The endoplasmic reticulum (ER) plays a critical role in the synthesis and chaperoning of
membrane-associated and secreted proteins. The membrane is also an important site of …

A substantial fraction of eukaryotic gene products are synthesized by ribosomes attached at
the cytosolic face of the endoplasmic reticulum (ER) membrane. These polypeptides enter …

Protein misfolding in the endoplasmic reticulum (ER) contributes to the pathogenesis of
many diseases. Although oxidative stress can disrupt protein folding, how protein misfolding …

THE PAST TWO DECADES have brought remarkable progress in our understanding of the
molecular basis of hemophilia A. This disease, which has already been documented as a …

This is the second edition of our little red book Lectins published in 1989. In the intervening
years well over 10,000 articles have appeared with lectins as the main subject, and more …

▪ Abstract An unconventional mechanism for retaining improperly folded glycoproteins and
facilitating acquisition of their native tertiary and quaternary structures operates in the …

The mechanisms that determine how folding attempts are interrupted to target folding-
incompetent proteins for endoplasmic reticulum–associated degradation (ERAD) are poorly …

Terminally misfolded proteins in the endoplasmic reticulum (ER) are retrotranslocated to the
cytoplasm and degraded by proteasomes through a mechanism known as ER-associated …

The endoplasmic reticulum (ER) is the subcellular site where proteins following the
secretory pathway acquire their proper tertiary and, in certain cases, quaternary structures …

Factor VIII (FVIII) functions as a cofactor within the intrinsic pathway of blood coagulation.
Quantitative or qualitative deficiencies of FVIII result in the inherited bleeding disorder …