Zobrazeno 1 - 7 of 7 pro vyhledávání: '"Manon Mirgaux"'
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Akademický článek
Domain architecture of the Mycobacterium tuberculosis MabR (Rv2242), a member of the PucR transcription factor family
Autor: Véronique Megalizzi, Abdalkarim Tanina, Camille Grosse, Manon Mirgaux, Pierre Legrand, Gaëtan Dias Mirandela, Alexandre Wohlkönig, Pablo Bifani, René Wintjens
Publikováno v: Heliyon, Vol 10, Iss 22, Pp e40494- (2024)
MabR (Rv2242), a PucR-type transcription factor, plays a crucial role in regulating mycolic acid biosynthesis in Mycobacterium tuberculosis. To understand its regulatory mechanisms, we determined the crystal structures of its N-terminal and C-termina
Externí odkaz: https://doaj.org/article/439bd49e186942b88d4665f0fff4e6f4
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2
Akademický článek
Structural study of bioisosteric derivatives of 5-(1H-indol-3-yl)-benzotriazole and their ability to form chalcogen bonds
Autor: Manon Mirgaux, Tanguy Scaillet, Arina Kozlova, Nikolay Tumanov, Raphaël Frederick, Laurie Bodart, Johan Wouters
Publikováno v: Acta Crystallographica Section E: Crystallographic Communications, Vol 78, Iss 4, Pp 418-424 (2022)
Recently, interest in the isosteric replacement of a nitrogen atom to selenium, sulfur or oxygen atoms has been highlighted in the design of potential inhibitors for cancer research. In this context, the structures of 5-(1H-indol-3-yl)-2,1,3-benzotri
Externí odkaz: https://doaj.org/article/8439de2cfcb8490baac398c80349d671
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3
Investigation of bound and unbound phosphoserine phosphatase conformations through elastic network models and molecular dynamics simulations
Autor: Laurence Leherte, Manon Mirgaux, Marie Haufroid, Johan Wouters
Publikováno v: Leherte, L, Haufroid, M, Mirgaux, M & Wouters, J 2020, ' Investigation of bound and unbound phosphoserine phosphatase conformations through Elastic Network Models and Molecular Dynamics simulations ', Journal of Biomolecular Structure & Dynamics, vol. 39, no. 11, pp. 3958-3974 . https://doi.org/10.1080/07391102.2020.1772883
The human phosphoserine phosphatase (hPSP) catalyses the last step in the biosynthesis of L-serine. It involves conformational changes of the enzyme lid once the substrate, phosphoserine (PSer), is bound in the active site. Here, Elastic Network Mode
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2bdc94e3871b98f14649031b2628e7d4
https://doi.org/10.1080/07391102.2020.1772883
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4
Temporary Intermediates of L-Trp Along the Reaction Pathway of human Indoleamine 2,3-dioxygenase 1 and Identification of an Exo Site
Autor: Manon Mirgaux, Laurence Leherte, Johan Wouters
Publikováno v: Mirgaux, M, Leherte, L & Wouters, J 2021, ' Temporary Intermediates of L-Trp Along the Reaction Pathway of human Indoleamine 2,3-dioxygenase 1 and Identification of an Exo Site ', International Journal of Tryptophan Research, vol. 14, pp. 1-11 . https://doi.org/10.1177/11786469211052964
International Journal of Tryptophan Research : IJTR
International Journal of Tryptophan Research, Vol 14 (2021)
Protein dynamics governs most of the fundamental processes in the human body. Particularly, the dynamics of loops located nearan active site can be involved in the positioning of the substrate and the reaction mechanism. The understanding of the func
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95895590320cc64f0255142c9d7ab69d
https://pure.unamur.be/ws/files/61998089/ArticleFinal.pdf
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5
Crystal structures and snapshots along the reaction pathway of human phosphoserine phosphatase
Autor: Marie Haufroid, Manon Mirgaux, Johan Wouters, Laurence Leherte
Publikováno v: Acta Crystallographica Section D Structural Biology. 75:592-604
The equilibrium between phosphorylation and dephosphorylation is one of themost important processes that takes place in living cells. Human phosphoserinephosphatase (hPSP) is a key enzyme in the production of serine by thedephosphorylation of phospho
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e9b60931ff04972906d84a41e3c2cc5
https://doi.org/10.1107/s2059798319006867
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6
Influence of the presence of the heme cofactor on the JK-loop structure in indoleamine-2,3-dioxygenase-1
Autor: Johan Wouters, Manon Mirgaux, Laurence Leherte
Publikováno v: Mirgaux, M, Leherte, L & Wouters, J 2020, ' Influence of the presence of the heme cofactor on the JK-loop structure in indoleamine-2,3-dioxygenase-1 ', Acta crystallographica. Section D: Structural Biology, vol. 76, pp. 1211-1221 . https://doi.org/10.1107/S2059798320013510
Indoleamine 2,3-dioxygenase 1 has sparked interest as an immunotherapeutictarget in cancer research. Its structure includes a loop, named the JK-loop, thatcontrols the orientation of the substrate or inhibitor within the active site.However, little h
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab1aea99978399e7909dd482461b2abd
https://pure.unamur.be/ws/files/53018589/publi_ido.pdf
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