D. J. Selkoe and J. Hardy, The amyloid hypothesis of Alzheimer's disease at 25 years, EMBO Mol. Med, vol.8, pp.595-608, 2016.

C. Haass, C. Kaether, G. Thinakaran, and S. Sisodia, Trafficking and proteolytic processing of APP. Cold Spring Harb, Perspect. Med, vol.2, pp.6270-006270, 2012.

X. Bai, An atomic structure of human ?-secretase, Nature, vol.525, pp.212-217, 2015.

M. A. Wälti, Atomic-resolution structure of a disease-relevant A?(1-42) amyloid fibril, Proc. Natl Acad. Sci. USA, vol.113, pp.4976-4984, 2016.

M. T. Colvin, Atomic resolution structure of monomorphic A?42 amyloid fibrils, J. Am. Chem. Soc, vol.138, pp.9663-9674, 2016.

L. Gremer, Fibril structure of amyloid-?(1-42) by cryo-electron microscopy, Science, vol.358, pp.116-119, 2017.

B. R. Roberts, Biochemically-defined pools of amyloid-? in sporadic Alzheimer's disease: correlation with amyloid PET, Brain, vol.140, pp.1486-1498, 2017.

D. W. Dickson, Correlations of synaptic and pathological markers with cognition of the elderly, Neurobiol. Aging, vol.16, pp.298-304, 1995.

C. Lendel, A Hexameric peptide barrel as building block of amyloid-? Protofibrils, Angew. Chem. Int. Ed, vol.53, pp.12756-12760, 2014.

P. K. Mandal and J. W. Pettegrew, Alzheimer's disease: soluble oligomeric A? (1-40) peptide in membrane mimic environment from solution NMR and circular dichroism studies, Neurochem Res, vol.29, pp.1-6, 2004.

D. J. Tew, Stabilization of neurotoxic soluble beta-sheet-rich conformations of the Alzheimer's disease amyloid-beta peptide, Biophys. J, vol.94, pp.2752-2766, 2008.

L. Yu, Structural characterization of a soluble amyloid ?-peptide oligomer, Biochemistry, vol.48, pp.1870-1877, 2009.

N. Arispe, E. Rojas, and H. B. Pollard, Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum, Proc. Natl Acad. Sci. USA, vol.90, pp.567-571, 1993.

Y. Hirakura, M. C. Lin, and B. L. Kagan, Alzheimer amyloid a?1-42 channels: Effects of solvent, pH, and congo red, J. Neurosci. Res, vol.57, pp.458-466, 1999.

H. Lin, R. Bhatia, and R. Lal, Amyloid beta protein forms ion channels: implications for Alzheimer's disease pathophysiology, FASEB J, vol.15, pp.2433-2444, 2001.

S. M. Butterfield and H. A. Lashuel, Amyloidogenic protein-membrane interactions: mechanistic insight from model systems, Angew. Chem. Int. Ed, vol.49, pp.5628-5654, 2010.

I. Benilova, E. Karran, and B. De-strooper, The toxic A? oligomer and Alzheimer's disease: an emperor in need of clothes, Nat. Neurosci, vol.15, pp.349-357, 2012.

M. Serra-batiste, A?42 assembles into specific ?-barrel pore-forming oligomers in membrane-mimicking environments, Proc. Natl Acad. Sci. USA, vol.113, pp.10866-10871, 2016.

M. Serra-batiste, Preparation of a well-defined and stable ?-barrel poreforming A?42 oligomer, Methods Mol. Biol, vol.1779, pp.13-22, 2018.

T. Cierpicki and J. Otlewski, Amide proton temperature coefficients as hydrogen bond indicators in proteins, J. Biomol. NMR, vol.21, pp.249-261, 2001.

Y. Wang and E. Tajkhorshid, The Simshape Method for Protein-Detergent Interaction Research, Biophys. J, vol.114, p.679, 2018.

