A. Buell

发表

Nanostructured films from hierarchical self-assembly of amyloidogenic proteins.

Alexander K. Buell, M. Welland, T. Knowles, 2010, Nature nanotechnology.

Direct Observation of Heterogeneous Amyloid Fibril Growth Kinetics via Two-Color Super-Resolution Microscopy

Clemens F. Kaminski, Alexander K. Buell, Christopher M. Dobson, 2013, Nano letters.

The growth of amyloid fibrils: rates and mechanisms.

Alexander K. Buell, A. Buell, 2019, The Biochemical journal.

β-Synuclein suppresses both the initiation and amplification steps of α-synuclein aggregation via competitive binding to surfaces

Alexander K. Buell, C. Dobson, M. Vendruscolo, 2016, Scientific Reports.

Mutations associated with familial Parkinson’s disease alter the initiation and amplification steps of α-synuclein aggregation

Alexander K. Buell, C. Dobson, M. Vendruscolo, 2016, Proceedings of the National Academy of Sciences.

Nanobodies raised against monomeric ɑ-synuclein inhibit fibril formation and destabilize toxic oligomeric species

Craig D. Hughes, C. Dobson, D. Klenerman, 2017, BMC Biology.

Quantitative thermophoretic study of disease-related protein aggregates

Alexander K. Buell, D. Braun, C. Dobson, 2016, Scientific Reports.

Relationship between Prion Propensity and the Rates of Individual Molecular Steps of Fibril Assembly

Alexander K. Buell, C. Dobson, M. Welland, 2011, The Journal of Biological Chemistry.

Glycation modulates alpha-synuclein fibrillization kinetics: A sweet spot for inhibition

Alexander K. Buell, D. Otzen, Annekatrin König, 2022, The Journal of biological chemistry.

Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2

Alexander K. Buell, C. Dobson, Gary W. Jones, 2013, Philosophical Transactions of the Royal Society B: Biological Sciences.

Influence of specific HSP 70 domains on fibril formation of the yeast prion protein Ure 2

C. Dobson, Gary W. Jones, L. Itzhaki, 2013 .

Ostwald’s rule of stages governs structural transitions and morphology of dipeptide supramolecular polymers

C. Dobson, L. Adler-Abramovich, E. Gazit, 2014, Nature Communications.

Biological and Bio-inspired Nanomaterials: Properties and Assembly Mechanisms

Alexander K. Buell, T. Knowles, S. Perrett, 2019, Advances in Experimental Medicine and Biology.

Interaction of Therapeutic d-Peptides with Aβ42 Monomers, Thermodynamics, and Binding Analysis.

Alexander K. Buell, D. Willbold, A. Buell, 2022, ACS chemical neuroscience.

Position‐Dependent Electrostatic Protection against Protein Aggregation

C. Dobson, X. Salvatella, M. Vendruscolo, 2009, Chembiochem : a European journal of chemical biology.

A rationally designed six-residue swap generates comparability in the aggregation behavior of α-synuclein and β-synuclein.

Alexander K. Buell, C. Dobson, C. Roodveldt, 2012, Biochemistry.

Cancer cell migration on straight, wavy, loop and grid microfibre patterns

Alexander K. Buell, E. Terentjev, Wenyu Wang, 2022, Biofabrication.

Mass photometric detection and quantification of nanoscale α-synuclein phase separation

Alexander K. Buell, A. Buell, S. Ray, 2022, bioRxiv.

Stability matters, too – the thermodynamics of amyloid fibril formation

A. Buell, 2022, Chemical science.

Probing small molecule binding to amyloid fibrils.

Alexander K. Buell, C. Dobson, G. Tóth, 2011, Physical chemistry chemical physics : PCCP.

α-Synuclein-derived lipoparticles in the study of α-Synuclein amyloid fibril formation

Alexander K. Buell, G. Schröder, M. Etzkorn, 2019, Chemistry and physics of lipids.

An engineered monomer binding-protein for α-synuclein efficiently inhibits the proliferation of amyloid fibrils

Alexander K. Buell, C. Dobson, A. Voigt, 2019, bioRxiv.

Microfluidics and the quantification of biomolecular interactions.

Alexander K. Buell, D. Otzen, A. Buell, 2021, Current opinion in structural biology.

The properties of α-synuclein secondary nuclei are dominated by the solution conditions rather than the seed fibril strain.

Alexander K. Buell, S. Linse, A. Buell, 2019, ACS chemical neuroscience.

Thermodynamics of amyloid fibril formation from chemical depolymerization.

