@article {2014|1645,
	title = {Type VI secretion and bacteriophage tail tubes share a common assembly pathway.},
	journal = {Embo Rep.},
	volume = {15},
	year = {2014},
	month = {mar},
	pages = {315{\textendash}21},
	abstract = {<p>The Type VI secretion system (T6SS) is a widespread macromolecular structure that delivers protein effectors to both eukaryotic and prokaryotic recipient cells. The current model describes the T6SS as an inverted phage tail composed of a sheath-like structure wrapped around a tube assembled by stacked Hcp hexamers. Although recent progress has been made to understand T6SS sheath assembly and dynamics, there is no evidence that Hcp forms tubes in vivo. Here we show that Hcp interacts with TssB, a component of the T6SS sheath. Using a cysteine substitution approach, we demonstrate that Hcp hexamers assemble tubes in an ordered manner with a head-to-tail stacking that are used as a scaffold for polymerization of the TssB/C sheath-like structure. Finally, we show that VgrG but not TssB/C controls the proper assembly of the Hcp tubular structure. These results highlight the conservation in the assembly mechanisms between the T6SS and the bacteriophage tail tube/sheath.</p>},
	keywords = {Amino Acid Sequence, Bacterial Secretion Systems, Escherichia coli, Escherichia coli Proteins, Molecular Sequence Data, Protein Binding, Protein Multimerization, Protein Structure, Tertiary, Virulence Factors},
	issn = {1469-3178},
	doi = {10.1002/embr.201337936},
	author = {Brunet, Yannick R and J{\'e}r{\^o}me H{\'e}nin and Celia, Herv{\'e} and Cascales, Eric}
}
@article {2009|1830,
	title = {Replica exchange molecular dynamics simulations of coarse-grained proteins in implicit solvent.},
	journal = {J. Phys. Chem. B},
	volume = {113},
	number = {1},
	year = {2009},
	month = {jan},
	pages = {267{\textendash}274},
	keywords = {Amino Acid Sequence, Computer Simulation, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Peptides, Protein Folding, Protein Structure, Proteins, Secondary, Solvents, Temperature, Thermodynamics},
	doi = {10.1021/jp805309e},
	author = {Y Chebaro and Xiao Dong and Rozita Laghaei and Philippe Derreumaux and Normand Mousseau}
}
@article {2009|2009,
	title = {Structural diversity of the soluble trimers of the human amylin(20-29) peptide revealed by molecular dynamics simulations},
	journal = {J. Chem. Phys.},
	volume = {130},
	number = {12},
	year = {2009},
	month = {mar},
	pages = {125101},
	keywords = {Amino Acid Sequence, Amyloid, Humans, Models, Molecular, Molecular Sequence Data, Peptide Fragments, Protein Multimerization, Protein Structure, Quaternary, Solubility, Solvents},
	doi = {10.1063/1.3097982},
	author = {Mo, Yuxiang and Lu, Yan and Wei, Guanghong and Philippe Derreumaux}
}
@article {1995|1941,
	title = {Solution structure of oligonucleotides covalently linked to a psoralen derivative.},
	journal = {Nucleic Acids Res.},
	volume = {23},
	number = {5},
	year = {1995},
	month = {mar},
	pages = {788{\textendash}795},
	abstract = {<p>Psoralen (pso) was attached via its C-5 position to the 5\&$\#$39;-phosphate group of an oligodeoxynucleotide d(TAAGCCG) by a hexamethylene linker (m6). Complex formation between pso-m6-d(TAAGCCG) and the complementary strands d(CGGCTTA)[7-7mer] or d(CGGCTTAT)[7-8mer] was investigated by nuclear magnetic resonance in aqueous solution. Structural informations derived from DQF-COSY and NOESY maps, revealed that the mini double helix adopts a B-form conformation and that the deoxyriboses preferentially adopt a C2\&$\#$39;-endo conformation. The nOe connectivities observed between the protons of the bases or the sugars in each duplex, and the protons of the psoralen and the hexamethylene chain, led us to propose a model involving an equilibrium between two conformations due to different locations of the psoralen. Upon UV-irradiation, the psoralen moiety cross-linked the two DNA strands at the level of 5\&$\#$39;TpA3\&$\#$39; sequences. NMR studies of the single major photo-cross-linked duplex pso-m6-d(TAAGCCG) and d(CGGCTTA) were performed. The stereochemistry of the diadduct is indeed cis-syn at both cyclobutane rings. In addition, the effects of this diadduct on the helical structure are analyzed in detail.</p>},
	keywords = {Base Sequence, chemistry, chemistry/radiation effects, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Nucleic Acid Conformation, Oligodeoxyribonucleotides, Psoralens, Solutions},
	author = {O. Bornet and Chantal Pr{\'e}vost and F. Vovelle and M. Chassignol and N. T. Thuong and G. Lancelot}
}
