The heat shock protein 90 (HSP90) chaperone machinery is a key regulator of proteostasis
under both physiological and stress conditions in eukaryotic cells. As HSP90 has several …

Numerous genetic and environmental insults impede the ability of cells to properly fold and
posttranslationally modify secretory and transmembrane proteins in the endoplasmic …

The B cell receptor (BCR) initiates immune responses through antigen recognition. We
report a 3.3-angstrom cryo–electron microscopy structure of human immunoglobulin M (IgM) …

Recurrent mutations in the spliceosome are observed in several human cancers, but their
functional and therapeutic significance remains elusive. SF3B1, the most frequently mutated …

Analysis of the human genome reveals that approximately a third of all open reading frames
code for proteins that enter the endoplasmic reticulum (ER), demonstrating the importance of …

Transcytosis of polymeric IgA and IgM from the basolateral surface to the apical side of the
epithelium and subsequent secretion into mucosal fluids are mediated by the polymeric …

The inability of cells to properly fold, modify and assemble secretory and transmembrane
proteins leads to accumulation of misfolded proteins in the endoplasmic reticulum (ER) …

The biophysical rules that govern folding of small, single‐domain proteins in dilute solutions
are now quite well understood. The mechanisms underlying co‐translational folding of …

B cells use unconventional strategies for the production of a seemingly unlimited number of
antibodies from a very limited amount of DNA. These methods dramatically increase the …

Proteins that are expressed outside the cell must be synthesized, folded, and assembled in
a way that ensures they can function in their designate location. Accordingly, these proteins …