Proteomic analysis of high and low-motility frozen-thawed spermatozoa in yak provides important insights into the molecular mechanisms underlying sperm cryodamage.

[1]  Mingming Wang,et al.  Microbiome–Metabolome Reveals the Contribution of the Gut–Testis Axis to Sperm Motility in Sheep (Ovis aries) , 2023, Animals : an open access journal from MDPI.

[2]  X. Xiong,et al.  TMT-based quantitative proteomics analysis reveals the differential proteins between fresh and frozen-thawed sperm of yak (Bos grunniens). , 2023, Theriogenology.

[3]  Mingming Wang,et al.  Changes on proteomic and metabolomic profiling of cryopreserved sperm effected by melatonin. , 2022, Journal of Proteomics.

[4]  P. Bao,et al.  Identification and Validation of Yak (Bos grunniens) Frozen-Thawed Sperm Proteins Associated with Capacitation and the Acrosome Reaction. , 2022, Journal of proteome research.

[5]  P. Bao,et al.  Quantitative phosphoproteomics analyses reveal the regulatory mechanisms related to frozen-thawed sperm capacitation and acrosome reaction in yak (Bos grunniens) , 2022, Frontiers in Physiology.

[6]  Jie Yu,et al.  Proteomic analysis of donkey sperm reveals changes in acrosome enzymes and redox regulation during cryopreservation. , 2022, Journal of proteomics.

[7]  G. Rusco,et al.  Proteomic analysis of rabbit fresh and cryopreserved semen provides an important insight into molecular mechanisms of cryoinjuries to spermatozoa. , 2022, Theriogenology.

[8]  G. Quan,et al.  Identification and validation of ram sperm proteins associated with cryoinjuries caused by the cryopreservation process. , 2022, Theriogenology.

[9]  M. Chu,et al.  Heparin-induced and caffeine or ouabain supplemented capacitation of frozen-thawed yak (Bos grunniens) spermatozoa. , 2022, Reproduction in domestic animals = Zuchthygiene.

[10]  M. Yeste,et al.  Aldose Reductase B1 in Pig Seminal Plasma: Identification, Localization in Reproductive Tissues, and Relationship With Quality and Sperm Preservation , 2021, Frontiers in Cell and Developmental Biology.

[11]  M. C. Gil,et al.  In Stallion Spermatozoa, Superoxide Dismutase (Cu–Zn) (SOD1) and the Aldo-Keto-Reductase Family 1 Member b (AKR1B1) Are the Proteins Most Significantly Reduced by Cryopreservation , 2021, Journal of proteome research.

[12]  M. C. Gil,et al.  Proteomic profiling of stallion spermatozoa suggests changes in sperm metabolism and compromised redox regulation after cryopreservation. , 2020, Journal of proteomics.

[13]  A. J. Soler,et al.  Sperm Cryodamage in Ruminants: Understanding the Molecular Changes Induced by the Cryopreservation Process to Optimize Sperm Quality , 2020, International journal of molecular sciences.

[14]  X. Kong,et al.  Exendin‐4, a GLP‐1 receptor agonist regulates retinal capillary tone and restores microvascular patency after ischaemia–reperfusion injury , 2020, British journal of pharmacology.

[15]  M. J. Bragado,et al.  Molecular Mechanisms Involved in the Impairment of Boar Sperm Motility by Peroxynitrite-Induced Nitrosative Stress , 2020, International journal of molecular sciences.

[16]  Qunli Yu,et al.  Phosphoproteomic analysis of longissimus lumborum of different altitude yaks. , 2019, Meat science.

[17]  M. Alves,et al.  Antioxidants and Male Fertility: From Molecular Studies to Clinical Evidence , 2019, Antioxidants.

[18]  H. Rodríguez-Martínez,et al.  Transcriptome analysis reveals that fertilization with cryopreserved sperm downregulates genes relevant for early embryo development in the horse , 2019, bioRxiv.

[19]  A. Agarwal,et al.  Sperm cryopreservation: A review on current molecular cryobiology and advanced approaches. , 2018, Reproductive biomedicine online.