Alexander K. Buell, A. Buell, N. Vettore, 2019, Physical chemistry chemical physics : PCCP.

Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils

Alexander K. Buell, C. Dobson, D. Topgaard, 2019, The journal of physical chemistry letters.

Protein aggregation in crowded environments.

Alexander K. Buell, Christopher M Dobson, Tuomas P J Knowles, 2010, Journal of the American Chemical Society.

The Nucleation of Protein Aggregates - From Crystals to Amyloid Fibrils.

Alexander K. Buell, A. Buell, 2017, International review of cell and molecular biology.

The physical chemistry of the amyloid phenomenon: thermodynamics and kinetics of filamentous protein aggregation.

Alexander K. Buell, C. Dobson, T. Knowles, 2014, Essays in biochemistry.

On the kinetics of protein aggregation

Alexander K. Buell, A. Buell, 2011 .

Expanding the solvent chemical space for self-assembly of dipeptide nanostructures.

Alexander K. Buell, L. Adler-Abramovich, E. Gazit, 2014, ACS nano.

A Label-Free, Quantitative Assay of Amyloid Fibril Growth Based on Intrinsic Fluorescence

Alexander K. Buell, C. Dobson, C. Kaminski, 2013, ChemBioChem.

Thermodynamics of amyloid fibril formation from non-equilibrium experiments of growth and dissociation.

Alexander K. Buell, W. Xue, A. Buell, 2021, Biophysical chemistry.

The Kinetics, Thermodynamics and Mechanisms of Short Aromatic Peptide Self-Assembly.

Alexander K. Buell, T. Mason, A. Buell, 2019, Advances in experimental medicine and biology.

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

Alexander K. Buell, A. Šarić, C. Dobson, 2018, Nature Chemistry.

The role of stable α-synuclein oligomers in the molecular events underlying amyloid formation.

Alexander K. Buell, C. Dobson, J. Enghild, 2014, Journal of the American Chemical Society.

Nanobodies raised against monomeric ɑ-synuclein inhibit fibril formation and destabilize toxic oligomeric species

Alexander K. Buell, Craig D. Hughes, C. Dobson, 2017, BMC Biology.

Nanobodies raised against monomeric ɑ-synuclein inhibit fibril formation and destabilize toxic oligomeric species

Craig D. Hughes, C. Dobson, D. Klenerman, 2017, BMC Biology.

Nanobodies raised against monomeric α-synuclein distinguish between fibrils at different maturation stages.

Alexander K. Buell, C. Dobson, L. Wyns, 2013, Journal of molecular biology.

Widespread amyloidogenicity potential of multiple myeloma patient-derived immunoglobulin light chains

Alexander K. Buell, S. Egelhaaf, P. Marcatili, 2023, BMC Biology.

Universal amyloidogenicity of patient-derived immunoglobulin light chains

Alexander K. Buell, S. Egelhaaf, Martial Rey, 2021, bioRxiv.

De Novo Sequencing of Antibody Light Chain Proteoforms from Patients with Multiple Myeloma.

Martial Rey, R. Fenk, R. Haas, 2021, Analytical chemistry.

The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth

Juami Hermine Mariama van Gils, Erik van Dijk, Alessia Peduzzo, 2019, PLoS Comput. Biol..

Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy

G. Schröder, R. Ravelli, D. Willbold, 2019, Nature Communications.

Secondary Nucleation and the Conservation of Structural Characteristics of Amyloid Fibril Strains

Alexander K. Buell, A. Buell, Saeid Hadi Alijanvand, 2021, Frontiers in Molecular Biosciences.

β-Turn exchanges in the α-synuclein segment 44-TKEG-47 reveal high sequence fidelity requirements of amyloid fibril elongation.

Marie P. Schützmann, Alexander K. Buell, W. Hoyer, 2020, Biophysical chemistry.

Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation.

C. Dobson, M. Vendruscolo, T. Knowles, 2015, Nature chemical biology.

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

Michele Vendruscolo, Sara Linse, Christopher M Dobson, 2014, Proceedings of the National Academy of Sciences.

Electrostatic effects in filamentous protein aggregation.

Alexander K. Buell, C. Dobson, X. Salvatella, 2013, Biophysical journal.

Biosensor‐based label‐free assays of amyloid growth

Alexander K. Buell, C. Dobson, M. Welland, 2009, FEBS letters.

