RMN biologique intégrative
Responsable d'équipe
Responsable d'équipe
Notre recherche porte sur le développement de méthodes RMN et leurs applications, avec d’autres techniques biophysiques, en biologie structurale et en biophysique des membranes, pour caractériser les facteurs de virulence ou les cibles thérapeutiques associés aux cancers ou aux relations hôte-pathogène, avec un accent particulier sur l’infection mycobactérienne.
Un groupe de recherche interdisciplinaire élucidant la structure moléculaire, la dynamique et les interactions des processus biologiques à l'aide de la RMN, de méthodes biophysiques et de simulations MD.
Le groupe de RMN biologique intégrative met à profit son expertise et son équipement de pointe pour poursuivre des projets ambitieux en biologie structurale ayant des implications importantes en pharmacologie. L’étude de la structure, de la dynamique et des interactions des biomolécules est essentielle pour élucider les processus biochimiques à une résolution atomique. Nous explorons continuellement de nouvelles voies, telles que la structure et la fonction d’assemblages membranaires complexes et l’influence de la dynamique macromoléculaire sur les interactions, dans le contexte des infections bactériennes et du cancer.
La relation entre l’hôte et le pathogène est médiée par de nombreux processus biologiques. Les mécanismes moléculaires par lesquels l’hôte détecte et répond à l’infection par des pathogènes et par lesquels les pathogènes contournent les défenses de l’hôte sont d’une importance primordiale pour le développement de nouvelles approches thérapeutiques.
– Nous cherchons à comprendre le mécanisme de défense de Mycobacterium tuberculosis contre l’intoxication métallique dans les phagocytes humains et à déchiffrer la réponse de l’hôte aux pathogènes, médiée au niveau moléculaire par une famille de récepteurs de surface cellulaire. Lors d’une infection par M. tuberculosis, les macrophages tentent d’intoxiquer la bactérie en augmentant la concentration de métaux tels que le cuivre et le zinc. Dans ce contexte, le groupe du Dr Olivier Neyrolles (IPBS) a identifié trois ATPases de type P1 de M. tuberculosis (CtpC, CtpG et CtpV), chacune co-exprimée avec une petite protéine associée à la membrane, PacL1, PacL2 et PacL3, respectivement. Alors que CtpC est nécessaire à la survie intracellulaire optimale de M. tuberculosis à des concentrations élevées de zinc, PacL1 est nécessaire à la résistance au zinc de M. tuberculosis, elle se colocalise en foyers avec CtpC et stabilise les plates-formes d’efflux à la membrane plasmique. PacL1 représente donc un nouveau type de métallochaperone dans la mesure où elle lie le zinc et stabilise CtpC. Nous étudions la sélectivité de ces métallochaperones vis-à-vis des métaux et le mécanisme de transfert des métaux vers le transporteur associé.
– Les lectines de type C (CLR) sont des protéines hôtes qui jouent un rôle clé dans le système immunitaire inné. Les CLR permettent aux cellules de reconnaître les molécules caractéristiques des agents pathogènes ou des cellules endommagées et de déclencher des voies de signalisation qui aboutissent à des effets protecteurs. Une meilleure compréhension de la signalisation des CLR au niveau moléculaire pourrait faciliter le développement d’agents thérapeutiques ciblant ces récepteurs. Les données structurales disponibles sont toutefois limitées et n’éclairent que partiellement la reconnaissance des ligands. Nous nous concentrons spécifiquement sur un ensemble de CLR transmembranaires (Mincle, Dectin-1, Dectin-2 et DCIR) qui jouent un rôle clé dans des pathologies telles que l’infection par M. tuberculosis et d’autres bactéries, les cancers et les maladies auto-immunes. Ces CLRs sont des représentants de divers mécanismes de signalisation. Notre objectif est de fournir une explication détaillée du couplage allostérique entre la liaison du ligand extracellulaire et le recrutement de la protéine partenaire intracellulaire qui aboutit à la réponse des cellules immunitaires.
