Publications 2018

1.  Serra-Batiste, M.; Tolchard, J.; Giusti, F.; Zoonens, M.; Carulla, N. Stabilization of a Membrane-Associated Amyloid-β Oligomer for Its Validation in Alzheimer’s Disease. Front Mol Biosci 2018, 5, 38 https://doi.org/10.3389/fmolb.2018.00038.

2.  Dumas, L.; Zito, F.; Auroy, P.; Johnson, X.; Peltier, G.; Alric, J. Structure-Function Analysis of Chloroplast Proteins via Random Mutagenesis Using Error-Prone PCR. Plant Physiology 2018, pp.01618.2017 https://doi.org/10.1104/pp.17.01618.

3.  Chipot, C.; Dehez, F.; Schnell, J. R.; Zitzmann, N.; Pebay-Peyroula, E.; Catoire, L. J.; Miroux, B.; Kunji, E. R. S.; Veglia, G.; Cross, T. A.; Schanda, P. Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies http://pubs.acs.org.insb.bib.cnrs.fr/doi/full/10.1021/acs.chemrev.7b00570 (accessed Mar 14, 2018).

4.  Casiraghi, M.; Damian, M.; Lescop, E.; Baneres, J.-L.; Catoire, L. J. Illuminating the Energy Landscape of GPCRs: The Key Contribution of Solution-State NMR Associated with Escherichia Coli as an Expression Host. Biochemistry 2018 https://doi.org/10.1021

5.   Dilworth, M. V.; Piel, M. S.; Bettaney, K. E.; Ma, P.; Luo, J.; Sharples, D.; Poyner, D. R.; Gross, S. R.; Moncoq, K.; J F Henderson, P.; Miroux, B.; Bill, R. M. Microbial Expression Systems for Membrane Proteins. Methods 2018 https://doi.org/10.1016/j.ymeth.2018.04.009.

6.   Le Bon, C.; Marconnet, A.; Masscheleyn, S.; Popot, J.-L.; Zoonens, M. Folding and Stabilizing Membrane Proteins in Amphipol A8-35. Methods 2018 https://doi.org/10.1016/j.ymeth.2018.04.012.

7.  Corey, R. A.; Pyle, E.; Allen, W. J.; Watkins, D. W.; Casiraghi, M.; Miroux, B.; Arechaga, I.; Politis, A.; Collinson, I. Specific Cardiolipin-SecY Interactions Are Required for Proton-Motive Force Stimulation of Protein Secretion. Proc. Natl. Acad. Sci. U.S.A. 2018 https://doi.org/10.1073/pnas.1721536115.

8.  Tifrea, D. F.; Pal, S.; Le Bon, C.; Giusti, F.; Popot, J.-L.; Cocco, M. J.; Zoonens, M.; de la Maza, L. M. Co-Delivery of Amphipol-Conjugated Adjuvant with Antigen, and Adjuvant Combinations, Enhance Immune Protection Elicited by a Membrane Protein-Based Vaccine against a Mucosal Challenge with Chlamydia. Vaccine 2018, 36 (45), 6640–6649 https://doi.org/10.1016/j.vaccine.2018.09.055.

9.   Vakirlis N, Hebert A S, Opulente D A, Achaz G, Hittinger C T, Fischer G, Coon J J and Lafontaine I (2018) A Molecular Portrait of De Novo Genes in Yeasts. Mol Biol Evol, 35(3):631-645

10.   Longatte G, Sayegh A, Delacotte J, Rappaport F, Wollman F-A, Guille-Collignon M and Lemaître F (2018) Investigation of photocurrents resulting from a living unicellular algae suspension with quinones over time. Chemical Science, 9(43):8271-8281

11.   Liponska A, Jamalli A, Kuras R, Suay L, Garbe E, Wollman F-A, Laalami S and Putzer H (2018) Tracking the elusive 5' exonuclease activity of Chlamydomonas reinhardtii RNase J. Plant Mol Biol, 96(6):641-653

12.   Buchert F, Hamon M, Gabelein P, Scholz M, Hippler M and Wollman F-A (2018) The labile interactions of cyclic electron flow effector proteins. J Biol Chem, 293(45):17559-17573

