Sugar‐coated sperm: Unraveling the functions of the mammalian sperm glycocalyx
Open accessAbstract
Mammalian spermatozoa are coated with a thick glycocalyx that is assembled during sperm development, maturation, and upon contact with seminal fluid. The sperm glycocalyx is critical for sperm survival in the female reproductive tract and is modified during capacitation. The complex interplay among the various glycoconjugates generates numerous signaling motifs that may regulate sperm function and, as a result, fertility. Nascent spermatozoa assemble their own glycans while the cells still possess a functional endoplasmic reticulum and Golgi in the seminiferous tubule, but once spermatogenesis is complete, they lose the capacity to produce glycoconjugates de novo. Sperm glycans continue to be modified, during epididymal transit by extracellular glycosidases and glycosyltransferases. Furthermore, epididymal cells secrete glycoconjugates (glycophosphatidylinositol-anchored glycoproteins and glycolipids) and glycan-rich microvesicles that can fuse with the maturing sperm membrane. The sperm glycocalyx mediates numerous functions in the female reproductive tract, including the following: inhibition of premature capacitation; passage through the cervical mucus; protection from innate and adaptive female immunity; formation of the sperm reservoir; and masking sperm proteins involved in fertilization. The immense diversity in sperm-associated glycans within and between species forms a remarkable challenge to our understanding of essential sperm glycan functions.
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Glycans appear to be involved at many steps in the reproductive process, including sperm migration to the site of fertilization.
“Glycans also appear to be involved at many steps in the reproductive process, and in the processes of sperm migration to the site of fertilization (942).”
From Biological roles of glycans (2017) · cites this paper as [942]
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Wiederschain, G. Y. (2009) · Biochemistry (Moscow) · doi:10.1134/s0006297909090156 · Cited by 4,089 · see citing works
Eberhard, W. G. (1996) · Princeton University Press eBooks · doi:10.1515/9780691207209 · Cited by 2,783 · see citing works
Sperm transport in the female reproductive tract
Suárez, S. S., & Pacey, A. A. (2005) · Human Reproduction Update · doi:10.1093/humupd/dmi047 · Cited by 1,111 · see citing works
Biswas, C., Zhang, Y., DeCastro, R., Guo, H., Nakamura, T., Kataoka, H., & Nabeshima, K. (1995) · PubMed · Cited by 716 · see citing works
Schultz, N. D., Hamra, F. K., & Garbers, D. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1635054100 · Cited by 577 · see citing works
A mutation in human CMP-sialic acid hydroxylase occurred after the Homo-Pan divergence
Chou, H.-H., Takematsu, H., Diaz, S. L., Iber, J. C., Nickerson, E., Wright, K. L., Muchmore, E. A., Nelson, D. L., Warren, S. T., & Varki, A. P. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.20.11751 · Cited by 576 · see citing works
Evolutionary considerations in relating oligosaccharide diversity to biological function
Gagneux, P., & Varki, A. (1999) · Glycobiology · doi:10.1093/glycob/9.8.747 · Cited by 495 · see citing works
Self-citationMeiotic Drive as an Evolutionary Force
Sandler, L., & Novitski, E. (1957) · The American Naturalist · doi:10.1086/281969 · Cited by 490 · see citing works
Ioffe, E., & Stanley, P. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.2.728 · Cited by 400 · see citing works
Regulation of sperm storage and movement in the mammalian oviduct
Suárez, S. S. (2008) · The International Journal of Developmental Biology · doi:10.1387/ijdb.072527ss · Cited by 357 · see citing works
Chou, H.-H., Hayakawa, T., Diaz, S. L., Krings, M., Indriati, E., Leakey, M. G., Pääbo, S., Satta, Y., Takahata, N., & Varki, A. P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.182257399 · Cited by 351 · see citing works
Significance of the Need for Sperm Capacitation Before Fertilization in Eutherian Mammals
BEDFORD, J. M. (1983) · Biology of Reproduction · doi:10.1095/biolreprod28.1.108 · Cited by 347 · see citing works
The Molecular Diversity of Glycosaminoglycans Shapes Animal Development
Bülow, H. E., & Hobert, O. (2006) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.22.010605.093433 · Cited by 340 · see citing works
Sharkey, D. J., Tremellen, K. P., Jasper, M. J., Gemzell‐Danielsson, K., & Robertson, S. A. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1102736 · Cited by 329 · see citing works
Padler-karavani, V., Yu, H., Cao, H.-Z., Chokhawala, H. A., Karp, F., Varki, N., Chen, X., & Varki, A. (2008) · Glycobiology · doi:10.1093/glycob/cwn072 · Cited by 322 · see citing works
N-glycan processing in ER quality control
Ruddock, L. W., & Molinari, M. (2006) · Journal of Cell Science · doi:10.1242/jcs.03225 · Cited by 303 · see citing works
Epididymosomes are involved in the acquisition of new sperm proteins during epididymal transit
Sullivan, R., Frenette, G., & Girouard, J. (2007) · Asian Journal of Andrology · doi:10.1111/j.1745-7262.2007.00281.x · Cited by 299 · see citing works
Fertilizing Capacity of Bovine Sperm may be Maintained by Binding to Oviductal Epithelial Cells1
Pollard, J. W., Plante, C., King, W. A., Hansen, P. J., BETTERIDGE, K. J., & Suárez, S. S. (1991) · Biology of Reproduction · doi:10.1095/biolreprod44.1.102 · Cited by 290 · see citing works
Igakura, T., Kadomatsu, K., Kaname, T., Muramatsu, H., Fan, Q., Miyauchi, T., Toyama, Y., Kuno, N., Yuasa, S., Takahashi, M., et al. (1998) · Developmental Biology · doi:10.1006/dbio.1997.8819 · Cited by 287 · see citing works
Links between CD147 Function, Glycosylation, and Caveolin-1
Tang, W., Chang, S. B., & Hemler, M. E. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-05-0402 · Cited by 241 · see citing works
Osheroff, J. E. (1999) · Molecular Human Reproduction · doi:10.1093/molehr/5.11.1017 · Cited by 240 · see citing works