Équipe
Chercheurs-Enseignants chercheurs
Andrew Atkinson (CR HC, CNRS)
Georges Czaplicki (PR1, UPS)
Pascal Demange (DR2, CNRS)
Guillaume Ferré (MCU, UPS)
Evert Haanappel (CR HC, CNRS)
Alain Milon (PR émérite, UPS)
Isabelle Muller (MCU HC, UPS)
Valérie Réat (CR, CNRS)
Olivier Saurel (IR HC, CNRS)
Ingénieurs
Dunkan Bégué
Nathalie Doncescu (IE HC, CNRS)
Yasmina Grimoire
Pascal Ramos (IE HC, UPS)
Doctorants
Floriane Audebert
Louis Benastre
Maxime Noriega
Nos projets de recherche (en anglais)
Architecture et fonction des plates-formes d'efflux membranaires bactériennes
Signalisation des cellules immunitaires par les lectines de type C
Autres collaborations
Ferré et al. (2023) Sodium is a negative allosteric regulator of the ghrelin receptor. Cell Rep
Schahl et al. (2022) Evidence for amylose inclusion complexes with multiple acyl chain lipids using solid-state NMR and theoretical approaches. Carbohydr Polym
Ferré et al. (2019) Structure and dynamics of G protein-coupled receptor-bound ghrelin reveal the critical role of the octanoyl chain. Proc Natl Acad Sci USA
Augenstreich et al. (2019) The conical shape of DIM lipids promotes Mycobacterium tuberculosis infection of macrophages. Proc Natl Acad Sci USA
Saurel et al. (2017) Local and global dynamics in Klebsiella pneumoniae outer membrane protein a in lipid bilayers probed at atomic resolution. J Am Chem Soc
Carel et al. (2017) Identification of specific posttranslational O-mycoloylations mediating protein targeting to the mycomembrane. Proc Natl Acad Sci USA
Macromolecular interactions by NMR: Solution structure of the THAP zinc finger of THAP1 in complex with its DNA target (PDB entry 2KO0). © Olivier Saurel
Institut de Pharmacologie et de Biologie Structurale (IPBS), Toulouse
Dr. Matthieu Chavent Multiscale Computational Immunology
Dr. Ahmed Amine Khamlichi Genetic Instability and Transcriptional Regulation
Dr. Lionel Mourey Structural Biophysics
Dr. Olivier Neyrolles Mycobacterial Interactions with Host Cells
Dr. Jérôme Nigou Immunomodulation by Mycobacterial Lipids and Glycoconjugates
G.CLIPS biotech
Dr. Rosie Dawaliby
Institut de Recherche en Santé Digestive (IRSD), Toulouse
Prof. Eric Oswald Pathogenesis and Commensalism of Enterobacteria
Laboratoire de Synthèse et Physico-Chimie de Molécules d’Intérêt Biologique (SPCMIB), Toulouse
Dr. Yves Génisson MoNALISA
Dr. Christian Lherbet SySMiC
Toulouse Biotechnology Institute (TBI), Toulouse
Dr. Didier Zerbib PHYGE – Integrated Physiology and Functional Genomics of
Microbial Systems
University of the Western Cape, South Africa
Prof. David J.R. Pugh Department of Biotechnology
Our laboratory is supported by grants from:
- Agence Nationale de la Recherche (ANR)
- Université de Toulouse III – Paul Sabatier
- Infrastructures en Biologie Santé et Agronomie (IBiSA)
- ERDF – REACT-EU
The complete list of our publications is available through Pubmed.
2024
Czaplicki, G., and Mazeres, S. (2024). Glophyt: a user-friendly, general-purpose program for nonlinear and multidimensional curve fitting via a hybrid stochastic and deterministic approach. Journal of Bioinformatics and Systems Biology 7, 219–226. https://doi.org/10.26502/jbsb.5107093.
Noriega, M., Corey, R.A., Haanappel, E., Demange, P., Czaplicki, G., Atkinson, R.A., and Chavent, M. (2024). Coarse-graining the recognition of a glycolipid by the C-type lectin mincle receptor. J. Phys. Chem. B. https://doi.org/10.1021/acs.jpcb.4c03242.
Menchon, G., Maveyraud, L., and Czaplicki, G. (2024). Molecular dynamics as a tool for virtual ligand screening. Methods Mol Biol 2714, 33–83. https://doi.org/10.1007/978-1-0716-3441-7_3.