13.   Nawrocki W J, Buchert F, Joliot P, Rappaport F, Bailleul B and Wollman F-A (2019) Chlororespiration Controls Growth Under Intermittent Light. Plant Physiol, 179(2):630-639

14.   Abdelkrim, Y.Z., Harigua-Souiai, E., Barhoumi, M., Banroques, J., Blondel, A., Guizani, I., Tanner, N.K. (2018) The steroid derivative 6-aminocholestanol inhibits the DEAD-box helicase eIF4A (LieIF4A) from the Trypanosomatid parasite Leishmania by perturbing the RNA and ATP binding sites. Mol Biochem Parasit. 226: 9-19. https://doi.org/10.1016/j.molbiopara.2018.10.001.

15.    J. Esque, M.S.P. Sansom, M. Baaden, C. Oguey (2018) Analyzing protein topology based on Laguerre tessellation of a pore-traversing water network. Sci Rep 20188: 13540

16.    Mazur, A.K. and Gladyshev, E. (2018) Partition of repeat-induced point mutations reveals structural aspects of homologous DNA-DNA pairing. Biophys. J., 115, 605-615. https://www.ncbi.nlm.nih.gov/pubmed/30086830

17.    M. E. Guerin, G. Stirnemann, and D. Giganti, Conformational entropy of a single peptide controlled under force governs protease recognition and catalysis, Proc. Natl. Acad. Sci. USA 115, 11525-30 (2018)

18.    G. Stirnemann, E. Duboué-Dijon and D. Laage, Ab Initio Simulations of Water Dynamics in Aqueous TMAO Solutions: Temperature and Concentration Effects, J. Phys. Chem. B 121, 11189-11197 (2018)

19.    Reza Salari, Thomas Joseph, Ruchi Lohia, Jérôme Hénin, and Grace Brannigan, A streamlined, general approach for computing ligand binding free energies and its application to GPCR-bound cholesterol, J. Chem. Theo. Comput. 14 (12), pp 6560–6573 (2018)

20.    O. Languin-Cattoën, S. Melchionna, P. Derreumaux, G. Stirnemann, and F. Sterpone, "Three Weaknesses for Three Perturbations: Comparing Protein Unfolding Under Shear, Force, and Thermal Stresses",  J. Phys. Chem. B (2018), 122 (50), pp 11922–11930

21.    M. Bernaschi, S. Melchionna,P. Derreumaux, F. Sterpone, S. Succi, "Multilevel Lattice Boltzmann-Particle Dynamics simulations at the Physics-Biology interface", J. Phys. (2018), 1136

22.    M. Kinoshita, Y. Lin, I. Dai, M. Okumura, N. Markova, J. E. Ladbury, F Sterpone  and  Y-Ho Lee, “Energy landscape of polymorphic amyloid generation of β2-microglobulin revealed by calorimetry”, (2018) Chem. Commun., 2018,54, 7995-7998

23.    Longatte, G., Sayegh, A., Delacotte, J., Rappaport, F., Wollman, F.-A., Guille Collignon, M. and Lemaître, F. (2018) Investigation of Photocurrents Resulting from Living Unicellular Algae Suspension with Quinones over Time. Chemical Science. <http://dx.doi.org/10.1039/C8SC03058H>http://dx.doi.org/10.1039/C8SC03058H

24.    Cohen MM.* and Tareste D.* Recent insights into the structure and function of Mitofusins in mitochondrial fusion. (2018) . F1000 Research. 7 (F1000 Faculty Rev):1983. *Corresponding authors

25.    Shai N, Yifrach E, van Roermund CWT, Cohen N, Bibi C, IJlst L, Cavellini L, Meurisse J, Schuster R, Zada L, Mari MC, Reggiori FM, Hughes AL, Escobar-Henriques M, Cohen MM, Waterham HR, Wanders RJA, Schuldiner M, Zalckvar E. Systematic mapping of contact sites reveals tethers and a function for the peroxisome-mitochondria contact. Nat Commun. 2018 May 2;9(1):1761. doi: 10.1038/s41467-018-03957-8.

