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 …

Abstract Iron-sulfur (Fe/S) proteins are present in virtually all living organisms and are
involved in numerous cellular processes such as respiration, photosynthesis, metabolic …

Aberrant phase separation of globular proteins is associated with many diseases. Here, we
use a model protein system to understand how the unfolded states of globular proteins drive …

Molecular chaperones are essential cellular components that aid in protein folding and
preventing the abnormal aggregation of disease-associated proteins. Mutations in one such …

Attempts to treat Alzheimer's disease with immunotherapy against the β-amyloid (Aβ)
peptide or with enzyme inhibitors to reduce Aβ production have not yet resulted in effective …

Chaperonins are large barrel-shaped complexes that mediate ATP-dependent protein
folding,–. The bacterial chaperonin GroEL forms juxtaposed rings that bind unfolded protein …

ATP-independent chaperones like trigger factor are generally assumed to play passive roles
in protein folding by acting as holding chaperones. Here we show that trigger factor plays a …

Bacteria do not simply express a constitutive panel of proteins but they instead undergo
dynamic changes in their protein repertoire in response to changes in nutritional status and …

The large abundance of small open reading frames (smORFs) in prokaryotic and eukaryotic
genomes and the plethora of smORF‐encoded small proteins became only apparent with …

UDP-glucose: glycoprotein glucosyltransferase (UGGT) 1 and 2 are central hubs in the
chaperone network of the endoplasmic reticulum (ER), acting as gatekeepers to the early …