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- 2020
- The role of fibril structure and surface hydrophobicity in secondary nucleation of amyloid fibrils
- The catalytic nature of protein aggregation
- Identification of on- And off-pathway oligomers in amyloid fibril formation
-
Ultrastructural evidence for self-replication of alzheimer-associated Aβ42 amyloid along the sides of fibrils
Tornquist, Mattias LU ; Cukalevski, Risto LU ; Weininger, Ulrich LU ; Meisl, Georg ; Knowles, Tuomas P.J. ; Leiding, Thom LU ; Malmendal, Anders LU ; Akke, Mikael LU
and Linse, Sara
LU
(2020)
In Proceedings of the National Academy of Sciences of the United States of America
117(21).
p.11265-11273
Mark
- Kinetic diversity of amyloid oligomers
- Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors
- Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide
- Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies
- 2019
-
Autocatalytic amplification of Alzheimer-associated Aβ42 peptide aggregation in human cerebrospinal fluid
Frankel, Rebecca LU ; Törnquist, Mattias LU ; Meisl, Georg ; Hansson, Oskar LU
; Andreasson, Ulf
; Zetterberg, Henrik
LU
; Blennow, Kaj
LU
; Frohm, Birgitta
LU
; Cedervall, Tommy
LU
and Knowles, Tuomas P.J.
, et al.
(2019)
In Communications Biology
2(1).
Mark
- A method of predicting the in vitro fibril formation propensity of Aβ40 mutants based on their inclusion body levels in E. coli