| Year |
Citation |
Score |
| 2024 |
Galvagnion C, Barclay A, Makasewicz K, Marlet FR, Moulin M, Devos JM, Linse S, Martel A, Porcar L, Sparr E, Pedersen MC, Roosen-Runge F, Arleth L, Buell AK. Structural characterisation of α-synuclein-membrane interactions and the resulting aggregation using small angle scattering. Physical Chemistry Chemical Physics : Pccp. PMID 38526443 DOI: 10.1039/d3cp05928f |
0.453 |
|
| 2024 |
Farzadfard A, Kunka A, Mason TO, Larsen JA, Norrild RK, Dominguez ET, Ray S, Buell AK. Thermodynamic characterization of amyloid polymorphism by microfluidic transient incomplete separation. Chemical Science. 15: 2528-2544. PMID 38362440 DOI: 10.1039/d3sc05371g |
0.507 |
|
| 2023 |
Ray S, Mason TO, Boyens-Thiele L, Farzadfard A, Larsen JA, Norrild RK, Jahnke N, Buell AK. Mass photometric detection and quantification of nanoscale α-synuclein phase separation. Nature Chemistry. PMID 37337111 DOI: 10.1038/s41557-023-01244-8 |
0.388 |
|
| 2023 |
Nath S, Buell AK, Barz B. Pyroglutamate-modified amyloid β(3-42) monomer has more β-sheet content than the amyloid β(1-42) monomer. Physical Chemistry Chemical Physics : Pccp. PMID 37306611 DOI: 10.1039/d2cp05961d |
0.834 |
|
| 2023 |
Shenoy J, Lends A, Berbon M, Bilal M, El Mammeri N, Bertoni M, Saad A, Morvan E, Grélard A, Lecomte S, Theillet FX, Buell AK, Kauffmann B, Habenstein B, Loquet A. Structural polymorphism of the low-complexity C-terminal domain of TDP-43 amyloid aggregates revealed by solid-state NMR. Frontiers in Molecular Biosciences. 10: 1148302. PMID 37065450 DOI: 10.3389/fmolb.2023.1148302 |
0.347 |
|
| 2023 |
Sternke-Hoffmann R, Pauly T, Norrild RK, Hansen J, Tucholski F, Høie MH, Marcatili P, Dupré M, Duchateau M, Rey M, Malosse C, Metzger S, Boquoi A, Platten F, Egelhaaf SU, ... ... Buell AK, et al. Widespread amyloidogenicity potential of multiple myeloma patient-derived immunoglobulin light chains. Bmc Biology. 21: 21. PMID 36737754 DOI: 10.1186/s12915-022-01506-w |
0.803 |
|
| 2022 |
Buell AK. Stability matters, too - the thermodynamics of amyloid fibril formation. Chemical Science. 13: 10177-10192. PMID 36277637 DOI: 10.1039/d1sc06782f |
0.494 |
|
| 2022 |
Bartl J, Zanini M, Bernardi F, Forget A, Blümel L, Talbot J, Picard D, Qin N, Cancila G, Gao Q, Nath S, Koumba IM, Wolter M, Kuonen F, Langini M, ... ... Buell A, et al. The HHIP-AS1 lncRNA promotes tumorigenicity through stabilization of dynein complex 1 in human SHH-driven tumors. Nature Communications. 13: 4061. PMID 35831316 DOI: 10.1038/s41467-022-31574-z |
0.747 |
|
| 2022 |
Leguizamon Herrera VL, Buell AK, Willbold D, Barz B. Interaction of Therapeutic d-Peptides with Aβ42 Monomers, Thermodynamics, and Binding Analysis. Acs Chemical Neuroscience. PMID 35580288 DOI: 10.1021/acschemneuro.2c00102 |
0.782 |
|
| 2022 |
Farzadfard A, König A, Petersen SV, Nielsen J, Vasili E, Dominguez-Meijide A, Buell AK, Outeiro TF, Otzen DE. Glycation modulates alpha-synuclein fibrillization kinetics: a sweet spot for inhibition. The Journal of Biological Chemistry. 101848. PMID 35314196 DOI: 10.1016/j.jbc.2022.101848 |
0.435 |
|
| 2022 |