26.    Lemaire SD, Tedesco D, Crozet P, Michelet L, Fermani S, Zaffagnini M, Henri J (2018) Crystal Structure of Chloroplastic Thioredoxin f2 from Chlamydomonas reinhardtii Reveals Distinct Surface Properties. Antioxidants 7, E171.

27.    Crozet P, Navarro FJ, Willmund F, Mehrshahi P, Bakowski K, Lauersen KJ, Pérez-Pérez M-E, Auroy P, Gorchs Rovira A, Sauret-Gueto S, Niemeyer J, Spaniol B, Theis J, Trösch R, Westrich L-D, Vavitsas K, Baier T, Hübner W, de Carpentier F, Cassarini M, Danon A, Henri J, Marchand CH, de Mia M, Sarkissian K, Baulcombe DC, Peltier G, Crespo J-L, Kruse O, Jensen P-E, Schroda M#, Smith AG#, Lemaire SD# (2018) Birth of a Photosynthetic Chassis: A MoClo Toolkit Enabling Synthetic Biology in the Microalga Chlamydomonas reinhardtii. ACS Synth. Biol. 7, 9, 2074-2086. Supp Tables and Figures #corresponding authors

28.    Maes A, Martinez X, Druart K, Laurent B, Guégan S, Marchand CH, Lemaire SD#, Baaden M# (2018) MinOmics, an Integrative and Immersive Tool for Multi-Omics Analysis. J. Integr Bioinform. 15(2). # Corresponding authors.

29.     Zhan Y, Marchand CH, Maes A, Mauries A, Sun Y, Dhaliwal JS, Uniacke J, Arragain S, Jiang H, Gold ND, Martin VJJ, Lemaire SD#, Zerges W# (2018). Pyrenoid functions revealed by proteomics in Chlamydomonas reinhardtii. PLoS One. 13(2):e0185039. Supp
#Corresponding authors

30.     Henri J, Chagot ME, Bourguet M, Abel Y, Terral G, Maurizy C, Aigueperse C, Georgescauld F, Vandermoere F, Saint-Fort R, Behm-Ansmant I, Charpentier B, Pradet-Balade B, Verheggen C, Bertrand E, Meyer P#, Cianférani S#, Manival X#, Quinternet M#. Deep Structural Analysis of RPAP3 and PIH1D1, Two Components of the HSP90 Co-chaperone R2TP Complex. Structure. 2018 Sep 4;26(9):1196-1209. doi: 10.1016/j.str.2018.06.002. # corresponding authors

31.     Coutelier H*, Xu Z*#, Morisse MC,  Lhuillier-Akakpo M, Pelet S, Charvin G, Dubrana K and TeixeiraMT#. (2018). Adaptation to DNA damage checkpoint in senescent telomerase-negative cells promotes genome instability. Genes & Dev. 32:1–15. [Supp]

32.     Zhan, Y., Marchand, C.H., Maes, A., Mauries, A., Sun, Y., Dhaliwal, J.S., Uniacke, J., Arragain, S., Jiang, H., Gold, N.D. et al. (2018) Pyrenoid functions revealed by proteomics in Chlamydomonas reinhardtii. PLoS One, 13, e0185039. http://www.ncbi.nlm.nih.gov/pubmed/29481573

33.     Wang, Y.J., Rico-Lastres, P., Lezamiz, A., Mora, M., Solsona, C., Stirnemann, G. and Garcia-Manyes, S. (2018) DNA Binding Induces a Nanomechanical Switch in the RRM1 Domain of TDP-43. J Phys Chem Lett, 9, 3800-3807. http://www.ncbi.nlm.nih.gov/pubmed/29924934

34.     Wang, X., Wisser, F.M., Canivet, J., Fontecave, M. and Mellot-Draznieks, C. (2018) Immobilization of a Full Photosystem in the Large-Pore MIL-101 Metal-Organic Framework for CO2 reduction. ChemSusChem. https://www.ncbi.nlm.nih.gov/pubmed/29978953

35.     Vakirlis, N., Hebert, A.S., Opulente, D.A., Achaz, G., Hittinger, C.T., Fischer, G., Coon, J.J. and Lafontaine, I. (2018) A Molecular Portrait of De Novo Genes in Yeasts. Mol Biol Evol, 35, 631-645. http://www.ncbi.nlm.nih.gov/pubmed/29220506

