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Recent Scientific Publications

Please follow the link (the DOI number) to the article at the journal homepage. Be aware that not all articles are open access.


Gaspar R, Lind M, Spaee, E, Linse S.

Anomalous Salt Dependence Reveals an Interplay of Attractive and Repulsive Electrostatic interactions in alpha-synuclein Fibril Formation.

QRBD 2020. Doi: 10.1017/grd2020.7


Linse S, Scheidt T, Bernfur K, Vendruscolo M, Dobson CM, Cohen SIA, Sileikis E, Lundqvist M, Qian F, O'Malley T, Bussiere T, Weinreb PH, Xu CK, Meisl G, Devenish SRA, Knowles TPJ, Hansson O.

Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies.

Nat Struct Mol Biol. 2020 Sep 28. doi: 10.1038/s41594-020-0505-6.


Törnquist M, Cukalevski R, Weininger U, Meisl G, Knowles TPJ, Leiding T, Malmendal A, Akke M, Linse S.

Ultrastructural evidence for self-replication of Alzheimer-associated Aβ42 amyloid along the sides of fibrils.

Proc Natl Acad Sci U S A. 2020 May 26;117(21):11265-11273. doi: 10.1073/pnas.1918481117.


Thacker D, Sanagavarapu K, Frohm B, Meisl G, Knowles TPJ, Linse S.

The role of fibril structure and surface hydrophobicity in secondary nucleation of amyloid fibrils.

Proc Natl Acad Sci U S A. 2020 Oct 13;117(41):25272-25283. doi: 10.1073/pnas.2002956117.


Dear AJ, Michaels TCT, Meisl G, Klenerman D, Wu S, Perrett S, Linse S, Dobson CM, Knowles TPJ.

Kinetic diversity of amyloid oligomers.

Proc Natl Acad Sci U S A. 2020 Jun 2;117(22):12087-12094. doi: 10.1073/pnas.1922267117.


Dear AJ, Meisl G, Michaels TCT, Zimmermann MR, Linse S, Knowles TPJ.

The catalytic nature of protein aggregation.

J Chem Phys. 2020 Jan 31;152(4):045101. doi: 10.1063/1.5133635.


Peduzzo A, Linse S, Buell AK.

The Properties of α-Synuclein Secondary Nuclei Are Dominated by the Solution Conditions Rather than the Seed Fibril Strain.

ACS Chem Neurosci. 2020 Mar 18;11(6):909-918. doi: 10.1021/acschemneuro.9b00594.


Michaels TCT, Šarić A, Curk S, Bernfur K, Arosio P, Meisl G, Dear AJ, Cohen SIA, Dobson CM, Vendruscolo M, Linse S, Knowles TPJ.

Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptide.

Nat Chem. 2020 May;12(5):445-451. doi: 10.1038/s41557-020-0452-1.


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

Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors.

Proc Natl Acad Sci U S A. 2020 Sep 29;117(39):24251-24257. doi: 10.1073/pnas.2006684117.


Dear AJ, Meisl G, Šarić A, Michaels TCT, Kjaergaard M, Linse S, Knowles TPJ.

Identification of on- and off-pathway oligomers in amyloid fibril formation.

Chem Sci. 2020 Jun 8;11(24):6236-6247. doi: 10.1039/c9sc06501f.


Zhang Y, Herling TW, Kreida S, Peter QAE, Kartanas T, Törnroth-Horsefield S, Linse S, Knowles TPJ.

A microfluidic strategy for the detection of membrane protein interactions.

Lab Chip. 2020 Aug 26;20(17):3230-3238. doi: 10.1039/d0lc00205d


Linse S.

Expression and Purification of Intrinsically Disordered Aβ Peptide and Setup of Reproducible Aggregation Kinetics Experiment.

Methods Mol Biol. 2020;2141:731-754. doi: 10.1007/978-1-0716-0524-0_38.


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

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

Nat Struct Mol Biol. 2020 Oct;27(10):886-891. doi: 10.1038/s41594-020-0471-z.


McGauran G, Linse S, O'Connell DJ.

Single Step Purification of Glycogen Synthase Kinase Isoforms from Small Scale Transient Expression in HEK293 Cells with a Calcium-Dependent Fragment Complementation System.

Methods Mol Biol. 2020;2095:385-396. doi: 10.1007/978-1-0716-0191-4_22



Sanagavarapu K, Nüske E, Nasir I, Meisl G, Immink JN, Sormanni P, Vendruscolo M, Knowles TPJ, Malmendal A, Cabaleiro-Lago C, Linse S.

A method of predicting the in vitro fibril formation propensity of Aβ40 mutants based on their inclusion body levels in E. coli.

Sci Rep. 2019 Mar 6;9(1):3680. doi:10.1038/s41598-019-39216-z.


Frankel R, Törnquist M, Meisl G, Hansson O, Andreasson U, Zetterberg H, Blennow K, Frohm B, Cedervall T, Knowles TPJ, Leiding T, Linse S.

Autocatalytic amplification of Alzheimer-associated Aβ42 peptide aggregation in human cerebrospinal fluid.

Commun Biol. 2019 Oct 8;2:365. doi:10.1038/s42003-019-0612-2.


