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.
2020
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.
2019
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
2018
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
PEPTIDE SELF-ASSEMBLY: METHODS AND PROTOCOLS
Book Series: Methods in Molecular Biology, Volume: 1777 Pages: 307-320 Published: 2018 10.1007/978-1-4939-7811-3_19
2017
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
2016
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
2015
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
http://pubs.acs.org/doi/abs/10.1021%2Fjacs.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
2014
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
2013
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
2012
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