The biological functions of proteins are governed by their three-dimensional fold. Protein
folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically …

Most proteins must fold into precise three-dimensional conformations to fulfill their biological
functions. Here we review recent concepts emerging from studies of protein folding in vitro …

As nascent polypeptides exit ribosomes, they are engaged by a series of processing,
targeting, and folding factors. Here, we present a selective ribosome profiling strategy that …

Proteins generally must fold into precise three-dimensional conformations to fulfill their
biological functions. In the cell, this fundamental process is aided by molecular chaperones …

The early events in the life of newly synthesized proteins in the cellular environment are
remarkably complex. Concurrently with their synthesis by the ribosome, nascent …

Introduction Molecular chaperones prevent aggregation and misfolding of proteins in the
cellular environment and are thus central to maintaining protein homeostasis. Molecular …

Ribosomes, which are central to protein synthesis and convert transcribed mRNAs into
polypeptide chains, have been the focus of structural and biochemical studies for more than …

Disulfide bonds are covalent bonds formed post-translationally by the oxidation of a pair of
cysteines. A disulfide bond can serve structural, catalytic, and signaling roles. However …

Newly synthesized proteins require the assistance of molecular chaperones to efficiently fold
into functional three-dimensional structures in the crowded environment of the cell. At first …

Protein transport via the Sec translocon represents an evolutionary conserved mechanism
for delivering cytosolically-synthesized proteins to extra-cytosolic compartments. The Sec …