Duncan, A.L., Gao, Y., Haanappel, E., Im, W., and Chavent, M. (2024). Recent advances in modeling membrane β-barrel proteins using molecular dynamics simulations: from their lipid environments to their assemblies. Methods Mol Biol 2778, 311–330. https://doi.org/10.1007/978-1-0716-3734-0_19.
Bories, P., Rima, J., Tranier, S., Marcoux, J., Grimoire, Y., Tomaszczyk, M., Launay, A., Fata, K., Marrakchi, H., Burlet-Schiltz, O., et al. (2024). HadBD dehydratase from Mycobacterium tuberculosis fatty acid synthase type II: A singular structure for a unique function. Protein Sci 33, e4964. https://doi.org/10.1002/pro.4964.
Baybekov, S., Llompart, P., Marcou, G., Gizzi, P., Galzi, J.-L., Ramos, P., Saurel, O., Bourban, C., Minoletti, C., and Varnek, A. (2024). Kinetic solubility: experimental and machine-learning modeling perspectives. Mol Inform 43, e202300216. https://doi.org/10.1002/minf.202300216.
Anazia, K., Koenekoop, L., Ferré, G., Petracco, E., Gutiérrez-de-Teran, H., and Eddy, M.T. (2024). Interaction networks within disease-associated GαS variants characterized by an integrative biophysical approach. J Biol Chem, 107497. https://doi.org/10.1016/j.jbc.2024.107497.
2023
Pritzlaff, A., Ferré, G., Dargassies, E., Williams, C.O., Gonzalez, D.D., and Eddy, M.T. (2023). Conserved protein-polymer interactions across structurally diverse polymers underlie alterations to protein thermal unfolding. ACS Cent Sci 9, 685–695. https://doi.org/10.1021/acscentsci.2c01522.
Kalakoutis, M., Pollock, R.D., Lazarus, N.R., Atkinson, R.A., George, M., Berber, O., Woledge, R.C., Ochala, J., and Harridge, S.D.R. (2023). Revisiting specific force loss in human permeabilised single skeletal muscle fibres obtained from older individuals. Am J Physiol Cell Physiol. https://doi.org/10.1152/ajpcell.00525.2022.
Ferré, G., Gomes, A.A.S., Louet, M., Damian, M., Bisch, P.M., Saurel, O., Floquet, N., Milon, A., and Banères, J.-L. (2023). Sodium is a negative allosteric regulator of the ghrelin receptor. Cell Rep 42, 112320. https://doi.org/10.1016/j.celrep.2023.112320.
Crosas-Molist, E., Graziani, V., Maiques, O., Pandya, P., Monger, J., Samain, R., George, S.L., Malik, S., Salise, J., Morales, V., et al. (2023). AMPK is a mechano-metabolic sensor linking cell adhesion and mitochondrial dynamics to Myosin-dependent cell migration. Nat Commun 14, 2740. https://doi.org/10.1038/s41467-023-38292-0.
Atkinson, R.A. (2023) NMR of proteins and nucleic acids. Nucl Magn Reson 49, 200-221. https://doi.org/10.1039/9781837672455
2022
Schahl, A., Lemassu, A., Jolibois, F., and Réat, V. (2022). Evidence for amylose inclusion complexes with multiple acyl chain lipids using solid-state NMR and theoretical approaches. Carbohydr Polym 276, 118749. https://doi.org/10.1016/j.carbpol.2021.118749.
Pritzlaff, A., Ferré, G., Mulry, E., Lin, L., Gopal Pour, N., Savin, D.A., Harris, M.E., and Eddy, M.T. (2022). Atomic-scale view of protein-PEG interactions that redirect the thermal unfolding pathway of PEGylated human galectin-3. Angew Chem Int Ed Engl 61, e202203784. https://doi.org/10.1002/anie.202203784.
Lauressergues, D., Ormancey, M., Guillotin, B., San Clemente, H., Camborde, L., Duboé, C., Tourneur, S., Charpentier, P., Barozet, A., Jauneau, A., et al. (2022). Characterization of plant microRNA-encoded peptides (miPEPs) reveals molecular mechanisms from the translation to activity and specificity. Cell Rep 38, 110339. https://doi.org/10.1016/j.celrep.2022.110339.
