Calcium Signaling, Cell, vol.131, issue.6, pp.1047-1058, 2007. ,
DOI : 10.1016/j.cell.2007.11.028
Intracellular pH Sensors: Design Principles and Functional Significance, Physiology, vol.22, issue.1, pp.30-39, 2007. ,
DOI : 10.1152/physiol.00035.2006
Crystal Structure of the Low-pH Form of the Vesicular Stomatitis Virus Glycoprotein G, Science, vol.313, issue.5784, pp.187-191, 2006. ,
DOI : 10.1126/science.1127683
Structure of the Prefusion Form of the Vesicular Stomatitis Virus Glycoprotein G, Science, vol.315, issue.5813, pp.843-848, 2007. ,
DOI : 10.1126/science.1135710
URL : https://hal.archives-ouvertes.fr/hal-00167649
Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation, The EMBO Journal, vol.23, issue.4, pp.728-738, 2004. ,
DOI : 10.1038/sj.emboj.7600064
The envelope glycoprotein from tick-borne encephalitis virus at 2
?? resolution, Nature, vol.375, issue.6529, pp.291-298, 1995. ,
DOI : 10.1038/375291a0
A ligand-binding pocket in the dengue virus envelope glycoprotein, Proc. Natl Acad. Sci. USA, pp.6986-6991, 2003. ,
DOI : 10.1073/pnas.0832193100
Structure of the dengue virus envelope protein after membrane fusion, Nature, vol.427, issue.6972, pp.313-319, 2004. ,
DOI : 10.1038/nature02165
Role of Electrostatic Repulsion in Controlling pH-Dependent Conformational Changes of Viral Fusion Proteins, Structure, vol.21, issue.7, pp.1085-1096, 2013. ,
DOI : 10.1016/j.str.2013.05.009
The pH sensor for flavivirus membrane fusion, The Journal of Cell Biology, vol.70, issue.2, pp.177-179, 2008. ,
DOI : 10.1038/nsb990
Folding DNA to create nanoscale shapes and patterns, Nature, vol.4, issue.7082, pp.297-302, 2006. ,
DOI : 10.1038/nature04586
DNA Origami with Complex Curvatures in Three-Dimensional Space, Science, vol.332, issue.6027, pp.342-346, 2011. ,
DOI : 10.1126/science.1202998
Self-assembly of a nanoscale DNA box with a controllable lid, Nature, vol.211, issue.7243, pp.73-76, 2009. ,
DOI : 10.1038/nature07971
Building Programmable Jigsaw Puzzles with RNA, Science, vol.306, issue.5704, pp.2068-2072, 2004. ,
DOI : 10.1126/science.1104686
Organization of Intracellular Reactions with Rationally Designed RNA Assemblies, Science, vol.333, issue.6041, pp.470-474, 2011. ,
DOI : 10.1126/science.1206938
Complete shift of ferritin oligomerization toward nanocage assembly via engineered protein???protein interactions, Chemical Communications, vol.273, issue.34, pp.3528-3530, 2013. ,
DOI : 10.1039/c3cc40886h
Structure of a 16-nm Cage Designed by Using Protein Oligomers, Science, vol.336, issue.6085, pp.1129-1129, 2012. ,
DOI : 10.1126/science.1219351
Obey the Peptide Assembly Rules, Science, vol.340, issue.6132, pp.561-562, 2013. ,
DOI : 10.1126/science.1237708
Self-Assembling Cages from Coiled-Coil Peptide Modules, Science, vol.340, issue.6132, pp.595-599, 2013. ,
DOI : 10.1126/science.1233936
Peptide-amphiphile nanofibers: A versatile scaffold for the preparation of self-assembling materials, Proc. Natl Acad. Sci. USA 99, pp.5133-5138, 2002. ,
DOI : 10.1073/pnas.072699999
Control of peptide nanotube diameter by chemical modifications of an aromatic residue involved in a single close contact, Proc. Natl Acad. Sci. USA, pp.7679-7684, 2011. ,
DOI : 10.1073/pnas.1017343108
URL : https://hal.archives-ouvertes.fr/inserm-00716817
