Results 1 to 10 of about 153,321 (216)

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
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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
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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, Sarah J. Backe, Dimitra Bourboulia, Mehdi Mollapour, Mark R. Woodford   +4 more
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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
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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, Aditi Sharma, Lalit Sharma, Aayush Sehgal, Gokhan Zengin, Roxana Brata, Ovidiu Fratila, Simona Bungau   +7 more
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Chain-Selective Isotopic Labeling of the Heterodimeric Type III Secretion Chaperone, Scc4:Scc1, Reveals the Total Structural Rearrangement of the Chlamydia trachomatis Bi-Functional Protein, Scc4

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, Samantha M. Keane, Li Shen, Megan A. Macnaughtan   +3 more
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DnaK3 Is Involved in Biogenesis and/or Maintenance of Thylakoid Membrane Protein Complexes in the Cyanobacterium Synechocystis sp. PCC 6803

Life, 2020
DnaK3, a highly conserved cyanobacterial chaperone of the Hsp70 family, binds to cyanobacterial thylakoid membranes, and an involvement of DnaK3 in the biogenesis of thylakoid membranes has been suggested. As shown here, light triggers synthesis of DnaK3
Adrien Thurotte, Tobias Seidel, Ruven Jilly, Uwe Kahmann, Dirk Schneider   +4 more
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Mechanistic Insight Into the Interaction Between Helicobacter pylori Urease Subunit α and Its Molecular Chaperone Hsp60

Frontiers in Microbiology, 2019
Helicobacter pylori is the etiologic agent in a variety of gastroduodenal diseases. As its key pathogenic factors, both urease and Hsp60 play important roles in the pathogenesis of H. pylori.
Huilin Zhao, Yulong Wu, Zheng Xu, Ran Ma, Yunfei Ding, Xuelian Bai, Qianyu Rong, Ying Zhang, Boqing Li, Xiaofei Ji   +9 more
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Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) Ubiquitylation as a Novel Pharmaceutical Target for Cystic Fibrosis

Pharmaceuticals, 2020
Mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) gene decrease the structural stability and function of the CFTR protein, resulting in cystic fibrosis. Recently, the effect of CFTR-targeting combination therapy has dramatically
Ryosuke Fukuda, Tsukasa Okiyoneda
doaj   +1 more source