Norrild RK, Vettore N, Coden A, Xue WF, Buell AK. Corrigendum to "Thermodynamics of amyloid fibril formation from non-equilibrium experiments of growth and dissociation" [Biophysical Chemistry 271 (2021) 106549]. Biophysical Chemistry. 283: 106764. PMID 35139467 DOI: 10.1016/j.bpc.2022.106764 |
0.83 |
|
| 2022 |
Mohammad-Beigi H, Zanganeh M, Scavenius C, Eskandari H, Farzadfard A, Shojaosadati SA, Enghild JJ, Otzen DE, Buell AK, Sutherland DS. A Protein Corona Modulates Interactions of α-Synuclein with Nanoparticles and Alters the Rates of the Microscopic Steps of Amyloid Formation. Acs Nano. PMID 34982538 DOI: 10.1021/acsnano.1c08825 |
0.327 |
|
| 2021 |
Nath S, Roy P, Mandal R, Roy R, Buell AK, Sengupta N, Tarafdar PK. Hydroxy-Porphyrin as an effective, endogenous molecular clamp during early stages of amyloid fibrillation. Chemistry, An Asian Journal. PMID 34570963 DOI: 10.1002/asia.202100965 |
0.824 |
|
| 2021 |
Dupré M, Duchateau M, Sternke-Hoffmann R, Boquoi A, Malosse C, Fenk R, Haas R, Buell AK, Rey M, Chamot-Rooke J. Sequencing of Antibody Light Chain Proteoforms from Patients with Multiple Myeloma. Analytical Chemistry. PMID 34292722 DOI: 10.1021/acs.analchem.1c01955 |
0.764 |
|
| 2021 |
Hadi Alijanvand S, Peduzzo A, Buell AK. Secondary Nucleation and the Conservation of Structural Characteristics of Amyloid Fibril Strains. Frontiers in Molecular Biosciences. 8: 669994. PMID 33937341 DOI: 10.3389/fmolb.2021.669994 |
0.854 |
|
| 2021 |
Buell AK. Editorial for the special issue "Protein misfolding and amyloid aggregation" of Biophysical Chemistry. Biophysical Chemistry. 272: 106566. PMID 33713996 DOI: 10.1016/j.bpc.2021.106566 |
0.481 |
|
| 2021 |
Norrild RK, Vettore N, Coden A, Xue WF, Buell AK. Thermodynamics of amyloid fibril formation from non-equilibrium experiments of growth and dissociation. Biophysical Chemistry. 271: 106549. PMID 33578107 DOI: 10.1016/j.bpc.2021.106549 |
0.859 |
|
| 2021 |
Barz B, Buell AK, Nath S. Compact fibril-like structure of amyloid β-peptide (1-42) monomers. Chemical Communications (Cambridge, England). PMID 33399148 DOI: 10.1039/d0cc06607a |
0.83 |
|
| 2020 |
Agerschou ED, Schützmann MP, Reppert N, Wördehoff MM, Shaykhalishahi H, Buell AK, Hoyer W. β-Turn exchanges in the α-synuclein segment 44-TKEG-47 reveal high sequence fidelity requirements of amyloid fibril elongation. Biophysical Chemistry. 269: 106519. PMID 33333378 DOI: 10.1016/j.bpc.2020.106519 |
0.464 |
|
| 2020 |
van Gils JHM, van Dijk E, Peduzzo A, Hofmann A, Vettore N, Schützmann MP, Groth G, Mouhib H, Otzen DE, Buell AK, Abeln S. The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth. Plos Computational Biology. 16: e1007767. PMID 32365068 DOI: 10.1371/Journal.Pcbi.1007767 |
0.829 |
|
| 2020 |
Sternke-Hoffmann R, Boquoi A, Lopez Y Niedenhoff D, Platten F, Fenk R, Haas R, Buell AK. Biochemical and biophysical characterisation of immunoglobulin free light chains derived from an initially unbiased population of patients with light chain disease. Peerj. 8: e8771. PMID 32211238 DOI: 10.7717/Peerj.8771 |
0.798 |
|
| 2020 |
Sternke-Hoffmann R, Peduzzo A, Bolakhrif N, Haas R, Buell AK. The Aggregation Conditions Define Whether EGCG is an Inhibitor or Enhancer of -Synuclein Amyloid Fibril Formation. International Journal of Molecular Sciences. 21. PMID 32183378 DOI: 10.3390/Ijms21061995 |
