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Items: 1 to 50 of 224

1.

Secondary nucleation in amyloid formation.

Törnquist M, Michaels TCT, Sanagavarapu K, Yang X, Meisl G, Cohen SIA, Knowles TPJ, Linse S.

Chem Commun (Camb). 2018 Jul 6. doi: 10.1039/c8cc02204f. [Epub ahead of print]

PMID:
29978862
2.

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

Kreida S, Roche JV, Olsson C, Linse S, Törnroth-Horsefield S.

Faraday Discuss. 2018 Jul 4. doi: 10.1039/c8fd00065d. [Epub ahead of print]

PMID:
29972182
3.

Simplifying G protein-coupled receptor isolation with a calcium-dependent fragment complementation affinity system.

Mhurchú NN, Zoubak L, McGauran G, Linse S, Yeliseev AA, O'Connell DJ.

Biochemistry. 2018 Jun 29. doi: 10.1021/acs.biochem.8b00469. [Epub ahead of print]

PMID:
29956929
4.

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

Yang X, Meisl G, Frohm B, Thulin E, Knowles TPJ, Linse S.

Proc Natl Acad Sci U S A. 2018 Jun 26;115(26):E5849-E5858. doi: 10.1073/pnas.1803539115. Epub 2018 Jun 12.

5.

Kinetic Analysis of Amyloid Formation.

Meisl G, Michaels TCT, Linse S, Knowles TPJ.

Methods Mol Biol. 2018;1779:181-196. doi: 10.1007/978-1-4939-7816-8_12.

PMID:
29886534
6.

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

Dalton SR, Vienneau AR, Burstein SR, Xu RJ, Linse S, Londergan CH.

Biochemistry. 2018 Jul 3;57(26):3702-3712. doi: 10.1021/acs.biochem.8b00283. Epub 2018 Jun 5.

7.

Production and Use of Recombinant Aβ for Aggregation Studies.

O'Malley TT, Linse S, Walsh DM.

Methods Mol Biol. 2018;1777:307-320. doi: 10.1007/978-1-4939-7811-3_19.

PMID:
29744844
8.

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

Habchi J, Chia S, Galvagnion C, Michaels TCT, Bellaiche MMJ, Ruggeri FS, Sanguanini M, Idini I, Kumita JR, Sparr E, Linse S, Dobson CM, Knowles TPJ, Vendruscolo M.

Nat Chem. 2018 Jun;10(6):673-683. doi: 10.1038/s41557-018-0031-x. Epub 2018 May 7.

PMID:
29736006
9.

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

Cohen SIA, Cukalevski R, Michaels TCT, Šarić A, Törnquist M, Vendruscolo M, Dobson CM, Buell AK, Knowles TPJ, Linse S.

Nat Chem. 2018 May;10(5):523-531. doi: 10.1038/s41557-018-0023-x. Epub 2018 Mar 26.

PMID:
29581486
10.

Conformational Ensembles of Calmodulin Revealed by Nonperturbing Site-Specific Vibrational Probe Groups.

Kelly KL, Dalton SR, Wai RB, Ramchandani K, Xu RJ, Linse S, Londergan CH.

J Phys Chem A. 2018 Mar 22;122(11):2947-2955. doi: 10.1021/acs.jpca.8b00475. Epub 2018 Mar 9.

11.

Aggregate Size Dependence of Amyloid Adsorption onto Charged Interfaces.

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

Langmuir. 2018 Jan 30;34(4):1266-1273. doi: 10.1021/acs.langmuir.7b03155. Epub 2018 Jan 17.

12.

Secondary nucleation of monomers on fibril surface dominates α-synuclein aggregation and provides autocatalytic amyloid amplification.

Gaspar R, Meisl G, Buell AK, Young L, Kaminski CF, Knowles TPJ, Sparr E, Linse S.

Q Rev Biophys. 2017 Jan;50:e6. doi: 10.1017/S0033583516000172.

PMID:
29233218
13.

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

Saar KL, Zhang Y, Müller T, Kumar CP, Devenish S, Lynn A, Łapińska U, Yang X, Linse S, Knowles TPJ.

Lab Chip. 2017 Dec 19;18(1):162-170. doi: 10.1039/c7lc00797c.

PMID:
29192926
14.

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

Meisl G, Rajah L, Cohen SAI, Pfammatter M, Šarić A, Hellstrand E, Buell AK, Aguzzi A, Linse S, Vendruscolo M, Dobson CM, Knowles TPJ.

Chem Sci. 2017 Oct 1;8(10):7087-7097. doi: 10.1039/c7sc01965c. Epub 2017 Aug 31.

15.

Proton-Assisted Recoupling (PAR) in Peptides and Proteins.

Donovan KJ, Jain SK, Silvers R, Linse S, Griffin RG.

J Phys Chem B. 2017 Dec 7;121(48):10804-10817. doi: 10.1021/acs.jpcb.7b08934. Epub 2017 Nov 27.

PMID:
29043804
16.

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

Meisl G, Yang X, Dobson CM, Linse S, Knowles TPJ.