[20]  B. Pukazhenthi,et al.  Pretreatment with cholesterol-loaded cyclodextrins prevents loss of motility associated proteins during cryopreservation of addra gazelle (Nanger dama ruficollis) spermatozoa. , 2018, Cryobiology.

[21]  G. Borgstahl,et al.  A Review of the Catalytic Mechanism of Human Manganese Superoxide Dismutase , 2018, Antioxidants.

[22]  Robert Sullivan,et al.  Proteomic Markers of Functional Sperm Population in Bovines: Comparison of Low- and High-Density Spermatozoa Following Cryopreservation. , 2018, Journal of proteome research.

[23]  R. Aitken.  Reactive oxygen species as mediators of sperm capacitation and pathological damage , 2017, Molecular reproduction and development.

[24]  A. Moura,et al.  Sperm membrane proteins associated with the boar semen cryopreservation. , 2017, Animal reproduction science.

[25]  F. Treulén,et al.  Nitrosative stress by peroxynitrite impairs ATP production in human spermatozoa , 2017, Andrologia.

[26]  A. Ciereszko,et al.  Analysis of bull (Bos taurus) seminal vesicle fluid proteome in relation to seminal plasma proteome. , 2017, Journal of dairy science.

[27]  A. Talebi,et al.  Etiologies of sperm oxidative stress , 2016, International journal of reproductive biomedicine.

[28]  T. Inui,et al.  Active site cysteine-null glyceraldehyde-3-phosphate dehydrogenase (GAPDH) rescues nitric oxide-induced cell death. , 2016, Nitric oxide : biology and chemistry.

[29]  Wan-Xi Yang,et al.  Myosin superfamily: The multi-functional and irreplaceable factors in spermatogenesis and testicular tumors. , 2016, Gene.

[30]  A. R. Baloch,et al.  Epidermal growth factor enhances the developmental competence of yak (Bos grunniens) preimplantation embryos by modulating the expression of survivin and HSP70 , 2015 .

[31]  A. Ciereszko,et al.  Impact of cryopreservation on bull () semen proteome. , 2015, Journal of animal science.

[32]  V. Labas,et al.  The identification of proteomic markers of sperm freezing resilience in ram seminal plasma. , 2015, Journal of proteomics.

[33]  M. Yeste.  Recent Advances in Boar Sperm Cryopreservation: State of the Art and Current Perspectives. , 2015, Reproduction in domestic animals = Zuchthygiene.

[34]  L. Samanta,et al.  Sperm Proteome , 2015, Reproductive Sciences.

[35]  R. Aitken,et al.  Investigation of the stallion sperm proteome by mass spectrometry. , 2015, Reproduction.

[36]  F. Treulén,et al.  Peroxynitrite-mediated nitrosative stress decreases motility and mitochondrial membrane potential in human spermatozoa. , 2015, Molecular human reproduction.

[37]  K. Takebayashi,et al.  Porcine sperm capacitation involves tyrosine phosphorylation and activation of aldose reductase. , 2014, Reproduction.

[38]  C. Yin,et al.  Proteomic characteristics of human sperm cryopreservation , 2014, Proteomics.

[39]  E. de Mercado,et al.  Effect of the holding time at 15 °C prior to cryopreservation, the thawing rate and the post-thaw incubation temperature on the boar sperm quality after cryopreservation. , 2014, Animal reproduction science.

[40]  He-Ping chen,et al.  Stable overexpression of DJ‐1 protects H9c2 cells against oxidative stress under a hypoxia condition , 2013, Cell biochemistry and function.

[41]  J. Ramalho-Santos,et al.  Human Sperm Tail Proteome Suggests New Endogenous Metabolic Pathways* , 2012, Molecular & Cellular Proteomics.

[42]  F. Vialard,et al.  Cryopreservation of human spermatozoa decreases the number of motile normal spermatozoa, induces nuclear vacuolization and chromatin decondensation. , 2012, Journal of andrology.

[43]  R. Gajbhiye,et al.  Sperm phosphoproteome profiling by ultra performance liquid chromatography followed by data independent analysis (LC-MS(E)) reveals altered proteomic signatures in asthenozoospermia. , 2012, Journal of proteomics.