Galvagnion C, Topgaard D, Makasewicz K, Buell AK, Linse S, Sparr E, Dobson CM.

Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils.

J Phys Chem Lett. 2019 Dec 19;10(24):7872-7877. doi: 10.1021/acs.jpclett.9b03005.


Sparr E, Linse S.

Lipid-protein interactions in amyloid formation.

Biochim Biophys Acta Proteins Proteom. 2019 May;1867(5):455-457. doi: 10.1016/j.bbapap.2019.03.006.


Weiffert T, Meisl G, Flagmeier P, De S, Dunning CJR, Frohm B, Zetterberg H, Blennow K, Portelius E, Klenerman D, Dobson CM, Knowles TPJ, Linse S.

Increased Secondary Nucleation Underlies Accelerated Aggregation of the Four-Residue N-Terminally Truncated Aβ42 Species Aβ5-42.

ACS Chem Neurosci. 2019 May 15;10(5):2374-2384. doi: 10.1021/acschemneuro.8b00676


Scheidt T, Łapińska U, Kumita JR, Whiten DR, Klenerman D, Wilson MR, Cohen SIA, Linse S, Vendruscolo M, Dobson CM, Knowles TPJ, Arosio P.

Secondary nucleation and elongation occur at different sites on Alzheimer's amyloid-β aggregates.

Sci Adv. 2019 Apr 17;5(4):eaau3112. doi: 10.1126/sciadv.aau3112.


Aspuru-Guzik A, Baik MH, Balasubramanian S, Banerjee R, Bart S, Borduas- Dedekind N, Chang S, Chen P, Corminboeuf C, Coudert FX, Cronin L, Crudden C, Cuk T, Doyle AG, Fan C, Feng X, Freedman D, Furukawa S, Ghosh S, Glorius F, Jeffries-El M, Katsonis N, Li A, Linse SS, Marchesan S, Maulide N, Milo A, Narayan ARH, Naumov P, Nevado C, Nyokong T, Palacin R, Reid M, Robinson C, Robinson G, Sarpong R, Schindler C, Schlau-Cohen GS, Schmidt TW, Sessoli R, Shao-Horn Y, Sleiman H, Sutherland J, Taylor A, Tezcan A, Tortosa M, Walsh A, Watson AJB, Weckhuysen BM, Weiss E, Wilson D, Yam VW, Yang X, Ying JY, Yoon T, You SL, Zarbin AJG, Zhang H.

Charting a course for chemistry.

Nat Chem. 2019

Apr;11(4):286-294. doi: 10.1038/s41557-019-0236-7.


Pogostin BH, Linse S, Olsson U.

Fibril Charge Affects α-Synuclein Hydrogel Rheological Properties.

Langmuir. 2019 Dec 17;35(50):16536-16544. doi: 10.1021/acs.langmuir.9b02516.


Gaspar R, Pallbo J, Weininger U, Linse S, Sparr E.

Ganglioside lipids accelerate α-synuclein amyloid formation.

Biochim Biophys Acta Proteins Proteom. 2019 May;1867(5):508-518. doi: 10.1016/j.bbapap.2018.07.004.


Jensen KS, Linse S, Nilsson M, Akke M, Malmendal A.

Revealing Well-Defined Soluble States during Amyloid Fibril Formation by Multilinear Analysis of NMR Diffusion Data.

J Am Chem Soc. 2019 Nov 27;141(47):18649-18652. doi: 10.1021/jacs.9b07952.


Ermert D, Laabei M, Weckel A, Mörgelin M, Lundqvist M, Björck L, Ram S, Linse S, Blom AM.

The Molecular Basis of Human IgG-Mediated Enhancement of C4b-Binding Protein Recruitment to Group A Streptococcus.

Front Immunol. 2019 Jun 4;10:1230. doi: 10.3389/fimmu.2019.01230.


Khan MAI, Respondek M, Kjellström S, Deep S, Linse S, Akke M.

Cu/Zn Superoxide Dismutase Forms Amyloid Fibrils under Near-Physiological Quiescent Conditions: The Roles of Disulfide Bonds and Effects of Denaturant.

ACS Chem Neurosci. 2017 Sep 20;8(9):2019-2026. doi: 10.1021/acschemneuro.7b00162.


Boza-Serrano A, Ruiz R, Sanchez-Varo R, García-Revilla J, Yang Y, Jimenez-Ferrer I, Paulus A, Wennström M, Vilalta A, Allendorf D, Davila JC, Stegmayr J, Jiménez S, Roca-Ceballos MA, Navarro-Garrido V, Swanberg M, Hsieh CL, Real LM, Englund E, Linse S, Leffler H, Nilsson UJ, Brown GC, Gutierrez A, Vitorica J, Venero JL, Deierborg T.

Galectin-3, a novel endogenous TREM2 ligand, detrimentally regulates inflammatory response in Alzheimer's disease.

Acta Neuropathol. 2019 Aug;138(2):251-273. doi: 10.1007/s00401-019-02013-z


Limbocker, R., Chia, S., Ruggeri, F.S., Perni, M., Cascella, R., Heller, G.T., Meisl, G., Mannini, B., Habchi, J., Michaels, T.C.T., Challa, P.K., Ahn, M., Casford, S.T., Fernando, N., Xu, C.K., Kloss, N.D., Cohen, S.I.A., Kumita, J.R., Cecchi, C., Zasloff, M., Linse, S., Knowles, T.P.J., Chiti, F., Vendruscolo, M., and Dobson, C.M.

Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes

Nature Communicationsvolume,2019, 10, Article number: 225, 10.1038/s41467-018-07699-5



Chia, S., Habchi, J., Michaels, T.C.T., Cohen, S.I.A., Linse, S., Dobson, C.M., Knowles, T.P.J., and Vendruscolo, M.

SAR by kinetics for drug discovery in protein misfolding diseases

PNAS, 2018, vol. 115, no. 41, 10245-10250, 10.1073/pnas.1807884115


Gaspar, R., Jon Pallbo, J., Ulrich Weininger, U., Sara Linse S., and Sparr, E.

Ganglioside lipids accelerate α-synuclein amyloid formation

BBA - Proteins and Proteomics, 2018, 1866, 1062-1072, 10.1016/j.bbapap.2018.07.004


Kreida, S., Roche, J.V., Olsson, C., Linse, S., and Törnroth-Horsefield, S.

Protein–protein interactions in AQP regulation – biophysical characterization of AQP0–CaM and AQP2–LIP5 complex formation

Faraday Discuss., 2018, 209, 35-54, 10.1039/C8FD00065D


Weiffert, T., and Linse, S.

Protein stabilization with retained function of monellin using a split GFP system

Scientific Reports, 2018, 8, Article number: 12763, 10.1038/s41598-018-31177-z


Törnquist, M., Michaels, T.C.T., Sanagavarapu, K., Yang, X., Meisl, G., Cohen, S.I.A., Knowles, T.P.J, and Linse, S.

Secondary nucleation in amyloid formation

Chem. Commun., 2018, 54, 8667-8684, 10.1039/c8cc02204f


Ní Mhurchú, N., Zoubak, L., Gavin McGauran, G., Linse, S., Yeliseev, A., and O’Connell, D.J.

Simplifying G Protein-Coupled Receptor Isolation with a Calcium-Dependent Fragment Complementation Affinity System

Biochemistry, 2018, 57, 4383-4390, 10.1021/acs.biochem.8b00469


Dalton, S.R., Vienneau, A.R., Burstein, S.R., Xu, R.J., Linse, S., and Londergan, C.H.,

Cyanylated Cysteine Reports Site-Specific Changes at Protein–Protein-Binding Interfaces Without Perturbation

Biochemistry, 2018, 57, 3702–3712, 10.1021/acs.biochem.8b00283


Yang, X., Meisl, G., Frohm, B., Thulin, E., Knowles, T.P.T., and Linse, S.

On the role of sidechain size and charge in the aggregation of Aβ42 with familial mutations

PNAS, 2018, 115, E5849–E5858, 10.1073/pnas.1803539115


Månsson, C., van Cruchten, R.T.P., Weininger, U., Yang, X., Cukalevski, R., Arosio, P., Dobson, C.M., Knowles, T.P.J., Akke, M., Linse, S., and Emanuelsson, C.

Conserved S/T-residues of the human chaperone DNAJB6 are required for effective inhibition of Aβ42 amyloid fibril formation

Biochemistry, 2018, 10.1021/acs.biochem.8b00353


Meisl, G., Michaels, T.C.T., Linse, S., and Knowles, T.P.J.

Kinetic Analysis of Amyloid Formation

June 2018Methods in molecular biology (Clifton, N.J.) 1779:181-196

DOI: 10.1007/978-1-4939-7816-8_12

In book: Amyloid Proteins


Habchi, J., Chia, S., Galvagnion, C., Michaels, T.C.T., Bellaiche, M.M.J., Ruggeri, F.S., Sanguanini, M., Idini, I., Kumita, J.R., Sparr, E., Linse, S., Dobson, C.M., Knowles T.P.J., and Vendruscolo, M.

Cholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes

Nature Chemistryvolume 10, pages673–683 (2018) 10.1038/s41557-018-0031-x


Cohen, S.I.A., Cukalevski, R., Michaels, T.C.T., Šarić, A., Törnquist, M., Vendruscolo, M., Dobson, C.M., Buell, A.K., Knowles, T.P.J., and Linse, S.

Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide

Nature Chemistry (2018), 10.1038/s41557-018-0023-x


Tesei, G., Hellstrand, E., Sanagavarapu, K., Linse, S., Sparr, E., Vacha, R., and Lund, M.

Aggregate Size Dependence of Amyloid Adsorption onto Charged Interfaces

Langmuir 2018, 34, 1266−1273, : 10.1021/acs.langmuir.7b03155


Saar, K.L., Zhang, Y., Müller, T., Kumar, C.P., Devenish, S., Lynn, A., Łapińska, U., Yang, X., Linse, S., and Knowles, T.P.T.

On-chip label-free protein analysis with downstream electrodes for direct removal of electrolysis products

Lab Chip, 2018, 18, 162, 10.1039/c7lc00797c

Mattsson, K., Aguilar, R., Torstensson, O., Perry, D., Bernfur, K., Linse, S., Hansson, L.A., Åkerfeldt, K.S., and Cedervall, T.