0.827 |
|
| 2020 |
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 Chemical Neuroscience. 11: 909-918. PMID 32069013 DOI: 10.1021/Acschemneuro.9B00594 |
0.855 |
|
| 2019 |
Sneideris T, Sakalauskas A, Sternke-Hoffmann R, Peduzzo A, Ziaunys M, Buell AK, Smirnovas V. The Environment Is a Key Factor in Determining the Anti-Amyloid Efficacy of EGCG. Biomolecules. 9. PMID 31835741 DOI: 10.3390/biom9120855 |
0.812 |
|
| 2019 |
Galvagnion C, Topgaard D, Makasewicz K, Buell AK, Linse S, Sparr E, Dobson CM. Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils. The Journal of Physical Chemistry Letters. 7872-7877. PMID 31790267 DOI: 10.1021/Acs.Jpclett.9B03005 |
0.569 |
|
| 2019 |
Vettore N, Buell AK. Thermodynamics of amyloid fibril formation from chemical depolymerization. Physical Chemistry Chemical Physics : Pccp. PMID 31755512 DOI: 10.1039/C9Cp04524D |
0.858 |
|
| 2019 |
Mason TO, Buell AK. The Kinetics, Thermodynamics and Mechanisms of Short Aromatic Peptide Self-Assembly. Advances in Experimental Medicine and Biology. 1174: 61-112. PMID 31713197 DOI: 10.1007/978-981-13-9791-2_3 |
0.423 |
|
| 2019 |
Buell AK. The growth of amyloid fibrils: rates and mechanisms. The Biochemical Journal. 476: 2677-2703. PMID 31654060 DOI: 10.1042/Bcj20160868 |
0.619 |
|
| 2019 |
Röder C, Vettore N, Mangels LN, Gremer L, Ravelli RBG, Willbold D, Hoyer W, Buell AK, Schröder GF. Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy. Nature Communications. 10: 3754. PMID 31434882 DOI: 10.1038/S41467-019-11320-8 |
0.834 |
|
| 2019 |
Agerschou ED, Flagmeier P, Saridaki T, Galvagnion C, Komnig D, Heid L, Prasad V, Shaykhalishahi H, Willbold D, Dobson CM, Voigt A, Falkenbürger B, Hoyer W, Buell AK. An engineered monomer binding-protein for α-synuclein efficiently inhibits the proliferation of amyloid fibrils. Elife. 8. PMID 31389332 DOI: 10.7554/Elife.46112 |
0.594 |
|
| 2019 |
Falke M, Victor J, Wördehoff MM, Peduzzo A, Zhang T, Schröder G, Buell AK, Hoyer W, Etzkorn M. α-Synuclein-derived lipoparticles in the study of α-Synuclein amyloid fibril formation. Chemistry and Physics of Lipids. PMID 30826264 DOI: 10.1016/J.Chemphyslip.2019.02.009 |
0.84 |
|
| 2019 |
Agerschou ED, Flagmeier P, Saridaki T, Galvagnion C, Komnig D, Heid L, Prasad V, Shaykhalishahi H, Willbold D, Dobson CM, Voigt A, Falkenburger B, Hoyer W, Buell AK. Author response: An engineered monomer binding-protein for α-synuclein efficiently inhibits the proliferation of amyloid fibrils Elife. DOI: 10.7554/Elife.46112.035 |
0.595 |
|
| 2018 |
Viennet T, Wördehoff MM, Uluca B, Poojari C, Shaykhalishahi H, Willbold D, Strodel B, Heise H, Buell AK, Hoyer W, Etzkorn M. Structural insights from lipid-bilayer nanodiscs link α-Synuclein membrane-binding modes to amyloid fibril formation. Communications Biology. 1: 44. PMID 30271927 DOI: 10.1038/s42003-018-0049-z |
0.324 |
|
| 2018 |
van der Wateren IM, Knowles TPJ, Buell AK, Dobson CM, Galvagnion C. C-terminal truncation of α-synuclein promotes amyloid fibril amplification at physiological pH. Chemical Science. 9: 5506-5516. PMID 30061982 DOI: 10.1039/C8Sc01109E |
0.61 |
|
| 2018 |