A. Ehkirch, Hyphenation of size exclusion chromatography to native ion mobility mass spectrometry for the analytical characterization of therapeutic antibodies and related products, J. Chromatogr. B Anal. Technol. Biomed. Life Sci, vol.1086, pp.176-183, 2018.
URL : https://hal.archives-ouvertes.fr/hal-02327936

A. Laganowsky, E. Reading, J. T. Hopper, and C. V. Robinson, Mass spectrometry of intact membrane protein complexes, Nat. Protoc, vol.8, pp.639-651, 2013.

A. Leitner, Chemical cross-linking/mass spectrometry targeting acidic residues in proteins and protein complexes, Proc. Natl Acad. Sci. USA, vol.111, pp.9455-9460, 2014.

E. Sitkiewicz, J. Ol?dzki, J. Pozna?ski, and M. Dadlez, Di-Tyrosine cross-link decreases the collisional cross-section of A? peptide dimers and trimers in the gas phase: an ion mobility study, PLoS ONE, vol.9, pp.100200-100214, 2014.

K. Pagel, E. Natan, Z. Hall, A. R. Fersht, and C. V. Robinson, Intrinsically disordered p53 and its complexes populate compact conformations in the gas phase, Angew. Chem. Int. Ed. Engl, vol.52, pp.361-365, 2013.

R. Friemann, D. S. Larsson, Y. Wang, and D. Van-der-spoel, Molecular dynamics simulations of a membrane protein-micelle complex in vacuo, J. Am. Chem. Soc, vol.131, pp.16606-16607, 2009.

B. Strodel, J. W. Lee, C. S. Whittleston, and D. J. Wales, Transmembrane structures for Alzheimer's A?(1-42) oligomers, J. Am. Chem. Soc, vol.132, pp.13300-13312, 2010.

C. Poojari, A. Kukol, and B. Strodel, How the amyloid-? peptide and membranes affect each other: an extensive simulation study, Biochim. Biophys. Acta, vol.1828, pp.327-339, 2013.

G. Maglia, A. J. Heron, D. Stoddart, D. Japrung, and H. Bayley, Analysis of single nucleic acid molecules with protein nanopores, Methods Enzymol, vol.475, pp.591-623, 2010.

J. Kim, Engineered bacterial outer membrane vesicles with enhanced functionality, J. Mol. Biol, vol.380, pp.51-66, 2008.

Y. Su, A. J. Waring, P. Ruchala, and M. Hong, Membrane-bound dynamic structure of an arginine-rich cell-penetrating peptide, the protein transduction domain of HIV TAT, from solid-state NMR, Biochemistry, vol.49, pp.6009-6020, 2010.

J. M. Mcdonald, N. J. Cairns, L. Taylor-reinwald, D. Holtzman, and D. M. Walsh, The levels of water-soluble and triton-soluble A? are increased in Alzheimer's disease brain, Brain Res, vol.1450, pp.138-147, 2012.

Z. O. Shenkarev, Molecular mechanism of action of ?-hairpin antimicrobial peptide arenicin: oligomeric structure in dodecylphosphocholine micelles and pore formation in planar lipid bilayers, Biochemistry, vol.50, pp.6255-6265, 2011.

S. J. Soscia, The Alzheimer's disease-associated amyloid beta-protein is an antimicrobial peptide, PLoS ONE, vol.5, p.9505, 2010.

D. K. Kumar, Amyloid-? peptide protects against microbial infection in mouse and worm models of Alzheimer's disease, Sci. Transl. Med, vol.8, pp.340-72, 2016.

L. Li, I. Vorobyov, A. D. Mackerell, and T. W. Allen, Is arginine charged in a membrane?, Biophys. J, vol.94, pp.11-13, 2008.

C. P. Moon and K. G. Fleming, Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers, Proc. Natl Acad. Sci. USA, vol.108, pp.10174-10177, 2011.

D. M. Walsh, A facile method for expression and purification of the Alzheimer's disease-associated amyloid beta-peptide, FEBS J, vol.276, pp.1266-1281, 2009.

R. Assenberg, Expression, purification and crystallization of a lyssavirus matrix (M) protein, Acta Crystallogr. Sect. F. Struct. Biol. Cryst. Commun, vol.64, pp.258-262, 2008.

