Year |
Citation |
Score |
2020 |
Monsellier E, Bendifallah M, Redeker V, Melki R. Polypeptides derived from α-Synuclein binding partners to prevent α-Synuclein fibrils interaction with and take-up by cells. Plos One. 15: e0237328. PMID 32790707 DOI: 10.1371/Journal.Pone.0237328 |
0.324 |
|
2016 |
Monsellier E, Bousset L, Melki R. α-Synuclein and huntingtin exon 1 amyloid fibrils bind laterally to the cellular membrane. Scientific Reports. 6: 19180. PMID 26757959 DOI: 10.1038/Srep19180 |
0.341 |
|
2015 |
Monsellier E, Redeker V, Ruiz-Arlandis G, Bousset L, Melki R. Molecular interaction between the chaperone Hsc70 and the N-terminal flank of huntingtin exon 1 modulates aggregation. The Journal of Biological Chemistry. 290: 2560-76. PMID 25505179 DOI: 10.1074/Jbc.M114.603332 |
0.4 |
|
2014 |
Månsson C, Kakkar V, Monsellier E, Sourigues Y, Härmark J, Kampinga HH, Melki R, Emanuelsson C. DNAJB6 is a peptide-binding chaperone which can suppress amyloid fibrillation of polyglutamine peptides at substoichiometric molar ratios. Cell Stress & Chaperones. 19: 227-39. PMID 23904097 DOI: 10.1007/S12192-013-0448-5 |
0.372 |
|
2012 |
Ramazzotti M, Monsellier E, Kamoun C, Degl'Innocenti D, Melki R. Polyglutamine repeats are associated to specific sequence biases that are conserved among eukaryotes. Plos One. 7: e30824. PMID 22312432 DOI: 10.1371/Journal.Pone.0030824 |
0.389 |
|
2010 |
Monsellier E, Ramazzotti M, Taddei N, Chiti F. A computational approach for identifying the chemical factors involved in the glycosaminoglycans-mediated acceleration of amyloid fibril formation. Plos One. 5: e11363. PMID 20613870 DOI: 10.1371/Journal.Pone.0011363 |
0.426 |
|
2009 |
Motamedi-Shad N, Monsellier E, Torrassa S, Relini A, Chiti F. Kinetic analysis of amyloid formation in the presence of heparan sulfate: faster unfolding and change of pathway. The Journal of Biological Chemistry. 284: 29921-34. PMID 19700762 DOI: 10.1074/Jbc.M109.018747 |
0.432 |
|
2009 |
Motamedi-Shad N, Monsellier E, Chiti F. Amyloid formation by the model protein muscle acylphosphatase is accelerated by heparin and heparan sulphate through a scaffolding-based mechanism. Journal of Biochemistry. 146: 805-14. PMID 19675100 DOI: 10.1093/Jb/Mvp128 |
0.399 |
|
2008 |
Monsellier E, Ramazzotti M, Taddei N, Chiti F. Aggregation propensity of the human proteome. Plos Computational Biology. 4: e1000199. PMID 18927604 DOI: 10.1371/Journal.Pcbi.1000199 |
0.445 |
|
2007 |
Monsellier E, Ramazzotti M, de Laureto PP, Tartaglia GG, Taddei N, Fontana A, Vendruscolo M, Chiti F. The distribution of residues in a polypeptide sequence is a determinant of aggregation optimized by evolution. Biophysical Journal. 93: 4382-91. PMID 17766358 DOI: 10.1529/Biophysj.107.111336 |
0.34 |
|
2007 |
Monsellier E, Chiti F. Prevention of amyloid-like aggregation as a driving force of protein evolution. Embo Reports. 8: 737-42. PMID 17668004 DOI: 10.1038/Sj.Embor.7401034 |
0.444 |
|
2006 |
Monsellier E, Bedouelle H. Improving the stability of an antibody variable fragment by a combination of knowledge-based approaches: validation and mechanisms. Journal of Molecular Biology. 362: 580-93. PMID 16926023 DOI: 10.1016/J.Jmb.2006.07.044 |
0.496 |
|
2005 |
Monsellier E, Bedouelle H. Quantitative measurement of protein stability from unfolding equilibria monitored with the fluorescence maximum wavelength. Protein Engineering, Design & Selection : Peds. 18: 445-56. PMID 16087653 DOI: 10.1093/Protein/Gzi046 |
0.505 |
|
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