Protein aggregation and neurodegenerative disease, Nature Medicine, vol.99, issue.7, pp.10-17, 2004. ,
DOI : 10.1038/nm1066
Prion hypothesis: the end of the controversy?, Trends in Biochemical Sciences, vol.36, issue.3, pp.151-158, 2011. ,
DOI : 10.1016/j.tibs.2010.11.001
Folding proteins in fatal ways, Nature, vol.426, issue.6968, pp.900-904, 2003. ,
DOI : 10.1038/nature02264
The role of the ubiquitin-proteasomal pathway in Parkinson's disease and other neurodegenerative disorders, Trends in Neurosciences, vol.24, pp.7-14, 2001. ,
DOI : 10.1016/S0166-2236(01)00003-0
A single amino acid substitution in a proteasome subunit triggers aggregation of ubiquitinated proteins in stressed neuronal cells, Journal of Neurochemistry, vol.40, issue.1, pp.19-28, 2004. ,
DOI : 10.1111/j.1471-4159.2004.02456.x
Role of the unfolded protein response in cell death, Apoptosis, vol.19, issue.1, pp.5-13, 2006. ,
DOI : 10.1007/s10495-005-3088-0
Molecular mechanisms of nitrosative stress-mediated protein misfolding in neurodegenerative diseases, Cellular and Molecular Life Sciences, vol.64, issue.13, pp.1609-1620, 2007. ,
DOI : 10.1007/s00018-007-6525-0
S-Nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration, Nature, vol.304, issue.7092, pp.513-517, 2006. ,
DOI : 10.1038/nature04782
The ubiquitin???proteasome pathway in Parkinson's disease and other neurodegenerative diseases, Trends in Cell Biology, vol.14, issue.12, pp.703-711, 2004. ,
DOI : 10.1016/j.tcb.2004.10.006
Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis, Nature, vol.385, issue.6619, pp.787-793, 1997. ,
DOI : 10.1038/385787a0
Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains, Protein Science, vol.37, issue.3, pp.509-517, 1999. ,
DOI : 10.1110/ps.8.3.509
Chemical modification of insulin in amyloid fibrils, Protein Science, vol.70, issue.11, pp.2637-2641, 2003. ,
DOI : 10.1110/ps.0360403
Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro, Proc. Natl Acad. Sci. USA, pp.7021-7026, 2003. ,
DOI : 10.1073/pnas.1237797100
Site-specific modification of Alzheimer's peptides by cholesterol oxidation products enhances aggregation energetics and neurotoxicity, Proc. Natl Acad. Sci. USA, pp.18563-18568, 2009. ,
DOI : 10.1073/pnas.0804758106
Principles of protein folding, misfolding and aggregation, Seminars in Cell & Developmental Biology, vol.15, issue.1, pp.3-16, 2004. ,
DOI : 10.1016/j.semcdb.2003.12.008
Opinion: What is the role of protein aggregation in neurodegeneration?, Nature Reviews Molecular Cell Biology, vol.62, issue.11, pp.891-898, 2005. ,
DOI : 10.1016/S0733-8619(01)00020-2
Diseases of protein conformation: what do in vitro experiments tell us about in vivo diseases?, Trends in Biochemical Sciences, vol.28, issue.11, pp.585-592, 2003. ,
DOI : 10.1016/j.tibs.2003.09.009
Cell Death, Cell, vol.116, issue.2, pp.205-219, 2004. ,
DOI : 10.1016/S0092-8674(04)00046-7
Apoptosis: a basic biological phenomenon with wide-ranging implications in human disease, Journal of Internal Medicine, vol.104, issue.6, pp.479-517, 2005. ,
DOI : 10.1038/nm1101-1241
The bcl2 family: regulators of the cellular life-or-death switch, Nature Reviews Cancer, vol.2, issue.9, pp.647-656, 2002. ,
DOI : 10.1038/nrc883
The Bcl-2 protein family: sensors and checkpoints for life-or-death decisions, Molecular Immunology, vol.39, issue.11, pp.615-647, 2003. ,
DOI : 10.1016/S0161-5890(02)00252-3
Interactions among members of the Bcl-2 protein family analyzed with a yeast twohybrid system, Proc. Natl Acad. Sci. USA, pp.9238-9242, 1994. ,
