Published in Proc Natl Acad Sci U S A on May 23, 2013
The amyloid state and its association with protein misfolding diseases. Nat Rev Mol Cell Biol (2014) 2.99
A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers. Nat Struct Mol Biol (2015) 2.53
Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases. Nat Med (2014) 1.85
The intersection of amyloid beta and tau at synapses in Alzheimer's disease. Neuron (2014) 1.59
Direct observations of amyloid β self-assembly in live cells provide insights into differences in the kinetics of Aβ(1-40) and Aβ(1-42) aggregation. Chem Biol (2014) 1.53
Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils. J Am Chem Soc (2016) 1.49
Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer's disease. Proc Natl Acad Sci U S A (2016) 1.42
Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation. Proc Natl Acad Sci U S A (2014) 1.31
Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides. Proc Natl Acad Sci U S A (2014) 1.25
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation. Nat Chem Biol (2015) 1.22
Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet. Proc Natl Acad Sci U S A (2013) 1.20
Amyloid β oligomers in Alzheimer's disease pathogenesis, treatment, and diagnosis. Acta Neuropathol (2015) 1.11
Microglia constitute a barrier that prevents neurotoxic protofibrillar Aβ42 hotspots around plaques. Nat Commun (2015) 1.11
Amyloid β-protein oligomers and Alzheimer's disease. Alzheimers Res Ther (2013) 1.07
Acceleration of α-synuclein aggregation by exosomes. J Biol Chem (2014) 1.04
Direct observation of heterogeneous amyloid fibril growth kinetics via two-color super-resolution microscopy. Nano Lett (2013) 1.02
Transient dynamics of Aβ contribute to toxicity in Alzheimer's disease. Cell Mol Life Sci (2014) 1.01
Soluble, prefibrillar α-synuclein oligomers promote complex I-dependent, Ca2+-induced mitochondrial dysfunction. J Biol Chem (2014) 1.00
Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation. J Biol Chem (2014) 0.99
Physical and structural basis for polymorphism in amyloid fibrils. Protein Sci (2014) 0.99
On the lag phase in amyloid fibril formation. Phys Chem Chem Phys (2015) 0.98
Quaternary Structure Defines a Large Class of Amyloid-β Oligomers Neutralized by Sequestration. Cell Rep (2015) 0.96
Engineering enhanced protein disaggregases for neurodegenerative disease. Prion (2015) 0.96
Amyloid polymorphism: structural basis and neurobiological relevance. Neuron (2015) 0.95
Rare individual amyloid-β oligomers act on astrocytes to initiate neuronal damage. Biochemistry (2014) 0.94
Isomerization of Asp7 leads to increased toxic effect of amyloid-β42 on human neuronal cells. Cell Death Dis (2013) 0.94
The binding of apolipoprotein E to oligomers and fibrils of amyloid-β alters the kinetics of amyloid aggregation. Biochemistry (2014) 0.93
High resolution structural characterization of Aβ42 amyloid fibrils by magic angle spinning NMR. J Am Chem Soc (2015) 0.93
An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer's disease. Sci Adv (2016) 0.93
Association of hypometabolism and amyloid levels in aging, normal subjects. Neurology (2014) 0.92
An imaging and systems modeling approach to fibril breakage enables prediction of amyloid behavior. Biophys J (2013) 0.92
Heterogeneous seeding of a prion structure by a generic amyloid form of the fungal prion-forming domain HET-s(218-289). J Biol Chem (2013) 0.92
A mechanistic model of tau amyloid aggregation based on direct observation of oligomers. Nat Commun (2015) 0.91
Small liposomes accelerate the fibrillation of amyloid β (1-40). J Biol Chem (2014) 0.88
The OPEP protein model: from single molecules, amyloid formation, crowding and hydrodynamics to DNA/RNA systems. Chem Soc Rev (2014) 0.88
