Results 1 to 10 of about 226,086 (342)
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 +7 more
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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 +2 more
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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 +4 more
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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 +4 more
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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 +6 more
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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.
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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 +7 more
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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
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Current Opinion in Structural Biology, 2014 The folding and assembly of myosin motor proteins is essential for most movement processes at the cellular, but also at the organism level. Importantly, myosins, which represent a very diverse family of proteins, require the activity of general and specialized folding factors to develop their full motor function.
Hellerschmied, Doris, Clausen, Tim
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Biomolecules, 2020 Scc4 is an unusual bi-functional protein from Chlamydia trachomatis (CT) that functions as a type III secretion system (T3SS) chaperone and an RNA polymerase (RNAP)-binding protein.
Thilini O. Ukwaththage +3 more
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