The Amyloid State and Its Association with Protein Misfolding Diseases Pathological and Functional Amyloid Formation Orchestrated by the Secretory Pathway Functional Amyloid Formation within Mammalian Tissue Functional Amyloid ? from Bacteria to Humans Functional Amyloids As Natural Storage of Peptide Hormones in Pituitary Secretory Granules Structural Insights into Functional and Pathological Amyloid, ) Otzen, D. Functional Amyloid: Turning Swords into Plowshares (9) Podlubnaya, Z. A.; Bobylev, A. G. On Functional Amyloids of Muscle Proteins of Titin Family, pp.333-366, 2003. ,
PMEL: a pigment cell-specific model for functional amyloid formation, Pigment Cell & Melanoma Research, vol.91, issue.3, pp.300-315 ,
DOI : 10.1073/pnas.91.15.7076
URL : http://onlinelibrary.wiley.com/doi/10.1111/pcmr.12067/pdf
Functional Amyloids in Bacteria Nanoscale Mechanical Characterisation of Amyloid Fibrils Discovered in a Natural Adhesive, Int. Microbiol. J. Biol. Phys, vol.2014, issue.1725, pp.65-73, 2007. ,
A unique biofilm in human deep mycoses: fungal amyloid is bound by host serum amyloid P component, npj Biofilms and Microbiomes, vol.206, issue.1, 2015. ,
DOI : 10.1093/infdis/jis521
URL : https://www.nature.com/articles/npjbiofilms20159.pdf
Functionalised amyloid fibrils for roles in cell adhesion, Biomaterials, vol.29, issue.11, pp.29-1553, 2008. ,
DOI : 10.1016/j.biomaterials.2007.11.028
Role of Escherichia coli Curli Operons in Directing Amyloid Fiber Formation, Science, vol.295, issue.5556, pp.851-855, 2001. ,
DOI : 10.1126/science.1067484
URL : http://europepmc.org/articles/pmc2838482?pdf=render
A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils, Genes & Development, vol.17, issue.14, pp.17-1714, 2003. ,
DOI : 10.1101/gad.264303
, Hydrophobins, the Fungal Coat Unravelled. Biochim. Biophys. Acta BBA, issue.17, pp.1469-79, 2000.
Amyloids protect the silkmoth oocyte and embryo, FEBS Letters, vol.4, issue.3, pp.141-145, 2000. ,
DOI : 10.1093/nar/25.24.4876
Prolactin and Growth Hormone Aggregates in Secretory Granules: The Need to Understand the Structure of the Aggregate, Endocrine Reviews, vol.33, issue.2, pp.254-270 ,
DOI : 10.1210/er.2011-1002
Is There Structural Specificity in the Reversible Protein Aggregates That Are Stored in Secretory Granules?, Journal of Molecular Neuroscience, vol.22, issue.1-2, pp.43-49, 2004. ,
DOI : 10.1385/JMN:22:1-2:43
Autogel: A New Lanreotide Prolonged Release Formulation, Proc Int Symp Control Rel Bio Mat, vol.25, pp.798-799, 1998. ,
Amyloid as a Depot for the Formulation of Long-Acting Drugs, PLoS Biology, vol.3, issue.2, p.17, 2008. ,
DOI : 10.1371/journal.pbio.0060017.st002
Biomimetic organization: Octapeptide self-assembly into nanotubes of viral capsid-like dimension, Proc. Natl. Acad. Sci, pp.100-10258, 2003. ,
DOI : 10.1073/pnas.97.3.1079
Spontaneous fibrillation of the native neuropeptide hormone Somatostatin-14, Journal of Structural Biology, vol.160, issue.2, pp.211-223, 2007. ,
DOI : 10.1016/j.jsb.2007.08.006
URL : https://hal.archives-ouvertes.fr/hal-00264528
Lamination and spherulite-like compaction of a hormone???s native amyloid-like nanofibrils: spectroscopic insights into key interactions, Faraday Discussions, vol.110, 2013. ,
DOI : 10.1073/pnas.1219476110
Directing peptide crystallization through curvature control of nanotubes, Journal of Peptide Science, vol.19, issue.03, pp.20-508 ,
DOI : 10.1154/1.1763152
URL : https://hal.archives-ouvertes.fr/cea-01201911
, et al. Atomic View of the Histidine Environment Stabilizing Higher-PH Conformations of PH-Dependent Proteins, pp.2015-7771
Reversible Morphological Control of Cholecystokinin Tetrapeptide Amyloid Assemblies as a Function of pH, The Journal of Physical Chemistry B, vol.121, issue.14, pp.3059-3069 ,
DOI : 10.1021/acs.jpcb.7b02448
URL : https://hal.archives-ouvertes.fr/cea-01510377
, Early Aggregation Preceding the Nucleation of Insulin Amyloid Fibrils as Monitored by Small Angle X-Ray Scattering. Sci. Rep, 2015.
