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High-Efficiency Expression and Purification of DNAJB6b Based on the pH-Modulation of Solubility and Denaturant-Modulation of Size
High-Efficiency Expression and Purification of DNAJB6b Based on the pH-Modulation of Solubility and Denaturant-Modulation of Size
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High-Efficiency Expression and Purification of DNAJB6b Based on the pH-Modulation of Solubility and Denaturant-Modulation of Size

Linse, Sara

Molecules (Basel, Switzerland), 2022-01, Vol.27 (2), p.418 [Periódico revisado por pares]

Switzerland: MDPI AG

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2
Amyloids and protein aggregation
Amyloids and protein aggregation
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Amyloids and protein aggregation

Linse, Sara ; Knowles, Tuomas

Chemical science (Cambridge), 2023-06, Vol.14 (24), p.6491-6492 [Periódico revisado por pares]

England: Royal Society of Chemistry

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3
Food chain transport of nanoparticles affects behaviour and fat metabolism in fish
Food chain transport of nanoparticles affects behaviour and fat metabolism in fish
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Food chain transport of nanoparticles affects behaviour and fat metabolism in fish

Cedervall, Tommy ; Hansson, Lars-Anders ; Lard, Mercy ; Frohm, Birgitta ; Linse, Sara Bansal, Vipul

PloS one, 2012-02, Vol.7 (2), p.e32254 [Periódico revisado por pares]

United States: Public Library of Science

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4
Retardation of Aβ42 fibril formation by apolipoprotein A-I and recombinant HDL particles
Retardation of Aβ42 fibril formation by apolipoprotein A-I and recombinant HDL particles
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Retardation of Aβ42 fibril formation by apolipoprotein A-I and recombinant HDL particles

Frankel, Rebecca ; Sparr, Emma ; Linse, Sara

The Journal of biological chemistry, 2023-11, Vol.299 (11), p.105273-105273, Article 105273 [Periódico revisado por pares]

United States: Elsevier Inc

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5
Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation
Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation
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Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation

Buell, Alexander K. ; Galvagnion, Céline ; Gaspar, Ricardo ; Sparr, Emma ; Vendruscolo, Michele ; Knowles, Tuomas P. J. ; Linse, Sara ; Dobson, Christopher M.

Proceedings of the National Academy of Sciences - PNAS, 2014-05, Vol.111 (21), p.7671-7676 [Periódico revisado por pares]

United States: National Academy of Sciences

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6
Membrane lipid co-aggregation with α-synuclein fibrils
Membrane lipid co-aggregation with α-synuclein fibrils
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Membrane lipid co-aggregation with α-synuclein fibrils

Hellstrand, Erik ; Nowacka, Agnieszka ; Topgaard, Daniel ; Linse, Sara ; Sparr, Emma van der Wel, Patrick

PloS one, 2013-10, Vol.8 (10), p.e77235-e77235 [Periódico revisado por pares]

United States: Public Library of Science

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7
Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides
Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides
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Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides

Meisl, Georg ; Yang, Xiaoting ; Hellstrand, Erik ; Frohm, Birgitta ; Kirkegaard, Julius B ; Cohen, Samuel I A ; Dobson, Christopher M ; Linse, Sara ; Knowles, Tuomas P J

Proceedings of the National Academy of Sciences - PNAS, 2014-07, Vol.111 (26), p.9384-9389 [Periódico revisado por pares]

United States: National Academy of Sciences

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8
Kinetic diversity of amyloid oligomers
Kinetic diversity of amyloid oligomers
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Kinetic diversity of amyloid oligomers

Dear, Alexander J. ; Michaels, Thomas C. T. ; Meisl, Georg ; Klenerman, David ; Wu, Si ; Perrett, Sarah ; Linse, Sara ; Dobson, Christopher M. ; Knowles, Tuomas P. J.

Proceedings of the National Academy of Sciences - PNAS, 2020-06, Vol.117 (22), p.12087-12094 [Periódico revisado por pares]

United States: National Academy of Sciences

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9
On the Aggregation of Apolipoprotein A-I
On the Aggregation of Apolipoprotein A-I
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On the Aggregation of Apolipoprotein A-I

Frankel, Rebecca ; Sparr, Emma ; Linse, Sara

International journal of molecular sciences, 2022-08, Vol.23 (15), p.8780 [Periódico revisado por pares]

Basel: MDPI AG

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10
Amyloid-β peptide 37, 38 and 40 individually and cooperatively inhibit amyloid-β 42 aggregation
Amyloid-β peptide 37, 38 and 40 individually and cooperatively inhibit amyloid-β 42 aggregation
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Amyloid-β peptide 37, 38 and 40 individually and cooperatively inhibit amyloid-β 42 aggregation

Braun, Gabriel A ; Dear, Alexander J ; Sanagavarapu, Kalyani ; Zetterberg, Henrik ; Linse, Sara

Chemical science (Cambridge), 2022-02, Vol.13 (8), p.2423-2439 [Periódico revisado por pares]

England: Royal Society of Chemistry

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