https://ogma.newcastle.edu.au/vital/access/ /manager/Index ${session.getAttribute("locale")} 5 Evidence for the involvement of PECAM-1 in a receptor mediated signal-transduction pathway regulating capacitation-associated tyrosine phosphorylation in human spermatozoa https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:1527 Wed 11 Apr 2018 16:54:55 AEST ]]> Degradation of APCcdc²⁰ and APCcdh¹ substrates during the second meiotic division in mouse eggs https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:6544 Wed 11 Apr 2018 16:31:09 AEST ]]> Chemotaxis towards hyaluronan is dependent on CD44 expression and modulated by cell type variation in CD44-hyaluronan binding https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:1383 Wed 11 Apr 2018 15:51:49 AEST ]]> Cell cycle-dependent repetitive Ca²⁺ waves induced by a cytosolic sperm extract in mature ascidian eggs mimic those observed at fertilization https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:6551 Wed 11 Apr 2018 15:20:31 AEST ]]> Analysis of the mechanism by which calcium negatively regulates the tyrosine phoshorylation cascade associated with sperm capacitation https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:2527 Wed 11 Apr 2018 14:30:38 AEST ]]> A novel mechanism controls the Ca²⁺ oscillations triggered by activation of ascidian eggs and has an absolute requirement for Cdk1 activity https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:6552 Wed 11 Apr 2018 13:43:05 AEST ]]> Tyrosine phosphorylation activates surface chaperones facilitating sperm-zona recognition https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:2442 Wed 11 Apr 2018 12:48:34 AEST ]]> Calmodulin-dependent protein kinase II, and not protein kinase C, is sufficient for triggering cell-cycle resumption in mammalian eggs https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:6543 Wed 11 Apr 2018 12:03:05 AEST ]]> Identification of SRC as a key PKA-stimulated tyrosine kinase involved in the capacitation-associated hyperactivation of murine spermatozoa https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:1286 Wed 11 Apr 2018 11:40:47 AEST ]]> Exploring the mechanism of action of the sperm-triggered calcium-wave pacemaker in ascidian zygotes https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:6550 Wed 11 Apr 2018 10:31:25 AEST ]]> Tyrosine phosphorylation activates surface chaperones facilitating sperm-zona recognition https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:908 Sat 24 Mar 2018 08:30:00 AEDT ]]> The presence of a truncated base excision repair pathway in human spermatozoa that is mediated by OGG1 https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:20027 Sat 24 Mar 2018 07:50:55 AEDT ]]> CABYR is essential for fibrous sheath integrity and progressive motility in mouse spermatozoa https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:29533 2+-binding tyrosine-phosphorylation-regulated protein (CABYR) has been implicated in sperm physiological function in several in vitro studies. It has also been implicated as a potential cause of and diagnostic tool in asthenozoospermic human males. CABYR is known to be localized to the fibrous sheath, an accessory structure in the flagellar principal piece. Utilizing the CRISPR–Cas9 technology, we have knocked out this gene in mice to understand its role in male fertility. Cabyr-knockout male mice showed severe subfertility with a defect in sperm motility as well as a significant disorganization in the fibrous sheath. Further, abnormal configuration of doublet microtubules was observed in the Cabyr-knockout spermatozoa, suggesting that the fibrous sheath is important for the correct organization of the axoneme. Our results show that it is the role of CABYR in the formation of the fibrous sheath that is essential for male fertility.]]> Sat 24 Mar 2018 07:32:26 AEDT ]]> Mammalian TRP on channels are insensitive to membrane stretch https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:38687 Fri 17 Dec 2021 14:01:20 AEDT ]]>