Brown JWP, Meisl G, Knowles TPJ, Buell AK, Dobson CM, Galvagnion C. Kinetic barriers to α-synuclein protofilament formation and conversion into mature fibrils. Chemical Communications (Cambridge, England). PMID 29951679 DOI: 10.1039/C8Cc03002B |
0.666 |
|
| 2018 |
Ziehm T, Buell AK, Willbold D. Role of Hydrophobicity and Charge of Amyloid-Beta Oligomer Eliminating d-Peptides in the Interaction with Amyloid-Beta Monomers. Acs Chemical Neuroscience. 9: 2679-2688. PMID 29893543 DOI: 10.1021/Acschemneuro.8B00132 |
0.43 |
|
| 2018 |
Cohen SIA, Cukalevski R, Michaels TCT, Šarić A, Törnquist M, Vendruscolo M, Dobson CM, Buell AK, Knowles TPJ, Linse S. Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide. Nature Chemistry. PMID 29581486 DOI: 10.1038/S41557-018-0023-X |
0.729 |
|
| 2018 |
Gang H, Galvagnion C, Meisl G, Müller T, Buell AK, Levin A, Dobson CM, Mu BZ, Knowles TPJ. A microfluidic diffusion platform for characterizing the size of lipid vesicles and the thermodynamics of protein-lipid interactions. Analytical Chemistry. PMID 29313342 DOI: 10.1021/Acs.Analchem.7B04820 |
0.503 |
|
| 2017 |
Gaspar R, Meisl G, Buell AK, Young L, Kaminski CF, Knowles TPJ, Sparr E, Linse S. Secondary nucleation of monomers on fibril surface dominates α-synuclein aggregation and provides autocatalytic amyloid amplification. Quarterly Reviews of Biophysics. 50: e6. PMID 29233218 DOI: 10.1017/S0033583516000172 |
0.571 |
|
| 2017 |
Meisl G, Rajah L, Cohen SAI, Pfammatter M, Šarić A, Hellstrand E, Buell AK, Aguzzi A, Linse S, Vendruscolo M, Dobson CM, Knowles TPJ. Scaling behaviour and rate-determining steps in filamentous self-assembly. Chemical Science. 8: 7087-7097. PMID 29147538 DOI: 10.1039/C7Sc01965C |
0.677 |
|
| 2017 |
Mason TO, Michaels TCT, Levin A, Dobson CM, Gazit E, Knowles TPJ, Buell AK. Thermodynamics of polypeptide supramolecular assembly in the short chain limit. Journal of the American Chemical Society. PMID 28994295 DOI: 10.1021/Jacs.7B00229 |
0.619 |
|
| 2017 |
Dammers C, Schwarten M, Buell AK, Willbold D. Pyroglutamate-modified Aβ(3-42) affects aggregation kinetics of Aβ(1-42) by accelerating primary and secondary pathways. Chemical Science. 8: 4996-5004. PMID 28970886 DOI: 10.1039/C6Sc04797A |
0.611 |
|
| 2017 |
Wördehoff MM, Shaykhalishahi H, Groß L, Gremer L, Stoldt M, Buell AK, Willbold D, Hoyer W. Opposed Effects of Dityrosine Formation in Soluble and Aggregated α-Synuclein on Fibril Growth. Journal of Molecular Biology. 429: 3018-3030. PMID 28918091 DOI: 10.1016/J.Jmb.2017.09.005 |
0.507 |
|
| 2017 |
Iljina M, Hong L, Horrocks MH, Ludtmann MH, Choi ML, Hughes CD, Ruggeri FS, Guilliams T, Buell AK, Lee JE, Gandhi S, Lee SF, Bryant CE, Vendruscolo M, Knowles TPJ, et al. Nanobodies raised against monomeric ɑ-synuclein inhibit fibril formation and destabilize toxic oligomeric species. Bmc Biology. 15: 57. PMID 28673288 DOI: 10.1186/S12915-017-0390-6 |
0.689 |
|
| 2017 |
Fisher E, Zhao Y, Richardson R, Janik M, Buell AK, Aigbirhio FI, Toth G. Detection and Characterization of Small Molecule Interactions with Fibrillar Protein Aggregates using Microscale Thermophoresis. Acs Chemical Neuroscience. PMID 28640595 DOI: 10.1021/Acschemneuro.7B00228 |
0.509 |
|
| 2017 |
