Search Results - "Myles, Diana G"
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A Role for Sperm Surface Protein Disulfide Isomerase Activity in Gamete Fusion: Evidence for the Participation of ERp57
Published in Developmental cell (01-06-2006)“…In mammals, sperm-egg interaction is based on molecular events either unique to gametes or also present in somatic cells. In gamete fusion, it is unknown which…”
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Cell–cell membrane fusion during mammalian fertilization
Published in FEBS letters (22-05-2007)“…The mechanism of sperm–egg fusion in mammals is a research area that has greatly benefited from the use of gene deletion technology. Because fertilization is…”
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Penetration, Adhesion, and Fusion in Mammalian Sperm-Egg Interaction
Published in Science (American Association for the Advancement of Science) (21-06-2002)“…Fertilization is the sum of the cellular mechanisms that pass the genome from one generation to the next and initiate development of a new organism. A typical,…”
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Oocyte CD9 is enriched on the microvillar membrane and required for normal microvillar shape and distribution
Published in Developmental biology (01-04-2007)“…Microvilli are found on the surface of many cell types, including the mammalian oocyte, where they are thought to act in initial contact of sperm and oocyte…”
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Identification of an ADAM2-ADAM3 Complex on the Surface of Mouse Testicular Germ Cells and Cauda Epididymal Sperm
Published in The Journal of biological chemistry (15-06-2007)“…Male mice lacking ADAM2 (fertilin β) or ADAM3 (cyritestin) are infertile; cauda epididymal sperm (mature sperm) from these mutant mice cannot bind to the egg…”
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Can the presence of wild-type oocytes during insemination rescue the fusion defect of CD9 null oocytes?
Published in Molecular reproduction and development (01-07-2009)Get full text
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Characterization of mouse sperm TMEM190, a small transmembrane protein with the trefoil domain: evidence for co-localization with IZUMO1 and complex formation with other sperm proteins
Published in Reproduction (Cambridge, England) (01-04-2011)“…TMEM190, a small transmembrane protein containing the trefoil domain, was previously identified by our proteomic analysis of mouse sperm. Two structural…”
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A Role for the Disintegrin Domain of Cyritestin, a Sperm Surface Protein Belonging to the ADAM Family, in Mouse Sperm-Egg Plasma Membrane Adhesion and Fusion
Published in The Journal of cell biology (07-04-1997)“…Sperm-egg plasma membrane fusion is preceded by sperm adhesion to the egg plasma membrane. Cell-cell adhesion frequently involves multiple adhesion molecules…”
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Residues SFQ (173-175) in the large extracellular loop of CD9 are required for gamete fusion
Published in Development (Cambridge) (15-04-2002)“…Gamete fusion is the fundamental first step initiating development of a new organism. Female mice with a gene knockout for the tetraspanin CD9 (CD9 KO mice)…”
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Direct binding of the ligand PSG17 to CD9 requires a CD9 site essential for sperm-egg fusion
Published in Molecular biology of the cell (01-12-2003)“…The function currently attributed to tetraspanins is to organize molecular complexes in the plasma membrane by using multiple cis-interactions. Additionally,…”
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Defects in Secretory Pathway Trafficking During Sperm Development in Adam2 Knockout Mice
Published in Biology of reproduction (01-11-2005)“…Adam2 -null and Adam3 -null male mice exhibit reduced levels of one or more ADAM proteins on mature sperm, in addition to the loss of the genetically targeted…”
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A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion
Published in Nature (London) (19-03-1992)“…The union of sperm and egg is a special membrane fusion event that gives a signal to begin development. We have hypothesized that proteins mediating cell-cell…”
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The ADAM gene family: surface proteins with adhesion and protease activity
Published in Trends in Genetics (01-02-2000)“…An ADAM is a transmembrane protein that contains a disintegrin and metalloprotease domain and, therefore, it potentially has both cell adhesion and protease…”
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Proteomic analysis of sperm regions that mediate sperm-egg interactions
Published in Proteomics (Weinheim) (01-06-2006)“…The sperm interacts with three oocyte‐associated structures during fertilization: the cumulus cell layer surrounding the oocyte, the egg extracellular matrix…”
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Cell adhesion and fertilization: Steps in oocyte transport, sperm-zona pellucida interactions, and sperm-egg fusion
Published in Biology of reproduction (2003)“…Fertilization in mammals requires the successful completion of many steps, starting with the transport of gametes in the reproductive tract and ending with…”
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Defects in Secretory Pathway Trafficking During Sperm Development in Adam2 Knockout Mice1
Published in Biology of reproduction (01-11-2005)“…Adam2-null and Adam3-null male mice exhibit reduced levels of one or more ADAM proteins on mature sperm, in addition to the loss of the genetically targeted…”
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Cell Adhesion and Fertilization: Steps in Oocyte Transport, Sperm-Zona Pellucida Interactions, and Sperm-Egg Fusion1
Published in Biology of reproduction (01-01-2003)“…Fertilization in mammals requires the successful completion of many steps, starting with the transport of gametes in the reproductive tract and ending with…”
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Fertilization Defects in Sperm from Mice Lacking Fertilin β
Published in Science (American Association for the Advancement of Science) (18-09-1998)“…Fertilin, a member of the ADAM family, is found on the plasma membrane of mammalian sperm. Sperm from mice lacking fertilin β were shown to be deficient in…”
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None of the integrins known to be present on the mouse egg or to be ADAM receptors are essential for sperm–egg binding and fusion
Published in Developmental biology (15-02-2003)“…Antibody inhibition and α6β1 ligand binding experiments indicate that the egg integrin α6β1 functions as a receptor for sperm during gamete fusion; yet, eggs…”
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ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions
Published in The Journal of cell biology (01-10-1995)“…The ADAMs, a newly discovered gene family encoding membrane proteins with a disintegrin and metalloprotease domain, are described. ADAMs are unique in that…”
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