Linse S - Search Results

1

The chaperone domain BRICHOS prevents CNS toxicity of amyloid-β peptide in Drosophila melanogaster.

Hermansson E, Schultz S, Crowther D, Linse S, Winblad B, Westermark G, Johansson J, Presto J. Hermansson E, et al. Among authors: linse s. Dis Model Mech. 2014 Jun;7(6):659-65. doi: 10.1242/dmm.014787. Epub 2014 Mar 28. Dis Model Mech. 2014. PMID: 24682783 Free PMC article.

2

BRICHOS domains efficiently delay fibrillation of amyloid β-peptide.

Willander H, Presto J, Askarieh G, Biverstål H, Frohm B, Knight SD, Johansson J, Linse S. Willander H, et al. Among authors: linse s. J Biol Chem. 2012 Sep 7;287(37):31608-17. doi: 10.1074/jbc.M112.393157. Epub 2012 Jul 16. J Biol Chem. 2012. PMID: 22801430 Free PMC article.

3

Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism.

Cohen SI, Linse S, Luheshi LM, Hellstrand E, White DA, Rajah L, Otzen DE, Vendruscolo M, Dobson CM, Knowles TP. Cohen SI, et al. Among authors: linse s. Proc Natl Acad Sci U S A. 2013 Jun 11;110(24):9758-63. doi: 10.1073/pnas.1218402110. Epub 2013 May 23. Proc Natl Acad Sci U S A. 2013. PMID: 23703910 Free PMC article.

4

The BRICHOS domain, amyloid fibril formation, and their relationship.

Knight SD, Presto J, Linse S, Johansson J. Knight SD, et al. Among authors: linse s. Biochemistry. 2013 Oct 29;52(43):7523-31. doi: 10.1021/bi400908x. Epub 2013 Oct 17. Biochemistry. 2013. PMID: 24099305

5

Effects of polyamino acids and polyelectrolytes on amyloid β fibril formation.

Assarsson A, Linse S, Cabaleiro-Lago C. Assarsson A, et al. Among authors: linse s. Langmuir. 2014 Jul 29;30(29):8812-8. doi: 10.1021/la501414j. Epub 2014 Jul 14. Langmuir. 2014. PMID: 24978100 Free PMC article.

6

Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation.

Månsson C, Arosio P, Hussein R, Kampinga HH, Hashem RM, Boelens WC, Dobson CM, Knowles TP, Linse S, Emanuelsson C. Månsson C, et al. Among authors: linse s. J Biol Chem. 2014 Nov 7;289(45):31066-76. doi: 10.1074/jbc.M114.595124. Epub 2014 Sep 12. J Biol Chem. 2014. PMID: 25217638 Free PMC article.

7

A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers.

Cohen SIA, Arosio P, Presto J, Kurudenkandy FR, Biverstal H, Dolfe L, Dunning C, Yang X, Frohm B, Vendruscolo M, Johansson J, Dobson CM, Fisahn A, Knowles TPJ, Linse S. Cohen SIA, et al. Among authors: linse s. Nat Struct Mol Biol. 2015 Mar;22(3):207-213. doi: 10.1038/nsmb.2971. Epub 2015 Feb 16. Nat Struct Mol Biol. 2015. PMID: 25686087 Free PMC article.

8

An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer's disease.

Habchi J, Arosio P, Perni M, Costa AR, Yagi-Utsumi M, Joshi P, Chia S, Cohen SI, Müller MB, Linse S, Nollen EA, Dobson CM, Knowles TP, Vendruscolo M. Habchi J, et al. Among authors: linse s. Sci Adv. 2016 Feb 12;2(2):e1501244. doi: 10.1126/sciadv.1501244. eCollection 2016 Feb. Sci Adv. 2016. PMID: 26933687 Free PMC article.

9

Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation.

Arosio P, Michaels TC, Linse S, Månsson C, Emanuelsson C, Presto J, Johansson J, Vendruscolo M, Dobson CM, Knowles TP. Arosio P, et al. Among authors: linse s. Nat Commun. 2016 Mar 24;7:10948. doi: 10.1038/ncomms10948. Nat Commun. 2016. PMID: 27009901 Free PMC article.

10

Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication.

Munke A, Persson J, Weiffert T, De Genst E, Meisl G, Arosio P, Carnerup A, Dobson CM, Vendruscolo M, Knowles TPJ, Linse S. Munke A, et al. Among authors: linse s. Proc Natl Acad Sci U S A. 2017 Jun 20;114(25):6444-6449. doi: 10.1073/pnas.1700407114. Epub 2017 Jun 5. Proc Natl Acad Sci U S A. 2017. PMID: 28584111 Free PMC article.

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