Interpreting the Aggregation Kinetics of Amyloid Peptides, Journal of Molecular Biology, vol.360, issue.4, pp.882-892, 2006. ,
DOI : 10.1016/j.jmb.2006.05.033
Kinetics and thermodynamics of amyloid formation from direct measurements of fluctuations in fibril mass, Proc. Natl. Acad. Sci, pp.104-10016, 2007. ,
DOI : 10.1016/S0076-6879(98)90032-5
Kinetics of Amyloid Aggregation: A Study of the GNNQQNY Prion Sequence Simultaneous Measurement of Amyloid Fibril Formation by Dynamic Light Scattering and Fluorescence Reveals Complex Aggregation Kinetics, PLoS Comput. Biol. PLoS ONE, vol.2012, issue.81, pp.1002782-1002815 ,
Resolution of Oligomeric Species during the Aggregation of A? 1?40 Using 19 F NMR, Biochemistry (Mosc.), vol.2013, issue.11, pp.52-1903 ,
Structure-Specific Intrinsic Fluorescence of Protein Amyloids Used to Study their Kinetics of Aggregation, In Bionanoimaging, pp.147-155, 2014. ,
DOI : 10.1016/B978-0-12-394431-3.00013-4
Primary Nucleation Kinetics of Short Fibril-Forming Amyloidogenic Peptides, The Journal of Physical Chemistry B, vol.119, issue.39, pp.12568-12579 ,
DOI : 10.1021/acs.jpcb.5b05799
, Biochemistry, vol.44, issue.40, pp.44-13365, 2005.
DOI : 10.1021/bi0508284
Multistep Conformation Selection in Amyloid Assembly, Journal of the American Chemical Society, vol.139, issue.47, pp.139-17007 ,
DOI : 10.1021/jacs.7b09362
Defining the Dynamic Conformational Networks of Cross-?? Peptide Assembly, Israel Journal of Chemistry, vol.9, issue.6-7, pp.55-61 ,
DOI : 10.1371/journal.pone.0094745
Kinetic Intermediates in Amyloid Assembly, Journal of the American Chemical Society, vol.136, issue.43, pp.136-15146 ,
DOI : 10.1021/ja508621b
On the lag phase in amyloid fibril formation, Physical Chemistry Chemical Physics, vol.107, issue.12, pp.7606-7618 ,
DOI : 10.1073/pnas.0913046107
Structural, morphological, and functional diversity of amyloid oligomers, FEBS Letters, vol.418, issue.19PartA, pp.589-2640 ,
DOI : 10.1038/418291a
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.132-4230, 2010. ,
DOI : 10.1021/ja9088023
URL : https://hal.archives-ouvertes.fr/hal-00470362
Peptide nanotubes: molecular organisations, self-assembly mechanisms and applications, Soft Matter, vol.24, issue.19, pp.9583-9628, 2011. ,
DOI : 10.1021/la802009t
Circular dichroism spectroscopy of membrane proteins, Chemical Society Reviews, vol.1808, issue.18, pp.4859-4872 ,
DOI : 10.1016/j.bbamem.2011.06.009
Structure and Assembly Properties of the N-Terminal Domain of the Prion Ure2p in Isolation and in Its Natural Context, PLoS ONE, vol.5, issue.3, p.9760, 2010. ,
DOI : 10.1371/journal.pone.0009760.s005
URL : https://hal.archives-ouvertes.fr/hal-01183211
-42) Peptide Self-Aggregation: Elucidation of Inhibitors' Mechanism of Action, Insight Into the Kinetic of Amyloid ChemBioChem, vol.1, issue.817, pp.2152-2161, 2007. ,
Synchrotron radiation circular-dichroism spectroscopy as a tool for investigating protein structures, Journal of Synchrotron Radiation, vol.7, issue.5, pp.289-295, 2000. ,
DOI : 10.1107/S0909049500009262
Conformational Changes by Synchrotron Radiation Circular Dichroism Spectroscopy, Nature Structural Biology, vol.7, issue.9, p.708, 2000. ,
DOI : 10.1038/78915
Synchrotron radiation circular dichroism spectroscopy of proteins: secondary structure, fold recognition and structural genomics, Current Opinion in Chemical Biology, vol.5, issue.5, pp.567-571, 2001. ,
DOI : 10.1016/S1367-5931(00)00243-X
Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy, Proc. Natl. Acad. Sci. 2015, pp.112-3095 ,
DOI : 10.1039/b306055c
URL : https://hal.archives-ouvertes.fr/hal-01485547
Circular and linear dichroism of proteins, Physical Chemistry Chemical Physics, vol.28, issue.17, p.2020, 2007. ,
DOI : 10.1110/ps.8.2.370
The effect on the Human Uterus of Two Newly Developed Competitive Inhibitors of Oxytocin and Vasopressin, Acta Obstetricia et Gynecologica Scandinavica, vol.64, issue.6, pp.499-504, 1985. ,
DOI : 10.3109/00016348509156728
, Tractocile 7.5 mg/ml Concentrate for Solution for Infusion -Summary of Product Characteristics (SPC) -(eMC) http://www.medicines.org.uk/emc/medicine, 2017.
Synthetic antagonists of the myometrial response to vasopressin and oxytocin, Journal of Endocrinology, vol.111, issue.1, pp.125-131, 1986. ,
DOI : 10.1677/joe.0.1110125
Structural Role of Counterions Adsorbed on Self-Assembled Peptide Nanotubes, Journal of the American Chemical Society, vol.134, issue.1, pp.723-733 ,
DOI : 10.1021/ja210299g
URL : https://hal.archives-ouvertes.fr/hal-00910874
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
The application of circular dichroism to studies of protein folding and unfolding, Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, vol.1338, issue.2, pp.161-185, 1997. ,
DOI : 10.1016/S0167-4838(96)00190-2
The Use of Circular Dichroism in the Investigation of Protein Structure and Function, Current Protein & Peptide Science, vol.1, issue.4, pp.349-384, 2000. ,
DOI : 10.2174/1389203003381315
How to study proteins by circular dichroism, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.1751, issue.2, pp.1751-119, 2005. ,
DOI : 10.1016/j.bbapap.2005.06.005
Circular Dichroism Techniques: Biomolecular and Nanostructural Analyses- A Review, Chemical Biology & Drug Design, vol.446, issue.2, pp.101-120, 2009. ,
DOI : 10.1155/2002/280646
Methods to Estimate the Conformation of Proteins and Polypeptides from Circular Dichroism Data, Analytical Biochemistry, vol.235, issue.1, pp.1-10, 1996. ,
DOI : 10.1006/abio.1996.0084
Using circular dichroism spectra to estimate protein secondary structure, Nature Protocols, vol.79, issue.6, pp.2876-2890, 2007. ,
DOI : 10.1016/j.bbapap.2005.06.005
[4] Circular dichroism, In Methods in Enzymology Biochemical Spectroscopy, vol.246, pp.34-71, 1995. ,
DOI : 10.1016/0076-6879(95)46006-3
Peptide models for ??-turns., International Journal of Peptide and Protein Research, vol.102, issue.4, pp.411-419, 1984. ,
DOI : 10.1111/j.1399-3011.1982.tb02608.x
Exploring the Self-Assembly of a Short Aromatic A??(16???24) Peptide, Langmuir, vol.29, issue.8, 2013. ,
DOI : 10.1021/la304585a
Vacuum ultraviolet circular dichroism of fibronectin dominant tyrosine effects, Journal of Molecular Biology, vol.197, issue.4, pp.743-745, 1987. ,
DOI : 10.1016/0022-2836(87)90481-5
UV Transition Moments of Tyrosine, The Journal of Physical Chemistry B, vol.118, issue.31, pp.9247-9257 ,
DOI : 10.1021/jp5065352
Principles of Fluorescence Spectroscopy Fluorometric Determination of Amyloid Fibrils in Vitro Using the Fluorescent Dye, Thioflavin T1, Anal. Biochem, vol.177, issue.722, pp.244-249, 1989. ,
Use of the Phase Diagram Method to Analyze the Protein Unfolding-Refolding Reactions:?? Fishing Out the ???Invisible??? Intermediates, Journal of Proteome Research, vol.3, issue.3, pp.485-494, 2004. ,
DOI : 10.1021/pr034094y
, Biochemistry, vol.42, issue.9, pp.42-2720, 2003.