Disaggregation of gold nanoparticles by Daphnia magna

NANOTOXICOLOGY, 2018, 12, 885-90, 10.1080/17435390.2018.1485982

O'Malley, T.T., Linse, S., and Walsh, D.M.

Production and Use of Recombinant A beta for Aggregation Studies

Book Series: Methods in Molecular Biology,   Volume: 1777   Pages: 307-320   Published: 2018 10.1007/978-1-4939-7811-3_19




Saar, K.L., Zhang, Y., Müller, T., Kumar, C.P., Devenish, S., Lynn, A., Lapinska, U., Yang, X., Linse, S., and Knowles, T.P.J.

On-chip label-free protein analysis with downstream electrodes for direct removal of electrolysis products.

Lab on a Chip, 2017, 10.1039/C7LC00797C


Donovan, K.J., Jain, S.K., Silvers, R., Linse, S., and Griffin, R.G.,

Proton Assisted Recoupling (PAR) in Peptides and Proteins.

J. Phys. Chem. B, 2017, 10.1021/acs.jpcb.7b08934


Mattsson, K., Johnson, E.V., Malmendal, A., Linse, S., Hansson, L.-A., and Cedervall, T.

Brain damage and behavioural disorders in fish induced by plastic nanoparticles delivered through the food chain.

Scientific Reports, 2017, 7: 11452, 10.1038/s41598-017-10813-0


Meisl, G., Rajah, L.,  Cohen, S.A.I.,  Pfammatter, M.,  Šarić, A.,  Hellstrand, E.,  Buell, A.K.,  Aguzzi, A.,  Linse, S.,  Vendruscolo, M.,  Dobson, C.M.,  and  Knowles, T.P.J.

Scaling behaviour and rate-determining steps in filamentous self-assembly.

Chem. Sci., 2017, 10.1039/C7SC01965C


Meisl, G., Yang, X., Dobson, C.M., Linse. S., and Knowles, T.P.J.

Modulation of electrostatic interactions to reveal a reaction network unifying the aggregation behaviour of the Aβ42 peptide and its variants

Chem. Sci., 2017, 8, 4352-4362, 10.1039/c7sc00215g


Khan, M.A.I., Respondek, M., Kjellström, S., Deep, S., Linse, S., and Akke, M.

Cu/Zn Superoxide Dismutase Forms Amyloid Fibrils under Near-Physiological Quiescent Conditions: The Roles of Disulfide Bonds and Effects of Denaturant

ACS Chemical Neuroscience, 2017, 10.1021/acschemneuro.7b00162


Chia, S., Flagmeier, P., Habchi, J, Lattanzi, V., Linse, S., Dobson, C.M., Knowles, T.P.J., and Vendruscolo, M.

Monomeric and fibrillar α-synuclein exert opposite effects on the catalytic cycle that promotes the proliferation of Aβ42 aggregates

PNAS, 2017, 114, 8005-8010, 10.1073/pnas.1700239114


Munke, A., Persson, J., Weiffert, T., De Genst, E., Meisl, G., Arosio, P., Carnerup, A., Dobson, C.M., Vendruscolo, M., Knowles, T.P.J., and Linse, S.

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

PNAS, 2017, 114, 6444-6449, 10.1073/pnas.1700407114


Linse, S.,

Monomer-dependent secondary nucleation in amyloid formation

Biophys Rev, 2017, 10.1007/s12551-017-0289-z


Aprile, F.A., Sormanni, P., Perni, M., Arosio, P., Linse, S., Knowles, T.P.J., Dobson, C.M., and Vendruscolo, M.

Selective targeting of primary and secondarynucleation pathways in Ab42 aggregation using arational antibody scanning method.

Sci. Adv. 2017; 3: e1700488 10.1126/sciadv.1700488


Gaspar, R., Meisl, G., Buell, A.K., Young, L., Kaminski, C.F., and Knowles, T.P.J.

Acceleration of α-synuclein aggregation

Amyloid-The Journal of Protein Folding Disorders Volume 24, 2017 - Issue sup1, 10.1080/13506129.2017.1292904


Donovan, K.J., Silvers, R., Linse, S., and Griffin, R.G.

A 3D MAS NMR experiment utilizing through-space 15N-15N correlations

J. Am. Chem. Soc., 2017, 10.1021/jacs.7b01159


Lundqvist, M., Augustsson, C., Lilja, M., Lundkvist, K., Dahlbäck, B., Linse, S., and Cedervall, T.

The nanoparticle protein corona formed in human blood or human blood fractions

PLOS One, 2017, 10.1371/journal.pone.0175871



Habchi, J., Chia, S., Limbocker, R., Mannini, B., Ahn, M., Perni, M., Hansson, O., Arosio, P., Kumita, J.R., Kumar Challa, P., Cohen, S.I.A, Linse, S., Dobson, C.M., Knowles, T.P.J., and Vendruscolo, M.

Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer’s disease

PNAS,2016, 10.1073/pnas.1615613114


Padayachee, E.R., Zetterberg, H. , Portelius, E. , Borén, J., Molinuevo, J.L., Andreasen, N., Cukalevski, R., Linse, S., Blennow, K. and Andreasson, U. 