Structure of Bax, Cell, vol.103, issue.4, pp.645-654, 2000. ,
DOI : 10.1016/S0092-8674(00)00167-7
Bax and Bak Coalesce into Novel Mitochondria-Associated Clusters during Apoptosis, The Journal of Cell Biology, vol.14, issue.6, pp.1265-1276, 2001. ,
DOI : 10.1016/S0092-8674(00)81382-3
Bax Is Present as a High Molecular Weight Oligomer/Complex in the Mitochondrial Membrane of Apoptotic Cells, Journal of Biological Chemistry, vol.276, issue.15, pp.11615-11623, 2001. ,
DOI : 10.1074/jbc.M010810200
BCL-2 Selectively Interacts with the BID-induced Open Conformer of BAK, Inhibiting BAK Auto-oligomerization, Journal of Biological Chemistry, vol.278, issue.27, pp.25039-25045, 2003. ,
DOI : 10.1074/jbc.M302930200
BH3-only proteins in apoptosis and beyond: an overview, Oncogene, vol.12, pp.2-19, 2008. ,
DOI : 10.1101/gad.1045603
Apoptosis Initiated When BH3 Ligands Engage Multiple Bcl-2 Homologs, Not Bax or Bak, Science, vol.315, issue.5813, pp.856-859, 2007. ,
DOI : 10.1126/science.1133289
How do BCL-2 proteins induce mitochondrial outer membrane permeabilization? Trends Cell, Biol, vol.18, pp.157-164, 2008. ,
bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell death, Cell, vol.74, issue.4, pp.597-608, 1993. ,
DOI : 10.1016/0092-8674(93)90508-N
Structural biology of the Bcl-2 family of proteins, Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, vol.1644, issue.2-3, pp.1644-83, 2004. ,
DOI : 10.1016/j.bbamcr.2003.08.012
bcl-XL is the major bcl-x mRNA form expressed during murine development and its product localizes to mitochondria, Development, vol.120, pp.3033-3042, 1994. ,
Role of Bax and Bak in mitochondrial morphogenesis, Nature, vol.21, issue.7112, pp.658-662, 2006. ,
DOI : 10.1038/nature05111
ARF Induces Autophagy by Virtue of Interaction with Bcl-xl, Journal of Biological Chemistry, vol.284, issue.5, pp.2803-2810, 2008. ,
DOI : 10.1074/jbc.M804705200
Nuclear colocalization and interaction between bcl-xL and cdk1(cdc2) during G2/M cell-cycle checkpoint, Oncogene, vol.122, issue.40, pp.5851-5865, 2007. ,
DOI : 10.1038/sj.onc.1210396
BCL-xL Regulates Synaptic Plasticity, Molecular Interventions, vol.6, issue.4, pp.208-222, 2006. ,
DOI : 10.1124/mi.6.4.7
Cytosolto-membrane redistribution of Bax and Bcl-X(L) during apoptosis, Proc. Natl Acad. Sci. USA, pp.3668-3672, 1997. ,
X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death, Nature, vol.381, issue.6580, pp.335-341, 1996. ,
DOI : 10.1038/381335a0
Identification of a novel regulatory domain in Bcl-xL and Bcl-2, The EMBO Journal, vol.16, issue.5, pp.968-977, 1997. ,
DOI : 10.1093/emboj/16.5.968
Modulation of cell death by Bcl-xL through caspase interaction, Proc. Natl Acad. Sci. USA, pp.554-559, 1998. ,
DOI : 10.1073/pnas.95.2.554
Bcl-xL Deamidation Is a Critical Switch in the Regulation of the Response to DNA Damage, Cell, vol.111, issue.1, pp.51-62, 2002. ,
DOI : 10.1016/S0092-8674(02)00972-8
Bcl-xL sequesters its C-terminal membrane anchor in soluble, cytosolic homodimers, The EMBO Journal, vol.18, issue.10, pp.2146-2155, 2004. ,
DOI : 10.1016/S0092-8674(00)81382-3
BCL-XL Dimerization by Three-dimensional Domain Swapping, Journal of Molecular Biology, vol.356, issue.2, pp.367-381, 2006. ,
DOI : 10.1016/j.jmb.2005.11.032
Evidence that Membrane Insertion of the Cytosolic Domain of Bcl-xL is Governed by an Electrostatic Mechanism, Journal of Molecular Biology, vol.359, issue.4, pp.1045-1058, 2006. ,
DOI : 10.1016/j.jmb.2006.03.052