The Sialome—Far More Than the Sum of Its Parts
Cohen, M., & Varki, A. P. (2010) · OMICS A Journal of Integrative Biology · doi:10.1089/omi.2009.0148 · Cited by 232 · see citing works
Ventelä, S., Toppari, J., & Parvinen, M. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-10-0647 · Cited by 216 · see citing works
Evolution and pathophysiology of the human natural anti-?-galactosyl IgG (anti-Gal) antibody
Galili, U. (1993) · Springer Seminars in Immunopathology · doi:10.1007/bf00201098 · Cited by 199 · see citing works
Rooney, I. A., Atkinson, J. P., Krul, E. S., Schonfeld, G., Polakoski, K. L., Saffitz, J. E., & Morgan, B. P. (1993) · The Journal of Experimental Medicine · doi:10.1084/jem.177.5.1409 · Cited by 199 · see citing works
Chui, D., Oh‐eda, M., Liao, Y.-F., Panneerselvam, K., Lal, A., Marek, K. W., Freeze, H. H., Moremen, K. W., Fukuda, M. N., & Marth, J. D. (1997) · Cell · doi:10.1016/s0092-8674(00)80322-0 · Cited by 198 · see citing works
Genetic remodeling of protein glycosylation in vivo induces autoimmune disease
Chui, D., Sellakumar, G., Green, R. S., Sutton‐Smith, M., McQuistan, T. J., Marek, K. W., Morris, H. R., Dell, A., & Marth, J. D. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.3.1142 · Cited by 192 · see citing works
Hammond, E., Khurana, A., Shridhar, V., & Dredge, K. S. (2014) · Frontiers in Oncology · doi:10.3389/fonc.2014.00195 · Cited by 192 · see citing works
The leukocytic reaction of the human uterine cervix to spermatozoa
Pandya, I. J., & COHEN, J. (1985) · Fertility and Sterility · doi:10.1016/s0015-0282(16)48442-6 · Cited by 192 · see citing works
Seminal DNase Frees Spermatozoa Entangled in Neutrophil Extracellular Traps
Alghamdi, A. S., & Foster, D. N. (2005) · Biology of Reproduction · doi:10.1095/biolreprod.105.045666 · Cited by 186 · see citing works
Björkman, Y. A., Thomsson, K. A., Larsson, J. M. H., Ekerhovd, E., & Hansson, G. C. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m600439-mcp200 · Cited by 184 · see citing works
Emmprin (CD147), a cell surface regulator of matrix metalloproteinase production and function
Toole, B. P. (2003) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(03)54015-7 · Cited by 174 · see citing works
Kirchhoff, C., & Hale, G. (1996) · Molecular Human Reproduction · doi:10.1093/molehr/2.3.177 · Cited by 170 · see citing works
Post‐mating Inflammatory Responses of the Uterus
Katila, T. (2012) · Reproduction in Domestic Animals · doi:10.1111/j.1439-0531.2012.02120.x · Cited by 164 · see citing works
Foresta, C., Patassini, C., Bertoldo, A., Menegazzo, M., Francavilla, F., Barzon, L., & Ferlin, A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0015036 · Cited by 163 · see citing works
A Common Mutation in the Defensin DEFB126 Causes Impaired Sperm Function and Subfertility
Tollner, T. L., Venners, S. A., Hollox, E. J., Yudin, A. I., Liu, X., Tang, G., Xing, H., Kays, R. J., Lau, T., Overstreet, J. W., et al. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002289 · Cited by 160 · see citing works
A unified vision of the building blocks of life
Marth, J. D. (2008) · Nature Cell Biology · doi:10.1038/ncb0908-1015 · Cited by 157 · see citing works
Taylor, R. E., Gregg, C. J., Padler‐Karavani, V., Ghaderi, D., Yu, H., Huang, S., Sorensen, R. U., Chen, X., Jaime Inostroza, S., Nizet, V., et al. (2010) · The Journal of Experimental Medicine · doi:10.1084/jem.20100575 · Cited by 156 · see citing works
Region-specific gene expression in the epididymis
Belleannée, C., Thimon, V., & Sullivan, R. (2012) · Cell and Tissue Research · doi:10.1007/s00441-012-1381-0 · Cited by 155 · see citing works
Germ Cell Survival Through Carbohydrate-Mediated Interaction with Sertoli Cells
Akama, T. O., Nakagawa, H., Sugihara, K., Narisawa, S., Οhyama, C., Nishimura, S., O’Brien, D. A., Moremen, K. W., Millán, J. L., & Fukuda, M. N. (2002) · Science · doi:10.1126/science.1065570 · Cited by 153 · see citing works
Dobrinski, I., Smith, T. T., Suárez, S. S., & Ball, B. A. (1997) · Biology of Reproduction · doi:10.1095/biolreprod56.4.861 · Cited by 152 · see citing works
Calsperin Is a Testis-specific Chaperone Required for Sperm Fertility
Ikawa, M., Tokuhiro, K., Yamaguchi, R., Benham, A. M., Tamura, T., Wada, I., Satouh, Y., Inoue, N., & Okabe, M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.140152 · Cited by 149 · see citing works
The human sperm protein PH‐20 has hyaluronidase activity
Gmachl, M., Sagan, S., Ketter, S., & Kreil, G. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80873-s · Cited by 145 · see citing works
The glycocalyx of the sperm surface
Schröter, S. (1999) · Human Reproduction Update · doi:10.1093/humupd/5.4.302 · Cited by 145 · see citing works
Takamiya, K., Yamamoto, A., Furukawa, K., Zhao, J., Fukumoto, S., Yamashiro, S., Okada, M., Haraguchi, M., Shin, M., Kishikawa, M., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.21.12147 · Cited by 142 · see citing works
Tateno, H., Krapf, D., Hino, T., Sánchez‐Cárdenas, C., Darszon, A., Yanagimachi, R., & Visconti, P. E. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1317113110 · Cited by 140 · see citing works
Yudin, A. I., Generao, S. E., Tollner, T. L., Treece, C. A., Overstreet, J. W., & Cherr, G. N. (2005) · Biology of Reproduction · doi:10.1095/biolreprod.105.042432 · Cited by 133 · see citing works
Wang, Y., Tan, J., Sutton‐Smith, M., Ditto, D., Panico, M., Campbell, R. M., Varki, N. M., Long, J. M., Jaeken, J., Levinson, S. R., et al. (2001) · Glycobiology · doi:10.1093/glycob/11.12.1051 · Cited by 133 · see citing works
Ariga, T., Miyatake, T., & Yu, R. K. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22393 · Cited by 128 · see citing works
Yamaguchi, R., Yamagata, K., Ikawa, M., Moss, S. B., & Okabe, M. (2006) · Biology of Reproduction · doi:10.1095/biolreprod.106.052977 · Cited by 128 · see citing works
Evolution of carbohydrate antigens—microbial forces shaping host glycomes?
