Publications
54 results found
Stramer BM, Dionne MS, 2014, Unraveling tissue repair immune responses in flies, SEMINARS IN IMMUNOLOGY, Vol: 26, Pages: 310-314, ISSN: 1044-5323
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- Citations: 9
Dionne MS, 2014, Immune-metabolic interaction in <i>Drosophila</i>, FLY, Vol: 8, Pages: 75-79, ISSN: 1933-6934
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- Citations: 21
Clark RI, Walker DW, Dionne MS, 2014, Metabolic and immune integration in aging and age-related disease, AGING-US, Vol: 6, Pages: 3-4, ISSN: 1945-4589
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- Citations: 6
Pean CB, Dionne MS, 2014, Intracellular infections in <i>Drosophila melanogaster</i>: Host defense and mechanisms of pathogenesis, DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY, Vol: 42, Pages: 57-66, ISSN: 0145-305X
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- Citations: 11
Clark RI, Tan SWS, Pean CB, et al., 2013, MEF2 Is an In Vivo Immune-Metabolic Switch, CELL, Vol: 155, Pages: 435-447, ISSN: 0092-8674
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- Citations: 114
Dionne MS, 2013, Comparative immunology: allorecognition and variable surface receptors outside the jawed vertebrates, CURRENT OPINION IN IMMUNOLOGY, Vol: 25, Pages: 608-612, ISSN: 0952-7915
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- Citations: 3
Pilatova M, Dionne MS, 2012, <i>Burkholderia thailandensis</i> Is Virulent in <i>Drosophila melanogaster</i>, PLOS ONE, Vol: 7, ISSN: 1932-6203
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- Citations: 15
Clark RI, Woodcock KJ, Geissmann F, et al., 2011, Multiple TGF-β Superfamily Signals Modulate the Adult <i>Drosophila</i> Immune Response, CURRENT BIOLOGY, Vol: 21, Pages: 1672-1677, ISSN: 0960-9822
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- Citations: 72
Dionne MS, Schneider DS, 2008, Models of infectious diseases in the fruit fly <i>Drosophila melanogaster</i>, DISEASE MODELS & MECHANISMS, Vol: 1, Pages: 43-49, ISSN: 1754-8403
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- Citations: 81
Dionne MS, Schneider DS, 2008, Host-pathogen interactions in Drosophila, DISEASE MODELS & MECHANISMS, Vol: 1, Pages: 67-68, ISSN: 1754-8403
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- Citations: 2
Shirasu-Hiza MM, Dionne MS, Pham LN, et al., 2007, Interactions between circadian rhythm and immunity in <i>Drosophila melanlogaster</i>, CURRENT BIOLOGY, Vol: 17, Pages: R353-R355, ISSN: 0960-9822
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- Citations: 73
Pham LN, Dionne MS, Shirasu-Hiza M, et al., 2007, A specific primed immune response in <i>Drosophila</i> is dependent on phagocytes, PLOS PATHOGENS, Vol: 3, ISSN: 1553-7366
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- Citations: 390
Schneider DS, Ayres JS, Brandt SM, et al., 2007, <i>Drosophila eiger</i> mutants are sensitive to extracellular pathogens, PLOS PATHOGENS, Vol: 3, ISSN: 1553-7366
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- Citations: 86
Dionne MS, Pham LN, Shirasu-Hiza M, et al., 2006, <i>Akt</i> and <i>foxo</i> dysregulation contribute to infection-induced wasting in <i>Drosophila</i>, CURRENT BIOLOGY, Vol: 16, Pages: 1977-1985, ISSN: 0960-9822
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- Citations: 229
Gordon MD, Dionne MS, Schneider DS, et al., 2005, WntD is a feedback inhibitor of Dorsal/NF-κB in <i>Drosophila</i> development and immunity, NATURE, Vol: 437, Pages: 746-749, ISSN: 0028-0836
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- Citations: 124
Brandt SM, Dionne MS, Khush RS, et al., 2004, Secreted bacterial effectors and host-produced eiger/TNF drive death in a <i>Salmonella</i>-infected fruit fly, PLOS BIOLOGY, Vol: 2, Pages: 2067-2075, ISSN: 1544-9173
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- Citations: 118