Gaspar R, Meisl G, Buell AK, Young L, Kaminski CF, Knowles TPJ, Sparr E, Linse S. Acceleration of α-synuclein aggregation. Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis. 24: 20-21. PMID 28434341 DOI: 10.1080/13506129.2017.1292904 |
0.47 |
|
| 2017 |
Buell AK. The Nucleation of Protein Aggregates - From Crystals to Amyloid Fibrils. International Review of Cell and Molecular Biology. 329: 187-226. PMID 28109328 DOI: 10.1016/Bs.Ircmb.2016.08.014 |
0.576 |
|
| 2016 |
Šarić A, Buell AK, Meisl G, Michaels TCT, Dobson CM, Linse S, Knowles TPJ, Frenkel D. Physical determinants of the self-replication of protein fibrils. Nature Physics. 12: 874-880. PMID 31031819 DOI: 10.1038/Nphys3828 |
0.624 |
|
| 2016 |
Brown JW, Buell AK, Michaels TC, Meisl G, Carozza J, Flagmeier P, Vendruscolo M, Knowles TP, Dobson CM, Galvagnion C. β-Synuclein suppresses both the initiation and amplification steps of α-synuclein aggregation via competitive binding to surfaces. Scientific Reports. 6: 36010. PMID 27808107 DOI: 10.1038/Srep36010 |
0.701 |
|
| 2016 |
Flagmeier P, Meisl G, Vendruscolo M, Knowles TP, Dobson CM, Buell AK, Galvagnion C. Mutations associated with familial Parkinson's disease alter the initiation and amplification steps of α-synuclein aggregation. Proceedings of the National Academy of Sciences of the United States of America. PMID 27573854 DOI: 10.1073/Pnas.1604645113 |
0.686 |
|
| 2016 |
Zhang Y, Buell AK, Müller T, De Genst E, Benesch J, Dobson CM, Knowles TP. Protein aggregate-ligand binding assays based on microfluidic diffusional separation. Chembiochem : a European Journal of Chemical Biology. PMID 27472818 DOI: 10.1002/Cbic.201600384 |
0.601 |
|
| 2016 |
Mason TO, Michaels TC, Levin A, Gazit E, Dobson CM, Buell AK, Knowles TP. Synthesis of non-equilibrium supra-molecular peptide polymers on a microfluidic platform. Journal of the American Chemical Society. PMID 27387359 DOI: 10.1021/Jacs.6B04136 |
0.5 |
|
| 2016 |
Galvagnion C, Brown JW, Ouberai MM, Flagmeier P, Vendruscolo M, Buell AK, Sparr E, Dobson CM. Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of α-synuclein. Proceedings of the National Academy of Sciences of the United States of America. PMID 27298346 DOI: 10.1073/Pnas.1601899113 |
0.655 |
|
| 2016 |
Pinotsi D, Michel CH, Buell AK, Laine RF, Mahou P, Dobson CM, Kaminski CF, Kaminski Schierle GS. Nanoscopic insights into seeding mechanisms and toxicity of α-synuclein species in neurons. Proceedings of the National Academy of Sciences of the United States of America. PMID 26993805 DOI: 10.1073/Pnas.1516546113 |
0.643 |
|
| 2016 |
Wolff M, Mittag JJ, Herling TW, Genst ED, Dobson CM, Knowles TP, Braun D, Buell AK. Quantitative thermophoretic study of disease-related protein aggregates. Scientific Reports. 6: 22829. PMID 26984748 DOI: 10.1038/Srep22829 |
0.643 |
|
| 2016 |
Costantini G, Budrikis Z, Taloni A, Buell AK, Zapperi S, La Porta CA. Fluctuations in Protein Aggregation: Design of Preclinical Screening for Early Diagnosis of Neurodegenerative Disease Physical Review Applied. 6. DOI: 10.1103/Physrevapplied.6.034012 |
0.388 |
|
| 2016 |