Jackson, V., Hermann, J., Tynan, C.J., Rolfe, D.J., Corey, R.A., Duncan, A.L., Noriega, M., Chu, A., Kalli, A.C., Jones, E.Y., et al. (2022). The guidance and adhesion protein FLRT2 dimerizes in cis via dual small-X3-small transmembrane motifs. Structure 30, 1354-1365.e5. https://doi.org/10.1016/j.str.2022.05.014.
Ferré, G., Anazia, K., Silva, L.O., Thakur, N., Ray, A.P., and Eddy, M.T. (2022). Global insights into the fine tuning of human A2AAR conformational dynamics in a ternary complex with an engineered G protein viewed by NMR. Cell Rep 41, 111844. https://doi.org/10.1016/j.celrep.2022.111844.
Demange, P., Joly, E., Marcoux, J., Zanon, P.R.A., Listunov, D., Rullière, P., Barthes, C., Noirot, C., Izquierdo, J.-B., Rozié, A., et al. (2022). SDR enzymes oxidize specific lipidic alkynylcarbinols into cytotoxic protein-reactive species. Elife 11, e73913. https://doi.org/10.7554/eLife.73913.
Chadelle, L., Liu, J., Choesmel-Cadamuro, V., Karginov, A.V., Froment, C., Burlet-Schiltz, O., Gandarillas, S., Barreira, Y., Segura, C., Van Den Berghe, L., et al. (2022). PKCθ-mediated serine/threonine phosphorylations of FAK govern adhesion and protrusion dynamics within the lamellipodia of migrating breast cancer cells. Cancer Lett 526, 112–130. https://doi.org/10.1016/j.canlet.2021.11.026.
Boudehen, Y.-M., Faucher, M., Maréchal, X., Miras, R., Rech, J., Rombouts, Y., Sénèque, O., Wallat, M., Demange, P., Bouet, J.-Y., et al. (2022). Mycobacterial resistance to zinc poisoning requires assembly of P-ATPase-containing membrane metal efflux platforms. Nat Commun 13, 4731. https://doi.org/10.1038/s41467-022-32085-7.
Atkinson, R.A. (2022) NMR of proteins and nucleic acids. Nucl Magn Reson 48, 249-270. https://doi.org/10.1039/9781839167690
2021
Young, J.D., Ma, M.T., Eykyn, T.R., Atkinson, R.A., Abbate, V., Cilibrizzi, A., Hider, R.C., and Blower, P.J. (2021). Dipeptide inhibitors of the prostate specific membrane antigen (PSMA): a comparison of urea and thiourea derivatives. Bioorganic & Medicinal Chemistry Letters, 128044. https://doi.org/10.1016/j.bmcl.2021.128044.
Schahl, A., Gerber, I.C., Réat, V., and Jolibois, F. (2021). Diversity of the hydrogen bond network and its impact on NMR Parameters of amylose B polymorph: a study using molecular dynamics and DFT calculations within periodic boundary conditions. J Phys Chem B 125, 158–168. https://doi.org/10.1021/acs.jpcb.0c08631.
Javaid, S., Zafar, H., Atia-Tul-Wahab, Gervais, V., Ramos, P., Muller, I., Milon, A., Atta-Ur-Rahman, and Choudhary, M.I. (2021). Identification of new lead molecules against anticancer drug target TFIIH subunit P8 using biophysical and molecular docking studies. Bioorg Chem 114, 105021. https://doi.org/10.1016/j.bioorg.2021.105021.
Hungnes, I.N., Al-Salemee, F., Gawne, P.J., Eykyn, T., Atkinson, R.A., Terry, S.Y.A., Clarke, F., Blower, P.J., Pringle, P.G., and Ma, M.T. (2021). One-step, kit-based radiopharmaceuticals for molecular SPECT imaging: a versatile diphosphine chelator for 99mTc radiolabelling of peptides. Dalton Trans 50, 16156–16165. https://doi.org/10.1039/d1dt03177e.
Baybekov, S., Marcou, G., Ramos, P., Saurel, O., Galzi, J.-L., and Varnek, A. (2021). DMSO solubility assessment for fragment-based screening. Molecules 26, 3950. https://doi.org/10.3390/molecules26133950.
Atkinson, R.A. (2021) NMR of proteins and nucleic acids. Nucl Magn Reson 47, 204-239. https://doi.org/10.1039/9781839164965
2020
Schahl, A., Réat, V., and Jolibois, F. (2020). Structures and NMR spectra of short amylose-lipid complexes. Insight using molecular dynamics and DFT quantum chemical calculations. Carbohydr Polym 235, 115846. https://doi.org/10.1016/j.carbpol.2020.115846.