Bishop, J. R., & Gagneux, P. (2007) · Glycobiology · doi:10.1093/glycob/cwm005 · Cited by 126 · see citing works
Self-citationThe Leukocytic Reaction of the Human Uterine Cervix
Thompson, L. A., Barratt, C. L. R., Bolton, A. E., & Cooke, I. D. (1992) · American Journal of Reproductive Immunology · doi:10.1111/j.1600-0897.1992.tb00765.x · Cited by 123 · see citing works
Macaque sperm coating protein DEFB126 facilitates sperm penetration of cervical mucus
Tollner, T. L., Yudin, A. I., Treece, C. A., Overstreet, J. W., & Cherr, G. N. (2008) · Human Reproduction · doi:10.1093/humrep/den276 · Cited by 118 · see citing works
Male Germ Cells Require Polyenoic Sphingolipids with Complex Glycosylation for Completion of Meiosis
Rabionet, M., van der Spoel, A. C., Chuang, C., von Tümpling-Radosta, B., Litjens, M., Bouwmeester, D., Hellbusch, C. C., Körner, C., Wiegandt, H., Gorgas, K., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800870200 · Cited by 111 · see citing works
Ceballos, A., Lenicov, F. R., Sabatté, J., Rodrígues, C. R., Cabrini, M., Jancic, C. C., Raiden, S., Donaldson, M. J., Pasqualini, R. A., Marín-Briggiler, C. I., et al. (2009) · The Journal of Experimental Medicine · doi:10.1084/jem.20091579 · Cited by 110 · see citing works
Multifunctional glycoprotein DEFB126—a curious story of defensin-clad spermatozoa
Tollner, T. L., Bevins, C. L., & Cherr, G. N. (2012) · Nature Reviews Urology · doi:10.1038/nrurol.2012.109 · Cited by 109 · see citing works
Holt, C. E., & Dickson, B. J. (2005) · Neuron · doi:10.1016/j.neuron.2005.03.021 · Cited by 107 · see citing works
Tollner, T. L., Yudin, A. I., Tarantal, A. F., Treece, C. A., Overstreet, J. W., & Cherr, G. N. (2007) · Biology of Reproduction · doi:10.1095/biolreprod.107.064071 · Cited by 107 · see citing works
Transcription in Haploid Male Germ Cells
Dadoune, J., Siffroi, J., & Alfonsi, M. F. (2004) · International review of cytology · doi:10.1016/s0074-7696(04)37001-4 · Cited by 104 · see citing works
Glycodelin from seminal plasma is a differentially glycosylated form of contraceptive glycodelin-A
Koistinen, H. K., Koistinen, R., Dell, A., Morris, H. R., Easton, R. L., Patankar, M. S., Oehninger, S., Clark, G. F., & Seppälä, M. T. (1996) · Molecular Human Reproduction · doi:10.1093/molehr/2.10.759 · Cited by 98 · see citing works
Post-Synthetic Regulation of HS Structure: The Yin and Yang of the Sulfs in Cancer
Vivès, R. R., Seffouh, A., & Lortat‐Jacob, H. (2014) · Frontiers in Oncology · doi:10.3389/fonc.2013.00331 · Cited by 97 · see citing works
Drake, P. M., Nathan, J. K., Stock, C. M., Chang, P. V., Muench, M. O., Nakata, D., Reader, J. R., Gip, P., Golden, K. P. K., Weinhold, B., et al. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.10.6850 · Cited by 95 · see citing works
Netzel–Arnett, S., Bugge, T. H., Hess, R. A., Carnes, K. I., Stringer, B. W., Scarman, A. L., Hooper, J. D., Tonks, I. D., Kay, G. F., & Antalis, T. (2009) · Biology of Reproduction · doi:10.1095/biolreprod.109.076273 · Cited by 95 · see citing works
Fujihara, Y., Okabe, M., & Ikawa, M. (2014) · Biology of Reproduction · doi:10.1095/biolreprod.113.112888 · Cited by 95 · see citing works
Diekman, A. B. (2003) · Cellular and Molecular Life Sciences CMLS · doi:10.1007/s000180300025 · Cited by 92 · see citing works
Novel Class of Glycosphingolipids Involved in Male Fertility
Sandhoff, R., Geyer, R., Jennemann, R., Paret, C., Kiss, É., Yamashita, T., Gorgas, K., Sijmonsma, T., Iwamori, M., Finaz, C., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502775200 · Cited by 89 · see citing works
Hyaluronan in cervical epithelia protects against infection-mediated preterm birth
Akgul, Y., Word, R. A., Ensign, L. M., Yamaguchi, Y., Lydon, J. P., Hanes, J. S., & Mahendroo, M. (2014) · Journal of Clinical Investigation · doi:10.1172/jci78765 · Cited by 88 · see citing works
Saxena, D., Oh-oka, T., Kadomatsu, K., Muramatsu, T., & Toshimori, K. (2002) · Reproduction · doi:10.1530/rep.0.1230435 · Cited by 87 · see citing works
Cellular Organization of GlycosylationPreprint
Varki, A. P., Esko, J. D., & Colley, K. (2009) · doi:10.1101/glycobiology.3e.004 · Cited by 86 · see citing works
Dobrinski, I., Ignotz, G. G., Thomas, P., & Ball, B. A. (1996) · American Journal of Veterinary Research · doi:10.2460/ajvr.1996.57.11.1635 · Cited by 83 · see citing works
Sialidases on Mammalian Sperm Mediate Deciduous Sialylation during Capacitation
Ma, F., Wu, D. H., Deng, L., Secrest, P., Zhao, J., Varki, N. M., Lindheim, S. R., & Gagneux, P. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.380584 · Cited by 81 · see citing works
Self-citationTulsiani, D. R. P. (2006) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2005.12.025 · Cited by 81 · see citing works
Glycosylation of Rat Sperm Plasma Membrane during Epididymal Maturation1
Tulsiani, D. R. P., Skudlarek, M. D., Holland, M. K., & Orgebin‐Crist, M. (1993) · Biology of Reproduction · doi:10.1095/biolreprod48.2.417 · Cited by 81 · see citing works
Sexual selection by female immunity against paternal antigens can fix loss of function alleles
Ghaderi, D., Springer, S. A., Ma, F., Cohen, M., Secrest, P., Taylor, R. E., Varki, A., & Gagneux, P. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102302108 · Cited by 79 · see citing works
Self-citationTulsiani, D. R. P., Mc, O.-C., & Skudlarek, M. D. (1998) · PubMed · Cited by 79 · see citing works
Mucin gene expression in human male urogenital tract epithelia
Russo, C. L., Spurr-Michaud, S. J., Tisdale, A. S., Pudney, J. A., Anderson, D. J., & Gipson, I. K. (2006) · Human Reproduction · doi:10.1093/humrep/del164 · Cited by 77 · see citing works
Expression of Bisecting Type and Lewisx/Lewisy Terminated N-Glycans on Human Sperm
Pang, P., Tissot, B., Drobnis, E. Z., Šutovský, P., Morris, H. R., Clark, G. F., & Dell, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705134200 · Cited by 77 · see citing works
Glycan Evolution in Response to Collaboration, Conflict, and Constraint
Springer, S. A., & Gagneux, P. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.424523 · Cited by 76 · see citing works
Self-citationNakanishi, T., Isotani, A., Yamaguchi, R., Ikawa, M., Baba, T., Suárez, S. S., & Okabe, M. (2004) · Biology of Reproduction · doi:10.1095/biolreprod.104.028647 · Cited by 76 · see citing works
Heparan sulfate: a key regulator of embryonic stem cell fate
Kraushaar, D. C., Dalton, S., & Wang, L. (2013) · Biological Chemistry · doi:10.1515/hsz-2012-0353 · Cited by 75 · see citing works
Chiu, P. C. N., Chung, M., Koistinen, R., Koistinen, H. K., Seppälä, M. T., Ho, P., Ng, E. H. Y., Lee, C., & Yeung, W. S. B. (2006) · Journal of Cell Science · doi:10.1242/jcs.03258 · Cited by 74 · see citing works
Anatomic distribution of lectin-binding sites in mouse testis and epididymis
Lee, M.-C., & Damjanov, I. (1984) · Differentiation · doi:10.1111/j.1432-0436.1984.tb01410.x · Cited by 68 · see citing works
Cornwall, G. A. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-1-4939-0817-2_8 · Cited by 65 · see citing works
Chiu, P. C. N., Chung, M., Koistinen, R., Koistinen, H. K., Seppälä, M. T., Ho, P., Ng, E. H. Y., Lee, C., & Yeung, W. S. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607482200 · Cited by 64 · see citing works
Sperm-Coating Antigens Secreted by the Epididymis and Seminal Vesicle of the Rat1
Dravland, J. E., & Joshi, M. S. (1981) · Biology of Reproduction · doi:10.1095/biolreprod25.3.649 · Cited by 62 · see citing works
Simon, P., Bäumner, S., Busch, O., Röhrich, R. C., Kaese, M., Richterich, P., Wehrend, A., M⊘ller, K. B., Gerardy‐Schahn, R., Mühlenhoff, M., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.451112 · Cited by 61 · see citing works
Roles of glycodelin in modulating sperm function
Yeung, W. S. B., Lee, C., Koistinen, R., Koistinen, H. K., Seppälä, M. T., Ho, P. C., & Chiu, P. C. N. (2006) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2005.12.038 · Cited by 60 · see citing works
Female postmating immune responses, immune system evolution and immunogenic males
Morrow, E. H., & Innocenti, P. (2011) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/j.1469-185x.2011.00214.x · Cited by 54 · see citing works
Batista, F., Lu, L., Williams, S. A., & Stanley, P. (2012) · Biology of Reproduction · doi:10.1095/biolreprod.111.098103 · Cited by 51 · see citing works
Bi, J., Li, Y., Sun, F., Saalbach, A., Klein, C., Miller, D. J., Hess, R. A., & Nowak, R. A. (2013) · Developmental Biology · doi:10.1016/j.ydbio.2013.05.023 · Cited by 50 · see citing works
Toshimori, K., Araki, S., Öra, C., & Eddy, E. M. (1991) · Archives of Andrology · doi:10.3109/01485019108987656 · Cited by 48 · see citing works
A testis-specific regulator of complex and hybrid N-glycan synthesis
Huang, H.-H., & Stanley, P. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201004102 · Cited by 47 · see citing works
Sialyglycoconjugates release during in vitro capacitation of human spermatozoa.