Non-chaperone proteins can inhibit aggregation and cytotoxicity of Alzheimer amyloid β peptide. J Biol Chem (2014) 0.87
Fibril elongation by Aβ(17-42): kinetic network analysis of hybrid-resolution molecular dynamics simulations. J Am Chem Soc (2014) 0.87
Targeting the proper amyloid-beta neuronal toxins: a path forward for Alzheimer's disease immunotherapeutics. Alzheimers Res Ther (2014) 0.86
A critical appraisal of the pathogenic protein spread hypothesis of neurodegeneration. Nat Rev Neurosci (2016) 0.86
Charge dependent retardation of amyloid β aggregation by hydrophilic proteins. ACS Chem Neurosci (2014) 0.85
Single-molecule FRET studies on alpha-synuclein oligomerization of Parkinson's disease genetically related mutants. Sci Rep (2015) 0.85
pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers. Proc Natl Acad Sci U S A (2015) 0.84
Validation and Characterization of a Novel Peptide That Binds Monomeric and Aggregated β-Amyloid and Inhibits the Formation of Neurotoxic Oligomers. J Biol Chem (2015) 0.84
Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation. Nat Commun (2016) 0.84
Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation. Proc Natl Acad Sci U S A (2015) 0.84
HSP70 protects human neuroblastoma cells from apoptosis and oxidative stress induced by amyloid peptide isoAsp7-Aβ(1-42). Cell Death Dis (2015) 0.83
SOD1 aggregation in ALS mice shows simplistic test tube behavior. Proc Natl Acad Sci U S A (2015) 0.83
Current and future treatment of amyloid diseases. J Intern Med (2016) 0.83
Recruitment of Light Chains by Homologous and Heterologous Fibrils Shows Distinctive Kinetic and Conformational Specificity. Biochemistry (2016) 0.82
SOD1 protein aggregates stimulate macropinocytosis in neurons to facilitate their propagation. Mol Neurodegener (2015) 0.82
Fiber-dependent and -independent toxicity of islet amyloid polypeptide. Biophys J (2014) 0.82
A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity. Proc Natl Acad Sci U S A (2017) 0.82
The Role of Amyloid-β Oligomers in Toxicity, Propagation, and Immunotherapy. EBioMedicine (2016) 0.81
N-Terminal Extensions Retard Aβ42 Fibril Formation but Allow Cross-Seeding and Coaggregation with Aβ42. J Am Chem Soc (2015) 0.81
Implications for Alzheimer's disease of an atomic resolution structure of amyloid-β(1-42) fibrils. Proc Natl Acad Sci U S A (2016) 0.81
Flavone derivatives as inhibitors of insulin amyloid-like fibril formation. PLoS One (2015) 0.81
The relationship between iron dyshomeostasis and amyloidogenesis in Alzheimer's disease: Two sides of the same coin. Neurobiol Dis (2015) 0.81
Fibril growth and seeding capacity play key roles in α-synuclein-mediated apoptotic cell death. Cell Death Differ (2015) 0.81
The chaperone domain BRICHOS prevents CNS toxicity of amyloid-β peptide in Drosophila melanogaster. Dis Model Mech (2014) 0.81
Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases. Sci Rep (2016) 0.80
Amplification of Tau fibrils from minute quantities of seeds. Biochemistry (2014) 0.80
Direct High Affinity Interaction between Aβ42 and GSK3α Stimulates Hyperphosphorylation of Tau. A New Molecular Link in Alzheimer's Disease? ACS Chem Neurosci (2015) 0.80
Brazilin inhibits amyloid β-protein fibrillogenesis, remodels amyloid fibrils and reduces amyloid cytotoxicity. Sci Rep (2015) 0.80
Mechanisms of amyloid formation revealed by solution NMR. Prog Nucl Magn Reson Spectrosc (2015) 0.80
Introduction of d-Glutamate at a Critical Residue of Aβ42 Stabilizes a Prefibrillary Aggregate with Enhanced Toxicity. Chemistry (2016) 0.79
Cerebrospinal fluid-induced retardation of amyloid β aggregation correlates with Alzheimer's disease and the APOE ε4 allele. Brain Res (2016) 0.79
Alternative salt bridge formation in Aβ-a hallmark of early-onset Alzheimer's disease? Front Mol Biosci (2015) 0.79
