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Maffeis, Viviana et al. (2024) ‘Advancing the Design of Artificial Nano-organelles for Targeted Cellular Detoxification of Reactive Oxygen Species’, Nano Letters, 24(9), pp. 2698–2704. Available at: https://doi.org/10.1021/acs.nanolett.3c03888.
Maharana, Jagannath et al. (2024) ‘Molecular insights into atypical modes of b-arrestin interaction with seven transmembrane receptors’, Science, 383(6678), pp. 101–108. Available at: https://doi.org/10.1126/science.adj3347.
Seyfizadeh, Narges et al. (2024) ‘Development of a highly effective combination monoclonal antibody therapy against Herpes simplex virus’, Journal of Biomedical Science, 31. Available at: https://doi.org/10.1186/s12929-024-01045-2.
Yadav, Manish K. et al. (2024) ‘Structure-guided engineering of biased-agonism in the human niacin receptor via single amino acid substitution’, Nature Communications, 15. Available at: https://doi.org/10.1038/s41467-024-46239-2.
Belluati, A. et al. (2023) ‘Artificial cell synthesis using biocatalytic polymerization-induced self-assembly’, Nature Chemistry, null. Available at: https://doi.org/10.1038/s41557-023-01391-y.
Biou, Valérie et al. (2023) ‘Author Correction: Structural and molecular determinants for the interaction of ExbB from Serratia marcescens and HasB, a TonB paralog’, Communications biology, 6(1), p. 67. Available at: https://doi.org/10.1038/s42003-022-04256-1.
Kipfer, E.T. et al. (2023) ‘Rapid cloning-free mutagenesis of new SARS-CoV-2 variants using a novel reverse genetics platform’, eLife, 12. Available at: https://doi.org/10.7554/elife.89035.
Maharana, J. et al. (2023) ‘Structural snapshots uncover a key phosphorylation motif in GPCRs driving β-arrestin activation’, Molecular Cell, 83, pp. 2091–2107.e7. Available at: https://doi.org/10.1016/j.molcel.2023.04.025.
Najer, A. et al. (2023) ‘Differences in Human Plasma Protein Interactions between Various Polymersomes and Stealth Liposomes as Observed by Fluorescence Correlation Spectroscopy’, Macromolecular Bioscience, 23. Available at: https://doi.org/10.1002/mabi.202200424.
Saunders, C. et al. (2023) ‘Revealing Population Heterogeneity in Vesicle-Based Nanomedicines Using Automated, Single Particle Raman Analysis’, ACS Nano, 17, pp. 11713–11728. Available at: https://doi.org/10.1021/acsnano.3c02452.
Yadav, M.K. et al. (2023) ‘Molecular basis of anaphylatoxin binding, activation, and signaling bias at complement receptors’, Cell, 186, pp. 4956–4973.e21. Available at: https://doi.org/10.1016/j.cell.2023.09.020.
Biou, Valérie et al. (2022) ‘Structural and molecular determinants for the interaction of ExbB from Serratia marcescens and HasB, a TonB paralog’, Communications biology, 5(1), p. 355. Available at: https://doi.org/10.1038/s42003-022-03306-y.
Botte, Mathieu et al. (2022) ‘Cryo-EM structures of a LptDE transporter in complex with Pro-macrobodies offer insight into lipopolysaccharide translocation’, Nature Communications, 13(1), p. 1826. Available at: https://doi.org/10.1038/s41467-022-29459-2.
Müller, Christoph et al. (2022) ‘Molecular interplay of an assembly machinery for nitrous oxide reductase’, Nature, 608(7923), pp. 626–631. Available at: https://doi.org/10.1038/s41586-022-05015-2.
Rifaie-Graham, Omar et al. (2022) ‘Photoswitchable gating of non-equilibrium enzymatic feedback in chemically communicating polymersome nanoreactors’, Nature Chemistry, 15(1), pp. 110–118. Available at: https://doi.org/10.1038/s41557-022-01062-4.