Cerebrospinal fluid-induced retardation of amyloid β aggregation correlates with Alzheimer's disease and the APOE ε4 allele

Brain Research, 2016, 1651, 11-16, 10.1016/j.brainres.2016.09.022


Sanagavarapu, K., Weiffert, T., Mhurchú, N.N., O’Connell, D., and Linse, S.

Calcium Binding and Disulfide Bonds Regulate the Stability of Secretagogin towards Thermal and Urea Denaturation

PLOSone, 2016, 10.1371/journal.pone.0165709


O'Malley, T.T.; Wittbold, W.M., Linse, S., and Walsh D.M.

The aggregation paths and products of Aβ42 dimers are distinct from Aβ42 monomer

Biochemistry, 2016, 10.1021/acs.biochem.6b00453


Šarić, A., Buell, A.K., Meisl, G., Michaels, T.C.T., Dobson, C.M., Linse, S., Knowles T.P.J., and Frenkel D.,

Physical determinants of the self-replication of protein fibrils

Nature Physics, 2016, 10.1038/nphys3828


Colvin, M.T., Silvers, R., Ni, Q.Z., Can, T.V., Sergeyev, I.V., Rosay, M., Donovan, K.J., Michael, B., Wall, J.S., Linse, S., and Griffin, R.G.,

Atomic Resolution Structure of Monomorphic AB42 Amyloid Fibrils

J. Am. Chem. Soc., 2016, 10.1021/jacs.6b05129


Herling, T.W., O’Connell, D.J., Bauer, M.C., Persson, J., Weininger, U., Knowles, T.P.J., and Linse, S.

A Microfluidic Platform for Real-Time Detection and Quantification of Protein-Ligand Interactions

Biophys J., 2016, 110(9), 1957-66, 10.1016/j.bpj.2016.03.038


Kakkar, V., Månsson, C., de Mattos, E.P., Bergink, S., van der Zwaag, M., van Waarde, M.A.W.H., Kloosterhuis, N.J., Melki, R., van Cruchten, R.T.P., Al-Karadaghi, S., Arosio, P., Dobson, C.M., Knowles, T.P.J., Bates, G.P., van Deursen, J.M., Linse, S., van de Sluis, B., Emanuelsson, C., and Kampinga, H.H.

The S/T-Rich Motif in the DNAJB6 Chaperone Delays Polyglutamine Aggregation and the Onset of Disease in a Mouse Model

Molecular Cell, 2016, 10.1016/j.molcel.2016.03.017


Arosioa, P., Cedervall, T.,  Knowles, T.P.J., Linse, S.

Analysis of the length distribution of amyloid fibrils by centrifugal sedimentation

Analytical Biochemistry, 2016, 10.1016/j.ab.2016.03.015


Arosio, P., Michaels, T.C.T., Linse, S., Månsson, C., Emanuelsson, C., Presto, J., Johansson, J., Vendruscolo, M., Dobson C.M., and Knowles, T.P.J.

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

Nature Communications 7, 2016, Article number: 10948, 10.1038/ncomms10948


Habchi, J., Arosio, P., Perni, M., Costa, A.R., Yagi-Utsumi, M., Joshi, P., Chia, S., Cohen, S.I.A., Müller, M.B.D., Linse, S., Nollen, E.A.A., Dobson, C.M., Knowles, T.P.J., and Vendruscolo, M.

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

Science Advances, 2016, Vol. 2, no. 2, e1501244, 10.1126/sciadv.1501244


Meisl, G., Yang, X., Frohm, B., Knowles T.P.J., and Linse, S.

Quantitative analysis of intrinsic and extrinsic factors in the aggregation mechanism of Alzheimer-associated Aβ-peptide

Scientific Reports, 2016,  6, Article number: 18728, doi:10.1038/srep18728


Meisl, G., Kirkegaard, J.B., Arosio, P., Michaels, T.C.T., Vendruscolo, M., Dobson, C.M., Linse, S., and Knowles T.P.J.

Molecular mechanisms of protein aggregation from global fitting of kinetic models.

Nature Protocols, 2016, 11, 252–272, 10.1038/nprot.2016.010


Arosio, P., Müller, T., Rajah, L., Yates, E.V., Aprile, F.A., Zhang, Y., Cohen, S.I.A., White, D.A., Herling, T.W., De Genst, E.J., Linse, S., Vendruscolo, M., Dobson, C.M, and Knowles T.P.J.

Microfluidic Diffusion Analysis of the Sizes and Interactions of Proteins under Native Solution Conditions.

ACS Nano, 10.1021/acsnano.5b04713



Dunning, C.J., McGauran, G., Willén, K., Gouras, G.K., O'Connell,D.J., and Linse, S.

A direct high affinity interaction between Aβ42 and GSK3α stimulates hyperphosphorylation of tau. A new molecular link in Alzheimer's disease?

ACS Chem. Neurosci., 10.1021/acschemneuro.5b00262


Szczepankiewics, O., Linse, B., Meisl, G., Thulin, E., Frohm, B., Frigerio, C.S., Colvin, T.M. Jacavone, A.C., Griffin, R.G., Knowles, T.P.J., Walsh, D.M., and Linse, S.

N-terminal extensions retard Abeta42 fibril formation but allow cross-seeding and co-aggregation with Abeta42.