Focarelli, R., Rosati, F., & Terrana, B. (1990) · PubMed · Cited by 46 · see citing works
Watanabe, H., Takeo, T., Tojo, H., Sakoh, K., Berger, T., Nakagata, N., Mak, T. W., & Kondoh, G. (2014) · Development · doi:10.1242/dev.105148 · Cited by 44 · see citing works
Tulsiani, D. R. P. (2003) · Microscopy Research and Technique · doi:10.1002/jemt.10313 · Cited by 41 · see citing works
Sequential activation of Notch family receptors during mouse spermatogenesis
Mori, S., Kadokawa, Y., Hoshinaga, K., & Marunouchi, T. (2003) · Development Growth & Differentiation · doi:10.1046/j.1440-169x.2003.00670.x · Cited by 40 · see citing works
Sialylglycoconjugates Release During In Vitro Capacitation of Human Spermatozoa
Focarelli, R., Rosati, F., & Terrana, B. (1990) · Journal of Andrology · doi:10.1002/j.1939-4640.1990.tb01587.x · Cited by 39 · see citing works
Langsdorf, A. E., Schumacher, V., Shi, X., Tran, T., Zaia, J., Jain, S. R., Taglienti, M. E., Kreidberg, J. A., Fine, A., & Ai, X. (2010) · Glycobiology · doi:10.1093/glycob/cwq133 · Cited by 37 · see citing works
Lectin histochemistry in the human epididymis
Arenas, M. I., Miguel, M. P. D., de Bethencourt, F. R., Fraile, B., Royuela, M., & Paniagua, R. (1996) · Reproduction · doi:10.1530/jrf.0.1060313 · Cited by 36 · see citing works
Skudlarek, M. D., Tulsiani, D. R. P., Nagdas, S. K., & Orgebin‐Crist, M. (1993) · Biology of Reproduction · doi:10.1095/biolreprod49.2.204 · Cited by 35 · see citing works
Equatorin is not essential for acrosome biogenesis but is required for the acrosome reaction
Hao, J., Chen, M., Ji, S., Wang, X., Wang, Y., Huang, X., Yang, L., Wang, Y., Cui, X., Lv, L., et al. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.01.080 · Cited by 34 · see citing works
Löhr, M. J., Kaltner, H., Schwartz‐Albiez, R., Sinowatz, F., & Gabius, H. (2010) · Anatomia Histologia Embryologia · doi:10.1111/j.1439-0264.2010.01019.x · Cited by 34 · see citing works
Kratz, E. M., Poland, D. C. W., van Dijk, W., & Kątnik‐Prastowska, I. (2003) · Clinica Chimica Acta · doi:10.1016/s0009-8981(03)00084-6 · Cited by 33 · see citing works
Presence and Regional Distribution of Sialyl Transferase in the Epididymis of the Rat1
Bernal, A., Torres, J., Reyes, A., & Rosado, A. (1980) · Biology of Reproduction · doi:10.1095/biolreprod23.2.290 · Cited by 32 · see citing works
Epitope analysis for human sperm-immobilizing monoclonal antibodies, MAb H6-3C4, 1G12 and campath-1
Hasegawa, A. (2003) · Molecular Human Reproduction · doi:10.1093/molehr/gag045 · Cited by 32 · see citing works
Bianchi, P. G., de Agostini, A. I., Fournier, J., Guidetti, C., Tarozzi, N., Bizzaro, D., & Manicardi, G. C. (2004) · Journal of Assisted Reproduction and Genetics · doi:10.1023/b:jarg.0000029492.54243.3c · Cited by 28 · see citing works
Histochemical changes in cervical mucus-secreting epithelium during the normal menstrual cycle
Gilks, C. B., Reid, P. E., Clement, P. B., & Owen, D. A. (1989) · Fertility and Sterility · doi:10.1016/s0015-0282(16)60492-2 · Cited by 26 · see citing works
MUC1 in normal and impaired spermatogenesis
Franke, F. E. (2001) · Molecular Human Reproduction · doi:10.1093/molehr/7.6.505 · Cited by 26 · see citing works
The sperm agglutination antigen-1 (SAGA-1) glycoforms of CD52 are O-glycosylated
Parry, S., Wong, N., Easton, R. L., Panico, M., Haslam, S. M., Morris, H. R., Anderson, P., Klotz, K. L., Herr, J. C., Diekman, A. B., et al. (2007) · Glycobiology · doi:10.1093/glycob/cwm076 · Cited by 25 · see citing works
Expression of basigin in reproductive tissues of estrogen receptor-α or -β null mice
Chen, L., Bi, J., Nakai, M., Bunick, D., Couse, J. F., Korach, K. S., & Nowak, R. A. (2010) · Reproduction · doi:10.1530/rep-10-0069 · Cited by 24 · see citing works
Glycodelin: a molecule with multi-functions on spermatozoa.
Yeung, W. S. B., Lee, C., Koistinen, R. A., Koistinen, H. K., Seppälä, M. T., Ho, P. C., & Chiu, P. C. N. (2007) · PubMed · Cited by 23 · see citing works
Functional aspects of CD52 in reproduction
Koyama, K., Hasegawa, A., & Komori, S. (2009) · Journal of Reproductive Immunology · doi:10.1016/j.jri.2009.06.263 · Cited by 22 · see citing works
Diekman, A. B., Norton, E. J., Klotz, K., Watkodk, V. A., & Herr, J. C. (1999) · Immunological Reviews · doi:10.1111/j.1600-065x.1999.tb01350.x · Cited by 21 · see citing works
Expression of Prnp mRNA (Prion Protein Gene) in Mouse Spermatogenic Cells
Fujisawa, M., Kanai, Y., Nam, S.-Y., Maeda, S., Nakamuta, N., Kanô, K., Kurohmaru, M., & Hayashi, Y. (2004) · Journal of Reproduction and Development · doi:10.1262/jrd.50.565 · Cited by 21 · see citing works
The role of N-glycans in spermatogenesis
Fukuda, M., & Akama, T. O. (2003) · Cytogenetic and Genome Research · doi:10.1159/000076817 · Cited by 20 · see citing works
Fukuda, M. N., & Akama, T. O. (2002) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(02)00407-5 · Cited by 20 · see citing works
Antigenic epitope for sperm-immobilizing antibody detected in infertile women
Hasegawa, A., & Koyama, K. (2005) · Journal of Reproductive Immunology · doi:10.1016/j.jri.2005.06.005 · Cited by 15 · see citing works
Surface heterogeneity of bovine sperm revealed by aqueous two-phase partition
Cartwright, E. J., Cowin, A. J., & Sharpe, P. T. (1991) · Bioscience Reports · doi:10.1007/bf01127502 · Cited by 13 · see citing works
Expression of Mucin Genes in the Human Testis and Its Relationship to Spermatogenesis
Seo, J. T., Lee, J. S., Jun, J. H., & Yang, M. H. (2005) · Yonsei Medical Journal · doi:10.3349/ymj.2005.46.5.667 · Cited by 8 · see citing works
Flickinger, C. J., Herr, J. C., McGee, R. S., Sigman, M., Evans, R. J., Sutherland, W. M., Summers, T. A., Spell, D. R., & Conklin, D. J. (2009) · Andrologia · doi:10.1111/j.1439-0272.1990.tb02080.x · Cited by 7 · see citing works
Lutfi, H., Hasegawa, A., & Komori, S. (2012) · Journal of Reproductive Immunology · doi:10.1016/j.jri.2012.01.002 · Cited by 7 · see citing works
Stage-specific mouse testis cell surface alterations detected by fluorescence-labeled lectins
LEMAIRE, L., & Heinlein, U. A. O. (1992) · Cell Biology International Reports · doi:10.1016/s0309-1651(06)80009-3 · Cited by 5 · see citing works
Dynamics of a human seminal vesicle specific protein.