Bcl-2 family members: integrators of survival and death signals in physiology and pathology, Biochim. Biophys. Acta, pp.1644-95, 2004. ,
Experimental investigation of protein folding and misfolding, Methods, vol.34, issue.1, pp.4-14, 2004. ,
DOI : 10.1016/j.ymeth.2004.03.002
Cooperative polymerization reactions. Analytical approximations, numerical examples, and experimental strategy, Biophysical Journal, vol.50, issue.4, pp.583-599, 1986. ,
DOI : 10.1016/S0006-3495(86)83498-1
The cooperative nature of G-F transformation of actin, Biochimica et Biophysica Acta, vol.57, issue.1, pp.22-31, 1962. ,
DOI : 10.1016/0006-3002(62)91073-9
Mechanism of Formation of Amyloid Protofibrils of Barstar from Soluble Oligomers: Evidence for Multiple Steps and Lateral Association Coupled to Conformational Conversion, Journal of Molecular Biology, vol.367, issue.4, pp.1186-1204, 2007. ,
DOI : 10.1016/j.jmb.2007.01.039
Mechanisms of Protein Fibril Formation: Nucleated Polymerization with Competing Off-Pathway Aggregation, Biophysical Journal, vol.94, issue.2, pp.379-391, 2008. ,
DOI : 10.1529/biophysj.107.117168
Refinement of noncalorimetric determination of the change in heat capacity, ??Cp, of protein unfolding and validation across a wide temperature range, Proteins: Structure, Function, and Bioinformatics, vol.38, issue.4, pp.1607-1616, 2008. ,
DOI : 10.1002/prot.22016
Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding, Protein Science, vol.5, issue.5, pp.2138-2148, 1995. ,
DOI : 10.1002/pro.5560050521
[18] Quantification of ??-sheet amyloid fibril structures with thioflavin T, Methods Enzymol, vol.309, pp.274-284, 1999. ,
DOI : 10.1016/S0076-6879(99)09020-5
Therapeutic Applications of Cell-Penetrating Peptides, Methods Mol. Biol, vol.683, pp.535-551, 2011. ,
DOI : 10.1007/978-1-60761-919-2_38
Comparison of CPP Uptake Methods, Methods Mol. Biol, vol.683, pp.207-217, 2011. ,
DOI : 10.1007/978-1-60761-919-2_15
Intracellular delivery of quantum dots mediated by a histidine- and arginine-rich HR9 cell-penetrating peptide through the direct membrane translocation mechanism, Biomaterials, vol.32, issue.13, pp.3520-3537, 2011. ,
DOI : 10.1016/j.biomaterials.2011.01.041
Mechanisms of Cellular Uptake of Cell-Penetrating Peptides, Journal of Biophysics, vol.18, issue.2, p.414729, 2011. ,
DOI : 10.1042/BJ20061100
Rationalization of the effects of mutations on peptide andprotein aggregation rates, Nature, vol.424, issue.6950, pp.805-808, 2003. ,
DOI : 10.1038/nature01891
Amyloid formation by globular proteins under native conditions, Nature Chemical Biology, vol.16, issue.1, pp.15-22, 2009. ,
DOI : 10.1038/nchembio.131
The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitro, The EMBO Journal, vol.21, issue.12, pp.2903-2911, 2002. ,
DOI : 10.1093/emboj/cdf303
Evidence for a Mechanism of Amyloid Formation Involving Molecular Reorganisation within Native-like Precursor Aggregates, Journal of Molecular Biology, vol.351, issue.4, pp.910-922, 2005. ,
DOI : 10.1016/j.jmb.2005.06.043
Conformational Conversion May Precede or Follow Aggregate Elongation on Alternative Pathways of Amyloid Protofibril Formation, Journal of Molecular Biology, vol.385, issue.4, pp.1266-1276, 2009. ,
DOI : 10.1016/j.jmb.2008.11.033
Exploring the Mechanism of Formation of Native-like and Precursor Amyloid Oligomers for the Native Acylphosphatase from Sulfolobus solfataricus, Structure, vol.14, issue.6, pp.993-1001, 2006. ,
DOI : 10.1016/j.str.2006.03.014