Mansfield BE, Dionne MS, Schneider DS, et al., 2003, Exploration of host-pathogen interactions using <i>Listeria monocytogenes</i> and <i>Drosophila melanogaster</i>, CELLULAR MICROBIOLOGY, Vol: 5, Pages: 901-911, ISSN: 1462-5814
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- Citations: 138
Khokha MK, Hsu D, Brunet LJ, et al., 2003, Gremlin is the BMP antagonist required for maintenance of Shh and Fgf signals during limb patterning, NATURE GENETICS, Vol: 34, Pages: 303-307, ISSN: 1061-4036
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- Citations: 293
Dionne MS, Ghori N, Schneider DS, 2003, <i>Drosophila melanogaster</i> is a genetically tractable model host for <i>Mycobacterium marinum</i>, INFECTION AND IMMUNITY, Vol: 71, Pages: 3540-3550, ISSN: 0019-9567
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- Citations: 129
Dionne MS, Brunet LJ, Eimon PM, et al., 2002, Noggin is required for correct guidance of dorsal root ganglion axons, DEVELOPMENTAL BIOLOGY, Vol: 251, Pages: 283-293, ISSN: 0012-1606
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- Citations: 13
Dionne MS, Schneider DS, 2002, Screening the fruitfly immune system., Genome Biol, Vol: 3
The anti-microbial defense system of Drosophila shows functional similarities with the vertebrate innate immune system. Two recent gene-expression profiling studies of fruitflies challenged with infectious agents have identified key molecular players in the fruitfly's response to bacterial and fungal infection, as well as a large number of immune-regulated genes with unknown immunological function.
Dionne MS, Skarnes WC, Harland RM, 2001, Mutation and analysis of <i>Dan</i>, the founding member of the Dan family of transforming growth factor β antagonists, MOLECULAR AND CELLULAR BIOLOGY, Vol: 21, Pages: 636-643, ISSN: 0270-7306
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- Citations: 73
GIBNEY G, CAMP S, DIONNE M, et al., 1990, MUTAGENESIS OF ESSENTIAL FUNCTIONAL RESIDUES IN ACETYLCHOLINESTERASE, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 87, Pages: 7546-7550, ISSN: 0027-8424
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- Citations: 137
Gibney G, Camp S, Dionne M, et al., 1990, Mutagenesis of essential functional residues in acetylcholinesterase, Proceedings of the National Academy of Sciences of the United States of America, Vol: 87, Pages: 7551-7554, ISSN: 0027-8424
The cholinesterases are serine hydrolases that show no global similarities in sequence with either the trypsin or the subtilisin family of serine proteases. The cholinesterase superfamily includes several esterases with distinct functions and other proteins devoid of the catalytic serine and known esterase activity. To identify the residues involved in catalysis and conferring specificity on the enzyme, we have expressed wild-type Torpedo acetylcholinesterase (EC 3.1.1.7) and several site-directed mutants in a heterologous system. Mutation of serine-200 to cysteine results in diminished activity, while its mutation to valine abolishes detectable activity. Two conserved histidines can be identified at positions 425 and 440 in the cholinesterase family; glutamine replacement at position 440 eliminates activity whereas the mutation at 425 reduces activity only slightly. The assignment of the catalytic histidine to position 440 defines a rank ordering of catalytic residues in cholinesterases distinct from trypsin and subtilisin and suggests a convergence of a catalytic triad to form a third, distinct family of serine hydrolases. Mutation of glutamate-199 to glutamine yields an enzyme with a higher Km and without the substrate-inhibition behavior characteristic of acetylcholinesterase. Hence, modification of the acidic amino acid adjacent to the serine influences substrate association and the capacity of a second substrate molecule to affect catalysis.
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