Dammers C, Buell A, Schwarten M, Willbold D. P4-309: Peass(3-42) Increases Aggregation Propensity of ass(1-42) by Accelerating Primary and Secondary Pathways Alzheimer's & Dementia. 12: P1152-P1152. DOI: 10.1016/J.Jalz.2016.07.052 |
0.383 |
|
| 2015 |
Michaels TC, Yde P, Willis JC, Jensen MH, Otzen D, Dobson CM, Buell AK, Knowles TP. The length distribution of frangible biofilaments. The Journal of Chemical Physics. 143: 164901. PMID 26520548 DOI: 10.1063/1.4933230 |
0.556 |
|
| 2015 |
Galvagnion C, Buell AK. [Fundamental mechanisms of amyloid fibril formation by alpha-synuclein in Parkinson's disease: quantitative modelling]. Medecine Sciences : M/S. 31: 597-600. PMID 26152159 DOI: 10.1051/Medsci/20153106008 |
0.469 |
|
| 2015 |
Galvagnion C, Buell AK, Meisl G, Michaels TC, Vendruscolo M, Knowles TP, Dobson CM. Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation. Nature Chemical Biology. 11: 229-34. PMID 25643172 DOI: 10.1038/Nchembio.1750 |
0.706 |
|
| 2015 |
Huynen C, Willet N, Buell AK, Duwez AS, Jerôme C, Dumoulin M. Influence of the protein context on the polyglutamine length-dependent elongation of amyloid fibrils. Biochimica Et Biophysica Acta. 1854: 239-48. PMID 25489872 DOI: 10.1016/J.Bbapap.2014.12.002 |
0.598 |
|
| 2015 |
Shimanovich U, Efimov I, Mason TO, Flagmeier P, Buell AK, Gedanken A, Linse S, Åkerfeldt KS, Dobson CM, Weitz DA, Knowles TP. Protein microgels from amyloid fibril networks. Acs Nano. 9: 43-51. PMID 25469621 DOI: 10.1021/Nn504869D |
0.514 |
|
| 2014 |
Levin A, Mason TO, Adler-Abramovich L, Buell AK, Meisl G, Galvagnion C, Bram Y, Stratford SA, Dobson CM, Knowles TP, Gazit E. Ostwald's rule of stages governs structural transitions and morphology of dipeptide supramolecular polymers. Nature Communications. 5: 5219. PMID 25391268 DOI: 10.1038/Ncomms6219 |
0.501 |
|
| 2014 |
Buell AK, Dobson CM, Knowles TPJ. The physical chemistry of the amyloid phenomenon: Thermodynamics and kinetics of fi lamentous protein aggregation Essays in Biochemistry. 56: 11-39. PMID 25131584 DOI: 10.1042/Bse0560011 |
0.673 |
|
| 2014 |
Buell AK, Galvagnion C, Gaspar R, Sparr E, Vendruscolo M, Knowles TP, Linse S, Dobson CM. Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation. Proceedings of the National Academy of Sciences of the United States of America. 111: 7671-6. PMID 24817693 DOI: 10.1073/Pnas.1315346111 |
0.738 |
|
| 2014 |
Cohen SI, Rajah L, Yoon CH, Buell AK, White DA, Sperling RA, Vendruscolo M, Terentjev EM, Dobson CM, Weitz DA, Knowles TP. Spatial propagation of protein polymerization. Physical Review Letters. 112: 098101. PMID 24655282 DOI: 10.1103/Physrevlett.112.098101 |
0.623 |
|
| 2014 |
Tóth G, Gardai SJ, Zago W, Bertoncini CW, Cremades N, Roy SL, Tambe MA, Rochet JC, Galvagnion C, Skibinski G, Finkbeiner S, Bova M, Regnstrom K, Chiou SS, Johnston J, ... ... Buell AK, et al. Targeting the intrinsically disordered structural ensemble of α-synuclein by small molecules as a potential therapeutic strategy for Parkinson's disease. Plos One. 9: e87133. PMID 24551051 DOI: 10.1371/Journal.Pone.0087133 |
0.643 |
|
| 2014 |
Lorenzen N, Nielsen SB, Buell AK, Kaspersen JD, Arosio P, Vad BS, Paslawski W, Christiansen G, Valnickova-Hansen Z, Andreasen M, Enghild JJ, Pedersen JS, Dobson CM, Knowles TPJ, Otzen DE. The role of stable α-synuclein oligomers in the molecular events underlying amyloid formation Journal of the American Chemical Society. 136: 3859-3868. PMID 24527756 DOI: 10.1021/Ja411577T |
