival in female Uterus1. Biol Reprod. 2016;94:123, 1\u20131310. https:\/\/doi.org\/10.1095\/biolreprod.115.137810.","journal-title":"Biol Reprod"},{"key":"12918_CR95","doi-asserted-by":"publisher","DOI":"10.3389\/fcell.2022.982931","volume":"10","author":"I Fliniaux","year":"2022","unstructured":"Fliniaux I, Marchand G, Molinaro C, Decloquement M, Martoriati A, Marin M, et al. Diversity of sialic acids and sialoglycoproteins in gametes and at fertilization. Front Cell Dev Biol. 2022;10:982931. https:\/\/doi.org\/10.3389\/fcell.2022.982931.","journal-title":"Front Cell Dev Biol"},{"key":"12918_CR96","doi-asserted-by":"publisher","first-page":"137","DOI":"10.1093\/biolre\/ioad067","volume":"109","author":"S Yi","year":"2023","unstructured":"Yi S, Feng Y, Wang Y, Ma F. Sialylation: fate decision of mammalian sperm development, fertilization, and male fertility. Biol Reprod. 2023;109:137\u201355. https:\/\/doi.org\/10.1093\/biolre\/ioad067.","journal-title":"Biol Reprod"},{"key":"12918_CR97","doi-asserted-by":"publisher","DOI":"10.1111\/imb.70002","author":"F Guerra","year":"2025","unstructured":"Guerra F, De Rouck S, Verhulst EC. SYNCAS \u2010mediated CRISPR \u2010Cas9 genome editing in the jewel wasp, Nasoniavitripennis. Insect Mol Biol. 2025. https:\/\/doi.org\/10.1111\/imb.70002.","journal-title":"Insect Mol Biol"}],"container-title":["BMC Genomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/article\/10.1186\/s12864-026-12918-1","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1186\/s12864-026-12918-1.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1186\/s12864-026-12918-1.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,7,14]],"date-time":"2026-07-14T14:35:41Z","timestamp":1784039741000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1186\/s12864-026-12918-1"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,5,21]]},"references-count":97,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2026,12]]}},"alternative-id":["12918"],"URL":"https:\/\/doi.org\/10.1186\/s12864-026-12918-1","relation":{},"ISSN":["1471-2164"],"issn-type":[{"value":"1471-2164","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,5,21]]},"assertion":[{"value":"30 January 2026","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"30 April 2026","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"21 May 2026","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"Not applicable.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics approval and consent to participate"}},{"value":"The authors declare no competing interests.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"613"}}