Specific aromatic foldamers potently inhibit spontaneous and seeded Aβ42 and Aβ43 fibril assembly. Biochem J (2014) 0.79
Amyloid β-Protein Assembly and Alzheimer's Disease: Dodecamers of Aβ42, but Not of Aβ40, Seed Fibril Formation. J Am Chem Soc (2016) 0.79
Effects of polyamino acids and polyelectrolytes on amyloid β fibril formation. Langmuir (2014) 0.79
Generic amyloidogenicity of mammalian prion proteins from species susceptible and resistant to prions. Sci Rep (2015) 0.79
Nucleation of polymorphic amyloid fibrils. Biophys J (2015) 0.78
Fluorescent filter-trap assay for amyloid fibril formation kinetics in complex solutions. ACS Chem Neurosci (2015) 0.78
β-Synuclein suppresses both the initiation and amplification steps of α-synuclein aggregation via competitive binding to surfaces. Sci Rep (2016) 0.78
Quantitative analysis of intrinsic and extrinsic factors in the aggregation mechanism of Alzheimer-associated Aβ-peptide. Sci Rep (2016) 0.78
Capping of aβ42 oligomers by small molecule inhibitors. Biochemistry (2014) 0.78
Determination of critical nucleation number for a single nucleation amyloid-β aggregation model. Math Biosci (2016) 0.78
Self-assembly of MPG1, a hydrophobin protein from the rice blast fungus that forms functional amyloid coatings, occurs by a surface-driven mechanism. Sci Rep (2016) 0.78
Peptide amyloid surface display. Biochemistry (2015) 0.78
Differences in protein concentration dependence for nucleation and elongation in light chain amyloid formation. Biochemistry (2017) 0.77
Strain-specific Fibril Propagation by an Aβ Dodecamer. Sci Rep (2017) 0.77
AβPP processing results in greater toxicity per amount of Aβ1-42 than individually expressed and secreted Aβ1-42 in Drosophila melanogaster. Biol Open (2016) 0.77
Exploring the aggregation free energy landscape of the amyloid-β protein (1-40). Proc Natl Acad Sci U S A (2016) 0.77
Imbalance in fatty-acid-chain length of gangliosides triggers Alzheimer amyloid deposition in the precuneus. PLoS One (2015) 0.77
Misfolding of amyloidogenic proteins and their interactions with membranes. Biomolecules (2013) 0.77
Clusterin Binds to Aβ1-42 Oligomers with High Affinity and Interferes with Peptide Aggregation by Inhibiting Primary and Secondary Nucleation. J Biol Chem (2016) 0.77
Key Points Concerning Amyloid Infectivity and Prion-Like Neuronal Invasion. Front Mol Neurosci (2016) 0.77
What Can the Kinetics of Amyloid Fibril Formation Tell about Off-pathway Aggregation? J Biol Chem (2015) 0.76
Interaction of toxic and non-toxic HypF-N oligomers with lipid bilayers investigated at high resolution with atomic force microscopy. Oncotarget (2016) 0.76
The Familial British Dementia Mutation Promotes Formation of Neurotoxic Cystine Cross-linked Amyloid Bri (ABri) Oligomers. J Biol Chem (2015) 0.76
Nucleus factory on cavitation bubble for amyloid β fibril. Sci Rep (2016) 0.76
High-speed atomic force microscopy reveals structural dynamics of amyloid β1-42 aggregates. Proc Natl Acad Sci U S A (2016) 0.76
The Luminescent Oligothiophene p-FTAA Converts Toxic Aβ1-42 Species into Nontoxic Amyloid Fibers with Altered Properties. J Biol Chem (2016) 0.76
Structure-Based Small Molecule Modulation of a Pre-Amyloid State: Pharmacological Enhancement of IAPP Membrane-Binding and Toxicity. Biochemistry (2015) 0.76
Engineering therapeutic protein disaggregases. Mol Biol Cell (2016) 0.76
Fragmentation and Coagulation in Supramolecular (Co)polymerization Kinetics. ACS Cent Sci (2016) 0.75
A minimal conformational switching-dependent model for amyloid self-assembly. Sci Rep (2016) 0.75
AFM-Based Single Molecule Techniques: Unraveling the Amyloid Pathogenic Species. Curr Pharm Des (2016) 0.75
Structural basis for the dissociation of α-synuclein fibrils triggered by pressure perturbation of the hydrophobic core. Sci Rep (2016) 0.75