36.     Trellet, M., Ferey, N., Flotynski, J., Baaden, M. and Bourdot, P. (2018) Semantics for an Integrative and Immersive Pipeline Combining Visualization and Analysis of Molecular Data. J Integr Bioinform, 15. http://www.ncbi.nlm.nih.gov/pubmed/29982236

37.     Sutherland, G.A., Grayson, K.J., Adams, N.B.P., Mermans, D.M.J., Jones, A.S., Robertson, A.J., Auman, D.B., Brindley, A.A., Sterpone, F., Tuffery, P. et al. (2018) Probing the quality control mechanism of the Escherichia coli twin-arginine translocase with folding variants of a de novo-designed heme protein. J Biol Chem, 293, 6672-6681. http://www.ncbi.nlm.nih.gov/pubmed/29559557

38.     Sterpone, F., Doutreligne, S., Tran, T.T., Melchionna, S., Baaden, M., Nguyen, P.H. and Derreumaux, P. (2018) Multi-scale simulations of biological systems using the OPEP coarse-grained model. Biochem Biophys Res Commun, 498, 296-304. http://www.ncbi.nlm.nih.gov/pubmed/28917842

39.     Sterpone, F., Derreumaux, P. and Melchionna, S. (2018) Molecular Mechanism of Protein Unfolding under Shear: A Lattice Boltzmann Molecular Dynamics Study. J Phys Chem B, 122, 1573-1579. http://www.ncbi.nlm.nih.gov/pubmed/29328657

40.     Sommer, C., Rumpel, S., Roy, S., Fares, C., Artero, V., Fontecave, M., Reijerse, E. and Lubitz, W. (2018) Spectroscopic investigations of a semi-synthetic [FeFe] hydrogenase with propane di-selenol as bridging ligand in the binuclear subsite: comparison to the wild type and propane di-thiol variants. J Biol Inorg Chem. http://www.ncbi.nlm.nih.gov/pubmed/29627860

41.     Shai, N., Yifrach, E., van Roermund, C.W.T., Cohen, N., Bibi, C., Ijlst, L., Cavellini, L., Meurisse, J., Schuster, R., Zada, L. et al. (2018) Systematic mapping of contact sites reveals tethers and a function for the peroxisome-mitochondria contact. Nature Communications, In Press.

42.     Serra-Batiste, M., Tolchard, J., Giusti, F., Zoonens, M. and Carulla, N. (2018) Stabilization of a Membrane-Associated Amyloid-beta Oligomer for Its Validation in Alzheimer's Disease. Front Mol Biosci, 5, 38. http://www.ncbi.nlm.nih.gov/pubmed/29725595

43.     Sacquin-Mora, S. (2018) Mechanical variations in proteins with large-scale motions highlight the formation of structural locks. J Struct Biol. http://www.ncbi.nlm.nih.gov/pubmed/29852221

44.     Roper, J.C., Mitrossilis, D., Stirnemann, G., Waharte, F., Brito, I., Fernandez-Sanchez, M.E., Baaden, M., Salamero, J. and Farge, E. (2018) The major beta-catenin/E-cadherin junctional binding site is a primary molecular mechano-transductor of differentiation in vivo. Elife, 7. https://www.ncbi.nlm.nih.gov/pubmed/30024850

45.     Perales-Calvo, J., Giganti, D., Stirnemann, G. and Garcia-Manyes, S. (2018) The force-dependent mechanism of DnaK-mediated mechanical folding. Sci Adv, 4, eaaq0243. http://www.ncbi.nlm.nih.gov/pubmed/29487911

46.     Nguyen, P.H., Del Castillo-Frias, M.P., Berthoumieux, O., Faller, P., Doig, A.J. and Derreumaux, P. (2018) Amyloid-beta/Drug Interactions from Computer Simulations and Cell-Based Assays. J Alzheimers Dis, 64, S659-S672. https://www.ncbi.nlm.nih.gov/pubmed/29562512

47.     Murail, S., Vasiliu, T., Neamtu, A., Barboiu, M., Sterpone, F. and Baaden, M. (2018) Water permeation across artificial I-quartet membrane channels: from structure to disorder. Faraday Discuss. https://www.ncbi.nlm.nih.gov/pubmed/29974103

