Chp1 is a dedicated chaperone at the ribosome that safeguards eEF1A biogenesis
M Minoia, J Quintana-Cordero, K Jetzinger… - Nature …, 2024 - nature.com
Cotranslational protein folding depends on general chaperones that engage highly diverse
nascent chains at the ribosomes. Here we discover a dedicated ribosome-associated …
nascent chains at the ribosomes. Here we discover a dedicated ribosome-associated …
A ribosome-associating chaperone mediates GTP-driven vectorial folding of nascent eEF1A
IM Sabbarini, D Reif, K Park, AJ McQuown… - Nature …, 2025 - nature.com
Eukaryotic translation elongation factor 1A (eEF1A) is a highly abundant, multi-domain
GTPase. Post-translational steps essential for eEF1A biogenesis are carried out by bespoke …
GTPase. Post-translational steps essential for eEF1A biogenesis are carried out by bespoke …
Regulation of Proteostasis and Stress Response: Insights into Hsf1 and Chaperone Dynamics
M Ciccarelli - 2024 - diva-portal.org
Protein homeostasis (proteostasis) refers to the balance between protein production, folding,
and degradation, and is coordinated by components of the proteostasis network. Preserving …
and degradation, and is coordinated by components of the proteostasis network. Preserving …
Identification and characterization of novel eukaryotic chaperones
A Nelliat - 2024 - search.proquest.com
Protein folding and assembly is aided by molecular chaperones that prevent aggregation of
unfolded or partially folded intermediates and guide them to their native folded state …
unfolded or partially folded intermediates and guide them to their native folded state …