▪ Abstract In the endoplasmic reticulum (ER), secretory and transmembrane proteins fold into
their native conformation and undergo posttranslational modifications important for their …

Conformational diseases are caused by mutations altering the folding pathway or final
conformation of a protein. Many conformational diseases are caused by mutations in …

Proteins synthesized in the endoplasmic reticulum (ER) are properly folded with the
assistance of ER chaperones. Malfolded proteins are disposed of by ER‐associated protein …

Replicative senescence of human diploid fibroblasts (HDFs) or melanocytes is caused by
the exhaustion of their proliferative potential. Stress-induced premature senescence (SIPS) …

How a cell responds to stress is a central problem in cardiovascular biology. Diverse
physiological stresses (eg, heat, hemodynamics, mutant proteins, and oxidative injury) …

BiP, an HSP70 molecular chaperone located in the lumen of the endoplasmic reticulum
(ER), binds newly-synthesized proteins as they are translocated into the ER and maintains …

In cells, both newly synthesized and pre-existing proteins are constantly endangered by
misfolding and aggregation. The accumulation of damaged proteins can perturb cellular …

Nearly all resident proteins of the organelles along the secretory pathway, as well as
proteins that are expressed at the cell surface or secreted from the cell, are first co …

We demonstrate the existence of a large endoplasmic reticulum (ER)-localized multiprotein
complex that is comprised of the molecular chaperones BiP; GRP94; CaBP1; protein …

Induction of macrophage necrosis is a strategy used by virulent Mycobacterium tuberculosis
(Mtb) to avoid innate host defense. In contrast, attenuated Mtb causes apoptosis, which limits …