Paganin-Gioanni, A., Rols, M.-P., Teissié, J., and Golzio, M. (2020). Cyclin B1 knockdown mediated by clinically approved pulsed electric fields siRNA delivery induces tumor regression in murine melanoma. Int J Pharm 573, 118732. https://doi.org/10.1016/j.ijpharm.2019.118732.
Nguyen, M.C., Saurel, O., Carivenc, C., Gavalda, S., Saitta, S., Tran, M.P., Milon, A., Chalut, C., Guilhot, C., Mourey, L., et al. (2020). Conformational flexibility of coenzyme A and its impact on the post-translational modification of acyl carrier proteins by 4’-phosphopantetheinyl transferases. FEBS J 287, 4729–4746. https://doi.org/10.1111/febs.15273.
Meilhoc, E., and Teissié, J. (2020). Electrotransformation of Saccharomyces cerevisiae. Methods Mol Biol 2050, 187–193. https://doi.org/10.1007/978-1-4939-9740-4_21.
Martinez, X., Chavent, M., and Baaden, M. (2020). Visualizing protein structures – tools and trends. Biochem Soc Trans 48, 499–506. https://doi.org/10.1042/BST20190621.
Manzo, G., Hind, C.K., Ferguson, P.M., Amison, R.T., Hodgson-Casson, A.C., Ciazynska, K.A., Weller, B.J., Clarke, M., Lam, C., Man, R.C.H., et al. (2020). A pleurocidin analogue with greater conformational flexibility, enhanced antimicrobial potency and in vivo therapeutic efficacy. Commun Biol 3, 697. https://doi.org/10.1038/s42003-020-01420-3.
Fontaine, C., Buscato, M., Vinel, A., Giton, F., Raymond-Letron, I., Kim, S.H., Katzenellenbogen, B.S., Katzenellenbogen, J.A., Gourdy, P., Milon, A., et al. (2020). The tissue-specific effects of different 17β-estradiol doses reveal the key sensitizing role of AF1 domain in ERα activity. Mol Cell Endocrinol 505, 110741. https://doi.org/10.1016/j.mce.2020.110741.
Fanelli, R., Berta, D., Földes, T., Rosta, E., Atkinson, R.A., Hofmann, H.-J., Shankland, K., and Cobb, A.J.A. (2020). Organocatalytic access to a cis-cyclopentyl-γ-amino acid: an intriguing model of selectivity and formation of a stable 10/12-helix from the corresponding γ/α-peptide. J. Am. Chem. Soc. 142, 1382–1393. https://doi.org/10.1021/jacs.9b10861.
Del Toro, D., Carrasquero-Ordaz, M.A., Chu, A., Ruff, T., Shahin, M., Jackson, V.A., Chavent, M., Berbeira-Santana, M., Seyit-Bremer, G., Brignani, S., et al. (2020). Structural basis of teneurin-latrophilin interaction in repulsive guidance of migrating neurons. Cell 180, 323-339.e19. https://doi.org/10.1016/j.cell.2019.12.014.
Dekoninck, K., Létoquart, J., Laguri, C., Demange, P., Bevernaegie, R., Simorre, J.-P., Dehu, O., Iorga, B.I., Elias, B., Cho, S.-H., et al. (2020). Defining the function of OmpA in the Rcs stress response. Elife 9. https://doi.org/10.7554/eLife.60861.
Augenstreich, J., Haanappel, E., Sayes, F., Simeone, R., Guillet, V., Mazeres, S., Chalut, C., Mourey, L., Brosch, R., Guilhot, C., et al. (2020). Phthiocerol dimycocerosates from Mycobacterium tuberculosis increase the membrane activity of bacterial effectors and host receptors. Front Cell Infect Microbiol 10, 420. https://doi.org/10.3389/fcimb.2020.00420.
Atkinson, R.A. (2020) NMR of proteins and nucleic acids. Nucl Magn Reson 46, 250-271. https://doi.org/10.1039/9781788010665
2019
Pasquet, L., Chabot, S., Bellard, E., Rols, M.-P., Teissié, J., and Golzio, M. (2019). Noninvasive gene electrotransfer in skin. Hum Gene Ther Methods 30, 17–22. https://doi.org/10.1089/hgtb.2018.051.