48.     Mouhand, A., Belfetmi, A., Catala, M., Larue, V., Zargarian, L., Brachet, F., Gorelick, R.J., Van Heijenoort, C., Mirambeau, G., Barraud, P. et al. (2018) Modulation of the HIV nucleocapsid dynamics finely tunes its RNA-binding properties during virion genesis. Nucleic Acids Res. http://www.ncbi.nlm.nih.gov/pubmed/29986076

49.     Maikova, A., Peltier, J., Boudry, P., Hajnsdorf, E., Kint, N., Monot, M., Poquet, I., Martin-Verstraete, I., Dupuy, B. and Soutourina, O. (2018) Discovery of new type I toxin-antitoxin systems adjacent to CRISPR arrays in Clostridium difficile. Nucleic Acids Res. http://www.ncbi.nlm.nih.gov/pubmed/29529286

50.     Maes, A., Martinez, X., Druart, K., Laurent, B., Guegan, S., Marchand, C.H., Lemaire, S.D. and Baaden, M. (2018) MinOmics, an Integrative and Immersive Tool for Multi-Omics Analysis. J Integr Bioinform, 15. http://www.ncbi.nlm.nih.gov/pubmed/29927748

51.     Longatte, G., Sayegh, A., Delacotte, J., Rappaport, F., Wollman, F.-A., Guille Collignon, M. and Lemaître, F. (2018) Investigation of Photocurrents Resulting from Living Unicellular Algae Suspension with Quinones over Time. Chemical Science. http://dx.doi.org/10.1039/C8SC03058H

52.     Liponska, A., Jamalli, A., Kuras, R., Suay, L., Garbe, E., Wollman, F.A., Laalami, S. and Putzer, H. (2018) Tracking the elusive 5' exonuclease activity of Chlamydomonas reinhardtii RNase J. Plant Mol Biol, 96, 641-653. http://www.ncbi.nlm.nih.gov/pubmed/29600502

53.     Le Bon, C., Marconnet, A., Masscheleyn, S., Popot, J.L. and Zoonens, M. (2018) Folding and stabilizing membrane proteins in amphipol A8-35. Methods. http://www.ncbi.nlm.nih.gov/pubmed/29678587

54.     Lagarde, N., Carbone, A. and Sacquin-Mora, S. (2018) Hidden partners: Using cross-docking calculations to predict binding sites for proteins with multiple interactions. Proteins, 86, 723-737. http://www.ncbi.nlm.nih.gov/pubmed/29664226

55.     Kocsis, I., Sorci, M., Vanselous, H., Murail, S., Sanders, S.E., Licsandru, E., Legrand, Y.M., van der Lee, A., Baaden, M., Petersen, P.B. et al. (2018) Oriented chiral water wires in artificial transmembrane channels. Sci Adv, 4, eaao5603. http://www.ncbi.nlm.nih.gov/pubmed/29582016

56.     Kim, R., Kanamaru, S., Mikawa, T., Prévost, C., Ishii, K., Ito, K., Uchiyama, S., Oda, M., Iwasaki, H., Kim, S.K. et al. (2018) RecA requires two molecules of Mg2+ ions for its optimal strand exchange activity in vitro. Nucleic Acids Research, 46, 2548-2559. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5861410/pdf/gky048.pdf

57.     Joseph, T.T. and Henin, J. (2018) Molecular Mechanics Parameterization of Anesthetic Molecules. Methods Enzymol, 602, 61-76. http://www.ncbi.nlm.nih.gov/pubmed/29588041

58.     Hitaishi, V., Clement, R., Bourassin, N., Baaden, M., de Poulpiquet, A., Sacquin-Mora, S., Ciaccafava, A. and Lojou, E. (2018) Controlling Redox Enzyme Orientation at Planar Electrodes. Catalysts, 8, 192. http://www.mdpi.com/2073-4344/8/5/192

