Elucidating protein–protein interaction (PPI) networks and their structural features within
cells is central to understanding fundamental biology and associations of cell phenotypes …

Protein aggregation is a hallmark of multiple human pathologies. Autophagy selectively
degrades protein aggregates via aggrephagy. How selectivity is achieved has been elusive …

The chaperonins are ubiquitous and essential nanomachines that assist in protein folding in
an ATP-driven manner. They consist of two back-to-back stacked oligomeric rings with …

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 …

Cells contain numerous abundant molecular machines assembled from multiple subunits.
Imbalances in subunit production and failed assembly generate orphan subunits that are …

Rotavirus (RV) replication takes place in the viroplasms, cytosolic inclusions that allow the
synthesis of virus genome segments and their encapsidation in the core shell, followed by …

The integrity of a cell's proteome depends on correct folding of polypeptides by chaperonins.
The chaperonin TCP-1 ring complex (TRiC) acts as obligate folder for> 10% of cytosolic …

The eukaryotic chaperonin TRiC/CCT assists the folding of about 10% of cytosolic proteins
through an ATP-driven conformational cycle, and the essential cytoskeleton protein tubulin …

The chaperone system (CS) of an organism is composed of molecular chaperones,
chaperone co-factors, co-chaperones, and chaperone receptors and interactors. It is present …

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 …