Biophysical studies of protein misfolding and aggregation in in vivo models of Alzheimer's and Parkinson's diseases - ERRATUM.

Sinnige T, Stroobants K, Dobson CM, Vendruscolo M

Rapid Structural, Kinetic, and Immunochemical Analysis of Alpha-Synuclein Oligomers in Solution.

Arter WE, Xu CK, Castellana-Cruz M, Herling TW, Krainer G, Saar KL, Kumita JR, Dobson CM, Knowles TPJ

Small-molecule sequestration of amyloid-β as a drug discovery strategy for Alzheimer's disease.

Heller GT, Aprile FA, Michaels TCT, Limbocker R, Perni M, Ruggeri FS, Mannini B, LĂśhr T, Bonomi M, Camilloni C, De Simone A, Felli IC, Pierattelli R, Knowles TPJ, Dobson CM, Vendruscolo M

The extent of protein hydration dictates the preference for heterogeneous or homogeneous nucleation generating either parallel or antiparallel β-sheet ι-synuclein aggregates.

Camino JD, Gracia P, Chen SW, Sot J, de la Arada I, SebastiĂĄn V, Arrondo JLR, GoĂąi FM, Dobson CM, Cremades N

Direct measurement of lipid membrane disruption connects kinetics and toxicity of Aβ42 aggregation.

Flagmeier P, De S, Michaels TCT, Yang X, Dear AJ, Emanuelsson C, Vendruscolo M, Linse S, Klenerman D, Knowles TPJ, Dobson CM

Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors.

Michaels TCT, Šarić A, Meisl G, Heller GT, Curk S, Arosio P, Linse S, Dobson CM, Vendruscolo M, Knowles TPJ

Amelioration of aggregate cytotoxicity by catalytic conversion of protein oligomers into amyloid fibrils.

Yang J, Dear AJ, Yao QQ, Liu Z, Dobson CM, Knowles TPJ, Wu S, Perrett S

A rationally designed bicyclic peptide remodels Aβ42 aggregation in vitro and reduces its toxicity in a worm model of Alzheimer's disease.

Ikenoue T, Aprile FA, Sormanni P, Ruggeri FS, Perni M, Heller GT, Haas CP, Middel C, Limbocker R, Mannini B, Michaels TCT, Knowles TPJ, Dobson CM, Vendruscolo M

Probing the unfolded protein response in long-lived naked mole-rats.

Du Z, Chakrabarti S, Kulaberoglu Y, Smith ESJ, Dobson CM, Itzhaki LS, Kumita JR

Structural Characterization of Covalently Stabilized Human Cystatin C Oligomers.

Chrabąszczewska M, Sieradzan AK, Rodziewicz-Motowidło S, Grubb A, Dobson CM, Kumita JR, Kozak M

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

Limbocker R, Mannini B, Ruggeri FS, Cascella R, Xu CK, Perni M, Chia S, Chen SW, Habchi J, Bigi A, Kreiser RP, Wright AK, Albright JA, Kartanas T, Kumita JR, Cremades N, Zasloff M, Cecchi C, Knowles TPJ, Chiti F, Vendruscolo M, Dobson CM

Half a century of amyloids: past, present and future.

Ke PC, Zhou R, Serpell LC, Riek R, Knowles TPJ, Lashuel HA, Gazit E, Hamley IW, Davis TP, Fändrich M, Otzen DE, Chapman MR, Dobson CM, Eisenberg DS, Mezzenga R

Rationally Designed Antibodies as Research Tools to Study the Structure-Toxicity Relationship of Amyloid-β Oligomers.

Limbocker R, Mannini B, Cataldi R, Chhangur S, Wright AK, Kreiser RP, Albright JA, Chia S, Habchi J, Sormanni P, Kumita JR, Ruggeri FS, Dobson CM, Chiti F, Aprile FA, Vendruscolo M

Rational design of a conformation-specific antibody for the quantification of Aβ oligomers.

Aprile FA, Sormanni P, Podpolny M, Chhangur S, Needham LM, Ruggeri FS, Perni M, Limbocker R, Heller GT, Sneideris T, Scheidt T, Mannini B, Habchi J, Lee SF, Salinas PC, Knowles TPJ, Dobson CM, Vendruscolo M

Biophysical studies of protein misfolding and aggregation in in vivo models of Alzheimer's and Parkinson's diseases.

Sinnige T, Stroobants K, Dobson CM, Vendruscolo M