59.     Harigua-Souiai, E., Abdelkrim, Y.Z., Bassoumi-Jamoussi, I., Zakraoui, O., Bouvier, G., Essafi-Benkhadir, K., Banroques, J., Desdouits, N., Munier-Lehmann, H., Barhoumi, M. et al. (2018) Identification of novel leishmanicidal molecules by virtual and biochemical screenings targeting Leishmania eukaryotic translation initiation factor 4A. PLoS Negl Trop Dis, 12, e0006160. http://www.ncbi.nlm.nih.gov/pubmed/29346371

60.     Fogeron, T., Todorova, T.K., Porcher, J.-P., Gomez-Mingot, M., Chamoreau, L.-M., Mellot-Draznieks, C., Li, Y. and Fontecave, M. (2018) A Bioinspired Nickel(bis-dithiolene) Complex as a Homogeneous Catalyst for Carbon Dioxide Electroreduction. ACS Catalysis, 8, 2030-2038. https://pubs.acs.org/doi/10.1021/acscatal.7b03383

61.     Elbahnsi, A., Retureau, R., Baaden, M., Hartmann, B. and Oguey, C. (2018) Holding the Nucleosome Together: A Quantitative Description of the DNA-Histone Interface in Solution. J Chem Theory Comput, 14, 1045-1058. http://www.ncbi.nlm.nih.gov/pubmed/29262675

62.     El Mishri, E.S., Boutant, E., Mouhand, A., Larue, V., Thomas, A., Richert, L., Vivet-Boudout, V., Mély, Y., Tisné, C., Muriaux, D. et al. (2018) The NC domain and the p6 PTAP motif of HIV-1 Gag both contribute to the interaction of Gag with the cellular TSG101-UEV domain. Biochem Biophys Acta, In press.

63.    Durand, S. and Condon, C. (2018) RNases and Helicases in Gram-Positive Bacteria. Microbiol Spectr, 6. http://www.ncbi.nlm.nih.gov/pubmed/29651979

64.     Dumas, L., Zito, F., Auroy, P., Johnson, X., Peltier, G. and Alric, J. (2018) Structure-Function Analysis of Chloroplast Proteins via Random Mutagenesis Using Error-Prone PCR. Plant Physiol, 177, 465-475. http://www.ncbi.nlm.nih.gov/pubmed/29703866

65.     Dilworth, M.V., Piel, M.S., Bettaney, K.E., Ma, P., Luo, J., Sharples, D., Poyner, D.R., Gross, S.R., Moncoq, K., Henderson, P.J.F. et al. (2018) Microbial expression systems for membrane proteins. Methods. http://www.ncbi.nlm.nih.gov/pubmed/29656078

66.     Dalier, F., Dubacheva, G.V., Coniel, M., Zanchi, D., Galtayries, A., Piel, M., Marie, E. and Tribet, C. (2018) Mixed Copolymer Adlayers Allowing Reversible Thermal Control of Single Cell Aspect Ratio. ACS Appl Mater Interfaces, 10, 2253-2258. http://www.ncbi.nlm.nih.gov/pubmed/29314825

67.     Crozet, P., Navarro, F.J., Willmund, F., Mehrshahi, P., Bakowski, K., Lauersen, K.J., Perez-Perez, M.E., Auroy, P., Gorchs Rovira, A., Sauret-Gueto, S. et al. (2018) Birth of a photosynthetic chassis: a MoClo toolkit enabling synthetic biology in the microalga Chlamydomonas reinhardtii. ACS Synth Biol. https://www.ncbi.nlm.nih.gov/pubmed/30165733

68.     Corey, R.A., Pyle, E., Allen, W.J., Watkins, D.W., Casiraghi, M., Miroux, B., Arechaga, I., Politis, A. and Collinson, I. (2018) Specific cardiolipin-SecY interactions are required for proton-motive force stimulation of protein secretion. Proc Natl Acad Sci U S A, 115, 7967-7972. https://www.ncbi.nlm.nih.gov/pubmed/30012626

69.     Condon, C., Piton, J. and Braun, F. (2018) Distribution of the ribosome associated endonuclease Rae1 and the potential role of conserved amino acids in codon recognition. RNA Biol, 1-13. http://www.ncbi.nlm.nih.gov/pubmed/29557713