Chem Sci. 2017 Jun 1;8(6):4352-4362. doi: 10.1039/c7sc00215g. Epub 2017 Apr 26.

17.

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

Mattsson K, Johnson EV, Malmendal A, Linse S, Hansson LA, Cedervall T.

Sci Rep. 2017 Sep 13;7(1):11452. doi: 10.1038/s41598-017-10813-0.

18.

Monomer-dependent secondary nucleation in amyloid formation.

Linse S.

Biophys Rev. 2017 Aug;9(4):329-338. doi: 10.1007/s12551-017-0289-z. Epub 2017 Aug 15. Review.

19.

Aggregation and Fibril Structure of AβM01-42 and Aβ1-42.

Silvers R, Colvin MT, Frederick KK, Jacavone AC, Lindquist S, Linse S, Griffin RG.

Biochemistry. 2017 Sep 12;56(36):4850-4859. doi: 10.1021/acs.biochem.7b00729. Epub 2017 Aug 30.

PMID:
28792214
20.

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

Chia S, Flagmeier P, Habchi J, Lattanzi V, Linse S, Dobson CM, Knowles TPJ, Vendruscolo M.

Proc Natl Acad Sci U S A. 2017 Jul 25;114(30):8005-8010. doi: 10.1073/pnas.1700239114. Epub 2017 Jul 11.

21.

Selective targeting of primary and secondary nucleation pathways in Aβ42 aggregation using a rational antibody scanning method.

Aprile FA, Sormanni P, Perni M, Arosio P, Linse S, Knowles TPJ, Dobson CM, Vendruscolo M.

Sci Adv. 2017 Jun 21;3(6):e1700488. doi: 10.1126/sciadv.1700488. eCollection 2017 Jun.

22.

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

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

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

23.

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.

Proc Natl Acad Sci U S A. 2017 Jun 20;114(25):6444-6449. doi: 10.1073/pnas.1700407114. Epub 2017 Jun 5.

24.

3D MAS NMR Experiment Utilizing Through-Space 15N-15N Correlations.

Donovan KJ, Silvers R, Linse S, Griffin RG.

J Am Chem Soc. 2017 May 17;139(19):6518-6521. doi: 10.1021/jacs.7b01159. Epub 2017 May 3.

PMID:
28447786
25.

Acceleration of α-synuclein aggregation.

Gaspar R, Meisl G, Buell AK, Young L, Kaminski CF, Knowles TPJ, Sparr E, Linse S.

Amyloid. 2017 Mar;24(sup1):20-21. doi: 10.1080/13506129.2017.1292904. No abstract available.

PMID:
28434341
26.

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

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

PLoS One. 2017 Apr 17;12(4):e0175871. doi: 10.1371/journal.pone.0175871. eCollection 2017.

27.

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

Habchi J, Chia S, Limbocker R, Mannini B, Ahn M, Perni M, Hansson O, Arosio P, Kumita JR, Challa PK, Cohen SI, Linse S, Dobson CM, Knowles TP, Vendruscolo M.

Proc Natl Acad Sci U S A. 2017 Jan 10;114(2):E200-E208. doi: 10.1073/pnas.1615613114. Epub 2016 Dec 23.

28.

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

Sanagavarapu K, Weiffert T, Ní Mhurchú N, O'Connell D, Linse S.

PLoS One. 2016 Nov 3;11(11):e0165709. doi: 10.1371/journal.pone.0165709. eCollection 2016.

29.

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

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

Brain Res. 2016 Nov 15;1651:11-16. doi: 10.1016/j.brainres.2016.09.022. Epub 2016 Sep 23.

30.

The Aggregation Paths and Products of Aβ42 Dimers Are Distinct from Those of the Aβ42 Monomer.

O'Malley TT, Witbold WM 3rd, Linse S, Walsh DM.

Biochemistry. 2016 Nov 8;55(44):6150-6161. Epub 2016 Oct 26.

31.

Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils.

Colvin MT, Silvers R, Ni QZ, Can TV, Sergeyev I, Rosay M, Donovan KJ, Michael B, Wall J, Linse S, Griffin RG.

J Am Chem Soc. 2016 Aug 3;138(30):9663-74. doi: 10.1021/jacs.6b05129. Epub 2016 Jul 14.

32.

Translocation of 40 nm diameter nanowires through the intestinal epithelium of Daphnia magna.

Mattsson K, Adolfsson K, Ekvall MT, Borgström MT, Linse S, Hansson LA, Cedervall T, Prinz CN.

Nanotoxicology. 2016 Oct;10(8):1160-7. doi: 10.1080/17435390.2016.1189615. Epub 2016 Jun 7.

33.

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

Herling TW, O'Connell DJ, Bauer MC, Persson J, Weininger U, Knowles TP, Linse S.

Biophys J. 2016 May 10;110(9):1957-66. doi: 10.1016/j.bpj.2016.03.038.

34.

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

Kakkar V, Månsson C, de Mattos EP, Bergink S, van der Zwaag M, van Waarde MAWH, Kloosterhuis NJ, Melki R, van Cruchten RTP, Al-Karadaghi S, Arosio P, Dobson CM, Knowles TPJ, Bates GP, van Deursen JM, Linse S, van de Sluis B, Emanuelsson C, Kampinga HH.