[44]  M. Vadnais,et al.  Characterization of capacitation, cryoinjury, and the role of seminal plasma in porcine sperm. , 2011, Theriogenology.

[45]  X. Pu,et al.  Down-regulation of DJ-1 protein in the ejaculated spermatozoa from Chinese asthenozoospermia patients. , 2011, Fertility and sterility.

[46]  H. Rodríguez-Martínez,et al.  Advances in Boar Semen Cryopreservation , 2010, Veterinary medicine international.

[47]  J. Bailey,et al.  Cryopreservation affects bovine sperm intracellular parameters associated with capacitation and acrosome exocytosis. , 2009, Reproduction, fertility, and development.

[48]  Jia-yin Liu,et al.  Role of translation by mitochondrial‐type ribosomes during sperm capacitation: An analysis based on a proteomic approach , 2009, Proteomics.

[49]  J. A. Sánchez,et al.  Cryobanking as tool for conservation of biodiversity: effect of brown trout sperm cryopreservation on the male genetic potential. , 2009, Theriogenology.

[50]  S. de Mateo,et al.  Sperm cell proteomics , 2009, Proteomics.

[51]  S. Karahuseyinoglu,et al.  Effects of cryopreservation on sperm parameters and ultrastructural morphology of human spermatozoa , 2008, Journal of Assisted Reproduction and Genetics.

[52]  R. Aitken,et al.  The role of proteomics in understanding sperm cell biology. , 2008, International journal of andrology.

[53]  Avijit Chakrabartty,et al.  Structure, folding, and misfolding of Cu,Zn superoxide dismutase in amyotrophic lateral sclerosis. , 2006, Biochimica et biophysica acta.

[54]  B. S. Prakash,et al.  Circadian variations in plasma concentrations of melatonin and prolactin during breeding and non-breeding seasons in yak (Poephagus grunniens L.). , 2005, Animal reproduction science.

[55]  Pablo Tamayo,et al.  Gene set enrichment analysis: A knowledge-based approach for interpreting genome-wide expression profiles , 2005, Proceedings of the National Academy of Sciences of the United States of America.

[56]  E. Mocé,et al.  Fertility evaluation of frozen/thawed semen. , 2005, Theriogenology.

[57]  H. Ariga,et al.  Immunocytochemical localization of DJ‐1 in human male reproductive tissue , 2003, Molecular reproduction and development.

[58]  P. Shannon,et al.  Cytoscape: A Software Environment for Integrated Models of Biomolecular Interaction Networks , 2003 .

[59]  L. Tres,et al.  Acroplaxome, an F-actin-keratin-containing plate, anchors the acrosome to the nucleus during shaping of the spermatid head. , 2003, Molecular biology of the cell.

[60]  K. Weitze,et al.  Storage of boar semen. , 2000, Animal reproduction science.

[61]  Sirshendu Chatterjee,et al.  Levels of antioxidant defenses are decreased in bovine spermatozoa after a cycle of freezing and thawing , 2000, Molecular reproduction and development.

[62]  F. Lahnsteiner.  Semen cryopreservation in the Salmonidae and in the northern pike. , 2000 .

[63]  J. Bailey,et al.  Semen cryopreservation in domestic animals: a damaging and capacitating phenomenon. , 2000, Journal of andrology.

[64]  E. Baldi,et al.  Extracellular calcium negatively modulates tyrosine phosphorylation and tyrosine kinase activity during capacitation of human spermatozoa. , 1996, Biology of reproduction.

[65]  M. Yeste.  Sperm cryopreservation update: Cryodamage, markers, and factors affecting the sperm freezability in pigs. , 2016, Theriogenology.

[66]  Elizabeth Noonan,et al.  World Health Organization reference values for human semen characteristics. , 2010, Human reproduction update.

[67]  E. Mocé,et al.  Rabbit sperm cryopreservation: a review. , 2009, Animal reproduction science.

[68]  C. O’Flaherty,et al.  Sperm activation: role of reactive oxygen species and kinases. , 2008, Biochimica et biophysica acta.

[69]  I. Fridovich,et al.  Superoxide radical and superoxide dismutases. , 1995, Annual review of biochemistry.