{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T14:36:20Z","timestamp":1779374180553,"version":"3.53.1"},"reference-count":97,"publisher":"SAGE Publications","issue":"5","license":[{"start":{"date-parts":[[2017,5,1]],"date-time":"2017-05-01T00:00:00Z","timestamp":1493596800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.sagepub.com\/page\/policies\/text-and-data-mining-license"}],"content-domain":{"domain":["journals.sagepub.com"],"crossmark-restriction":true},"short-container-title":["OMICS: A Journal of Integrative Biology"],"published-print":{"date-parts":[[2017,5]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Spermatogenesis is a complex and highly regulated process. The ability of spermatozoa to perform its function depends on multiple physiological and genetic factors that are not fully understood. Notably, due to lack of transcriptional and translational activity in spermatozoa, posttranslational modifications (PTMs) play key roles in determining their viability. PTMs not only confer structural changes in the proteome of the spermatozoa cells, but also increase the diversity of the proteome and introduce specific modifications that could be translated into functional changes in the affected spermatozoa. Multiple PTMs of active proteins have been identified in the developing spermatogonia. This review summarizes a diverse range of PTMs taking place in the developing spermatozoa, and analyzes their effects on male fertility and sperm viability. In particular, we discuss how SUMOylation, ubiquitination, phosphorylation, acetylation, glycosylation, and disulphide bond formation in proteins play a role in spermatogenesis, sperm maturation, movement of maturing spermatozoa to epididymis, capacitation, hyperactivation, spermatozoa motility, subversion of immune detection by spermatozoa, sperm to egg recognition and fusion, and the fertilization process. When possible, the specific proteins involved in these processes are highlighted. We point to existing knowledge gaps in the field of proteomics, and provide suggestions for future research on sperm viability and male fertility. We discuss briefly, as an example, the observations in water buffalo,\n                    <jats:italic toggle=\"yes\">Bubalus bubalis<\/jats:italic>\n                    , which provides both meat and milk, and therefore is a reliable source for energy and protein needs of human populations. In conclusions, understanding the ways in which PTMs impact mammalian fertility and reproduction is important to make significant strides for diagnostic and therapeutic strategies in the near future.\n                  <\/jats:p>","DOI":"10.1089\/omi.2016.0173","type":"journal-article","created":{"date-parts":[[2017,5,8]],"date-time":"2017-05-08T15:43:21Z","timestamp":1494258201000},"page":"245-256","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":74,"title":["Posttranslational Modifications in Spermatozoa and Effects on Male Fertility and Sperm Viability"],"prefix":"10.1177","volume":"21","author":[{"given":"Rahim Dad","family":"Brohi","sequence":"first","affiliation":[{"name":"Huazhong Agricultural University","place":["People's Republic of China"]},{"name":"Department of Hubei Province Engineering Research Center in Buffalo Breeding and Products","place":["People's Republic of China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Li-Jun","family":"Huo","sequence":"additional","affiliation":[{"name":"Huazhong Agricultural University","place":["People's Republic of China"]},{"name":"Department of Hubei Province Engineering Research Center in Buffalo Breeding and Products","place":["People's Republic of China"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"179","published-online":{"date-parts":[[2017,5]]},"reference":[{"key":"e_1_3_3_2_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2605.2005.00630.x"},{"key":"e_1_3_3_3_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M111.251579"},{"key":"e_1_3_3_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbamcr.2004.10.003"},{"key":"e_1_3_3_5_1","doi-asserted-by":"publisher","DOI":"10.1530\/rep.0.1260183"},{"key":"e_1_3_3_6_1","doi-asserted-by":"publisher","DOI":"10.1007\/s00441-015-2249-x"},{"key":"e_1_3_3_7_1","doi-asserted-by":"publisher","DOI":"10.1242\/jcs.03055"},{"key":"e_1_3_3_8_1","doi-asserted-by":"publisher","DOI":"10.1021\/pr300468m"},{"key":"e_1_3_3_9_1","doi-asserted-by":"publisher","DOI":"10.1021\/pr900513d"},{"key":"e_1_3_3_10_1","doi-asserted-by":"publisher","DOI":"10.1021\/pr1007224"},{"key":"e_1_3_3_11_1","first-page":"1","article-title":"Analysis of protein thiol changes occurring during rat sperm epididymal maturation","volume":"11","author":"Baker MA","year":"2014","unstructured":"Baker MA, , Weinberg A, , Hethertington L, , Villaverde AIS, , and Velkov T. 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