'I Do It All Alone': The Burdens and Benefits of Being Diagnosed With, and Treated for, Colorectal Cancer During the Covid-19 Pandemic.

Structure-Toxicity Relationship in Intermediate Fibrils from Îą-Synuclein Condensates.

Formation of amyloid loops in brain tissues is controlled by the flexibility of protofibril chains.

Microfluidic antibody affinity profiling of alloantibody-HLA interactions in human serum.

The role of structural dynamics in the thermal adaptation of hyperthermophilic enzymes.

N-Terminal Acetylation of Îą-Synuclein Slows down Its Aggregation Process and Alters the Morphology of the Resulting Aggregates.

The Pathological G51D Mutation in Alpha-Synuclein Oligomers Confers Distinct Structural Attributes and Cellular Toxicity.

The Hsc70 disaggregation machinery removes monomer units directly from Îą-synuclein fibril ends.

Accelerating Reaction Rates of Biomolecules by Using Shear Stress in Artificial Capillary Systems.

The Amyloid Fibril-Forming β-Sheet Regions of Amyloid β and ι-Synuclein Preferentially Interact with the Molecular Chaperone 14-3-3Μ.

Distinct responses of human peripheral blood cells to different misfolded protein oligomers.

The binding of the small heat-shock protein ÎąB-crystallin to fibrils of Îą-synuclein is driven by entropic forces.

Machine learning-aided protein identification from multidimensional signatures.

Observation of an Îą-synuclein liquid droplet state and its maturation into Lewy body-like assemblies.

Publisher Correction: Two human metabolites rescue a C. elegans model of Alzheimer's disease via a cytosolic unfolded protein response.