Carvalho, Vanessa et al. (2021) ‘The cytoplasmic domain of the AAA+ protease FtsH is tilted with respect to the membrane to facilitate substrate entry’, Journal of Biological Chemistry, 296, p. 100029. Available at: https://doi.org/10.1074/jbc.ra120.014739.
Horváthová, Lenka et al. (2021) ‘Analysis of diverse eukaryotes suggests the existence of an ancestral mitochondrial apparatus derived from the bacterial type II secretion system’, Nature Communications, 12(1), p. 2947. Available at: https://doi.org/10.1038/s41467-021-23046-7.
Rifaie-Graham, Omar et al. (2021) ‘Shear Stress-Responsive Polymersome Nanoreactors Inspired by the Marine Bioluminescence of Dinoflagellates’, Angewandte Chemie International Edition, 60(2), pp. 904–909. Available at: https://doi.org/10.1002/anie.202010099.
Acebrón, Iván et al. (2020) ‘Structural basis of Focal Adhesion Kinase activation on lipid membranes’, The EMBO Journal, 39(19), p. e104743. Available at: https://doi.org/10.15252/embj.2020104743.
Belluati, Andrea et al. (2020) ‘How Do the Properties of Amphiphilic Polymer Membranes Influence the Functional Insertion of Peptide Pores?’, Biomacromolecules, 21(2), pp. 701–715. Available at: https://doi.org/10.1021/acs.biomac.9b01416.
Dautin, Nathalie et al. (2020) ‘Role of the unique, non-essential phosphatidylglycerol::prolipoprotein diacylglyceryl transferase (Lgt) in; Corynebacterium glutamicum;’, Microbiology, 166(8), pp. 759–776. Available at: https://doi.org/10.1099/mic.0.000937.
Le Guennec, Maeva et al. (2020) ‘A helical inner scaffold provides a structural basis for centriole cohesion’, Science Advances, 6(7), p. eaaz4137. Available at: https://doi.org/10.1126/sciadv.aaz4137.
Liu, Juan et al. (2020) ‘DNA-directed arrangement of soft synthetic compartments and their behavior in vitro and in vivo’, Nanoscale, 12(17), pp. 9786–9799. Available at: https://doi.org/10.1039/d0nr00361a.
Sears, Avery E. et al. (2020) ‘Single particle cryo-EM of the complex between interphotoreceptor retinoid-binding protein and a monoclonal antibody’, FASEB Journal, 34(10), pp. 13918–13934. Available at: https://doi.org/10.1096/fj.202000796rr.
Gulati, S. et al. (2019) ‘EMD-9297: Cryo-EM structure of phosphodiesterase 6’, Electron Microscopy Data Bank. Edited by Gulati, S.; Palczewski, K.; Kovacik, L.; Stahlberg, H. (Electron Microscopy Data Bank).
Le Guennec, M. et al. (2019) ‘EMD-4929: Junction between microtubules triplets of in situ Chlamydomonas reinardtii centriole - inner core region’, Electron Microscopy Data Bank.
Le Guennec, M. et al. (2019) ‘EMD-4930: Microtubules triplet of in situ Chlamydomonas reinhardtii centriole - inner core region’, Electron Microscopy Data Bank.
Reis, Ana C. et al. (2019) ‘Comparative genomics reveals a novel genetic organization of the sad cluster in the sulfonamide-degrader “Candidatus Leucobacter sulfamidivorax” strain GP’, BMC genomics, 20(1), p. 885. Available at: https://doi.org/10.1186/s12864-019-6206-z.
Righetto, Ricardo D. et al. (2019) ‘Retrieving high-resolution information from disordered 2D crystals by single-particle cryo-EM’, Nature Communications, 10(1), p. 1722. Available at: https://doi.org/10.1038/s41467-019-09661-5.
