Suggestions(5)
Exact(1)
This interferes with the chaperones' essential functions of mediating folding of essential proteins.
Similar(59)
Such a global enhancement of E. coli cytosolic proteostasis capacity is able to mediate folding of a variety of client proteins, eliminating the necessity to know which chaperone or chaperonin pathway handles a particular protein-of-interest.
Heat shock proteins act as chaperones (mediating folding, assembly, and transport of other proteins) and also in response to cellular stresses, including temperature changes and the presence of viral and bacterial infections (Neuer et al. 2000); it is possible that HSPs may be expressed in response to the stresses that a female experiences while interacting with hosts during oviposition.
Here, we investigate the role of confinement in chaperonin mediated folding through molecular dynamics simulations.
Heat Shock Proteins (HSPs) are the major chaperones mediating (re) folding of proteins, ensuring that these proteins stay in their native formations during conditions of stress to the cell [ 4].
GRP78 (immunoglobulin heavy chain binding protein (BiP)) and GRP94 are the ER chaperones that are generally considered to be the most important for mediating the folding of newly synthesized immunoglobulin.
The GroEL/GroES chaperonin system mediates the folding of a range of newly synthesized polypeptides in the bacterial cytosol.
The SAM is also located in the OM, where it mediates correct folding of β-barrel proteins.
Slm9 affinity purifications also revealed interactions with subunits of the chaperonin CCT, which is known to mediate the folding of numerous proteins [23].
The GroEL protein mediates the folding of polypeptides, and it is found to be highly expressed in Buchnera and other p-endosymbionts.
HSP70 and its family members mediate the folding of newly translated proteins in the cytosol and organelles [57], [58] and also have been reported to promote ARE-mediated mRNA decay [59], [60].
Write better and faster with AI suggestions while staying true to your unique style.
Since I tried Ludwig back in 2017, I have been constantly using it in both editing and translation. Ever since, I suggest it to my translators at ProSciEditing.

Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com