0.722 |
|
| 2014 |
Mason TO, Chirgadze DY, Levin A, Adler-Abramovich L, Gazit E, Knowles TP, Buell AK. Expanding the solvent chemical space for self-assembly of dipeptide nanostructures. Acs Nano. 8: 1243-53. PMID 24422499 DOI: 10.1021/Nn404237F |
0.344 |
|
| 2014 |
Pinotsi D, Buell AK, Galvagnion C, Dobson CM, Kaminski Schierle GS, Kaminski CF. Direct observation of heterogeneous amyloid fibril growth kinetics via two-color super-resolution microscopy Nano Letters. 14: 339-345. PMID 24303845 DOI: 10.1021/Nl4041093 |
0.674 |
|
| 2014 |
Aprile FA, Meisl G, Buell AK, Flagmeier P, Dobson CM, Vendruscolo M, Knowles TP. Determination of Primary Nucleation Mechanisms of α-Synuclein Amyloid Aggregation Biophysical Journal. 106: 268a. DOI: 10.1016/J.Bpj.2013.11.1570 |
0.727 |
|
| 2013 |
Pica A, Merlino A, Buell AK, Knowles TP, Pizzo E, D'Alessio G, Sica F, Mazzarella L. Three-dimensional domain swapping and supramolecular protein assembly: insights from the X-ray structure of a dimeric swapped variant of human pancreatic RNase. Acta Crystallographica. Section D, Biological Crystallography. 69: 2116-23. PMID 24100329 DOI: 10.1107/S0907444913020507 |
0.435 |
|
| 2013 |
Pinotsi D, Buell AK, Dobson CM, Kaminski Schierle GS, Kaminski CF. A Label-Free, Quantitative Assay of Amyloid Fibril Growth Based on Intrinsic Fluorescence Chembiochem. 14: 846-850. PMID 23592254 DOI: 10.1002/Cbic.201300103 |
0.564 |
|
| 2013 |
Guilliams T, El-Turk F, Buell AK, O'Day EM, Aprile FA, Esbjörner EK, Vendruscolo M, Cremades N, Pardon E, Wyns L, Welland ME, Steyaert J, Christodoulou J, Dobson CM, De Genst E. Nanobodies raised against monomeric α-synuclein distinguish between fibrils at different maturation stages. Journal of Molecular Biology. 425: 2397-411. PMID 23557833 DOI: 10.1016/J.Jmb.2013.01.040 |
0.768 |
|
| 2013 |
Xu LQ, Wu S, Buell AK, Cohen SI, Chen LJ, Hu WH, Cusack SA, Itzhaki LS, Zhang H, Knowles TP, Dobson CM, Welland ME, Jones GW, Perrett S. Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 368: 20110410. PMID 23530260 DOI: 10.1098/Rstb.2011.0410 |
0.691 |
|
| 2013 |
Buell AK, Hung P, Salvatella X, Welland ME, Dobson CM, Knowles TPJ. Electrostatic effects in filamentous protein aggregation Biophysical Journal. 104: 1116-1126. PMID 23473495 DOI: 10.1016/J.Bpj.2013.01.031 |
0.653 |
|
| 2012 |
Roodveldt C, Andersson A, De Genst EJ, Labrador-Garrido A, Buell AK, Dobson CM, Tartaglia GG, Vendruscolo M. A rationally designed six-residue swap generates comparability in the aggregation behavior of α-synuclein and β-synuclein. Biochemistry. 51: 8771-8. PMID 23003198 DOI: 10.1021/Bi300558Q |
0.665 |
|
| 2012 |
Buell AK, Dobson CM, Welland ME. Measuring the kinetics of amyloid fibril elongation using quartz crystal microbalances Methods in Molecular Biology. 849: 101-119. PMID 22528086 DOI: 10.1007/978-1-61779-551-0_8 |
0.722 |
|
| 2012 |
Buell AK, Dhulesia A, White DA, Knowles TP, Dobson CM, Welland ME. Detailed analysis of the energy barriers for amyloid fibril growth. Angewandte Chemie (International Ed. in English). 51: 5247-51. PMID 22489083 DOI: 10.1002/Anie.201108040 |