Arnold, Stefan A. et al. (2018) ‘Miniaturizing EM Sample Preparation: Opportunities, Challenges, and ‘Visual Proteomics’’, Proteomics, 18(5-6), p. 1700176. Available at: https://doi.org/10.1002/pmic.201700176.
Biyani, Nikhil et al. (2018) ‘Image processing techniques for high-resolution structure determination from badly ordered 2D crystals’, Journal of Structural Biology, 203(2), pp. 120–134. Available at: https://doi.org/10.1016/j.jsb.2018.03.013.
Hunkeler, Moritz et al. (2018) ‘Structural basis for regulation of human acetyl-CoA carboxylase’, Nature, 558(7710), pp. 470–474. Available at: https://doi.org/10.1038/s41586-018-0201-4.
Kowal, Julia et al. (2018) ‘High-Resolution Cryoelectron Microscopy Structure of the Cyclic Nucleotide-Modulated Potassium Channel MloK1 in a Lipid Bilayer’, Structure, 26(1), pp. 20–27.e3. Available at: https://doi.org/10.1016/j.str.2017.11.012.
Rifaie-Graham, Omar et al. (2018) ‘Wavelength-Selective Light-Responsive DASA-Functionalized Polymersome Nanoreactors’, Journal of the American Chemical Society, 140(25), pp. 8027–8036. Available at: https://doi.org/10.1021/jacs.8b04511.
Schmidli, Claudio et al. (2018) ‘Miniaturized Sample Preparation for Transmission Electron Microscopy’, Journal of Visualized Experiments, (137), p. e57310. Available at: https://doi.org/10.3791/57310.
Subramanian, Rohit H. et al. (2018) ‘Self-Assembly of a Designed Nucleoprotein Architecture through Multimodal Interactions’, ACS Central Science, 4(11), pp. 1578–1586. Available at: https://doi.org/10.1021/acscentsci.8b00745.
Torrisi, L. et al. (2018) ‘Gold nanoparticles produced by laser ablation in water and in graphene oxide suspension’, Philosophical magazine, 98(24), pp. 2205–2220. Available at: https://doi.org/10.1080/14786435.2018.1478147.
Guilvout, Ingrid et al. (2017) ‘Prepore Stability Controls Productive Folding of the BAM-independent Multimeric Outer Membrane Secretin PulD’, Journal of Biological Chemistry, 292(1), pp. 328–338. Available at: https://doi.org/10.1074/jbc.m116.759498.
Rheinberger, Jan et al. (2017) ‘Two-dimensional crystallization of the mouse serotonin 5-HT3A receptor’, Micron, 92, pp. 19–24. Available at: https://doi.org/10.1016/j.micron.2016.10.004.
Ruan, Yi et al. (2017) ‘Direct visualization of glutamate transporter elevator mechanism by high-speed AFM’, Proceedings of the National Academy of Sciences of the United States of America, 114(7), pp. 1584–1588. Available at: https://doi.org/10.1073/pnas.1616413114.
Sejwal, Kushal et al. (2017) ‘Proteoliposomes - a system to study membrane proteins under buffer gradients by cryo-EM’, Nanotechnology Reviews, 6(1), pp. 57–74. Available at: https://doi.org/10.1515/ntrev-2016-0081.
Sejwal, Kushal et al. (2017) ‘Cryo-EM analysis of homodimeric full-length LRRK2 and LRRK1 protein complexes’, Scientific Reports, 7(1), p. 8667. Available at: https://doi.org/10.1038/s41598-017-09126-z.
Arnold, Stefan A. et al. (2016) ‘Total Sample Conditioning and Preparation of Nanoliter Volumes for Electron Microscopy’, ACS Nano, 10(5), pp. 4981–8. Available at: https://doi.org/10.1021/acsnano.6b01328.
Ayciriex, Sophie et al. (2016) ‘The lipidome associated with the γ-secretase complex is required for its integrity and activity’, Biochemical Journal, 473(3), pp. 321–334. Available at: https://doi.org/10.1042/bj20150448.