Cj, F., Jc, H., Rs, M., Sigman, M., Rj, E., Wm, S., Ta, S., Spell, D. R., & Conklin, D. J. (1990) · PubMed · Cited by 5 · see citing works
Familiari, G., & Motta, P. M. (1980) · PubMed · Cited by 2 · see citing works
Flagged first, then by citations
1 of the 126 references couldn’t be matched to a known paper.
Research works printed but not linked: 2
- Stanley P, Schachter H, Taniguchi N. 2009 N‐ Glycans In: Varki A, Cummings RD, Esko JD, Freeze HH, Stanley P, Bertozzi CR, Hart GW, Etzler ME, editors. Essentials of glycobiology. 2nd edition Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 2009 Chapter 13, pp 175– 198.
- Suarez SS, Pacey AA. 2006b Sperm transport in the female reproductive tract. Hum Reprod Update 12: 23– 37. 16272225
Cited by
Sorted by citations
Varki, A. (2017) · Glycobiology · doi:10.1093/glycob/cww086 · Cited by 2,635 · see citing works
“Glycans also appear to be involved at many steps in the reproductive process, and in the processes of sperm migration to the site of fertilization (942).”
BackgroundMolecular changes and signaling events occurring in spermatozoa during epididymal maturation
Gervasi, M. G., & Visconti, P. E. (2017) · Andrology · doi:10.1111/andr.12320 · Cited by 301 · see citing works
The Female Response to Seminal Fluid
Schjenken, J. E., & Robertson, S. A. (2020) · Physiological Reviews · doi:10.1152/physrev.00013.2018 · Cited by 208 · see citing works
The Interaction of the Gut Microbiota with the Mucus Barrier in Health and Disease in Human
Corfield, A. P. (2018) · Microorganisms · doi:10.3390/microorganisms6030078 · Cited by 134 · see citing works
Mechanisms of Cadmium-Induced Testicular Injury: A Risk to Male Fertility
Ali, W., Ma, Y., Zhu, J., Zou, H., & Liu, Z. (2022) · Cells · doi:10.3390/cells11223601 · Cited by 127 · see citing works
Eukaryotic protein glycosylation: a primer for histochemists and cell biologists
Corfield, A. P. (2016) · Histochemistry and Cell Biology · doi:10.1007/s00418-016-1526-4 · Cited by 120 · see citing works
Rapid genome shrinkage in a self-fertile nematode reveals sperm competition proteins
Yin, D., Schwarz, E. M., Thomas, C. G., Felde, R. L., Korf, I. F., Cutter, A. D., Schartner, C., Ralston, E. J., Meyer, B. J., & Haag, E. S. (2018) · Science · doi:10.1126/science.aao0827 · Cited by 106 · see citing works
Absence of Neu5Gc and Presence of Anti-Neu5Gc Antibodies in Humans—An Evolutionary Perspective
Altman, M. O., & Gagneux, P. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00789 · Cited by 112 · see citing works
Self-citationAn atlas of cell types in the mouse epididymis and vas deferens
Rinaldi, V. D., Donnard, E. R., Gellatly, K. J., Rasmussen, M., Küçükural, A., Yukselen, O., Garber, M. G., Sharma, U., & Rando, O. J. (2020) · eLife · doi:10.7554/elife.55474 · Cited by 102 · see citing works
Chicken semen cryopreservation and use for the restoration of rare genetic resources
Thélie, A., Bailliard, A., Seigneurin, F., Zerjal, T., Tixier‐Boichard, M., & Blesbois, É. (2018) · Poultry Science · doi:10.3382/ps/pey360 · Cited by 97 · see citing works
Emerging roles of protein mannosylation in inflammation and infection
Loke, I., Kolarich, D., Packer, N. H., & Thaysen‐Andersen, M. (2016) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2016.04.004 · Cited by 99 · see citing works
Posttranslational Modifications in Spermatozoa and Effects on Male Fertility and Sperm Viability
Dad, R., & Huo, L. (2017) · OMICS A Journal of Integrative Biology · doi:10.1089/omi.2016.0173 · Cited by 95 · see citing works
Sublethal sperm freezing damage: Manifestations and solutions
Pini, T., Leahy, T., & GRAAF, S. P. D. (2018) · Theriogenology · doi:10.1016/j.theriogenology.2018.06.006 · Cited by 93 · see citing works
Sialic acid and biology of life: An introduction
Ghosh, S. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-816126-5.00001-9 · Cited by 88 · see citing works
Simulating nature in sperm selection for assisted reproduction
Leung, E. T. Y., Lee, C., Tian, X., Lam, K. K. W., Li, R., Ng, E. H. Y., Yeung, W. S. B., & Chiu, P. C. N. (2021) · Nature Reviews Urology · doi:10.1038/s41585-021-00530-9 · Cited by 75 · see citing works
Proteomic Investigation of Ram Spermatozoa and the Proteins Conferred by Seminal Plasma
Pini, T., Leahy, T., Soleilhavoup, C., Tsikis, G., Labas, V., Combes‐Soia, L., Harichaux, G., Rickard, J. P., Druart, X., & GRAAF, S. P. D. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00530 · Cited by 75 · see citing works
Notable Aspects of Glycan-Protein Interactions
Cohen, M. (2015) · Biomolecules · doi:10.3390/biom5032056 · Cited by 57 · see citing works
Tecle, E., Reynoso, H., Wang, R., & Gagneux, P. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.008729 · Cited by 53 · see citing works
Self-citationJiang, Y., Shi, W., Ma, D.-D., Zhang, J., Ying, G., Zhang, H., & Ong, C. N. (2019) · Environment International · doi:10.1016/j.envint.2019.04.059 · Cited by 49 · see citing works
Glycomics: revealing the dynamic ecology and evolution of sugar molecules
Springer, S. A., & Gagneux, P. (2015) · Journal of Proteomics · doi:10.1016/j.jprot.2015.11.022 · Cited by 48 · see citing works
Self-citationThe fate of spermatozoa in the female reproductive tract: A comparative review
Rickard, J. P., Pool, K., Druart, X., & de Graaf, S. P. (2019) · Theriogenology · doi:10.1016/j.theriogenology.2019.05.044 · Cited by 45 · see citing works
Ali, W., Deng, K., Bian, Y., Liu, Z., & Zou, H. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114889 · Cited by 46 · see citing works
Reyes-San-Martin, C., Hamoh, T., Zhang, Y., Berendse, L., Klijn, C., Li, R., Elías-Llumbet, A., Sigaeva, A., Kawałko, J., Mzyk, A., et al. (2022) · ACS Nano · doi:10.1021/acsnano.2c02511 · Cited by 44 · see citing works
Freezing–Thawing Procedures Remodel the Proteome of Ram Sperm before and after In Vitro Capacitation
Peris‐Frau, P., Martín‐Maestro, A., Iniesta‐Cuerda, M., Sánchez‐Ajofrín, I., Mateos‐Hernández, L., Garde, J. J., Villar, M., & Soler, A. J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20184596 · Cited by 43 · see citing works