Pasquet, L., Bellard, E., Chabot, S., Markelc, B., Rols, M.-P., Teissié, J., and Golzio, M. (2019). Pre-clinical investigation of the synergy effect of interleukin-12 gene-electro-transfer during partially irreversible electropermeabilization against melanoma. J Immunother Cancer 7, 161. https://doi.org/10.1186/s40425-019-0638-5.
Martinez, X., Krone, M., Alharbi, N., Rose, A.S., Laramee, R.S., O’Donoghue, S., Baaden, M., and Chavent, M. (2019). Molecular graphics: bridging structural biologists and computer scientists. Structure 27, 1617–1623. https://doi.org/10.1016/j.str.2019.09.001.
Ladurantie, C., Coustets, M., Czaplicki, G., Demange, P., Mazères, S., Dauvillier, S., Teissié, J., Rols, M.-P., Milon, A., Ecochard, V., et al. (2019). A protein nanocontainer targeting epithelial cancers: rational engineering, biochemical characterization, drug loading and cell delivery. Nanoscale 11, 3248–3260. https://doi.org/10.1039/c8nr10249j.
Kotras, C., Fossépré, M., Roger, M., Gervais, V., Richeter, S., Gerbier, P., Ulrich, S., Surin, M., and Clément, S. (2019). A cationic tetraphenylethene as a light-up supramolecular probe for DNA G-quadruplexes. Front Chem 7, 493. https://doi.org/10.3389/fchem.2019.00493.
Hedger, G., Koldsø, H., Chavent, M., Siebold, C., Rohatgi, R., and Sansom, M.S.P. (2019). Cholesterol interaction sites on the transmembrane domain of the hedgehog signal transducer and class F G protein-coupled receptor smoothened. Structure 27, 549-559.e2. https://doi.org/10.1016/j.str.2018.11.003.
Guillet, V., Bordes, P., Bon, C., Marcoux, J., Gervais, V., Sala, A.J., Dos Reis, S., Slama, N., Mares-Mejía, I., Cirinesi, A.-M., et al. (2019). Structural insights into chaperone addiction of toxin-antitoxin systems. Nat Commun 10, 782. https://doi.org/10.1038/s41467-019-08747-4.
Galant, L., Delverdier, M., Lucas, M.-N., Raymond-Letron, I., Teissié, J., and Tamzali, Y. (2019). Calcium electroporation: the bioelectrochemical treatment of spontaneous equine skin tumors results in a local necrosis. Bioelectrochemistry 129, 251–258. https://doi.org/10.1016/j.bioelechem.2019.05.018.
Ferré, G., Louet, M., Saurel, O., Delort, B., Czaplicki, G., M’Kadmi, C., Damian, M., Renault, P., Cantel, S., Gavara, L., et al. (2019). Structure and dynamics of G protein-coupled receptor-bound ghrelin reveal the critical role of the octanoyl chain. Proc Natl Acad Sci U S A 116, 17525–17530. https://doi.org/10.1073/pnas.1905105116.
Ferré, G., Czaplicki, G., Demange, P., and Milon, A. (2019). Structure and dynamics of dynorphin peptide and its receptor. Vitam Horm 111, 17–47. https://doi.org/10.1016/bs.vh.2019.05.006.
Chabot, S., Bellard, E., Reynes, J.P., Tiraby, G., Teissié, J., and Golzio, M. (2019). Electrotransfer of CpG free plasmids enhances gene expression in skin. Bioelectrochemistry 130, 107343. https://doi.org/10.1016/j.bioelechem.2019.107343.
Augenstreich, J., Haanappel, E., Ferré, G., Czaplicki, G., Jolibois, F., Destainville, N., Guilhot, C., Milon, A., Astarie-Dequeker, C., and Chavent, M. (2019). The conical shape of DIM lipids promotes Mycobacterium tuberculosis infection of macrophages. Proc Natl Acad Sci U S A 116, 25649–25658. https://doi.org/10.1073/pnas.1910368116.