Grzegorzewicz, Anna E. et al. (2016) ‘Assembling of the Mycobacterium tuberculosis Cell Wall Core’, Journal of Biological Chemistry, 291(36), pp. 18867–79. Available at: https://doi.org/10.1074/jbc.m116.739227.
Hagmann, Anna et al. (2016) ‘Hybrid Structure of a Dynamic Single-Chain Carboxylase from Deinococcus radiodurans’, Structure, 24(8), pp. 1227–1236. Available at: https://doi.org/10.1016/j.str.2016.06.001.
Hunkeler, Moritz et al. (2016) ‘The dynamic organization of fungal acetyl-CoA carboxylase’, Nature Communications, 7, p. 11196. Available at: https://doi.org/10.1038/ncomms11196.
Jajcevic, Kristina, Chami, Mohamed and Sugihara, Kaori (2016) ‘Gold Nanowire Fabrication with Surface-Attached Lipid Nanotube Templates’, Small, 12(35), pp. 4830–4836. Available at: https://doi.org/10.1002/smll.201600431.
Liu, Juan et al. (2016) ‘DNA-Mediated Self-Organization of Polymeric Nanocompartments Leads to Interconnected Artificial Organelles’, Nano Letters, 16(11), pp. 7128–7136. Available at: https://doi.org/10.1021/acs.nanolett.6b03430.
Munguira, Ignacio et al. (2016) ‘Glasslike Membrane Protein Diffusion in a Crowded Membrane’, ACS Nano, 10(2), pp. 2584–90. Available at: https://doi.org/10.1021/acsnano.5b07595.
Nussbaumer, Martin G. et al. (2016) ‘Chaperonin-Dendrimer Conjugates for siRNA Delivery’, Advanced Science, 3(10), p. 1600046. Available at: https://doi.org/10.1002/advs.201600046.
Renzi, Francesco et al. (2016) ‘Evidence for a LOS and a capsular polysaccharide in Capnocytophaga canimorsus’, Scientific Reports, 6, p. 38914. Available at: https://doi.org/10.1038/srep38914.
Zambolin, Silvia et al. (2016) ‘Structural basis for haem piracy from host haemopexin by Haemophilus influenzae’, Nature communications, 7, p. 11590. Available at: https://doi.org/10.1038/ncomms11590.
Huysmans, Gerard H. M. et al. (2015) ‘Lipids assist the membrane insertion of a BAM-independent outer membrane protein’, Scientific Reports, 5, p. 15068. Available at: https://doi.org/10.1038/srep15068.
Levefaudes, Marjorie et al. (2015) ‘Diaminopimelic Acid Amidation in Corynebacteriales: NEW INSIGHTS INTO THE ROLE OF LtsA IN PEPTIDOGLYCAN MODIFICATION’, Journal of Biological Chemistry, 290(21), pp. 13079–94. Available at: https://doi.org/10.1074/jbc.m115.642843.
Sborgi, Lorenzo et al. (2015) ‘Structure and assembly of the mouse ASC inflammasome by combined NMR spectroscopy and cryo-electron microscopy’, Proceedings of the National Academy of Sciences of the United States of America, 112(43), pp. 13237–42. Available at: https://doi.org/10.1073/pnas.1507579112.
Car, Anja et al. (2014) ‘pH-responsive PDMS-b-PDMAEMA micelles for intracellular anticancer drug delivery’, Biomacromolecules, 15(9), pp. 3235–45. Available at: https://doi.org/10.1021/bm500919z.
Disconzi, Elena et al. (2014) ‘Bacterial secretins form constitutively open pores akin to general porins’, Journal of Bacteriology, 196(1), pp. 121–8. Available at: https://doi.org/10.1128/jb.00750-13.
Franke, Barbara et al. (2014) ‘Molecular basis for the fold organization and sarcomeric targeting of the muscle atrogin MuRF1’, Open biology, 4(3), p. 130172. Available at: https://doi.org/10.1098/rsob.130172.