Amyloid formation under physiological conditions proceeds via a native-like folding intermediate, Nature Structural & Molecular Biology, vol.12, issue.3, pp.195-201, 2006. ,
DOI : 10.1038/nsmb1058
Structurally Distinct Amyloid Protofibrils Form on Separate Pathways of Aggregation of a Small Protein, Biochemistry, vol.48, issue.27, pp.6441-6449, 2009. ,
DOI : 10.1021/bi900682w
Competition between Intramolecular and Intermolecular Interactions in an Amyloid-Forming Protein, Journal of Molecular Biology, vol.389, issue.4, pp.776-786, 2009. ,
DOI : 10.1016/j.jmb.2009.04.042
A Comparative Study of the Relationship Between Protein Structure and ??-Aggregation in Globular and Intrinsically Disordered Proteins, Journal of Molecular Biology, vol.342, issue.1, pp.345-353, 2004. ,
DOI : 10.1016/j.jmb.2004.06.088
Bcl-2 and Bax Interact via the BH1-3 Groove-BH3 Motif Interface and a Novel Interface Involving the BH4 Motif, Journal of Biological Chemistry, vol.285, issue.37, pp.28749-28763, 2010. ,
DOI : 10.1074/jbc.M110.148361
Bax Forms an Oligomer via Separate, Yet Interdependent, Surfaces, Journal of Biological Chemistry, vol.285, issue.23, pp.17614-17627, 2010. ,
DOI : 10.1074/jbc.M110.113456
Role of oxidative/nitrosative stress-mediated Bcl-2 regulation in apoptosis and malignant transformation, Annals of the New York Academy of Sciences, vol.43, issue.1, pp.1-6, 2010. ,
DOI : 10.1111/j.1749-6632.2010.05608.x
Low levels of asparagine deamidation can have a dramatic effect on aggregation of amyloidogenic peptides: Implications for the study of amyloid formation, Protein Science, vol.26, issue.2, pp.342-349, 2002. ,
DOI : 10.1110/ps.48702
Bcl-2/Bax: a rheostat that regulates an anti-oxidant pathway and cell death, Z. N. Semin. Cancer Biol, vol.4, pp.327-332, 1993. ,
RTX Calcium Binding Motifs Are Intrinsically Disordered in the Absence of Calcium: IMPLICATION FOR PROTEIN SECRETION, Journal of Biological Chemistry, vol.284, issue.3, pp.1781-1789, 2009. ,
DOI : 10.1074/jbc.M807312200
URL : https://hal.archives-ouvertes.fr/pasteur-00364637
Cellular Functions and X-ray Structure of Anthrolysin O, a Cholesterol-dependent Cytolysin Secreted by Bacillus anthracis, Journal of Biological Chemistry, vol.284, issue.21, pp.14645-14656, 2009. ,
DOI : 10.1074/jbc.M807631200
Characterization of the Regions Involved in the Calcium-Induced Folding of the Intrinsically Disordered RTX Motifs from the Bordetella pertussis Adenylate Cyclase Toxin, Journal of Molecular Biology, vol.397, issue.2, pp.534-549, 2010. ,
DOI : 10.1016/j.jmb.2010.01.031
URL : https://hal.archives-ouvertes.fr/hal-00512116
Adenylate Cyclase Toxin, Biochemistry, vol.49, issue.2, pp.318-328, 2010. ,
DOI : 10.1021/bi9016389
URL : https://hal.archives-ouvertes.fr/hal-00512114
Conformational States and Thermodynamics of ??-Lactalbumin Bound to Membranes: A Case Study of the Effects of pH, Calcium, Lipid Membrane Curvature and Charge, Journal of Molecular Biology, vol.349, issue.4, pp.890-905, 2005. ,
DOI : 10.1016/j.jmb.2005.04.036
URL : https://hal.archives-ouvertes.fr/hal-00384704
Cofactor effects on the protein folding reaction: Acceleration of ??-lactalbumin refolding by metal ions, Protein Science, vol.15, issue.4, pp.659-671, 2006. ,
DOI : 10.1110/ps.051904206
Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding, 1999. ,
ProtSA: a web application for calculating sequence specific protein solvent accessibilities in the unfolded ensemble, BMC Bioinformatics, vol.10, issue.1, p.104, 2009. ,
DOI : 10.1186/1471-2105-10-104