70.     Chipot, C., Dehez, F., Schnell, J.R., Zitzmann, N., Pebay-Peyroula, E., Catoire, L.J., Miroux, B., Kunji, E.R.S., Veglia, G., Cross, T.A. et al. (2018) Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies. Chem Rev, 118, 3559-3607. http://www.ncbi.nlm.nih.gov/pubmed/29488756

71.     Casiraghi, M., Damian, M., Lescop, E., Baneres, J.L. and Catoire, L.J. (2018) Illuminating the Energy Landscape of GPCRs: The Key Contribution of Solution-State NMR Associated with Escherichia coli as an Expression Host. Biochemistry, 57, 2297-2307. http://www.ncbi.nlm.nih.gov/pubmed/29607648

72.     Caserta, G., Papini, C., Adamska-Venkatesh, A., Pecqueur, L., Sommer, C., Reijerse, E., Lubitz, W., Gauquelin, C., Meynial-Salles, I., Pramanik, D. et al. (2018) Engineering an [FeFe]-Hydrogenase: Do Accessory Clusters Influence O2 Resistance and Catalytic Bias? J Am Chem Soc, 140, 5516-5526. http://www.ncbi.nlm.nih.gov/pubmed/29595965

73.     Brosse, A. and Guillier, M. (2018) Bacterial small RNAs in mixed regulatory networks. Microbiol. Spectrum In Press.

74.     Bou-Nader, C., Bregeon, D., Pecqueur, L., Fontecave, M. and Hamdane, D. (2018) Electrostatic Potential in the tRNA Binding Evolution of Dihydrouridine Synthases. Biochemistry. https://www.ncbi.nlm.nih.gov/pubmed/30149704

75.     Bou-Nader, C., Barraud, P., Pecqueur, L., Sacquin-Mora, S., Pérez, J., Velours, C., Fontecave, M., Tisné, C. and Hamdane, D. (2018) Molecular basis for transfer RNA substrate recognition by human dihydrouridine synthase. Nucleic Acids Res, In press.

76.     Boniello, G., Tribet, C., Marie, E., Croquette, V. and Zanchi, D. (2018) Rolling and Ageing in T-Ramp Soft Adhesion. Phys Rev. E 97, 012609.

77.     Berkovich, R., Fernandez, V.I., Stirnemann, G., Valle-Orero, J. and Fernandez, J.M. (2018) Segmentation and the Entropic Elasticity of Modular Proteins. J Phys Chem Lett, 9, 4707-4713. https://www.ncbi.nlm.nih.gov/pubmed/30058807

78.     Beedle, A.E.M., Mora, M., Davis, C.T., Snijders, A.P., Stirnemann, G. and Garcia-Manyes, S. (2018) Forcing the reversibility of a mechanochemical reaction. Nat Commun, 9, 3155. https://www.ncbi.nlm.nih.gov/pubmed/30089863

79.     Baumgardt, K., Gilet, L., Figaro, S. and Condon, C. (2018) The essential nature of YqfG, a YbeY homologue required for 3' maturation of Bacillus subtilis 16S ribosomal RNA is suppressed by deletion of RNase R. Nucleic Acids Res. http://www.ncbi.nlm.nih.gov/pubmed/29873764

80.     Barroso da Silva, F.L., Derreumaux, P. and Pasquali, S. (2018) Protein-RNA complexation driven by the charge regulation mechanism. Biochem Biophys Res Commun, 498, 264-273. http://www.ncbi.nlm.nih.gov/pubmed/28709871

81.     Baaden, M., Delalande, O., Ferey, N., Pasquali, S., Waldispuhl, J. and Taly, A. (2018) Ten simple rules to create a serious game, illustrated with examples from structural biology. PLoS Comput Biol, 14, e1005955. http://www.ncbi.nlm.nih.gov/pubmed/29518072

82.     Angius, F., Ilioaia, O., Amrani, A., Suisse, A., Rosset, L., Legrand, A., Abou-Hamdan, A., Uzan, M., Zito, F. and Miroux, B. (2018) A novel regulation mechanism of the T7 RNA polymerase based expression system improves overproduction and folding of membrane proteins. Sci Rep, 8, 8572. http://www.ncbi.nlm.nih.gov/pubmed/29872064

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