Results 71 to 80 of about 5,379 (199)
The Cpn10(1) co-chaperonin of A. thaliana functions only as a hetero-oligomer with Cpn20. [PDF]
The A. thaliana genome encodes five co-chaperonin homologs, three of which are destined to the chloroplast. Two of the proteins, Cpn10(2) and Cpn20, form functional homo-oligomers in vitro.
Anna Vitlin Gruber +3 more
doaj +1 more source
ABSTRACT Molecular chaperones play a central role in the plant proteostasis machinery by aiding the folding of nascent proteins, preventing aggregation, and repairing or degrading damaged proteins. These functions are especially essential during abiotic and biotic stress, which can destabilise cellular proteins and disrupt metabolic homoeostasis.
Mingfang Yang +10 more
wiley +1 more source
Chaperonins dependent increase of Cu,Zn Superoxide dismutase production in Escherichia coli [PDF]
Over-expression of the chaperonins GroEL and GroES significantly suppressed the temperature-dependent pattern of expression of Cu,Zn Superoxide dismutases in Escherichia coli and increased the yield of active enzyme.
Carrí, M.Teresa +9 more
core +1 more source
Abstract Sarcopenia and frailty are complex geriatric syndromes influenced by a combination of genetic and environmental factors. Recent studies suggest that specific genetic variants, DNA methylation patterns and shortened telomeres are associated with age‐related diseases and might contribute to the development of both sarcopenia and frailty. In this
Valentina Ginevičienė +10 more
wiley +1 more source
Wheat stripe rust, caused by Puccinia striiformis f. sp. tritici (Pst), is considered one of the most aggressive diseases to wheat production. In this study, we used an iTRAQ-based approach for the quantitative proteomic comparison of the incompatible ...
Yuheng Yang +3 more
doaj +1 more source
Proteomic signatures of equine dental tooth tissues in ageing and disease
Abstract Background Ageing and dental disease in horses lead to structural and functional deterioration of dental tissues, yet their molecular signatures remain poorly characterised. Understanding how these processes alter the protein composition of enamel, dentin, cementum and pulp is essential for improving equine oral health and identifying ...
Anders Jensen +8 more
wiley +1 more source
In NIID, expanded NOTCH2NLC repeats give rise to nuclear polyG inclusions. Tracer‐guided in situ cryo‐electron tomography enables cross‐scale structural analysis from mouse brain to native neuronal nuclei, revealing dense‐core/peripheral‐halo inclusions built from compact polyG ribbons.
Hui Dong +13 more
wiley +1 more source
Type I Chaperonins: Mechanism and Beyond
Type I chaperonins are key players in maintaining the proteome of bacteria and organelles of bacterial origin. They are well known for their crucial role in mediating protein folding.
Adina Breiman, Abdussalam Azem
core +1 more source
Streamlining Diagnosis of Bardet–Biedl Syndrome: New Diagnostic Algorithm With Updated Criteria
ABSTRACT Considerable advances have been made in our understanding of Bardet–Biedl syndrome (BBS), particularly in its core clinical features and molecular genetics, warranting an update to the existing diagnostic criteria framework. Using a rigorous, evidence‐based, and consensus‐driven process, a multidisciplinary group of international experts and ...
Jeremy J. Pomeroy +16 more
wiley +1 more source
Prokaryotic Chaperonins: Multiple Copies and Multitude Functions.
This book discusses recent advances in understanding of the chaperonins and particularly multiple chaperoninsThe book covers evolution and possible modes of distribution of the multiple chaperonins, which is a novel topic on chaperoninsNumerous halftones
Chapparapu Mahabala, Santosh Kumar; id_orcid
core +1 more source