Pyroglutamate-modified Aβ(3-42) affects aggregation kinetics of Aβ(1-42) by accelerating primary and secondary pathways

D. Willbold, A. Buell, M. Schwarten, 2017, Chemical science.

Binding of the molecular chaperone alphaB-crystallin to Abeta amyloid fibrils inhibits fibril elongation

Alexander K. Buell, C. Dobson, M. Welland, 2020 .

Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongation.

Alexander K. Buell, C. Dobson, M. Welland, 2011, Biophysical journal.

Physical determinants of the self-replication of protein fibrils

Alexander K. Buell, Tuomas P. J. Knowles, Christopher M. Dobson, 2016, Nature Physics.

The Environment Is a Key Factor in Determining the Anti-Amyloid Efficacy of EGCG

Alexander K. Buell, A. Buell, A. Sakalauskas, 2019, Biomolecules.

Targeting the Intrinsically Disordered Structural Ensemble of α-Synuclein by Small Molecules as a Potential Therapeutic Strategy for Parkinson’s Disease

Alexander K. Buell, Tuomas P. J. Knowles, Michele Vendruscolo, 2014, PloS one.

Capillary flow experiments for thermodynamic and kinetic characterization of protein liquid-liquid phase separation

Alexander K. Buell, Emil G. P. Stender, A. Buell, 2021, Nature Communications.

Nanoscopic insights into seeding mechanisms and toxicity of α-synuclein species in neurons

Alexander K. Buell, Romain F. Laine, Claire H. Michel, 2016, Proceedings of the National Academy of Sciences.

Interactions between amyloidophilic dyes and their relevance to studies of amyloid inhibitors.

Alexander K. Buell, C. Dobson, M. Welland, 2010, Biophysical journal.

Role of Hydrophobicity and Charge of Amyloid-Beta Oligomer Eliminating d-Peptides in the Interaction with Amyloid-Beta Monomers.

Alexander K. Buell, D. Willbold, A. Buell, 2018, ACS chemical neuroscience.

Monomeric amyloid β-peptide (1-42) significantly populates compact fibril-like conformations

Alexander K. Buell, A. Buell, B. Barz, 2020, bioRxiv.

Kinetic barriers to α-synuclein protofilament formation and conversion into mature fibrils.

C. Dobson, T. Knowles, A. Buell, 2018, Chemical communications.

Vrije Universiteit Brussel Nanobodies Raised against Monomeric alpha-Synuclein Distinguish between Fibrils at Different Maturation Stages

Alexander K. Buell, C. Dobson, L. Wyns, 2017 .

Influence of the protein context on the polyglutamine length-dependent elongation of amyloid fibrils.

Alexander K. Buell, C. Jérôme, Anne-Sophie Duwez, 2015, Biochimica et biophysica acta.

Spatial propagation of protein polymerization.

Alexander K. Buell, D A Weitz, M Vendruscolo, 2014, Physical review letters.

Quantitative Analysis of Diffusive Reactions at the Solid-Liquid Interface in Finite Systems.

E. Terentjev, T. Knowles, A. Buell, 2014, The journal of physical chemistry letters.

Protein microgels from amyloid fibril networks.

Alexander K. Buell, Sara Linse, Christopher M Dobson, 2015, ACS nano.

Structural insights from lipid-bilayer nanodiscs link α-Synuclein membrane-binding modes to amyloid fibril formation

B. Strodel, D. Willbold, M. Etzkorn, 2018, Communications Biology.

Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of α-synuclein

Alexander K. Buell, C. Dobson, M. Vendruscolo, 2016, Proceedings of the National Academy of Sciences.

Microfluidic Diffusion Platform for Characterizing the Sizes of Lipid Vesicles and the Thermodynamics of Protein-Lipid Interactions.

C. Dobson, Bozhong Mu, A. Levin, 2018, Analytical chemistry.

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

Alexander K. Buell, Laurence J Young, C. Kaminski, 2017, Quarterly Reviews of Biophysics.

Opposed Effects of Dityrosine Formation in Soluble and Aggregated α-Synuclein on Fibril Growth

Alexander K. Buell, D. Willbold, L. Gremer, 2017, Journal of molecular biology.

Structural polymorphism of the low-complexity C-terminal domain of TDP-43 amyloid aggregates revealed by solid-state NMR

Alexander K. Buell, B. Habenstein, François-Xavier Theillet, 2023, Frontiers in Molecular Biosciences.

Synthesis of Nonequilibrium Supramolecular Peptide Polymers on a Microfluidic Platform.

Alexander K. Buell, Christopher M. Dobson, Ehud Gazit, 2016, Journal of the American Chemical Society.