Abraham, M., Apostolov, R., Barnoud, J., Bauer, P., Blau, C., Bonvin, A.M.J.J., Chavent, M., Chodera, J., Čondić-Jurkić, K., Delemotte, L., et al. (2019). Sharing data from molecular simulations. J Chem Inf Model 59, 4093–4099. https://doi.org/10.1021/acs.jcim.9b00665.
2018
Menchon, G., Maveyraud, L., and Czaplicki, G. (2018). Molecular dynamics as a tool for virtual ligand screening. Methods Mol Biol 1762, 145–178. https://doi.org/10.1007/978-1-4939-7756-7_9.
Gervais, V., Muller, I., Mari, P.-O., Mourcet, A., Movellan, K.T., Ramos, P., Marcoux, J., Guillet, V., Javaid, S., Burlet-Schiltz, O., et al. (2018). Small molecule-based targeting of TTD-A dimerization to control TFIIH transcriptional activity represents a potential strategy for anticancer therapy. J Biol Chem 293, 14974–14988. https://doi.org/10.1074/jbc.RA118.003444.
Drożdż, W., Walczak, A., Bessin, Y., Gervais, V., Cao, X.-Y., Lehn, J.-M., Ulrich, S., and Stefankiewicz, A.R. (2018). Multivalent metallosupramolecular assemblies as effective DNA binding agents. Chemistry 24, 10802–10811. https://doi.org/10.1002/chem.201801552.
Drożdż, W., Bessin, Y., Gervais, V., Cao, X.-Y., Lehn, J.-M., Stefankiewicz, A.R., and Ulrich, S. (2018). Switching multivalent DNA complexation using metal-controlled cationic supramolecular self-assemblies. Chemistry 24, 1518–1521. https://doi.org/10.1002/chem.201705630.
Chavent, M., Karia, D., Kalli, A.C., Domański, J., Duncan, A.L., Hedger, G., Stansfeld, P.J., Seiradake, E., Jones, E.Y., and Sansom, M.S.P. (2018). Interactions of the EphA2 kinase domain with PIPs in membranes: implications for receptor function. Structure 26, 1025-1034.e2. https://doi.org/10.1016/j.str.2018.05.003.
Chavent, M., Duncan, A.L., Rassam, P., Birkholz, O., Hélie, J., Reddy, T., Beliaev, D., Hambly, B., Piehler, J., Kleanthous, C., et al. (2018). How nanoscale protein interactions determine the mesoscale dynamic organisation of bacterial outer membrane proteins. Nat Commun 9, 2846. https://doi.org/10.1038/s41467-018-05255-9.
2017
Saurel, O., Iordanov, I., Nars, G., Demange, P., Le Marchand, T., Andreas, L.B., Pintacuda, G., and Milon, A. (2017). Local and global dynamics in Klebsiella pneumoniae Outer membrane protein A in lipid bilayers probed at atomic resolution. J Am Chem Soc 139, 1590–1597. https://doi.org/10.1021/jacs.6b11565.
Duncan, A.L., Reddy, T., Koldsø, H., Hélie, J., Fowler, P.W., Chavent, M., and Sansom, M.S.P. (2017). Protein crowding and lipid complexity influence the nanoscale dynamic organization of ion channels in cell membranes. Sci Rep 7, 16647. https://doi.org/10.1038/s41598-017-16865-6.
Cukier, C.D., Tourdes, A., El-Mazouni, D., Guillet, V., Nomme, J., Mourey, L., Milon, A., Merdes, A., and Gervais, V. (2017). NMR secondary structure and interactions of recombinant human MOZART1 protein, a component of the gamma-tubulin complex. Protein Sci 26, 2240–2248. https://doi.org/10.1002/pro.3282.
Carel, C., Marcoux, J., Réat, V., Parra, J., Latgé, G., Laval, F., Demange, P., Burlet-Schiltz, O., Milon, A., Daffé, M., et al. (2017). Identification of specific posttranslational O-mycoloylations mediating protein targeting to the mycomembrane. Proc Natl Acad Sci U S A 114, 4231–4236. https://doi.org/10.1073/pnas.1617888114.
2016
Menchon, G., Bombarde, O., Trivedi, M., Négrel, A., Inard, C., Giudetti, B., Baltas, M., Milon, A., Modesti, M., Czaplicki, G., et al. (2016). Structure-based virtual ligand screening on the XRCC4/DNA Ligase IV interface. Sci Rep 6, 22878. https://doi.org/10.1038/srep22878.
