M
Michel Seman
Researcher at French Institute of Health and Medical Research
Publications - 100
Citations - 4428
Michel Seman is an academic researcher from French Institute of Health and Medical Research. The author has contributed to research in topics: T cell & NAD+ kinase. The author has an hindex of 32, co-authored 100 publications receiving 4168 citations. Previous affiliations of Michel Seman include University of Rouen & Instituto Butantan.
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Single domain antibodies: promising experimental and therapeutic tools in infection and immunity.
Janusz Wesolowski,Vanina Alzogaray,Jan Reyelt,Mandy Unger,Karla Juarez,Karla Juarez,Mariela Urrutia,Ana Cauerhff,Welbeck Danquah,Björn Rissiek,Felix Scheuplein,Nicole Schwarz,Sahil Adriouch,Olivier Boyer,Michel Seman,Alexei Licea,David V. Serreze,Fernando Alberto Goldbaum,Friedrich Haag,Friedrich Koch-Nolte +19 more
TL;DR: The results of several recent proof-of-principle studies are reviewed that open the exciting perspective of using sdAbs for modulating immune functions and for targeting toxins and microbes.
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Identification of a chemokine receptor encoded by human cytomegalovirus as a cofactor for HIV-1 entry.
TL;DR: The human cytomegalovirus encodes a beta-chemokine receptor (US28) that is distantly related to the human chemokine receptors CCR5 and CXCR4, which also serve as cofactors for the entry into cells of human immunodeficiency virus-type 1 (HIV-1).
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NAD-Induced T Cell Death: ADP-Ribosylation of Cell Surface Proteins by ART2 Activates the Cytolytic P2X7 Purinoceptor
Michel Seman,Sahil Adriouch,Felix Scheuplein,Christian Krebs,Dunja Freese,Gustavo Glowacki,Phillipe Deterre,Friedrich Haag,Friedrich Koch-Nolte +8 more
TL;DR: These results delineate an alternative mechanism for inducing T cell death and set an interesting precedent for immunoregulation via crosstalk between NAD-dependent ADP-ribosyltransferases and purinoceptors.
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Characterization of an Extracellular Lipase Encoded by LIP2 in Yarrowia lipolytica
TL;DR: No extracellular lipase activity was detected with the lip2 knockout (KO) strain, strongly suggesting thatextracellularlipase activity results from expression of the LIP2 gene.
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Cutting edge: a natural P451L mutation in the cytoplasmic domain impairs the function of the mouse P2X7 receptor.
TL;DR: It is demonstrated that an allelic mutation (P451L) in the predicted death domain of P2X7R confers a drastically reduced sensitivity to ATP-induced pore formation in cells from some commonly used strains of mice, i.e., C57BL/6 and DBA/2.