Genetic, environmental, and aging-related insults can promote the misfolding and
subsequent aggregation of secreted proteins implicated in the pathogenesis of numerous …

Aberrant protein aggregation is a defining feature of most neurodegenerative diseases.
During pathological aggregation, key proteins transition from their native state to alternative …

The extracellular protein, transthyretin is responsible for the transport of thyroxin and retinol
binding protein complex to the various parts of the body. In addition to this transport function …

Imbalances in secretory proteostasis induced by genetic, environmental, or aging-related
insults are pathologically associated with etiologically diverse protein misfolding diseases …

Protein folding in the cell is mediated by an extensive network of> 1,000 chaperones, quality
control factors, and trafficking mechanisms collectively termed the proteostasis network …

The critical toxic species in over 40 human diseases are misfolded proteins. Their interaction
with molecular chaperones such as Hsp90, which preferentially interacts with metastable …

ER dj3/DNAJB 11 is an endoplasmic reticulum (ER)‐targeted HSP 40 co‐chaperone that
performs multifaceted functions involved in coordinating ER and extracellular proteostasis …

Most eukaryotic secretory proteins are cotranslationally translocated through Sec61 into the
endoplasmic reticulum (ER). Because these proteins have evolved to fold in the ER, their …

The extracellular aggregation of destabilized transthyretin (TTR) variants is implicated in the
onset and pathogenesis of familial TTR-related amyloid diseases. One strategy to reduce …

The PERK arm of the unfolded protein response (UPR) regulates cellular proteostasis and
survival in response to endoplasmic reticulum (ER) stress. However, the impact of PERK …