Fribourg, Pierre Frederic et al. (2014) ‘3D cryo-electron reconstruction of BmrA, a bacterial multidrug ABC transporter in an inward-facing conformation and in a lipidic environment’, Journal of Molecular Biology, 426(10), pp. 2059–69. Available at: https://doi.org/10.1016/j.jmb.2014.03.002.
Gour, Nidhi et al. (2014) ‘Label-free, optical sensing of the supramolecular assembly into fibrils of a ditryptophan-DNA hybrid’, Chemical Communications, 50(52), pp. 6863–5. Available at: https://doi.org/10.1039/c4cc02631d.
Guilvout, Ingrid et al. (2014) ‘Independent domain assembly in a trapped folding intermediate of multimeric outer membrane secretins’, Structure, 22(4), pp. 582–9. Available at: https://doi.org/10.1016/j.str.2014.02.009.
Kowal, Julia et al. (2014) ‘Ligand-induced structural changes in the cyclic nucleotide-modulated potassium channel MloK1’, Nature communications, 5, p. 3106. Available at: https://doi.org/10.1038/ncomms4106.
Scherer, Sebastian et al. (2014) ‘2dx_automator: Implementation of a semiautomatic high-throughput high-resolution cryo-electron crystallography pipeline’, Journal of Structural Biology, 186(2), pp. 302–307. Available at: https://doi.org/10.1016/j.jsb.2014.03.016.
Vasquez, Daniela et al. (2014) ‘The Amine Content of PEGylated Chitosan Bombyx mori Nanoparticles Acts as a Trigger for Protein Delivery’, Langmuir, 30(4), pp. 965–75. Available at: https://doi.org/10.1021/la404558g.
Zivanovic, Yvan et al. (2014) ‘Insights into bacteriophage T5 structure from analysis of its morphogenesis genes and protein components’, Journal of virology, 88(2), pp. 1162–74. Available at: https://doi.org/10.1128/jvi.02262-13.
Breyton, Cécile et al. (2013) ‘Assessing the conformational changes of pb5, the receptor-binding protein of phage T5, upon binding to its Escherichia coli receptor FhuA’, Journal of Biological Chemistry, 288(42), pp. 30763–30772. Available at: https://doi.org/10.1074/jbc.m113.501536.
Degiacomi, Matteo T. et al. (2013) ‘Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism’, Nature Chemical Biology, 9(10), pp. 623–9. Available at: https://doi.org/10.1038/nchembio.1312.
Kowal, Julia et al. (2013) ‘Structure of the Dodecameric Yersinia enterocolitica Secretin YscC and Its Trypsin-Resistant Core’, Structure, 21(12), pp. 2152–61. Available at: https://doi.org/10.1016/j.str.2013.09.012.
Casuso, Ignacio et al. (2012) ‘Characterization of the motion of membrane proteins using high-speed atomic force microscopy’, Nature Nanotechnology, 7(8), pp. 525–9. Available at: https://doi.org/10.1038/nnano.2012.109.
Itel, F. et al. (2012) ‘CO2 permeability of cell membranes is regulated by membrane cholesterol and protein gas channels’, FASEB Journal, 26(12), pp. 5182–91. Available at: https://doi.org/10.1096/fj.12-209916.
Marchand, Christophe H. et al. (2012) ‘Biochemical disclosure of the mycolate outer membrane of Corynebacterium glutamicum’, Journal of Bacteriology, 194(3), pp. 587–97. Available at: https://doi.org/10.1128/jb.06138-11.
Nickerson, Nicholas N. et al. (2012) ‘A Single Amino Acid Substitution Changes the Self-Assembly Status of a Type IV Piliation Secretin’, Journal of Bacteriology, 194(18), pp. 4951–8. Available at: https://doi.org/10.1128/jb.00798-12.