Mol Cell. 2016 Apr 21;62(2):272-283. doi: 10.1016/j.molcel.2016.03.017. Epub 2016 Apr 14.

35.

Analysis of the length distribution of amyloid fibrils by centrifugal sedimentation.

Arosio P, Cedervall T, Knowles TP, Linse S.

Anal Biochem. 2016 Jul 1;504:7-13. doi: 10.1016/j.ab.2016.03.015. Epub 2016 Mar 28.

PMID:
27033008
36.

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.

Nat Commun. 2016 Mar 24;7:10948. doi: 10.1038/ncomms10948.

37.

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.

Sci Adv. 2016 Feb 12;2(2):e1501244. doi: 10.1126/sciadv.1501244. eCollection 2016 Feb.

38.

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

Meisl G, Yang X, Frohm B, Knowles TP, Linse S.

Sci Rep. 2016 Jan 13;6:18728. doi: 10.1038/srep18728.

39.

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

Meisl G, Kirkegaard JB, Arosio P, Michaels TC, Vendruscolo M, Dobson CM, Linse S, Knowles TP.

Nat Protoc. 2016 Feb;11(2):252-72. doi: 10.1038/nprot.2016.010. Epub 2016 Jan 7.

PMID:
26741409
40.

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

Arosio P, Müller T, Rajah L, Yates EV, Aprile FA, Zhang Y, Cohen SI, White DA, Herling TW, De Genst EJ, Linse S, Vendruscolo M, Dobson CM, Knowles TP.

ACS Nano. 2016 Jan 26;10(1):333-41. doi: 10.1021/acsnano.5b04713. Epub 2015 Dec 23.

PMID:
26678709
41.

Direct High Affinity Interaction between Aβ42 and GSK3α Stimulates Hyperphosphorylation of Tau. A New Molecular Link in Alzheimer's Disease?

Dunning CJ, McGauran G, Willén K, Gouras GK, O'Connell DJ, Linse S.

ACS Chem Neurosci. 2016 Feb 17;7(2):161-70. doi: 10.1021/acschemneuro.5b00262. Epub 2015 Dec 15.

42.

N-Terminal Extensions Retard Aβ42 Fibril Formation but Allow Cross-Seeding and Coaggregation with Aβ42.

Szczepankiewicz O, Linse B, Meisl G, Thulin E, Frohm B, Sala Frigerio C, Colvin MT, Jacavone AC, Griffin RG, Knowles T, Walsh DM, Linse S.

J Am Chem Soc. 2015 Nov 25;137(46):14673-85. doi: 10.1021/jacs.5b07849. Epub 2015 Nov 17.

43.

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

Yates EV, Müller T, Rajah L, De Genst EJ, Arosio P, Linse S, Vendruscolo M, Dobson CM, Knowles TP.

Nat Chem. 2015 Oct;7(10):802-9. doi: 10.1038/nchem.2344. Epub 2015 Sep 14.

PMID:
26391079
44.

High Throughput Screening Method to Explore Protein Interactions with Nanoparticles.

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

PLoS One. 2015 Aug 27;10(8):e0136687. doi: 10.1371/journal.pone.0136687. eCollection 2015.

45.

The Aβ40 and Aβ42 peptides self-assemble into separate homomolecular fibrils in binary mixtures but cross-react during primary nucleation.

Cukalevski R, Yang X, Meisl G, Weininger U, Bernfur K, Frohm B, Knowles TPJ, Linse S.

Chem Sci. 2015 Jul 1;6(7):4215-4233. doi: 10.1039/c4sc02517b. Epub 2015 May 8.

46.

High resolution structural characterization of Aβ42 amyloid fibrils by magic angle spinning NMR.

Colvin MT, Silvers R, Frohm B, Su Y, Linse S, Griffin RG.

J Am Chem Soc. 2015 Jun 17;137(23):7509-18. doi: 10.1021/jacs.5b03997. Epub 2015 Jun 4.

47.

Fluorescent filter-trap assay for amyloid fibril formation kinetics in complex solutions.

Nasir I, Linse S, Cabaleiro-Lago C.

ACS Chem Neurosci. 2015 Aug 19;6(8):1436-44. doi: 10.1021/acschemneuro.5b00104. Epub 2015 May 20.

48.

A microfluidic platform for quantitative measurements of effective protein charges and single ion binding in solution.

Herling TW, Arosio P, Müller T, Linse S, Knowles TP.

Phys Chem Chem Phys. 2015 May 14;17(18):12161-7. doi: 10.1039/c5cp00746a.

PMID:
25880209
49.

On the lag phase in amyloid fibril formation.

Arosio P, Knowles TP, Linse S.

Phys Chem Chem Phys. 2015 Mar 28;17(12):7606-18. doi: 10.1039/c4cp05563b. Review.

50.

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.

Nat Struct Mol Biol. 2015 Mar;22(3):207-213. doi: 10.1038/nsmb.2971. Epub 2015 Feb 16.

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