A framework for understanding the functions of biomolecular condensates across scales
AS Lyon, WB Peeples, MK Rosen - Nature Reviews Molecular Cell …, 2021 - nature.com
Biomolecular condensates are found throughout eukaryotic cells, including in the nucleus, in
the cytoplasm and on membranes. They are also implicated in a wide range of cellular …
the cytoplasm and on membranes. They are also implicated in a wide range of cellular …
The expanding amyloid family: Structure, stability, function, and pathogenesis
The hidden world of amyloid biology has suddenly snapped into atomic-level focus,
revealing over 80 amyloid protein fibrils, both pathogenic and functional. Unlike globular …
revealing over 80 amyloid protein fibrils, both pathogenic and functional. Unlike globular …
Mechanisms and pathology of protein misfolding and aggregation
Despite advances in machine learning-based protein structure prediction, we are still far
from fully understanding how proteins fold into their native conformation. The conventional …
from fully understanding how proteins fold into their native conformation. The conventional …
Amyloid fibrils in FTLD-TDP are composed of TMEM106B and not TDP-43
Frontotemporal lobar degeneration (FTLD) is the third most common neurodegenerative
condition after Alzheimer's and Parkinson's diseases. FTLD typically presents in 45 to 64 …
condition after Alzheimer's and Parkinson's diseases. FTLD typically presents in 45 to 64 …
Proteostasis of islet amyloid polypeptide: a molecular perspective of risk factors and protective strategies for type II diabetes
The possible link between hIAPP accumulation and β-cell death in diabetic patients has
inspired numerous studies focusing on amyloid structures and aggregation pathways of this …
inspired numerous studies focusing on amyloid structures and aggregation pathways of this …
Amyloid-type protein aggregation and prion-like properties of amyloids
This review will focus on the process of amyloid-type protein aggregation. Amyloid fibrils are
an important hallmark of protein misfolding diseases and therefore have been investigated …
an important hallmark of protein misfolding diseases and therefore have been investigated …
Cryo-EM structures of hIAPP fibrils seeded by patient-extracted fibrils reveal new polymorphs and conserved fibril cores
Amyloidosis of human islet amyloid polypeptide (hIAPP) is a pathological hallmark of type II
diabetes (T2D), an epidemic afflicting nearly 10% of the world's population. To visualize …
diabetes (T2D), an epidemic afflicting nearly 10% of the world's population. To visualize …
Amyloid cross-seeding: Mechanism, implication, and inhibition
Most neurodegenerative diseases such as Alzheimer's disease, type 2 diabetes, Parkinson's
disease, etc. are caused by inclusions and plaques containing misfolded protein …
disease, etc. are caused by inclusions and plaques containing misfolded protein …
Structural evolution of fibril polymorphs during amyloid assembly
Cryoelectron microscopy (cryo-EM) has provided unprecedented insights into amyloid fibril
structures, including those associated with disease. However, these structures represent the …
structures, including those associated with disease. However, these structures represent the …
Fibril structures of diabetes-related amylin variants reveal a basis for surface-templated assembly
Aggregation of the peptide hormone amylin into amyloid deposits is a pathological hallmark
of type-2 diabetes (T2D). While no causal link between T2D and amyloid has been …
of type-2 diabetes (T2D). While no causal link between T2D and amyloid has been …