Structural and fluctuational difference between two ends of Aβ amyloid fibril: MD simulations predict only one end has open conformations. Sci Rep (2016) 0.75
Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature (2002) 19.36
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science (2003) 18.18
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol (2007) 17.69
Protein folding and misfolding. Nature (2003) 14.92
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature (2002) 10.81
Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell (1993) 10.15
3D structure of Alzheimer's amyloid-beta(1-42) fibrils. Proc Natl Acad Sci U S A (2005) 8.60
Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective. Cell (2005) 8.40
Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science (2000) 6.16
Folding proteins in fatal ways. Nature (2003) 5.58
A theory of linear and helical aggregations of macromolecules. J Mol Biol (1962) 4.92
The physical basis of how prion conformations determine strain phenotypes. Nature (2006) 4.77
Sickle cell hemoglobin polymerization. Adv Protein Chem (1990) 4.48
Peripherally applied Abeta-containing inoculates induce cerebral beta-amyloidosis. Science (2010) 3.98
Analysis of protein aggregation kinetics. Methods Enzymol (1999) 3.97
An analytical solution to the kinetics of breakable filament assembly. Science (2009) 3.87
Oligomeric amyloid beta associates with postsynaptic densities and correlates with excitatory synapse loss near senile plaques. Proc Natl Acad Sci U S A (2009) 3.86
Mechanism of prion propagation: amyloid growth occurs by monomer addition. PLoS Biol (2004) 3.75
Kinetics of sickle hemoglobin polymerization. II. A double nucleation mechanism. J Mol Biol (1985) 3.74
Direct observation of the interconversion of normal and toxic forms of α-synuclein. Cell (2012) 3.39
Onset of heterogeneous crystal nucleation in colloidal suspensions. Nature (2004) 2.42
Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide. Proc Natl Acad Sci U S A (2009) 2.14
Amyloid-β forms fibrils by nucleated conformational conversion of oligomers. Nat Chem Biol (2011) 2.08
Fiber-dependent amyloid formation as catalysis of an existing reaction pathway. Proc Natl Acad Sci U S A (2007) 1.75
Amyloid β-protein aggregation produces highly reproducible kinetic data and occurs by a two-phase process. ACS Chem Neurosci (2009) 1.75
A facile method for expression and purification of the Alzheimer's disease-associated amyloid beta-peptide. FEBS J (2009) 1.71
From macroscopic measurements to microscopic mechanisms of protein aggregation. J Mol Biol (2012) 1.71
Kinetics of nucleation-controlled polymerization. A perturbation treatment for use with a secondary pathway. Biophys J (1984) 1.69
Games played by rogue proteins in prion disorders and Alzheimer's disease. Science (2003) 1.61
Critical nucleus size for disease-related polyglutamine aggregation is repeat-length dependent. Nat Struct Mol Biol (2011) 1.60
Kinetics of self-assembling microtubules: an "inverse problem" in biochemistry. Proc Natl Acad Sci U S A (1996) 1.59
Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments. J Chem Phys (2011) 1.52
Passive immunotherapy rapidly increases structural plasticity in a mouse model of Alzheimer disease. Neurobiol Dis (2008) 1.29
Spontaneous fragmentation of actin filaments in physiological conditions. Nature (1982) 1.26
Nucleated polymerization with secondary pathways. II. Determination of self-consistent solutions to growth processes described by non-linear master equations. J Chem Phys (2011) 1.23
Aβ40 and Aβ42 amyloid fibrils exhibit distinct molecular recycling properties. J Am Chem Soc (2011) 1.13