Sugihara, Kaori et al. (2012) ‘Directed self-assembly of lipid nanotubes from inverted hexagonal structures’, ACS Nano, 6(8), pp. 6626–32. Available at: https://doi.org/10.1021/nn300557s.
Aissaoui, Abderrahim et al. (2011) ‘Efficient topical delivery of plasmid DNA to lung in vivo mediated by putative triggered, PEGylated pDNA nanoparticles’, Journal of Controlled Release, 154(3), pp. 275–84. Available at: https://doi.org/10.1016/j.jconrel.2011.06.017.
Berrier, Catherine et al. (2011) ‘Coupled cell-free synthesis and lipid vesicle insertion of a functional oligomeric channel MscL MscL does not need the insertase YidC for insertion in vitro’, Biochimica et biophysica acta, 1808(1), pp. 41–6. Available at: https://doi.org/10.1016/j.bbamem.2010.09.018.
Chami, Mohamed et al. (2011) ‘Assembly of a protein ‘brush’ by end-grafting titin fragments to liposomes’, Journal of bioscience and bioengineering, 112(2), pp. 178–9. Available at: https://doi.org/10.1016/j.jbiosc.2011.04.014.
Coudray, N. et al. (2011) ‘Automated screening of 2D crystallization trials using transmission electron microscopy : a high-throughput tool-chain for sample preparation and microscopic analysis’, Journal of structural biology, 173(2), pp. 365–74. Available at: https://doi.org/10.1016/j.jsb.2010.09.019.
Dezi, Manuela et al. (2011) ‘Binding, reconstitution and 2D crystallization of membrane or soluble proteins onto functionalized lipid layer observed in situ by reflected light microscopy’, Journal of structural biology, 174(2), pp. 307–14. Available at: https://doi.org/10.1016/j.jsb.2010.12.001.
Egli, Stefan et al. (2011) ‘Biocompatible Functionalization of Polymersome Surfaces: A New Approach to Surface Immobilization and Cell Targeting Using Polymersomes’, Journal of the American Chemical Society, 133(12), pp. 4476–83. Available at: https://doi.org/10.1021/ja110275f.
Guilvout, Ingrid et al. (2011) ‘Multimerization-defective variants of dodecameric secretin PulD’, Research in Microbiology, 162(2), pp. 180–90. Available at: https://doi.org/10.1016/j.resmic.2011.01.006.
Hoang, Hanh H. et al. (2011) ‘Outer membrane targeting of Pseudomonas aeruginosa proteins shows variable dependence on the components of Bam and Lol machineries’, mBio, 2(6), pp. e00246–11. Available at: https://doi.org/10.1128/mbio.00246-11.
Bou Raad, Roland et al. (2010) ‘A deficiency in arabinogalactan biosynthesis affects Corynebacterium glutamicum mycolate outer membrane stability’, Journal of Bacteriology, 192(11), pp. 2691–700. Available at: https://doi.org/10.1128/jb.00009-10.
Abeyrathne, Priyanka D. et al. (2010) ‘Preparation of 2D crystals of membrane proteins for high-resolution electron crystallography data collection’, in Jensen, Grant J. (ed.) Cryo-EM Part A Sample Preparation and Data Collection. Elsevier (Methods in Enzymology), pp. 25–43. Available at: https://doi.org/10.1016/s0076-6879(10)81001-8.
Wang, Yingying et al. (2009) ‘Isolation and characterization of low nucleic acid (LNA)-content bacteria’, ISME Journal, 3(8), pp. 889–902. Available at: https://doi.org/10.1038/ismej.2009.46.
Boulanger, Pascale et al. (2008) ‘Phage T5 straight tail fiber is a multifunctional protein acting as a tape measure and carrying fusogenic and muralytic activities’, Journal of Biological Chemistry, 283(20), pp. 13556–64. Available at: https://doi.org/10.1074/jbc.m800052200.
