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Alexander J. Travis

Researcher at University of Pennsylvania

Publications -  7
Citations -  786

Alexander J. Travis is an academic researcher from University of Pennsylvania. The author has contributed to research in topics: Hexokinase & Capacitation. The author has an hindex of 7, co-authored 7 publications receiving 753 citations.

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The role of cholesterol efflux in regulating the fertilization potential of mammalian spermatozoa

TL;DR: The ability to capacitate sperm in vitro has been of great importance to both scientists and clinicians, and knowledge of how cholesterol efflux occurs in these cells, as well as how this efflux is integrated with transmembrane signaling to regulate sperm function, may reveal much about the fertilization process and may also provide insights into the role and dynamics of membraneolesterol efflux in somatic cell function.
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Functional relationships between capacitation-dependent cell signaling and compartmentalized metabolic pathways in murine spermatozoa.

TL;DR: The hypothesis that ATP specifically produced by a compartmentalized glycolytic pathway in the principal piece of the flagellum, as opposed to ATP generated by mitochondria in the mid-piece, is strictly required for protein tyrosine phosphorylation events that take place during sperm capacitation is supported.
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Expression and localization of caveolin-1, and the presence of membrane rafts, in mouse and Guinea pig spermatozoa.

TL;DR: Data indicated that sperm membranes possess distinct raft subdomains, and that caveolin-1 localized to regions appropriate for involvement with acrosomal biogenesis and exocytosis, as well as signaling pathways regulating such processes as capacitation and flagellar motility.
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Targeting of a Germ Cell-specific Type 1 Hexokinase Lacking a Porin-binding Domain to the Mitochondria as Well as to the Head and Fibrous Sheath of Murine Spermatozoa

TL;DR: The unusual distribution of HK1-sc in sperm suggests novel functions, such as extramitochondrial energy production, and also demonstrates that a hexokinase without a classical porin-binding domain can localize to mitochondria.
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Properties and localization of a tyrosine phosphorylated form of hexokinase in mouse sperm

TL;DR: Results suggest that mouse sperm contain at least one HK1 isoform that is present on the sperm head, has an extracellular domain, and behaves as an integral membrane protein.