Probing the structure-function relationship of Mycobacterium leprae HSP18 under different UV radiations.
Sign Up to like & getrecommendations! Published in 2018 at "International journal of biological macromolecules"
DOI: 10.1016/j.ijbiomac.2018.07.151
Abstract: Ultraviolet radiation, an effective sterilizing source, rapidly kills the causative organism (Mycobacterium leprae) of leprosy. But, the reasons behind this quick death are not clearly understood. Also, the impact of UV radiation on the antigen(s)… read more here.
Keywords: leprae; mycobacterium leprae; structure; function ... See more keywords
Bacterial RF3 senses chaperone function in co-translational folding.
Sign Up to like & getrecommendations! Published in 2021 at "Molecular cell"
DOI: 10.1016/j.molcel.2021.05.016
Abstract: Molecular chaperones assist with protein folding by interacting with nascent polypeptide chains (NCs) during translation. Whether the ribosome can sense chaperone defects and, in response, abort translation of misfolding NCs has not yet been explored.… read more here.
Keywords: bacterial rf3; rf3; rf3 senses; chaperone function ... See more keywords
Structural determinants of multimerization and dissociation in 2-Cys peroxiredoxin chaperone function.
Sign Up to like & getrecommendations! Published in 2021 at "Structure"
DOI: 10.1016/j.str.2021.04.007
Abstract: Peroxiredoxins (PRDXs) are abundant peroxidases present in all kingdoms of life. Recently, they have been shown to also carry out additional roles as molecular chaperones. To address this emerging supplementary function, this review focuses on… read more here.
Keywords: multimerization dissociation; determinants multimerization; function; chaperone function ... See more keywords
Deletion of Specific Conserved Motifs from the N-Terminal Domain of αB-Crystallin Results in the Activation of Chaperone Functions
Sign Up to like & getrecommendations! Published in 2022 at "International Journal of Molecular Sciences"
DOI: 10.3390/ijms23031099
Abstract: Smaller oligomeric chaperones of α-crystallins (αA- and αB-) have received increasing attention due to their improved therapeutic potential in preventing protein aggregating diseases. Our previous study suggested that deleting 54–61 residues from the N-terminal domain… read more here.
Keywords: chaperone function; deletion; crystallin; terminal domain ... See more keywords