The heat shock proteins (HSPs) are ubiquitous and conserved protein families in both
prokaryotic and eukaryotic organisms, and they maintain cellular proteostasis and protect …

Molecular chaperones are diverse families of multidomain proteins that have evolved to
assist nascent proteins to reach their native fold, protect subunits from heat shock during the …

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

The identification of proximate amino acids by chemical cross-linking and mass
spectrometry (XL-MS) facilitates the structural analysis of homogeneous protein complexes …

TRiC/CCT is a highly conserved and essential chaperonin that uses ATP cycling to facilitate
folding of approximately 10% of the eukaryotic proteome. This 1 MDa hetero-oligomeric …

EMAN2. 1 is a complete image processing suite for quantitative analysis of grayscale
images, with a primary focus on transmission electron microscopy, with complete workflows …

Protein folding in the cell requires the assistance of enzymes collectively called chaperones.
Among these, the chaperonins are 1-MDa ring-shaped oligomeric complexes that bind …

The ATP-dependent ring-shaped chaperonin TRiC/CCT is essential for cellular proteostasis.
To uncover why some eukaryotic proteins can only fold with TRiC assistance, we …

The cytoskeletal proteins tubulin and actin are the obligate substrates of TCP-1 ring
complex/Chaperonin containing TCP-1 (TRiC/CCT), and their folding involves co …

The eukaryotic chaperonin TRiC (also called CCT) is the obligate chaperone for many
essential proteins. TRiC is hetero-oligomeric, comprising two stacked rings of eight different …