Detailed analysis of the energy barriers for amyloid fibril growth. Angew Chem Int Ed Engl (2012) 1.03
Amyloid: little proteins, big clues. Nature (2011) 1.00
Novel mechanistic insight into the molecular basis of amyloid polymorphism and secondary nucleation during amyloid formation. J Mol Biol (2013) 0.95
Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem (2006) 22.87
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature (2002) 10.81
Understanding the nanoparticle-protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles. Proc Natl Acad Sci U S A (2007) 7.50
Simultaneous determination of protein structure and dynamics. Nature (2005) 5.28
Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J Mol Med (Berl) (2003) 5.15
Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature (2003) 4.98
The protofilament structure of insulin amyloid fibrils. Proc Natl Acad Sci U S A (2002) 4.08
Long-range interactions within a nonnative protein. Science (2002) 4.06
Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. Cell (2011) 3.98
Protein structure determination from NMR chemical shifts. Proc Natl Acad Sci U S A (2007) 3.96
An analytical solution to the kinetics of breakable filament assembly. Science (2009) 3.87
Amyloid formation by globular proteins under native conditions. Nat Chem Biol (2009) 3.72
High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy. Proc Natl Acad Sci U S A (2004) 3.58
Detailed identification of plasma proteins adsorbed on copolymer nanoparticles. Angew Chem Int Ed Engl (2007) 3.41
Direct observation of the interconversion of normal and toxic forms of α-synuclein. Cell (2012) 3.39
Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases. J Mol Biol (2005) 3.18
Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations. J Am Chem Soc (2005) 3.13
Role of intermolecular forces in defining material properties of protein nanofibrils. Science (2007) 2.94
Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR. Nature (2004) 2.84
The importance of sequence diversity in the aggregation and evolution of proteins. Nature (2005) 2.70
De novo designed peptide-based amyloid fibrils. Proc Natl Acad Sci U S A (2002) 2.59
The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation. EMBO J (2002) 2.59
Prediction of aggregation-prone regions in structured proteins. J Mol Biol (2008) 2.56
Protein drug stability: a formulation challenge. Nat Rev Drug Discov (2005) 2.51
A causative link between the structure of aberrant protein oligomers and their toxicity. Nat Chem Biol (2010) 2.48
Characterization of the nanoscale properties of individual amyloid fibrils. Proc Natl Acad Sci U S A (2006) 2.46
Molecular recycling within amyloid fibrils. Nature (2005) 2.39
Kinetic partitioning of protein folding and aggregation. Nat Struct Biol (2002) 2.37
Systematic in vivo analysis of the intrinsic determinants of amyloid Beta pathogenicity. PLoS Biol (2007) 2.35
Methods for the detection and analysis of protein-protein interactions. Proteomics (2007) 2.29
Structure of an intermediate state in protein folding and aggregation. Science (2012) 2.24
The nanoparticle-protein complex as a biological entity; a complex fluids and surface science challenge for the 21st century. Adv Colloid Interface Sci (2007) 2.22
Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril. Proc Natl Acad Sci U S A (2002) 2.18
Multiple tight phospholipid-binding modes of alpha-synuclein revealed by solution NMR spectroscopy. J Mol Biol (2009) 2.14
Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains. J Mol Biol (2004) 2.14
Relation between native ensembles and experimental structures of proteins. Proc Natl Acad Sci U S A (2006) 2.10
Detecting cryptic epitopes created by nanoparticles. Sci STKE (2006) 2.02
Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments. Proc Natl Acad Sci U S A (2003) 1.93