J. Am. Chem. Soc., 2015, 137 (46), 14673-14685, 10.1021/jacs.5b07849


Yates, E., Muller, T., Rajah, L., De Genst, E., Arosio, P., Linse, S., Vendruscolo, M., Dobson, C., and Knowles, T.

Latent analysis of unmodified biomolecules and their complexes in solution with attomole detection sensitivity

Nature Chemistry, 2015, 7(10), 802-9, 10.1038/nchem.2344


Nasir, I., Fatih, W., Svensson, A., Radu, D., Linse, S., Cabaleiro Lago, C., and Lundqvist, M.

High Throughput Screening Method to Explore Protein Interactions with Nanoparticles.

PLoS ONE, 2015, 10(8), e0 136687, 10.1371/journal.pone.0136687


Nasir, I., Linse, S., and Cabaleiro-Lago, C.

Fluorescent Filter-Trap Assay for Amyloid Fibril Formation Kinetics in Complex Solutions.

ACS Chemical Neuroscience, 2015, 6(8), 1436-1444, 10.1021/acschemneuro.5b00104


Colvin, M.T., Silvers, R., Frohm, B., Su, Y., Linse, S. and Griffin, R.G.

High Resolution Structural Characterization of Aβ42 Amyloid Fibrils by Magic Angle Spining NMR

J. Am. Chem. Soc., 2015, 137, 7509-7518, 10.1021/jacs.5b03997


Herling, T.W., Arosio, P., Mueller, T., Linse, S., and Knowels, T.P.J.

A Microfluidic Platform for Quantitative Measurments of Effective Protein Charges and Single Ion Binding In Solution.

Physical Chemistry Chemical Physics, 2015, 17(18), 12161-12167, 10.1039/c5cp00746a


Arosio, P., Knowles, T.P.J., and Linse, S.

On the Lag Phase in Amyloid Fibril Formation.

Physical Chemistry Chemical Physics, 2015, 17(12), 7606-7618, 10.1039/c4cp05563b


Wallerstein, J., Weininger, U., Khan, M. A. I., Linse, S. and Akke, M.

Site-Specific Protonation Kinetics of Acidic Side Chains in Proteins Determined by Ph-Dependent Carboxyl (13)C Nmr Relaxation

J. Am. Chem. Soc., 2015, 137, 3093-101, 10.1021/ja513205s


Cohen, S. I. A., Arosio, P., Presto, J., Kurudenkandy, F. R., Biverstal, H., Dolfe, L., Dunning, C., Yang, X., Frohm, B., Vendruscolo, M., Johansson, J., Dobson, C. M., Fisahn, A., Knowles, T. P. J. and Linse, S.

A Molecular Chaperone Breaks the Catalytic Cycle That Generates Toxic Abeta Oligomers

Nat. Struct. Mol. Biol., 2015, 22, 207-13, 10.1038/nsmb.2971


Sondergaard, M. T., Sorensen, A. B., Skov, L. L., Kjaer-Sorensen, K., Bauer, M. C., Nyegaard, M., Linse, S., Oxvig, C. and Overgaard, M. T.

Calmodulin Mutations Causing Catecholaminergic Polymorphic Ventricular Tachycardia Confer Opposing Functional and Biophysical Molecular Changes

The FEBS journal, 2015, 282, 803-16, 10.1111/febs.13184


Singh, B., Al Jubair, T., Morgelin, M., Sundin, A., Linse, S., Nilsson, U. J. and Riesbeck, K.

Haemophilus Influenzae Surface Fibril (Hsf) Is a Unique Twisted Hairpin-Like Trimeric Autotransporter

International Journal of Medical Microbiology, 2015, 305, 27-37, 10.1016/j.ijmm.2014.10.004


Shimanovich, U., Efimov, I., Mason, T. O., Flagmeier, P., Buell, A. K., Gedanken, A., Linse, S., Akerfeldt, K. S., Dobson, C. M., Weitz, D. A. and Knowles, T. P. J.

Protein Microgels from Amyloid Fibril Networks

Acs Nano, 2015, 9, 43-51, 10.1021/nn504869d


Mattsson, K., Ekvall, M. T., Hansson, L.-A., Linse, S., Malmendal, A. and Cedervall, T.

Altered Behavior, Physiology, and Metabolism in Fish Exposed to Polystyrene Nanoparticles

Environmental Science & Technology, 2015, 49, 553-561, 10.1021/es5053655


Cukalevski, R., Yang, X., Meisl, G., Weininger, U., Bemfur, K., Frohm, B., Knowles, T.P.J., and Linse, S.

The A beta 40 and A beta 42 Peptides Self-assemble into Seperate Homomolecular Fibrils in Binary Mixtures but Cross-react During Primary Nucleation.

Chemical Science, 2015, 6(7), 4215-4233, 10.1039/c4sc02517b


Jonsson, T., Memon, A. A., Sundquist, K., Sundquist, J., Olsson, S., Nalla, A., Bauer, M. and Linse, S.

Digested Wheat Gluten Inhibits Binding between Leptin and Its Receptor

BMC Biochemistry, 2015, 16, 10.1186/s12858-015-0032-y


Grey, M., Dunning, C. J., Gaspar, R., Grey, C., Brundin, P., Sparr, E. and Linse, S.

