Zobrazeno 1 - 10 of 143 pro vyhledávání: '"Christian, Roumestand"'
1
Akademický článek
The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited.
Autor: Mounia Lahfa, Philippe Barthe, Karine de Guillen, Stella Cesari, Mouna Raji, Thomas Kroj, Marie Le Naour-Vernet, François Hoh, Pierre Gladieux, Christian Roumestand, Jérôme Gracy, Nathalie Declerck, André Padilla
Publikováno v: PLoS Pathogens, Vol 20, Iss 5, p e1012176 (2024)
Magnaporthe AVRs and ToxB-like (MAX) effectors constitute a family of secreted virulence proteins in the fungus Pyricularia oryzae (syn. Magnaporthe oryzae), which causes blast disease on numerous cereals and grasses. In spite of high sequence diverg
Externí odkaz: https://doaj.org/article/05ba20d0e9b1499aaf7604f2e1ef2251
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2
Akademický článek
Does a Similar 3D Structure Mean a Similar Folding Pathway? The Presence of a C-Terminal α-Helical Extension in the 3D Structure of MAX60 Drastically Changes the Folding Pathway Described for Other MAX-Effectors from Magnaporthe oryzae
Autor: Mounia Lahfa, Assia Mouhand, Karine de Guillen, Philippe Barthe, Thomas Kroj, André Padilla, Christian Roumestand
Publikováno v: Molecules, Vol 28, Iss 16, p 6068 (2023)
Does a similar 3D structure mean a similar folding pathway? This question is particularly meaningful when it concerns proteins sharing a similar 3D structure, but low sequence identity or homology. MAX effectors secreted by the phytopathogenic fungus
Externí odkaz: https://doaj.org/article/4c4e5950cfbc46a188bf10f7ec703668
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3
Akademický článek
Paracrine Behaviors Arbitrate Parasite-Like Interactions Between Tumor Subclones
Autor: Robert J. Noble, Viola Walther, Christian Roumestand, Michael E. Hochberg, Urszula Hibner, Patrice Lassus
Publikováno v: Frontiers in Ecology and Evolution, Vol 9 (2021)
Explaining the emergence and maintenance of intratumor heterogeneity is an important question in cancer biology. Tumor cells can generate considerable subclonal diversity, which influences tumor growth rate, treatment resistance, and metastasis, yet
Externí odkaz: https://doaj.org/article/f49cf3321ef847b0a531a171088e8739
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4
Akademický článek
Comparative Assessment of NMR Probes for the Experimental Description of Protein Folding Pathways with High-Pressure NMR
Autor: Vincent Van Deuren, Yin-Shan Yang, Karine de Guillen, Cécile Dubois, Catherine Anne Royer, Christian Roumestand, Philippe Barthe
Publikováno v: Biology, Vol 10, Iss 7, p 656 (2021)
Multidimensional NMR intrinsically provides multiple probes that can be used for deciphering the folding pathways of proteins: NH amide and CαHα groups are strategically located on the backbone of the protein, while CH3 groups, on the side-chain of
Externí odkaz: https://doaj.org/article/459a9ae8186847b59c9d0e8f13a152f5
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6
Akademický článek
Combining High-Pressure Perturbation with NMR Spectroscopy for a Structural and Dynamical Characterization of Protein Folding Pathways
Autor: Cécile Dubois, Isaline Herrada, Philippe Barthe, Christian Roumestand
Publikováno v: Molecules, Vol 25, Iss 23, p 5551 (2020)
High-hydrostatic pressure is an alternative perturbation method that can be used to destabilize globular proteins. Generally perfectly reversible, pressure exerts local effects on regions or domains of a protein containing internal voids, contrary to
Externí odkaz: https://doaj.org/article/fe3b1ddb97aa4941a8e36f50e6022d5c
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7
Unravelling the Adaptation Mechanisms to High Pressure in Proteins
Autor: Antonino Caliò, Cécile Dubois, Stéphane Fontanay, Michael Marek Koza, François Hoh, Christian Roumestand, Philippe Oger, Judith Peters
Publikováno v: International Journal of Molecular Sciences; Volume 23; Issue 15; Pages: 8469
International Journal of Molecular Sciences
International Journal of Molecular Sciences, 2022, 23 (15), pp.8469. ⟨10.3390/ijms23158469⟩
International audience; Life is thought to have appeared in the depth of the sea under high hydrostatic pressure. Nowadays, it is known that the deep biosphere hosts a myriad of life forms thriving under high-pressure conditions. However, the evoluti
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e66a239c04bb1c1af2f8c875995cb102
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8
Akademický článek
Folding of the Ig-Like Domain of the Dengue Virus Envelope Protein Analyzed by High-Hydrostatic-Pressure NMR at a Residue-Level Resolution
Autor: Tomonori Saotome, Maxime Doret, Manjiri Kulkarni, Yin-Shan Yang, Philippe Barthe, Yutaka Kuroda, Christian Roumestand
Publikováno v: Biomolecules, Vol 9, Iss 8, p 309 (2019)
Dengue fever is a mosquito-borne endemic disease in tropical and subtropical regions, causing a significant public health problem in Southeast Asia. Domain III (ED3) of the viral envelope protein contains the two dominant putative epitopes and part o
Externí odkaz: https://doaj.org/article/8174b50c65734b0e87da34ca818b28fb
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9
Combining High-Pressure NMR and Geometrical Sampling to Obtain a Full Topological Description of Protein Folding Landscapes: Application to the Folding of Two MAX Effectors from Magnaporthe oryzae
Autor: Cécile Dubois, Mounia Lahfa, Joana Pissarra, Karine de Guillen, Philippe Barthe, Thomas Kroj, Christian Roumestand, André Padilla
Publikováno v: International Journal of Molecular Sciences
International Journal of Molecular Sciences, 2022, 23 (10), pp.5461. ⟨10.3390/ijms23105461⟩
International Journal of Molecular Sciences; Volume 23; Issue 10; Pages: 5461
International audience; Despite advances in experimental and computational methods, the mechanisms by which an unstructured polypeptide chain regains its unique three-dimensional structure remains one of the main puzzling questions in biology. Single
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::814eb776bcead070c4296fb0d6d8a972
https://hal.science/hal-03705665/document
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10
Comparative Assessment of NMR Probes for the Experimental Description of Protein Folding Pathways with High-Pressure NMR
Autor: Yinshan Yang, Vincent Van Deuren, Christian Roumestand, Catherine Anne Royer, Philippe Barthe, Cécile Dubois, Karine de Guillen
Publikováno v: Biology
Biology, MDPI 2021, 10 (7), pp.656. ⟨10.3390/biology10070656⟩
Biology, Vol 10, Iss 656, p 656 (2021)
Volume 10
Issue 7
Biology, 2021, 10 (7), pp.656. ⟨10.3390/biology10070656⟩
Simple Summary During the last decade, high-pressure multidimensional NMR has emerged as a very powerful tool to describe the folding landscapes of proteins. This is (i) because pressure is a gentle perturbation, the effects of which originate from l
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b5b96649aa2fe001e37c8d784ba3a347
https://hal.umontpellier.fr/hal-03472234
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