0.761 |
|
| 2012 |
Buell AK, Dhulesia A, White DA, Knowles TPJ, Dobson CM, Welland ME. Analyse der Energiebarrieren für das Wachstum von Amyloidfibrillen Angewandte Chemie. 124: 5339-5344. DOI: 10.1002/Ange.201108040 |
0.539 |
|
| 2011 |
Buell AK, Esbjörner EK, Riss PJ, White DA, Aigbirhio FI, Toth G, Welland ME, Dobson CM, Knowles TP. Probing small molecule binding to amyloid fibrils. Physical Chemistry Chemical Physics : Pccp. 13: 20044-52. PMID 22006124 DOI: 10.1039/C1Cp22283J |
0.723 |
|
| 2011 |
Shammas SL, Waudby CA, Wang S, Buell AK, Knowles TP, Ecroyd H, Welland ME, Carver JA, Dobson CM, Meehan S. Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongation. Biophysical Journal. 101: 1681-9. PMID 21961594 DOI: 10.1016/J.Bpj.2011.07.056 |
0.774 |
|
| 2011 |
Buell AK, Dhulesia A, Mossuto MF, Cremades N, Kumita JR, Dumoulin M, Welland ME, Knowles TP, Salvatella X, Dobson CM. Population of nonnative states of lysozyme variants drives amyloid fibril formation. Journal of the American Chemical Society. 133: 7737-43. PMID 21528861 DOI: 10.1021/Ja109620D |
0.755 |
|
| 2011 |
Wang YQ, Buell AK, Wang XY, Welland ME, Dobson CM, Knowles TPJ, Perrett S. Relationship between prion propensity and the rates of individual molecular steps of fibril assembly Journal of Biological Chemistry. 286: 12101-12107. PMID 21233211 DOI: 10.1074/Jbc.M110.208934 |
0.753 |
|
| 2010 |
Buell AK, Dobson CM, Knowles TPJ, Welland ME. Interactions between Amyloidophilic dyes and their relevance to studies of amyloid inhibitors Biophysical Journal. 99: 3492-3497. PMID 21081099 DOI: 10.1016/J.Bpj.2010.08.074 |
0.766 |
|
| 2010 |
Buell AK, Blundell JR, Dobson CM, Welland ME, Terentjev EM, Knowles TP. Frequency factors in a landscape model of filamentous protein aggregation. Physical Review Letters. 104: 228101. PMID 20873942 DOI: 10.1103/Physrevlett.104.228101 |
0.708 |
|
| 2010 |
Buell AK, White DA, Meier C, Welland ME, Knowles TP, Dobson CM. Surface attachment of protein fibrils via covalent modification strategies. The Journal of Physical Chemistry. B. 114: 10925-38. PMID 20695458 DOI: 10.1021/Jp101579N |
0.721 |
|
| 2010 |
White DA, Buell AK, Knowles TP, Welland ME, Dobson CM. Protein aggregation in crowded environments. Journal of the American Chemical Society. 132: 5170-5. PMID 20334356 DOI: 10.1021/Ja909997E |
0.755 |
|
| 2010 |
Knowles TP, Oppenheim TW, Buell AK, Chirgadze DY, Welland ME. Nanostructured films from hierarchical self-assembly of amyloidogenic proteins. Nature Nanotechnology. 5: 204-7. PMID 20190750 DOI: 10.1038/Nnano.2010.26 |
0.558 |
|
| 2009 |
White DA, Buell AK, Dobson CM, Welland ME, Knowles TP. Biosensor-based label-free assays of amyloid growth. Febs Letters. 583: 2587-92. PMID 19523953 DOI: 10.1016/J.Febslet.2009.06.008 |
0.694 |
|
| 2009 |
Buell AK, Tartaglia GG, Birkett NR, Waudby CA, Vendruscolo M, Salvatella X, Welland ME, Dobson CM, Knowles TP. Position-dependent electrostatic protection against protein aggregation. Chembiochem : a European Journal of Chemical Biology. 10: 1309-12. PMID 19415709 DOI: 10.1002/Cbic.200900144 |
0.777 |
|
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