Acceleration of Alpha-Synuclein Aggregation by Exosomes

Journal of Biological Chemistry, 2015, 290, 2969-2982, 10.1074/jbc.M114.585703


Frohm, B., DeNizio, J. E., Lee, D. S. M., Gentile, L., Olsson, U., Malm, J., Akerfeldt, K. S. and Linse, S.

A Peptide from Human Semenogelin I Self-Assembles into a Ph-Responsive Hydrogel

Soft Matter, 2015, 11, 414-421, 10.1039/c4sm01793e



Vacha, R., Linse, S. and Lund, M.

Surface Effects on Aggregation Kinetics of Amyloidogenic Peptides

Journal of the American Chemical Society, 2014, 136, 11776-11782, 10.1021/ja505502e


Sanfins, E., Augustsson, C., Dahlback, B., Linse, S. and Cedervall, T.

Size-Dependent Effects of Nanoparticles on Enzymes in the Blood Coagulation Cascade

Nano Letters, 2014, 14, 4736-4744, 10.1021/nl501863u


O'Malley, T. T., Oktaviani, N. A., Zhang, D., Lomakin, A., O'Nuallain, B., Linse, S., Benedek, G. B., Rowan, M. J., Mulder, F. A. A. and Walsh, D. M.

A Beta Dimers Differ from Monomers in Structural Propensity, Aggregation Paths and Population of Synaptotoxic Assemblies

Biochemical Journal, 2014, 461, 413-426, 10.1042/bj20140219


Meisl, G., Yang, X., Hellstrand, E., Frohm, B., Kirkegaard, J. B., Cohen, S. I. A., Dobson, C. M., Linse, S. and Knowles, T. P. J.

Differences in Nucleation Behavior Underlie the Contrasting Aggregation Kinetics of the a Beta 40 and a Beta 42 Peptides

Proceedings of the National Academy of Sciences of the United States of America, 2014, 111, 9384-9389, 10.1073/pnas.1401564111


Mansson, C., Arosio, P., Hussein, R., Kampinga, H. H., Hashem, R. M., Boelens, W. C., Dobson, C. M., Knowles, T. P. J., Linse, S. and Emanuelsson, C.

Interaction of the Molecular Chaperone Dnajb6 with Growing Arnyloid-Beta 42 (a Beta 42) Aggregates Leads to Sub-Stoichiometric Inhibition of Amyloid Formation

Journal of Biological Chemistry, 2014, 289, 31066-31076, 10.1074/jbc.M114.595124


Hermansson, E., Schultz, S., Crowther, D., Linse, S., Winblad, B., Westermark, G., Johansson, J. and Presto, J.

The Chaperone Domain Brichos Prevents Cns Toxicity of Amyloid-Beta Peptide in Drosophila Melanogaster

Disease Models & Mechanisms, 2014, 7, 659-665, 10.1242/dmm.014787


Dell'Orco, D., Lundqvist, M., Linse, S. and Cedervall, T.

Mathematical Modeling of the Protein Corona: Implications for Nanoparticulate Delivery Systems

Nanomedicine, 2014, 9, 851-858, 10.2217/nnm.14.39


Buell, A. K., Galvagnion, C., Gaspar, R., Sparr, E., Vendruscolo, M., Knowles, T. P. J., Linse, S. and Dobson, C. M.

Solution Conditions Determine the Relative Importance of Nucleation and Growth Processes in Alpha-Synuclein Aggregation

Proceedings of the National Academy of Sciences of the United States of America, 2014, 111, 7671-7676, 10.1073/pnas.1315346111


Assarsson, A., Linse, S. and Cabaleiro-Lago, C.

Effects of Polyamino Acids and Polyelectrolytes on Amyloid Beta Fibril Formation

Langmuir, 2014, 30, 8812-8818, 10.1021/la501414j


Assarsson, A., Hellstrand, E., Cabaleiro-Lago, C. and Linse, S.

Charge Dependent Retardation of Amyloid Beta Aggregation by Hydrophilic Proteins

Acs Chemical Neuroscience, 2014, 5, 266-274, 10.1021/cn400124r


Arosio, P., Cukalevski, R., Frohm, B., Knowles, T. P. J. and Linse, S.

Quantification of the Concentration of a Beta 42 Propagons During the Lag Phase by an Amyloid Chain Reaction Assay

Journal of the American Chemical Society, 2014, 136, 219-225, 10.1021/ja408765u



Slavov, N., Carey, J. and Linse, S.

Calmodulin Transduces Ca2+ Oscillations into Differential Regulation of Its Target Proteins

Acs Chemical Neuroscience, 2013, 4, 601-612, 10.1021/cn300218d


Knight, S. D., Presto, J., Linse, S. and Johansson, J.

The Brichos Domain, Amyloid Fibril Formation, and Their Relationship

Biochemistry, 2013, 52, 7523-7531, 10.1021/bi400908x


Hellstrand, E., Nowacka, A., Topgaard, D., Linse, S. and Sparr, E.

Membrane Lipid Co-Aggregation with Alpha-Synuclein Fibrils

Plos One, 2013, 8, 10.1371/journal.pone.0077235


Hellstrand, E., Kukora, S., Shuman, C. F., Steenbergen, S., Thulin, E., Kohli, A., Krouse, B., Linse, S. and Akerfeldt, K. S.