Precision Glycoproteomics Reveals Distinctive N-Glycosylation in Human Spermatozoa
Xin, M., You, S., Xu, Y., Shi, W., Zhu, B., Shen, J., Wu, J., Li, C., Chen, Z., Su, Y., et al. (2022) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2022.100214 · Cited by 43 · see citing works
Batra, V., Dagar, K., Nayak, S., Kumaresan, A., Kumar, R., & Datta, T. K. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01928 · Cited by 41 · see citing works
The biological mechanisms regulating sperm selection by the ovine cervix
Fair, S., Meade, K. G., Reynaud, K., Druart, X., & de Graaf, S. P. (2019) · Reproduction · doi:10.1530/rep-18-0595 · Cited by 40 · see citing works
Biological Functions and Large-Scale Profiling of Protein Glycosylation in Human Semen
Lan, R., Xin, M., Hao, Z., You, S., Xu, Y., Wu, J., Dang, L., Zhang, X., & Sun, S. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00795 · Cited by 40 · see citing works
A brief review of polysialic acid-based drug delivery systems
Zhang, Q., Li, S., He, L., & Feng, C. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.123151 · Cited by 37 · see citing works
Advancing Semen Evaluation Using Lipidomics
Evans, H. C., Dinh, T. T., Hardcastle, M. L., Gilmore, A. A., Uğur, M. R., Hitit, M., Jousan, F. D., Nicodemus, M. C., & Memili, E. (2021) · Frontiers in Veterinary Science · doi:10.3389/fvets.2021.601794 · Cited by 36 · see citing works
Jeong, J.-Y., Cha, Y. K., Ahn, S. R., Shin, J., Choi, Y., Park, T. H., & Hong, S. (2022) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c17349 · Cited by 36 · see citing works
Signal peptide peptidase‐like 2c impairs vesicular transport and cleaves SNARE proteins
Papadopoulou, A. A., Müller, S. A., Mentrup, T., Shmueli, M. D., Niemeyer, J., Haug‐Kröper, M., von Blume, J., Mayerhofer, A., Feederle, R., Schröder, B., et al. (2019) · EMBO Reports · doi:10.15252/embr.201846451 · Cited by 35 · see citing works
Pini, T., Leahy, T., & de Graaf, S. P. (2018) · Reproduction, Fertility and Development · doi:10.1071/rd17251 · Cited by 31 · see citing works
Fernández-Fuertes, B., Blanco, A., Reid, C. J., Meade, K. G., Fair, S., & Lonergan, P. (2018) · Reproduction · doi:10.1530/rep-17-0429 · Cited by 32 · see citing works
Impact of glycosylation on the unimpaired functions of the sperm
Cheon, Y., & Kim, C. (2015) · Daehan saengsik uihak hoeji/Clinical and experimental reproductive medicine · doi:10.5653/cerm.2015.42.3.77 · Cited by 32 · see citing works
Influence of in vitro capacitation time on structural and functional human sperm parameters
Gómez‐Torres, M. J., Sáez‐Espinosa, P., Huerta‐Retamal, N., Robles‐Gómez, L., Avilés, M., Aizpurúa, J., Velasco, I., & Romero, A. (2019) · Asian Journal of Andrology · doi:10.4103/aja.aja_104_19 · Cited by 31 · see citing works
Liu, S., Fang, L., Zhou, Y., Santos, D. J. D. A., Xiang, R., Daetwyler, H. D., Chamberlain, A. J., Cole, J. B., Li, C., Yu, Y., et al. (2019) · BMC Genomics · doi:10.1186/s12864-019-6228-6 · Cited by 30 · see citing works
Kekäläinen, J., & Evans, J. P. (2016) · Evolution · doi:10.1111/evo.13141 · Cited by 29 · see citing works
New horizons in human sperm selection for assisted reproduction
Nixon, B., Schjenken, J. E., Burke, N. D., Skerrett-Byrne, D. A., Hart, H. M., Iuliis, G. N. D., Martin, J. H., Lord, T., & Bromfield, E. G. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1145533 · Cited by 28 · see citing works
Batra, V., Maheshwarappa, A., Dagar, K., Kumar, S., Soni, A., Kumaresan, A., Kumar, R., & Datta, T. K. (2019) · BMC Evolutionary Biology · doi:10.1186/s12862-019-1535-8 · Cited by 26 · see citing works
Toni, L. D., Cosci, I., Carosso, A. R., Barzon, L., Engl, B., Foresta, C., & Garolla, A. (2020) · Biology of Reproduction · doi:10.1093/biolre/ioaa173 · Cited by 25 · see citing works
A Mouse Model for Dietary Xenosialitis
Ma, F., Deng, L., Secrest, P., Shi, L. Z., Zhao, J., & Gagneux, P. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.739169 · Cited by 21 · see citing works
Self-citationSiglec expression on the surface of human, bull and ram sperm
Alkhodair, K. M., Almhanna, H., McGetrick, J., Gedair, S., Gallagher, M. E., Fernández-Fuertes, B., Tharmalingam, T., Larsen, P., Fitzpatrick, E., Lonergan, P., et al. (2018) · Reproduction · doi:10.1530/rep-17-0475 · Cited by 21 · see citing works
Richardson, L., Hanrahan, J. P., Tharmalingam, T., Carrington, S. D., Lonergan, P., Evans, A. C. O., & Fair, S. (2019) · Reproduction · doi:10.1530/rep-18-0547 · Cited by 21 · see citing works
Abril-Parreño, L., Wilkinson, H., Krogenæs, A., Morgan, J., Gallagher, M. E., Reid, C. J., Druart, X., Fair, S., & Saldova, R. (2021) · Glycobiology · doi:10.1093/glycob/cwab085 · Cited by 20 · see citing works
Hart, H. M., Nixon, B., Martin, J. H., Aitken, R. J., & Iuliis, G. N. D. (2025) · Human Reproduction Open · doi:10.1093/hropen/hoaf040 · Cited by 19 · see citing works
Sperm surface changes and their consequences for sperm transit through the female reproductive tract
Rickard, J. P., & de Graaf, S. P. (2020) · Theriogenology · doi:10.1016/j.theriogenology.2020.02.018 · Cited by 19 · see citing works
Diversity of sialic acids and sialoglycoproteins in gametes and at fertilization
Fliniaux, I., Marchand, G., Molinaro, C., Decloquement, M., Martoriati, A., Marin, M., Bodart, J., Harduin‐Lepers, A., & Cailliau, K. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.982931 · Cited by 19 · see citing works
The sperm-interacting proteome in the bovine isthmus and ampulla during the periovulatory period
Mahé, C., Lavigne, R., Com, E., Pineau, C., Zlotkowska, A. M., Tsikis, G., Mermillod, P., Schoen, J., & Saint‐Dizier, M. (2023) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-022-00811-2 · Cited by 19 · see citing works
Khosravi, F., Michel, V., Galuska, C. E., Bhushan, S., Christian, P., Schuppe, H.-C., Pilatz, A. M. E., Galuska, S. P., & Meinhardt, A. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.718072 · Cited by 19 · see citing works
Precision Structural Interpretation of Site-Specific N- Glycans in Seminal Plasma
Xin, M., Xu, Y., You, S., Li, C., Zhu, B., Shen, J., Chen, Z., Shi, W., Xue, X., Shi, J., et al. (2022) · Journal of Proteome Research · doi:10.1021/acs.jproteome.2c00046 · Cited by 18 · see citing works