Biochemical and biophysical characterisation of immunoglobulin free light chains derived from an initially unbiased population of patients with light chain disease

R. Fenk, R. Haas, A. Buell, 2020, PeerJ.

Measuring the kinetics of amyloid fibril elongation using quartz crystal microbalances.

Alexander K. Buell, C. Dobson, M. Welland, 2012, Methods in molecular biology.

C-terminal truncation of α-synuclein promotes amyloid fibril amplification at physiological pH

Alexander K. Buell, C. Dobson, T. Knowles, 2018, Chemical science.

A structural and kinetic link between membrane association and amyloid fibril formation of α-Synuclein

Alexander K. Buell, B. Strodel, D. Willbold, 2017, bioRxiv.

1 A structural and kinetic link between membrane association and 1 amyloid fibril formation of α-Synuclein 2 3 4

Alexander K. Buell, B. Strodel, D. Willbold, 2017 .

Detection and Characterization of Small Molecule Interactions with Fibrillar Protein Aggregates Using Microscale Thermophoresis.

Alexander K. Buell, G. Tóth, F. Aigbirhio, 2017, ACS chemical neuroscience.

Population of nonnative states of lysozyme variants drives amyloid fibril formation.

Alexander K. Buell, C. Dobson, X. Salvatella, 2011, Journal of the American Chemical Society.

The Aggregation Conditions Define Whether EGCG is an Inhibitor or Enhancer of α-Synuclein Amyloid Fibril Formation

Alexander K. Buell, R. Haas, A. Buell, 2020, International journal of molecular sciences.

Detailed analysis of the energy barriers for amyloid fibril growth.

Alexander K. Buell, Christopher M Dobson, Tuomas P J Knowles, 2012, Angewandte Chemie.

Surface attachment of protein fibrils via covalent modification strategies.

Christopher M Dobson, Tuomas P J Knowles, Mark E Welland, 2010, The journal of physical chemistry. B.

Frequency factors in a landscape model of filamentous protein aggregation.

Alexander K. Buell, Jamie R Blundell, Eugene M Terentjev, 2010, Physical review letters.

Pyroglutamate-modified amyloid β(3-42) monomer has more β-sheet content than the amyloid β(1-42) monomer.

Alexander K. Buell, A. Buell, B. Barz, 2023, Physical chemistry chemical physics : PCCP.

Protein Aggregate‐Ligand Binding Assays Based on Microfluidic Diffusional Separation

Alexander K. Buell, C. Dobson, J. Benesch, 2016, Chembiochem : a European journal of chemical biology.

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

Alexander K. Buell, A. Šarić, C. Dobson, 2017, Chemical science.

Fluctuations in protein aggregation: Design of preclinical screening for early diagnosis of neurodegenerative disease

Alexander K. Buell, S. Zapperi, C. Porta, 2016, 1609.06843.

The length distribution of frangible biofilaments.

Julian C. W. Willis, C. Dobson, M. Jensen, 2015, The Journal of chemical physics.

Thermodynamics of Polypeptide Supramolecular Assembly in the Short-Chain Limit.

Alexander K. Buell, Ehud Gazit, Thomas C T Michaels, 2017, Journal of the American Chemical Society.

Compact fibril-like structure of amyloid β-peptide (1-42) monomers.

Alexander K. Buell, A. Buell, B. Barz, 2020, Chemical communications.

A Protein Corona Modulates Interactions of α-Synuclein with Nanoparticles and Alters the Rates of the Microscopic Steps of Amyloid Formation.

Alexander K. Buell, J. Enghild, D. Otzen, 2022, ACS nano.

Generation of robust bispecific antibodies through fusion of single-domain antibodies on IgG scaffolds: a comprehensive comparison of formats

Alexander K. Buell, A. Buell, S. Goletz, 2023, mAbs.

Three-dimensional domain swapping and supramolecular protein assembly: insights from the X-ray structure of a dimeric swapped variant of human pancreatic RNase.

Alexander K. Buell, L. Mazzarella, G. D'alessio, 2013, Acta crystallographica. Section D, Biological crystallography.

Mass photometric detection and quantification of nanoscale α-synuclein phase separation

Alexander K. Buell, T. Mason, A. Buell, 2023, Nature Chemistry.

Structural insights from lipid-bilayer nanodiscs link α-Synuclein membrane-binding modes to amyloid fibril formation

Alexander K. Buell, B. Strodel, D. Willbold, 2018, Communications Biology.