M. Serra-batiste, Alzheimer´s disease-associated A?42 peptide: expression and purification for NMR structural studies, Curr. Chem. Biol, vol.11, pp.50-62, 2017.

R. Kerfah, Scrambling free combinatorial labeling of alanine-?, isoleucine-?1, leucine-proS and valine-proS methyl groups for the detection of long range NOEs, J. Biomol. NMR, vol.61, pp.73-82, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01119770

C. R. Sanders and F. Sönnichsen, Solution NMR of membrane proteins: practice and challenges, Magn. Reson. Chem, vol.44, pp.24-40, 2006.

P. Rossi, Y. Xia, N. Khanra, G. Veglia, and C. G. Kalodimos, 15)N and (13)C-SOFAST-HMQC editing enhances 3D-NOESY sensitivity in highly deuterated, selectively [(1)H,(13)C]-labeled proteins, J. Biomol. NMR, vol.66, pp.259-271, 2016.

M. Mayzel, K. Kazimierczuk, and V. Y. Orekhov, The causality principle in the reconstruction of sparse NMR spectra, Chem. Commun, vol.50, pp.8947-8950, 2014.

V. Y. Orekhov and V. A. Jaravine, Analysis of non-uniformly sampled spectra with multi-dimensional decomposition, Prog. Nucl. Magn. Reson. Spectrosc, vol.59, pp.271-292, 2011.

H. Shao, S. Jao, K. Ma, and M. G. Zagorski, Solution structures of micellebound amyloid beta-(1-40) and beta-(1-42) peptides of Alzheimer's disease, J. Mol. Biol, vol.285, pp.755-773, 1999.

A. T. Brunger, Version 1.2 of the Crystallography and NMR system, Nat. Protoc, vol.2, pp.2728-2733, 2007.

W. Rieping, ARIA2: automated NOE assignment and data integration in NMR structure calculation, Bioinformatics, vol.23, pp.381-382, 2007.

Y. Shen and A. Bax, Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networks, J. Biomol. NMR, vol.56, pp.227-241, 2013.

J. P. Linge, M. A. Williams, C. A. Spronk, A. M. Bonvin, and M. Nilges, Refinement of protein structures in explicit solvent, Proteins, vol.50, pp.496-506, 2003.

R. A. Laskowski, M. W. Macarthur, D. S. Moss, and J. M. Thornton, PROCHECK: a program to check the stereochemical quality of protein structures, J. Appl. Cryst, vol.26, pp.283-291, 1993.

G. Vriend, WHAT IF: a molecular modeling and drug design program, J. Mol. Graph, vol.8, pp.52-56, 2001.

I. W. Davis, MolProbity: all-atom contacts and structure validation for proteins and nucleic acids, Nucleic Acids Res, vol.35, pp.375-383, 2007.

V. Gabelica, Recommendations for reporting ion mobility Mass Spectrometry measurements, Mass Spectrom. Rev, 2019.
URL : https://hal.archives-ouvertes.fr/hal-02012317

H. E. Revercomb and E. A. Mason, Theory of plasma chromatography/gaseous electrophoresis, Anal. Chem, vol.47, pp.970-983, 1975.

M. F. Bush, Collision cross sections of proteins and their complexes: a calibration framework and database for gas-phase structural biology, Anal. Chem, vol.82, pp.9557-9565, 2010.

E. G. Marklund, M. T. Degiacomi, C. V. Robinson, A. J. Baldwin, and J. L. Benesch, Collision cross sections for structural proteomics, Structure, vol.23, pp.791-799, 2015.

M. Cadene and B. T. Chait, A Robust, detergent-friendly method for mass spectrometric analysis of integral membrane proteins, Anal. Chem, vol.72, pp.5655-5658, 2000.
URL : https://hal.archives-ouvertes.fr/hal-02150358

S. Jo, T. Kim, V. G. Iyer, and W. Im, CHARMM-GUI: a web-based graphical user interface for CHARMM, J. computational Chem, vol.29, pp.1859-1865, 2008.

R. T. Mcgibbon, MDTraj: a modern open library for the analysis of molecular dynamics trajectories, Biophys. J, vol.109, pp.1528-1532, 2015.