Squalamine and Its Derivatives Modulate the Aggregation of Amyloid-β and α-Synuclein and Suppress the Toxicity of Their Oligomers.

Autor: Limbocker R; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, United Kingdom.; Department of Chemistry & Life Science, United States Military Academy, West Point, NY, United States., Staats R; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, United Kingdom., Chia S; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, United Kingdom., Ruggeri FS; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, United Kingdom.; Laboratory of Organic Chemistry, Wageningen University, Wageningen, Netherlands.; Laboratory of Physical Chemistry, Wageningen University, Wageningen, Netherlands., Mannini B; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, United Kingdom., Xu CK; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, United Kingdom., Perni M; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, United Kingdom., Cascella R; Department of Experimental and Clinical Biomedical Sciences, University of Florence, Florence, Italy., Bigi A; Department of Experimental and Clinical Biomedical Sciences, University of Florence, Florence, Italy., Sasser LR; Department of Chemistry & Life Science, United States Military Academy, West Point, NY, United States., Block NR; Department of Chemistry & Life Science, United States Military Academy, West Point, NY, United States., Wright AK; Department of Chemistry & Life Science, United States Military Academy, West Point, NY, United States., Kreiser RP; Department of Chemistry & Life Science, United States Military Academy, West Point, NY, United States., Custy ET; Department of Chemistry & Life Science, United States Military Academy, West Point, NY, United States., Meisl G; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, United Kingdom., Errico S; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, United Kingdom.; Department of Experimental and Clinical Biomedical Sciences, University of Florence, Florence, Italy., Habchi J; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, United Kingdom., Flagmeier P; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, United Kingdom., Kartanas T; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, United Kingdom., Hollows JE; Department of Chemistry & Life Science, United States Military Academy, West Point, NY, United States., Nguyen LT; Department of Chemistry & Life Science, United States Military Academy, West Point, NY, United States., LeForte K; Department of Chemistry & Life Science, United States Military Academy, West Point, NY, United States., Barbut D; Enterin Inc., Philadelphia, PA, United States., Kumita JR; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, United Kingdom., Cecchi C; Department of Experimental and Clinical Biomedical Sciences, University of Florence, Florence, Italy., Zasloff M; Enterin Inc., Philadelphia, PA, United States.; MedStar Georgetown Transplant Institute, School of Medicine, Georgetown University, Washington, DC, United States., Knowles TPJ; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, United Kingdom.; Cavendish Laboratory, Department of Physics, University of Cambridge, Cambridge, United Kingdom., Dobson CM; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, United Kingdom., Chiti F; Department of Experimental and Clinical Biomedical Sciences, University of Florence, Florence, Italy., Vendruscolo M; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, United Kingdom.

Publikováno v: Frontiers in neuroscience [Front Neurosci] 2021 Jun 18; Vol. 15, pp. 680026. Date of Electronic Publication: 2021 Jun 18 (Print Publication: 2021).

Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism.

Autor: Limbocker R; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.; Department of Chemistry and Life Science, United States Military Academy, West Point, NY, 10996, USA., Mannini B; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK., Ruggeri FS; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK., Cascella R; Department of Experimental and Clinical Biomedical Science, University of Florence, 50134, Florence, Italy., Xu CK; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK., Perni M; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK., Chia S; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK., Chen SW; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK., Habchi J; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK., Bigi A; Department of Experimental and Clinical Biomedical Science, University of Florence, 50134, Florence, Italy., Kreiser RP; Department of Chemistry and Life Science, United States Military Academy, West Point, NY, 10996, USA., Wright AK; Department of Chemistry and Life Science, United States Military Academy, West Point, NY, 10996, USA., Albright JA; Department of Chemistry and Life Science, United States Military Academy, West Point, NY, 10996, USA., Kartanas T; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK., Kumita JR; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK., Cremades N; Institute for Biocomputation and Physics of Complex Systems (BIFI)-Joint Unit BIFI-IQFR (CSIC), University of Zaragoza, 50018, Zaragoza, Spain., Zasloff M; MedStar-Georgetown Transplant Institute, Georgetown University School of Medicine, Washington, DC, 20010, USA., Cecchi C; Department of Experimental and Clinical Biomedical Science, University of Florence, 50134, Florence, Italy., Knowles TPJ; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.; Cavendish Laboratory, Department of Physics, University of Cambridge, Cambridge, CB3 0HE, UK., Chiti F; Department of Experimental and Clinical Biomedical Science, University of Florence, 50134, Florence, Italy. fabrizio.chiti@unifi.it., Vendruscolo M; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK. mv245@cam.ac.uk., Dobson CM; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.

Publikováno v: Communications biology [Commun Biol] 2020 Aug 13; Vol. 3 (1), pp. 435. Date of Electronic Publication: 2020 Aug 13.

Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases.

Autor: Rinauro, Dillon J.¹ (AUTHOR), Chiti, Fabrizio² (AUTHOR), Vendruscolo, Michele¹ (AUTHOR) mv245@cam.ac.uk, Limbocker, Ryan³ (AUTHOR) ryan.limbocker@westpoint.edu

Publikováno v: Molecular Neurodegeneration. 2/20/2024, Vol. 19 Issue 1, p1-32. 32p.

α-Synuclein oligomers and fibrils: partners in crime in synucleinopathies.

Autor: Bigi, Alessandra, Cascella, Roberta, Cecchi, Cristina

Publikováno v: Neural Regeneration Research; Nov2023, Vol. 18 Issue 11, p2332-2342, 11p

Research Progress and Applications of Multivalent, Multispecific and Modified Nanobodies for Disease Treatment.

Autor: Wang, Jiewen, Kang, Guangbo, Yuan, Haibin, Cao, Xiaocang, Huang, He, de Marco, Ario

Publikováno v: Frontiers in Immunology; 1/18/2022, p1-19, 19p