Hemmann, J.L., Saurel, O., Ochsner, A.M., Stodden, B.K., Kiefer, P., Milon, A., and Vorholt, J.A. (2016). The one-carbon carrier methylofuran from Methylobacterium extorquens AM1 contains a large number of α- and γ-linked glutamic acid residues. J Biol Chem 291, 9042–9051. https://doi.org/10.1074/jbc.M116.714741.
Cukier, C.D., Maveyraud, L., Saurel, O., Guillet, V., Milon, A., and Gervais, V. (2016). The C-terminal region of the transcriptional regulator THAP11 forms a parallel coiled-coil domain involved in protein dimerization. J Struct Biol 194, 337–346. https://doi.org/10.1016/j.jsb.2016.03.010.
Brison, Y., Malbert, Y., Czaplicki, G., Mourey, L., Remaud-Simeon, M., and Tranier, S. (2016). Structural insights into the carbohydrate binding ability of an α-(1→2) branching sucrase from glycoside hydrolase family 70. J Biol Chem 291, 7527–7540. https://doi.org/10.1074/jbc.M115.688796.
2015
Sinnige, T., Houben, K., Pritisanac, I., Renault, M., Boelens, R., and Baldus, M. (2015). Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach. J Biomol NMR 61, 321–332. https://doi.org/10.1007/s10858-014-9891-6.
O’Connor, C., White, K.L., Doncescu, N., Didenko, T., Roth, B.L., Czaplicki, G., Stevens, R.C., Wüthrich, K., and Milon, A. (2015). NMR structure and dynamics of the agonist dynorphin peptide bound to the human kappa opioid receptor. Proc Natl Acad Sci U S A 112, 11852–11857. https://doi.org/10.1073/pnas.1510117112.
Berthoumieu, O., Nguyen, P.H., Castillo-Frias, M.P.D., Ferre, S., Tarus, B., Nasica-Labouze, J., Noël, S., Saurel, O., Rampon, C., Doig, A.J., et al. (2015). Combined experimental and simulation studies suggest a revised mode of action of the anti-Alzheimer disease drug NQ-Trp. Chemistry 21, 12657–12666. https://doi.org/10.1002/chem.201500888.
Bartolami, E., Bessin, Y., Gervais, V., Dumy, P., and Ulrich, S. (2015). Dynamic expression of DNA complexation with self-assembled biomolecular clusters. Angew Chem Int Ed Engl 54, 10183–10187. https://doi.org/10.1002/anie.201504047.
Former lab members have moved to fresh woods, and pastures new
- Matthieu Chavent | CNRS Researcher, IPBS, Toulouse
- Adrien Schahl | Postdoctoral fellow, IPBS, Toulouse
- Virginie Gervais | CNRS Researcher I2BC, Saclay
- Guillaume Ferré | Lecturer, Université de Toulouse III – Paul Sabatier
- Nicolas Richet
- Marie Renault | Lecturer, Université de Toulouse III – Paul Sabatier
- Clément Carel | Masseur physiotherapist, Saint Orens de Gameville
- Guillaume Nars Doctor (endocrinology), CHU Strasbourg
- Parthasarathi Rath | Postdoctoral fellow, Biozentrum Basel, Switzerland
- Iordan Iordanov | Research associate, Semmelweis University, Budapest, Hungary
- Deborah Gater | Lecturer University, College London, United Kingdom
- Hélène Eury | Academic coordinator, Supexam, Rennes
- Olivier Cala | CNRS Research engineer, CRMN, Université de Lyon
- Léa Rougier | Teacher, College Elie Faure, Ste Foy La Grande
- Bruno Vincent | CNRS Engineer, Université de Strasbourg
- Corinne Hazan | General secretary, Artificial and Natural Intelligence Toulouse Institute
- Louic Vermeer | Data scientist, PGGM, Zeist, Netherlands
- Damien Bessiere | CNRS SAP engineer Toulouse
- Sébastien Campagne | INSERM Researcher, IECB, Bordeaux
- Masae Sugawara | Director of Paris Office Japan Science and Technology Agency, Paris
- Olivier Soubias | NIH Staff scientist, Bethesda, MD, USA