Guilvout, Ingrid et al. (2008) ‘In vitro multimerization and membrane insertion of bacterial outer membrane secretin PulD’, Journal of Molecular Biology, 382(1), pp. 13–23. Available at: https://doi.org/10.1016/j.jmb.2008.06.055.
Krehenbrink, Martin et al. (2008) ‘Artificial binding proteins (Affitins) as probes for conformational changes in secretin PulD’, Journal of molecular biology, 383(5), pp. 1058–68. Available at: https://doi.org/10.1016/j.jmb.2008.09.016.
Riek, Uwe et al. (2008) ‘Structural properties of AMP-activated protein kinase: dimerization, molecular shape, and changes upon ligand binding’, Journal of Biological Chemistry, 283(26), pp. 18331–43. Available at: https://doi.org/10.1074/jbc.m708379200.
Zuber, Benoît et al. (2008) ‘Direct visualization of the outer membrane of mycobacteria and corynebacteria in their native state’, Journal of Bacteriology, 190(16), pp. 5672–80. Available at: https://doi.org/10.1128/jb.01919-07.
Collin, Séverine et al. (2007) ‘YaeT-independent multimerization and outer membrane association of secretin PulD’, Molecular microbiology, 64(5), pp. 1350–7. Available at: https://doi.org/10.1111/j.1365-2958.2007.05743.x.
Javelle, Arnaud et al. (2007) ‘Structural and mechanistic aspects of Amt/Rh proteins’, Journal of Structural Biology, 158(3), pp. 472–81. Available at: https://doi.org/10.1016/j.jsb.2007.01.004.
Guilvout, Ingrid et al. (2006) ‘Bacterial outer membrane secretin PulD assembles and inserts into the inner membrane in the absence of its pilotin’, The EMBO journal, 25(22), pp. 5241–9. Available at: https://doi.org/10.1038/sj.emboj.7601402.
Lambert, Olivier et al. (2005) ‘Trimeric structure of OprN and OprM efflux proteins from Pseudomonas aeruginosa, by 2D electron crystallography’, Journal of Structural Biology, 150(1), pp. 50–7. Available at: https://doi.org/10.1016/j.jsb.2005.01.001.
Pretz, M. G. et al. (2005) ‘Functional and structural characterization of the minimal Sec translocase of the hyperthermophile Thermotoga maritima’, Extremophiles, 9(4), pp. 307–16. Available at: https://doi.org/10.1007/s00792-005-0446-3.
Tropis, Marielle et al. (2005) ‘The crucial role of trehalose and structurally related oligosaccharides in the biosynthesis and transfer of mycolic acids in Corynebacterineae’, Journal of Biological Chemistry, 280(28), pp. 26573–85. Available at: https://doi.org/10.1074/jbc.m502104200.
Kacem, Raoudha et al. (2004) ‘Importance of mycoloyltransferases on the physiology of Corynebacterium glutamicum’, Microbiology, 150(Pt 1), pp. 73–84. Available at: https://doi.org/10.1099/mic.0.26583-0.
Portevin, Damien et al. (2004) ‘A polyketide synthase catalyzes the last condensation step of mycolic acid biosynthesis in mycobacteria and related organisms’, Proceedings of the National Academy of Sciences of the United States of America, 101(1), pp. 314–9. Available at: https://doi.org/10.1073/pnas.0305439101.
Chami, Mohamed et al. (2002) ‘Priming and activation of mouse macrophages by trehalose 6,6′-dicorynomycolate vesicles from Corynebacterium glutamicum’, FEMS Immunology and Medical Microbiology, 32(2), pp. 141–147. Available at: https://doi.org/10.1111/j.1574-695x.2002.tb00546.x.
Chami, Mohamed et al. (2002) ‘Three-dimensional structure by cryo-electron microscopy of YvcC, an homodimeric ATP-binding cassette transporter from Bacillus subtilis’, Journal of Molecular Biology, 315(5), pp. 1075–85. Available at: https://doi.org/10.1006/jmbi.2001.5309.