Beta-defensins as marker for male fertility: a comprehensive review
Solanki, S. S., Kumar, V., Kashyap, P., Kumar, R., De, S., & Datta, T. K. (2022) · Biology of Reproduction · doi:10.1093/biolre/ioac197 · Cited by 18 · see citing works
Nature and Functions of Glands and Ducts in the Drosophila Reproductive Tract
Avila, F. W., Sanchez‐Lopez, J. A., McGlaughon, J., Sukirtha, R., Wolfner, M. F., & Heifetz, Y. (2016) · Springer eBooks · doi:10.1007/978-3-319-40740-1_11 · Cited by 18 · see citing works
Bornhöfft, K. F., Rebl, A., Gallagher, M. E., Viergutz, T., Zlatina, K., Reid, C. J., & Galuska, S. P. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02478 · Cited by 18 · see citing works
Luo, M., Su, T., Cheng, Q., Zhang, X. C., Cai, F., Yin, Z., Li, F., Yang, H., Liu, F., & Zhang, Y. (2023) · Journal of Proteome Research · doi:10.1021/acs.jproteome.3c00489 · Cited by 16 · see citing works
Bioproduction, purification, and application of polysialic acid
Wu, J., Zhan, X., Liu, L., & Xia, X. (2018) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-018-9336-3 · Cited by 16 · see citing works
Batra, V., Bhushan, V., Ali, S. A., Sarwalia, P., Pal, A., Karanwal, S., Solanki, S. S., Kumaresan, A., Kumar, R., & Datta, T. K. (2021) · BMC Genomics · doi:10.1186/s12864-021-07640-z · Cited by 16 · see citing works
Umezu, K., Hiradate, Y., NUMABE, T., Hara, K., & Tanemura, K. (2017) · Journal of Reproduction and Development · doi:10.1262/jrd.2017-065 · Cited by 16 · see citing works
Sialylation: fate decision of mammalian sperm development, fertilization, and male fertility
Yi, S., Feng, Y., Wang, Y., & Ma, F. (2023) · Biology of Reproduction · doi:10.1093/biolre/ioad067 · Cited by 15 · see citing works
Hanley, P. J. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1327769 · Cited by 15 · see citing works
Xin, A., Wu, Y., Lu, H., Cheng, L. T., Gu, Y., Diao, H., Chen, G., Wu, B., Li, Z., Tao, S., et al. (2018) · Clinical Proteomics · doi:10.1186/s12014-018-9195-z · Cited by 15 · see citing works
Advances in protein glycosylation and its role in tissue repair and regeneration
Yue, Z., Yu, Y., Gao, B., Wang, D., Sun, H., Feng, Y., Ma, Z., & Xie, X. (2023) · Glycoconjugate Journal · doi:10.1007/s10719-023-10117-8 · Cited by 16 · see citing works
Khezri, A., Narud, B., Stenseth, E., Zeremichael, T. T., Myromslien, F. D., Wilson, R. C., Ahmad, R., & Kommisrud, E. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.00922 · Cited by 14 · see citing works
Modifications in Biomacromolecules
Zhan, X., & Jabbari, A. (2022) · Biochemistry · doi:10.5772/intechopen.97318 · Cited by 13 · see citing works
Cheng, Q., Luo, M., Xu, Z., Li, F., & Zhang, Y. (2024) · iMetaOmics. · doi:10.1002/imo2.10 · Cited by 13 · see citing works
Moretti, E., Signorini, C., Noto, D., Tripodi, S. A., Menchiari, A., Sorrentino, E., & Collodel, G. (2022) · Journal of Inflammation Research · doi:10.2147/jir.s339515 · Cited by 12 · see citing works
Soluble protein fraction of human seminal plasma
Bianchi, L., Carnemolla, C., Viviani, V., Landi, C., Pavone, V., Luddi, A., Piomboni, P., & Bini, L. (2017) · Journal of Proteomics · doi:10.1016/j.jprot.2017.12.015 · Cited by 12 · see citing works
Boroujeni, P. B., Ebrahimian, S., Abedini, M., Chayjan, M. R., Hassani, M., Gourabi, H., Gilani, M. A. S., Sabbaghian, M., & Meybodi, A. M. (2019) · Reproductive BioMedicine Online · doi:10.1016/j.rbmo.2019.05.012 · Cited by 12 · see citing works
Shum, W. W., Zhang, B. L., Cao, A. S., Zhou, X., Shi, S. M., Zhang, Z. Y., Gu, L. Y., & Shi, S. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.827940 · Cited by 12 · see citing works
Orsolini, M. F., Verstraete, M., van Heule, M., Orellana-Guerrero, D., Ortega, A., Meyers, S. A., & Dini, P. (2022) · Theriogenology · doi:10.1016/j.theriogenology.2022.08.014 · Cited by 11 · see citing works
Molecular insights to the sperm–cervix interaction and the consequences for cryopreserved sperm
Warr, S., Pini, T., GRAAF, S. P. D., & Rickard, J. P. (2022) · Biology of Reproduction · doi:10.1093/biolre/ioac188 · Cited by 11 · see citing works
Rateb, S. A., Monaco, D., El-Bahrawy, K. A., Khalifa, M. A., El-Hamid, I. S. A., Kamel, A. M., Accogli, G., Lacalandra, G. M., & Desantis, S. (2019) · Animal Reproduction Science · doi:10.1016/j.anireprosci.2019.106121 · Cited by 11 · see citing works
Kashyap, P., Solanki, S. S., Datta, T. K., & Kumar, R. (2023) · Theriogenology · doi:10.1016/j.theriogenology.2023.05.005 · Cited by 10 · see citing works
Li, Y., Fu, B., Li, Y., Li, C., Zhai, Y., Feng, X., Wang, J., Zhang, Y., & Lu, H. (2024) · Analytical Chemistry · doi:10.1021/acs.analchem.4c01300 · Cited by 10 · see citing works
Nygaard, M. B., Herlihy, A. S., Jeanneau, C., Nielsen, J. E., Bennett, E., Jørgensen, N., Clausen, H., Mandel, U., Meyts, E. R., & Almstrup, K. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19102949 · Cited by 10 · see citing works
A comprehensive N-glycome map of porcine sperm membrane before and after capacitation
Li, Y., Zhai, Y., Fu, B., He, Y., Feng, Y., Ma, F., & Lu, H. (2024) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2024.122084 · Cited by 9 · see citing works
Jankovičová, J., Michalková, K., Sečová, P., Horovská, Ľ., & Antalíková, J. (2024) · Scientific Reports · doi:10.1038/s41598-024-81021-w · Cited by 9 · see citing works
Male reproductive tract extracellular vesicles display region-specific heterogeneity in mice
Batra, V., Morgan, H. L., Choi, K. K., Onion, D., Croxall, N. J., Arkill, K. P., Hallwood, J. H., James, V. H., & Watkins, A. J. (2025) · Reproduction · doi:10.1530/rep-25-0009 · Cited by 9 · see citing works
Hernández-Rodríguez, J., Arenas‐Ríos, E., Jiménez‐Morales, I., Barberena, E. C., Montes, S., Vigueras‐Villaseñor, R. M., & Arteaga‐Silva, M. (2021) · Reproduction Fertility and Development · doi:10.1071/rd20167 · Cited by 9 · see citing works
Specific lectin binding sites during in vitro capacitation and acrosome reaction in boar spermatozoa