Forster Resonance Energy Transfer Studies of Calmodulin Produced by Native Protein Ligation Reveal Inter-Domain Electrostatic Repulsion

Febs Journal, 2013, 280, 2675-2687, 10.1111/febs.12269


Hellstrand, E., Grey, M., Ainalem, M.-L., Ankner, J., Forsyth, V. T., Fragneto, G., Haertlein, M., Dauvergne, M.-T., Nilsson, H., Brundin, P., Linse, S., Nylander, T. and Sparr, E.

Adsorption of Alpha-Synuclein to Supported Lipid Bilayers: Positioning and Role of Electrostatics

Acs Chemical Neuroscience, 2013, 4, 1339-1351, 10.1021/cn400066t


Ekvall, M. T., Bianco, G., Linse, S., Linke, H., Backman, J. and Hansson, L.-A.

Three-Dimensional Tracking of Small Aquatic Organisms Using Fluorescent Nanoparticles

Plos One, 2013, 8, 10.1371/journal.pone.0078498


Cohen, S. I. A., Linse, S., Luheshi, L. M., Hellstrand, E., White, D. A., Rajah, L., Otzen, D. E., Vendruscolo, M., Dobson, C. M. and Knowles, T. P. J.

Proliferation of Amyloid-Beta 42 Aggregates Occurs through a Secondary Nucleation Mechanism

Proceedings of the National Academy of Sciences of the United States of America, 2013, 110, 9758-9763, 10.1073/pnas.1218402110



Willander, H., Presto, J., Askarieh, G., Biverstal, H., Frohm, B., Knight, S. D., Johansson, J. and Linse, S.

Brichos Domains Efficiently Delay Fibrillation of Amyloid Beta-Peptide

Journal of Biological Chemistry, 2012, 287, 31608-31617, 10.1074/jbc.M112.393157


Wahlstrom, A., Cukalevski, R., Danielsson, J., Jarvet, J., Onagi, H., Rebek, J., Jr., Linse, S. and Graslund, A.

Specific Binding of a Beta-Cyclodextrin Dimer to the Amyloid Beta Peptide Modulates the Peptide Aggregation Process

Biochemistry, 2012, 51, 4280-4289, 10.1021/bi300341j


Oslakovic, C., Cedervall, T., Linse, S. and Dahlback, B.

Polystyrene Nanoparticles Affecting Blood Coagulation

Nanomedicine-Nanotechnology Biology and Medicine, 2012, 8, 981-986, 10.1016/j.nano.2011.12.001


Ferreira, S. A., Oslakovic, C., Cukalevski, R., Frohm, B., Dahlback, B., Linse, S., Gama, F. M. and Cedervall, T.

Biocompatibility of Mannan Nanogel-Safe Interaction with Plasma Proteins

Biochimica Et Biophysica Acta-General Subjects, 2012, 1820, 1043-1051, 10.1016/j.bbagen.2012.04.015


Dell'Orco, D., Sulmann, S., Linse, S. and Koch, K.-W.

Dynamics of Conformational Ca2+-Switches in Signaling Networks Detected by a Planar Plasmonic Device

Analytical Chemistry, 2012, 84, 2982-2989, 10.1021/ac300213j


Dell'Orco, D., Lundqvist, M., Cedervall, T. and Linse, S.

Delivery Success Rate of Engineered Nanoparticles in the Presence of the Protein Corona: A Systems-Level Screening

Nanomedicine-Nanotechnology Biology and Medicine, 2012, 8, 1271-1281, 10.1016/j.nano.2012.02.006


Cukalevski, R., Boland, B., Frohm, B., Thulin, E., Walsh, D. and Linse, S.

Role of Aromatic Side Chains in Amyloid Beta-Protein Aggregation

Acs Chemical Neuroscience, 2012, 3, 1008-1016, 10.1021/cn300073s


Cedervall, T., Hansson, L.-A., Lard, M., Frohm, B. and Linse, S.

Food Chain Transport of Nanoparticles Affects Behaviour and Fat Metabolism in Fish

Plos One, 2012, 7, 10.1371/journal.pone.0032254


Cabaleiro-Lago, C., Szczepankiewicz, O. and Linse, S.

The Effect of Nanoparticles on Amyloid Aggregation Depends on the Protein Stability and Intrinsic Aggregation Rate

Langmuir, 2012, 28, 1852-1857, 10.1021/la203078w


Reddy, S. B., Anders, R. F., Beeson, J. G., Farnert, A., Kironde, F., Berenzon, S. K., Wahlgren, M., Linse, S. and Persson, K. E. M.

High Affinity Antibodies to Plasmodium Falciparum Merozoite Antigens Are Associated with Protection from Malaria

PLoS One, 2012, 7, 10.1371/journal.pone.0032242


Behnen, P., Davis, E., Delaney, E., Frohm, B., Bauer, M., Cedervall, T., O'Connell, D., Akerfeldt, K. S. and Linse, S.

Calcium-Dependent Interaction of Calmodulin with Human 80s Ribosomes and Polyribosomes

Biochemistry, 2012, 51, 6718-6727, 10.1021/bi3005939