Directing peptide crystallization through curvature control of nanotubes, Journal of Peptide Science, vol.19, issue.03, pp.508-516, 2014. ,
DOI : 10.1002/psc.2647
URL : https://hal.archives-ouvertes.fr/cea-01201911
Structural Role of Counterions Adsorbed on Self-Assembled Peptide Nanotubes, Journal of the American Chemical Society, vol.134, issue.1, pp.723-733, 2012. ,
DOI : 10.1021/ja210299g
URL : https://hal.archives-ouvertes.fr/hal-00910874
Biomimetic organization: Octapeptide self-assembly into nanotubes of viral capsid-like dimension, Proc. Natl Acad. Sci. USA, pp.10258-10262, 2003. ,
DOI : 10.1073/pnas.1730609100
Molecular Origin of the Self-Assembly of Lanreotide into Nanotubes: A Mutational Approach, Biophysical Journal, vol.94, issue.5, pp.1782-1795, 2008. ,
DOI : 10.1529/biophysj.107.108175
URL : https://hal.archives-ouvertes.fr/hal-00364066
The infrared absorption of amino acid side chains, Progress in Biophysics and Molecular Biology, vol.74, issue.3-5, pp.141-173, 2000. ,
DOI : 10.1016/S0079-6107(00)00021-3
Protonation, Tautomerization, and Rotameric Structure of Histidine: A Comprehensive Study by Magic-Angle-Spinning Solid-State NMR, Journal of the American Chemical Society, vol.133, issue.5 ,
DOI : 10.1021/ja108943n
Molecular basis for amyloid-beta polymorphism, Proc. Natl Acad. Sci. USA, pp.16938-16943, 2011. ,
Elucidation of the Self-Assembly Pathway of Lanreotide Octapeptide into ??-Sheet Nanotubes: Role of Two Stable Intermediates, Journal of the American Chemical Society, vol.132, issue.12, pp.4230-4241, 2010. ,
DOI : 10.1021/ja9088023
URL : https://hal.archives-ouvertes.fr/hal-00470362
Diffraction of X-rays by chain molecules, 1966. ,
Structural elucidation of Leuprolide and its analogues in solution: insight into their bioactive conformation, Amino Acids, vol.26, issue.3, pp.1147-1160, 2010. ,
DOI : 10.1007/s00726-010-0549-8
Structure of the monomeric outer-membrane porin OmpG in the open and closed conformation, The EMBO Journal, vol.254, issue.15, pp.3702-3713, 2006. ,
DOI : 10.1038/sj.emboj.7600330
Structural Basis for Innate Immune Sensing by M-ficolin and Its Control by a pH-dependent Conformational Switch, Journal of Biological Chemistry, vol.282, issue.49, pp.35814-35820, 2007. ,
DOI : 10.1074/jbc.M705741200
Experimental Observation of Double-Walled Peptide Nanotubes and Monodispersity Modeling of the Number of Walls, Langmuir, vol.29, issue.8, pp.2739-2745, 2013. ,
DOI : 10.1021/la304862f
URL : https://hal.archives-ouvertes.fr/hal-00814021
Computational Design of Self-Assembling Protein Nanomaterials with Atomic Level Accuracy, Science, vol.336, issue.6085, pp.1171-1174, 2012. ,
DOI : 10.1126/science.1219364
Tuning bilayer twist using chiral counterions, Nature, vol.399, issue.6736, pp.566-569, 1999. ,
DOI : 10.1038/21154
Cu nanocrystal growth on peptide nanotubes by biomineralization: Size control of Cu nanocrystals by tuning peptide conformation, Proc. Natl Acad. Sci. USA, pp.14678-14682, 2003. ,
DOI : 10.1073/pnas.2433456100
-Valine-Containing Polyacetylene by pH Change, Nano Letters, vol.1, issue.6, pp.323-328, 2001. ,
DOI : 10.1021/nl015540o
URL : https://hal.archives-ouvertes.fr/tel-00807841
Protein folding and misfolding, Nature, vol.426, issue.6968, pp.884-890, 2003. ,
DOI : 10.1038/nature02261