Prefibrillar amyloid aggregates could be generic toxins in higher organisms. J Neurosci (2006) 1.89
Life on the edge: a link between gene expression levels and aggregation rates of human proteins. Trends Biochem Sci (2007) 1.88
Determination of secondary structure populations in disordered states of proteins using nuclear magnetic resonance chemical shifts. Biochemistry (2012) 1.87
Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case. Proc Natl Acad Sci U S A (2004) 1.83
Interactions between folding factors and bacterial outer membrane proteins. Mol Microbiol (2005) 1.81
The Zyggregator method for predicting protein aggregation propensities. Chem Soc Rev (2008) 1.81
Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases. Proc Natl Acad Sci U S A (2002) 1.80
The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures. FASEB J (2007) 1.79
Prefibrillar amyloid protein aggregates share common features of cytotoxicity. J Biol Chem (2004) 1.79
The major birch allergen, Bet v 1, shows affinity for a broad spectrum of physiological ligands. J Biol Chem (2002) 1.76
Atomic structure and hierarchical assembly of a cross-β amyloid fibril. Proc Natl Acad Sci U S A (2013) 1.75
Fast and accurate predictions of protein NMR chemical shifts from interatomic distances. J Am Chem Soc (2009) 1.75
Amyloid β-protein aggregation produces highly reproducible kinetic data and occurs by a two-phase process. ACS Chem Neurosci (2009) 1.75
Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineering. Proc Natl Acad Sci U S A (2010) 1.72
A facile method for expression and purification of the Alzheimer's disease-associated amyloid beta-peptide. FEBS J (2009) 1.71
From macroscopic measurements to microscopic mechanisms of protein aggregation. J Mol Biol (2012) 1.71
Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils. PLoS Comput Biol (2007) 1.71
A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme. Nature (2003) 1.66
The MUMO (minimal under-restraining minimal over-restraining) method for the determination of native state ensembles of proteins. J Biomol NMR (2007) 1.65
Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme. Nat Struct Biol (2002) 1.64
Glycine residues appear to be evolutionarily conserved for their ability to inhibit aggregation. Structure (2005) 1.63
The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide. Nat Struct Mol Biol (2011) 1.62
Inhibition of amyloid beta protein fibrillation by polymeric nanoparticles. J Am Chem Soc (2008) 1.60
Direct characterization of amyloidogenic oligomers by single-molecule fluorescence. Proc Natl Acad Sci U S A (2008) 1.56
Nanobodies raised against monomeric α-synuclein distinguish between fibrils at different maturation stages. J Mol Biol (2013) 1.56
Exploring amyloid formation by a de novo design. Proc Natl Acad Sci U S A (2004) 1.55
Intermolecular structure determination of amyloid fibrils with magic-angle spinning and dynamic nuclear polarization NMR. J Am Chem Soc (2011) 1.54
Metastability of native proteins and the phenomenon of amyloid formation. J Am Chem Soc (2011) 1.53
Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments. J Chem Phys (2011) 1.52
Differential phospholipid binding of alpha-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopy. Biochemistry (2010) 1.50
Structure and functional properties of the Bacillus subtilis transcriptional repressor Rex. Mol Microbiol (2008) 1.49
Intercellular propagated misfolding of wild-type Cu/Zn superoxide dismutase occurs via exosome-dependent and -independent mechanisms. Proc Natl Acad Sci U S A (2014) 1.48
Automated assignment of SCOP and CATH protein structure classifications from FSSP scores. Proteins (2002) 1.48
ANS binding reveals common features of cytotoxic amyloid species. ACS Chem Biol (2010) 1.48