Heat shock proteins, first observed because they are preferentially synthesized by
organisms exposed to heat or other physiological stress, are also synthesized constitutively …

Many proteins in the cell require assistance from molecular chaperones at stages in their life
cycles in order to attain correctly folded states and functional conformations during protein …

Maintenance of the cellular proteome or proteostasis is an essential process that when
deregulated leads to diseases like neurological disorders and cancer. Central to …

The chaperonin containing t-complex polypeptide 1 (CCT) is a heterooligomeric molecular
chaperone assisting in the folding of actin, tubulin, and other cytosolic proteins. The …

Eukaryotic cilia and flagella are highly conserved structures composed of a canonical 9+ 2
microtubule axoneme. Comparative genomics of flagellated and non-flagellated eukaryotes …

Previously, we showed that the yeast Saccharomyces cerevisiae cold-sensitive mutation
tcp1-1 confers growth arrest concomitant with cytoskeletal disorganization and disruption of …

In recent years, the amount of molecular sequencing data from Tetrahymena thermophila
has dramatically increased. We analyzed G+ C content, codon usage, initiator codon context …

The bacterium Holospora oblusa is a macronuclear‐specific symbiont of the ciliate
Paramecium caudatum. H. obtusa‐bearing paramecia could survive even after the cells …

Molecular chaperones are a group of proteins that assists in the folding of newly synthesized
proteins or in the refolding of denatured proteins. The cytosolic chaperonin-containing t …

The chaperonin containing TCP‐1 (CCT) is a molecular chaperone consisting of eight
subunit species and assists in the folding of actin, tubulin and some other cytosolic proteins …