DOI : 10.1021/bi027166s
A possible role for ??-stacking in the self-assembly of amyloid fibrils, The FASEB Journal, vol.16, issue.1, pp.77-83, 2002. ,
DOI : 10.1006/jmbi.2000.3840
Role of Aromatic Interactions in Amyloid FormaYon by PepYdes Derived from Human Amylin ?, Biochemistry (Mosc, issue.50, pp.43-15901, 2004. ,
Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase, Protein Science, vol.15, issue.4, pp.862-870, 2006. ,
DOI : 10.1110/ps.051915806
Hydrophobic, Aromatic, and Electrostatic Interactions Play a Central Role in Amyloid Fibril Formation and Stability, Biochemistry, vol.50, issue.12, pp.50-2061, 2011. ,
DOI : 10.1021/bi101936c
[27] Circular dichroism and optical rotatory dispersion of proteins and polypeptides, Methods Enzym, vol.27, pp.675-735, 1973. ,
DOI : 10.1016/S0076-6879(73)27030-1
Aromatic side-chain contributions to the far ultraviolet circular dichroism of peptides and proteins, Biopolymers, vol.43, issue.6, pp.1451-1467, 1978. ,
DOI : 10.1088/0370-1298/69/3/307
Theoretical study of the contribution of aromatic side chains to the circular dichroism of basic bovine pancreatic trypsin inhibitor, Biochemistry, vol.28, issue.21, pp.28-8609, 1989. ,
DOI : 10.1021/bi00447a051
Circular dichroism studies of barnase and its mutants: Characterization of the contribution of aromatic side chains, Biochemistry, vol.32, issue.39, pp.32-10303, 1993. ,
DOI : 10.1021/bi00090a005
Progress towards understanding ??-sheet structure, Bioorganic & Medicinal Chemistry, vol.4, issue.6, pp.739-766, 1996. ,
DOI : 10.1016/0968-0896(96)00051-X
DISCO: a low-energy multipurpose beamline at synchrotron SOLEIL, Journal of Synchrotron Radiation, vol.16, issue.6, pp.16-835, 2009. ,
DOI : 10.1107/S0909049509034049
URL : https://hal.archives-ouvertes.fr/hal-01479318
Calibration and quality assurance procedures at the far UV linear and circular dichroism experimental station DISCO, Journal of Physics: Conference Series, vol.425, issue.12, pp.425-122014, 2013. ,
DOI : 10.1088/1742-6596/425/12/122014
CDtool???an integrated software package for circular dichroism spectroscopic data processing, analysis, and archiving, Analytical Biochemistry, vol.332, issue.2, pp.285-289, 2004. ,
DOI : 10.1016/j.ab.2004.06.002
Simultaneous determination of photometric accuracy during circular dichroism measurements, Analytical Methods, vol.26, issue.7, p.929, 2010. ,
DOI : 10.1039/b9ay00216b