An essential cellular machinery that has been identified and studied only relatively recently
is a collective of specialized proteins, molecular chaperones, that bind nonnative states of …

The budding yeast Saccharomyces cerevisiae is a powerful model organism for studying
fundamental aspects of eukaryotic cell biology. This Primer article presents a brief historical …

Viral clearance during hepatitis B virus (HBV) infection has been thought to reflect the
destruction of infected hepatocytes by CD8+ T lymphocytes. However, in this study, HBV …

▪ Abstract Recent years have witnessed dramatic advances in our understanding of how
newly translated proteins fold in the cell and the contribution of molecular chaperones to this …

The folding of most newly synthesized proteins in the cell requires the interaction of a variety
of protein cofactors known as molecular chaperones. These molecules recognize and bind …

Chaperonins assist protein folding with the consumption of ATP. They exist as multi-subunit
protein assemblies comprising rings of subunits stacked back to back. In Escherichia coli …

Although phenomenlogical models that account for cooperativity in allosteric systems date
back to the early and mid‐60's (eg, the KNF and MWC models), there is resurgent interest in …

The reproducibility and precision of biological patterning is limited by the accuracy with
which concentration profiles of morphogen molecules can be established and read out by …

The atomic force microscope (AFM) has a unique capability of allowing the high-resolution
imaging of biological samples on substratum surfaces in physiological solutions. Recent …

We describe the discovery of a heterohexameric chaperone protein, prefoldin, based on its
ability to capture unfolded actin. Prefoldin binds specifically to cytosolic chaperonin (c-cpn) …