AlphaFold and the amyloid landscape

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Cryo-EM structures of tau filaments from Alzheimer’s disease

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In vivo demonstration that α-synuclein oligomers are toxic

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Architecture of the human interactome defines protein communities and disease networks

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Direct-coupling analysis of residue coevolution captures native contacts across many protein families

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EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers

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Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils

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Moonlighting proteins

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Fuzzy complexes: polymorphism and structural disorder in protein–protein interactions

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Conformational properties of α-synuclein in its free and lipid-associated states 1 1Edited by P. E. Wright

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Mechanism of coupled folding and binding of an intrinsically disordered protein

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Linking folding and binding

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Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues

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Amyloid Fibrils of the HET-s(218–289) Prion Form a β Solenoid with a Triangular Hydrophobic Core

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What does it mean to be natively unfolded?

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Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

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Accurate De Novo Prediction of Protein Contact Map by Ultra-Deep Learning Model

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Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein

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Structural and functional characterization of two alpha-synuclein strains

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Correlated mutations and residue contacts in proteins

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Structures of filaments from Pick’s disease reveal a novel tau protein fold

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Release of long-range tertiary interactions potentiates aggregation of natively unstructured α-synuclein

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Structures of α-synuclein filaments from multiple system atrophy

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Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers

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PSICOV: precise structural contact prediction using sparse inverse covariance estimation on large multiple sequence alignments

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Protein aggregation and bioprocessing

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Comparison of kindreds with parkinsonism and α‐synuclein genomic multiplications

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Distinct α-Synuclein Strains Differentially Promote Tau Inclusions in Neurons

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Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers

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Intrinsic protein disorder in complete genomes.

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Propagation of Tau aggregates and neurodegeneration

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Intrinsically disordered proteins: a 10-year recap

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Cryo-EM structure of alpha-synuclein fibrils

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Design of therapeutic proteins with enhanced stability

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Intrinsically disordered proteins: regulation and disease

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Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners

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The physical basis of how prion conformations determine strain phenotypes

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Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure.

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Atomic View of a Toxic Amyloid Small Oligomer

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The role of structural disorder in the function of RNA and protein chaperones

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Inhibition of MDM2-mediated p53 Ubiquitination and Degradation by Ribosomal Protein L5

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Critical assessment of methods of protein structure prediction (CASP)—Round XIII

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A Protein-Chameleon: Conformational Plasticity of α-Synuclein, a Disordered Protein Involved in Neurodegenerative Disorders

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Heparin-induced tau filaments are polymorphic and differ from those in Alzheimer’s and Pick’s diseases

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Short Linear Motifs: Ubiquitous and Functionally Diverse Protein Interaction Modules Directing Cell Regulation

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The CamSol method of rational design of protein mutants with enhanced solubility

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Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation

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Structural disorder throws new light on moonlighting

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Strong underwater adhesives made by self-assembling multi-protein nanofibres

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Correlation of structural elements and infectivity of the HET-s prion

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Folding versus aggregation: Polypeptide conformations on competing pathways

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Neuropathology underlying clinical variability in patients with synucleinopathies

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Distance-based protein folding powered by deep learning

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Posttranslational Modifications Mediate the Structural Diversity of Tauopathy Strains

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Structure of an Intermediate State in Protein Folding and Aggregation

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Tissue damage in the amyloidoses: Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture

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Annular Protofibrils Are a Structurally and Functionally Distinct Type of Amyloid Oligomer

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Strategies for the assessment of protein aggregates in pharmaceutical biotech product development

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Competing Pathways Determine Fibril Morphology in the Self-assembly of β2-Microglobulin into Amyloid

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Transthyretin Aggregation under Partially Denaturing Conditions Is a Downhill Polymerization

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Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy

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Conformational Abs recognizing a generic amyloid fibril epitope

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Insights into prion strains and neurotoxicity

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Critical assessment of methods of protein structure prediction (CASP)—Round XII

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Protein aggregation and its impact on product quality

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Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS

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Partially Unfolded States of β2-Microglobulin and Amyloid Formation in Vitro

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Amyloid formation under physiological conditions proceeds via a native-like folding intermediate

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Aβ(1-40) Fibril Polymorphism Implies Diverse Interaction Patterns in Amyloid Fibrils

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A Diversity of Assembly Mechanisms of a Generic Amyloid Fold

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Atomic‐Resolution Three‐Dimensional Structure of Amyloid β Fibrils Bearing the Osaka Mutation

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Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation

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