Sort   by:  
 Page size 
ProteomicsProteomic changes in human sperm during sequential in vitro capacitation and acrosome reaction.
The male gamete is not completely mature after ejaculation and requires further events in the female genital tract to acquire fertilizing ability, including the processes of capacitation and acrosome reaction. In order to shed light on dynamic protein changes experienced by the sperm cell in prepara...
ORGANISM(S): Homo sapiens (Human) 
2019-12-17 | PXD014871 | Pride
Acrosome reaction Proteomics Mass spectrometry Tmt labeling Sperm Capacitation Spermatozoa 
ProteomicsThe Roles of PFOA and PFOS on Human Sperm Capacitation
PFOS and PFOA are persistent organic pollutants known to impair human reproduction, but their effects and molecular mechanisms on human sperm remain unclear. Here, we conducted comprehensive proteomic and phosphoproteomic profiling of human sperm exposed to PFOS and PFOA during capacitation to provi...
ORGANISM(S): Homo Sapiens 
PXD068914 |
ProteomicsIdentification and validation of yak (Bos grunniens) frozen-thawed sperm proteins associated with the capacitation and acrosome reaction
We used a comprehensive quantitative proteomic profiling based on LC-MS/MS combined with TMT labeling strategy to analyze frozen-thawed Ashidan yak spermatozoa proteomic dynamic changes under three sequential conditions: density gradient centrifugation-based purification（FTH sperm）, incubation in ca...
ORGANISM(S): Bos mutus grunniens (Wild yak) (Bos grunniens) 
2023-03-11 | PXD035038 | Pride
Yak sperm capacitation acrosome reaction proteomic 
ProteomicsEffect of capacitation on proteomic profile and mitochondrial parameters of spermatozoa in bulls
Sperm capacitation is a critical process for fertilization. This process involves several biochemical and physiological changes that have been extensively studied, but little is known about the changes that occur in the sperm’s proteomic profile. This work aims to analyze the effect in vitro capacit...
ORGANISM(S): Bos taurus (Bovine) 
2025-05-07 | PXD056424 | Pride
Bovine Spermatozoa Mitochondria Proteome 
ProteomicsSialylation of Asparagine 612 inhibits Aconitase activity during mouse sperm capacitation; A possible mechanism for the switch from oxidative phosphorylation to glycolysis.
Sialylation of Asparagine 612 inhibits Aconitase activity during mouse sperm capacitation; A possible mechanism for the switch from oxidative phosphorylation to glycolysis.
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
2020-07-21 | MSV000085806 | MassIVE
GenomicsEpigenetic dynamics during capacitation of naïve human pluripotent stem cells [PBAT]
Epigenetic dynamics during capacitation of naïve human pluripotent stem cells [PBAT]
PRJNA904047 | ENA
GenomicsGIV/Girdin Regulates Spatiotemporal Signaling during Sperm Capacitation and is Required for Male Fertility
GIV/Girdin Regulates Spatiotemporal Signaling during Sperm Capacitation and is Required for Male Fertility
PRJNA720623 | ENA
ProteomicsQuantitative Phosphoproteomics Analyses Reveal the Regulatiory Mechanisms Related to Frozen-thawed Sperm Capacitation and Acrosome Reaction in Yak (Bos grunniens)
Mammalian spermatozoa are not utterly mature after ejaculation and must undergo additional functional and structural changes within female reproductive tracts to achieve subsequent fertilization, including both capacitation and acrosome reaction (AR), which are dominated by post-translational modifi...
ORGANISM(S): Bos mutus grunniens (Wild yak) (Bos grunniens) 
2022-09-26 | PXD035751 | Pride
Yak sperm phosphoproteomics tmt lc-ms/ms 
ProteomicsCrocodile Sperm Proteome
In a reproductive strategy that is considered unique to the mammalian lineage, spermatozoa must undergo a series of physiological changes, termed capacitation, in the female reproductive tract prior to developing their capacity to fertilize an ovum. Here, we have employed a comparative proteomic str...
ORGANISM(S): Crocodylus Porosus (ncbitaxon:8502) 
2018-04-08 | MSV000082258 | MassIVE
UnknownChloride Is essential for capacitation and for the capacitation-associated increase in tyrosine phosphorylation.
Not available
S-EPMC2602906 | biostudies-literature
Sort   by:  
 Page size