Robles‐Gómez, L., González‐Brusi, L., Sáez‐Espinosa, P., Huerta‐Retamal, N., Cots, P., Avilés, M., & Gómez‐Torres, M. J. (2021) · Italian Journal of Animal Science · doi:10.1080/1828051x.2021.1886611 · Cited by 9 · see citing works
Li, R., Qu, J., Yan, K., Chen, Y., Zhao, X., Liu, Z., Xie, M., Zhang, Q., He, Y., Niu, J., et al. (2024) · Development · doi:10.1242/dev.202224 · Cited by 9 · see citing works
Silyukova, Y. (2020) · Sel skokhozyaistvennaya Biologiya · doi:10.15389/agrobiology.2020.6.1148eng · Cited by 9 · see citing works
Differential surface glycoprofile of buffalo bull spermatozoa during mating and non-mating periods
Accogli, G., Lacalandra, G. M., Aiudi, G. G., Cox, S. N., & Desantis, S. (2017) · animal · doi:10.1017/s1751731117000453 · Cited by 9 · see citing works
The correlation between human seminal plasma sialoproteins and ejaculate parameters
Páleníková, V., Pavlova, H., Kraus, D., Krátká, Z., Komrsková, K., & Manaskova-Postlerova, P. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.131341 · Cited by 8 · see citing works
Dohadwala, S., Shah, P., Farrell, M. K., Politch, J. A., Marathe, J. G., Costello, C. E., & Anderson, D. J. (2025) · Glycobiology · doi:10.1093/glycob/cwaf067 · Cited by 8 · see citing works
Marić, T., Bojanac, A. K., Matijević, A., Ceppi, M., Bruzzone, M., Evgeni, E., Pribić, T., Wójcik, I., Trbojević‐Akmačić, I., Lauc, G., et al. (2021) · Life · doi:10.3390/life11090989 · Cited by 8 · see citing works
Carpenter, E. J., Peng, C., Haregu, S., Twells, N., Woudstra, L., Sood, A., Cartmell, J., Woods, R. J., Mahal, L. K., Wang, S.-K., et al. (2025) · Science Advances · doi:10.1126/sciadv.adx6373 · Cited by 10 · see citing works
Complexity and modification of the bull sperm glycocalyx during epididymal maturation
Sečová, P., Hackerová, L., Horovská, Ľ., Michalková, K., Jankovičová, J., Manaskova-Postlerova, P., & Antalíková, J. (2024) · The FASEB Journal · doi:10.1096/fj.202400551rr · Cited by 7 · see citing works
Seminal plasma Alters surface Glycoprofile of dromedary camel cryopreserved epididymal spermatozoa
Desantis, S., Lacalandra, G. M., Batista, M., Amann, O. V., Antonelli, D., & Monaco, D. (2021) · Theriogenology · doi:10.1016/j.theriogenology.2021.03.008 · Cited by 7 · see citing works
Wang, N., Yang, M., He, D., Li, X., Zhang, X., Han, B., Liu, C., Hai, C., Li, G., & Zhao, Y. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.07.106 · Cited by 7 · see citing works
Cruz-Rivera, M. Y., Torres, J., Carrillo‐Farga, J., Wilkins, P. P., Flisser, A., & Mendlovic, F. (2019) · Journal of Parasitology · doi:10.1645/17-190 · Cited by 7 · see citing works
Gómez‐Torres, M. J., Robles‐Gómez, L., Huerta‐Retamal, N., Sáez‐Espinosa, P., Avilés, M., Aizpurúa, J., & Romero, A. (2020) · Microscopy and Microanalysis · doi:10.1017/s1431927620024630 · Cited by 7 · see citing works
Seminal Plasma Plays Important Roles in Fertility
Suárez, S. S., & Wolfner, M. F. (2017) · Cambridge University Press eBooks · doi:10.1017/9781316411124.008 · Cited by 7 · see citing works
An atlas of cell types in the mammalian epididymis and vas deferensPreprint
Rinaldi, V. D., Donnard, E., Gellatly, K. J., Rasmussen, M., Küçükural, A., Yukselen, O., Garber, M. G., Sharma, U., & Rando, O. J. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.01.24.918979 · Cited by 7 · see citing works
Cinque, S., Verheyden, Y., Adnane, S., Marino, A., Hanache, S., Vendramin, R., Cuomo, A., Poźniak, J., Calabuig, Á. C., Baldewijns, M. M. L. L., et al. (2025) · The Journal of Experimental Medicine · doi:10.1084/jem.20251507 · Cited by 6 · see citing works
Siglecs family used by pathogens for immune escape may engaged in immune tolerance in pregnancy
Chen, Y., Chen, H., & Zheng, Q. (2023) · Journal of Reproductive Immunology · doi:10.1016/j.jri.2023.104127 · Cited by 6 · see citing works
Sáez‐Espinosa, P., Boix, S. T., Huerta‐Retamal, N., Avilés, M., Aizpurúa, J., Romero, A., & Gómez‐Torres, M. J. (2017) · Revista Internacional de Andrología · doi:10.1016/j.androl.2017.03.002 · Cited by 6 · see citing works
Spatial Organization of the Sperm Cell Glycoproteome
Ji, R., Chiozzi, R. Z., van den Toorn, H., Leung, M. R., Zeev‐Ben‐Mordehai, T., Burke, N. D., Bromfield, E. G., Reiding, K. R., & Heck, A. J. R. (2024) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2024.100893 · Cited by 5 · see citing works
Global characterization of mouse testis O-glycoproteome landscape during spermatogenesis
Liu, Q., Lu, X., Deng, Y., Zhang, H., Wei, R., Li, H., Feng, Y., Wei, J., Ma, F., Zhang, Y., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-57980-7 · Cited by 5 · see citing works
de Jesús, S. M., Vigueras‐Villaseñor, R. M., Barberena, E. C., Hernández-Rodríguez, J., Pérez-Aguirre, S. G., Montes, S., Carrizales, L., Arrieta‐Cruz, I., & Arteaga‐Silva, M. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26104589 · Cited by 5 · see citing works
- Authors
- Tecle, E., & Gagneux, P.
- Affiliations
- University of California San Diego (US)
- Corresponding author
- Gagneux, Pascal
- Venue
- Molecular Reproduction and Development
- Publisher
- Wiley
- Published
- 2015-06-09
- Volume
- 82
- Issue
- 9
- Pages
- 635-650
- ISSN
- 1040-452X (ISSN-L)
- 1098-2795
- PMC
- PMC4744710
- OpenAlex
- W1796017043
- Cited by
- 190
- References
- 126
- Citations by year
- 2026: 17 · 2025: 22 · 2024: 19 · 2023: 17 · 2022: 22 · 2021: 27 · 2020: 17 · 2019: 16 · 2018: 10 · 2017: 10 · 2016: 9 · 2015: 4
- FWCI
- 1.67
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Molecular Reproduction and Development (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion, cc-by-nc-nd)
- Funders
- NIHGMS Grant (#1065732)
- UCSD (Core A P01HL107150)
- Topics
- Health Sciences › Medicine › Reproductive Medicine › Sperm and Testicular Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Reproductive Biology and Fertility
- Keywords
- sperm capacitation, epididymal maturation, seminal plasma, female reproductive tract, sperm survival, cervical mucus, sperm reservoir, glycolipids, microvesicles, sperm plasma membrane, fertility, spermatogenesis
- MeSH terms
- Animals, Female, Humans, Male, Spermatozoa, Glycocalyx, Mice
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