Results 1 to 10 of about 158,532 (263)

Cryo-EM structure of the diapause chaperone artemin

Frontiers in Molecular Biosciences, 2022
The protein artemin acts as both an RNA and protein chaperone and constitutes over 10% of all protein in Artemia cysts during diapause. However, its mechanistic details remain elusive since no high-resolution structure of artemin exists.
Amar D. Parvate, Samantha M. Powell, Jory T. Brookreson, Trevor H. Moser, Irina V. Novikova, Mowei Zhou, James E. Evans, James E. Evans   +7 more
doaj   +1 more source

αA-Crystallin-derived mini-chaperone modulates stability and function of cataract causing αAG98R-crystallin. [PDF]

PLoS ONE, 2012
A substitution mutation in human αA-crystallin (αAG98R) is associated with autosomal dominant cataract. The recombinant mutant αAG98R protein exhibits altered structure, substrate-dependent chaperone activity, impaired oligomer stability and aggregation ...
Murugesan Raju, Puttur Santhoshkumar, K Krishna Sharma   +2 more
doaj   +1 more source

Controlling drug resistance by targeting Plasmodium falciparum heat shock protein 70-1, a chaperone at the centre of protein quality control mechanism: a review

All Life, 2023
The survival of the malaria parasite is highly dependent on withstanding physiological stresses, which are a proportional response to parasite invasion within the hostile human host environment.
Douglas A. M. Ruhwaya, Brilliant Nyathi, Gadzikano Munyuki, Ryman Shoko, Grace Mugumbate   +4 more
doaj   +1 more source

TRAP1 Chaperones the Metabolic Switch in Cancer

Biomolecules, 2022
Mitochondrial function is dependent on molecular chaperones, primarily due to their necessity in the formation of respiratory complexes and clearance of misfolded proteins.
Laura A. Wengert, Sarah J. Backe, Dimitra Bourboulia, Mehdi Mollapour, Mark R. Woodford   +4 more
doaj   +1 more source

The unhappy chaperone [PDF]

QRB Discovery, 2021
Abstract Chaperones protect other proteins against misfolding and aggregation, a key requirement for maintaining biological function. Experimental observations of changes in solubility of amyloid proteins in the presence of certain chaperones are discussed here in terms of thermodynamic driving forces.
Sara Linse, Kyrre Thalberg, Tuomas P. J. Knowles   +2 more
openaire   +3 more sources

Multiple Roles of Flagellar Export Chaperones for Efficient and Robust Flagellar Filament Formation in Salmonella

Frontiers in Microbiology, 2021
FlgN, FliS, and FliT are flagellar export chaperones specific for FlgK/FlgL, FliC, and FliD, respectively, which are essential component proteins for filament formation.
Tohru Minamino, Yusuke V. Morimoto, Yusuke V. Morimoto, Miki Kinoshita, Keiichi Namba, Keiichi Namba, Keiichi Namba   +6 more
doaj   +1 more source

Identification and characterization of a gene conferring stress resistance in Escherichia coli and cyanobacteria. [PDF]

FEBS Open Bio
Functional screening identified PcSyn14890, a cyanobacteria‐specific protein that enhances growth and stress resistance in E. coli and Synechocystis PCC6803. Although we expected it to function as a molecular chaperone, it was unable to protect against thermal aggregation of GAPDH.
Yamada A, Tanaka T, Uehara M, Nakano K, Morishima K, Inoue R, Sugiyama M, Yohda M.   +7 more
europepmc   +2 more sources

Chaperone discovery [PDF]

BioEssays, 2012
AbstractMolecular chaperones assist de novo protein folding and facilitate the refolding of stress‐denatured proteins. The molecular chaperone concept was coined nearly 35 years ago, and since then, tremendous strides have been made in understanding how these factors support protein folding.
Quan, Shu, Bardwell, James C. A.
openaire   +3 more sources

Exploring the Multifaceted Therapeutic Potential of Withaferin A and Its Derivatives

Biomedicines, 2020
Withaferin A (WA), a manifold studied, C28-steroidal lactone withanolide found in Withania somnifera. Given its unique beneficial effects, it has gathered attention in the era of modern science.
Tapan Behl, Aditi Sharma, Lalit Sharma, Aayush Sehgal, Gokhan Zengin, Roxana Brata, Ovidiu Fratila, Simona Bungau   +7 more
doaj   +1 more source

Faithful chaperones [PDF]

Cellular and Molecular Life Sciences, 2011
This review describes the properties of some rare eukaryotic chaperones that each assist in the folding of only one target protein. In particular, we describe (1) the tubulin cofactors, (2) p47, which assists in the folding of collagen, (3) α-hemoglobin stabilizing protein (AHSP), (4) the adenovirus L4-100 K protein, which is a chaperone of the major ...
Szolajska, Ewa, Chroboczek, Jadwiga
openaire   +2 more sources