Results 71 to 80 of about 20,108 (219)

Cryo-EM structure of human mitochondrial HSPD1

open access: yesiScience, 2021
Summary: Chaperonins play an important role in folding newly synthesized or translocated proteins in all organisms. The bacterial chaperonin GroEL has served as a model system for the understanding of these proteins.
David P. Klebl   +7 more
doaj   +1 more source

Heat‐evolved coral photosymbionts exhibit dampened stress responses across distinct physiological contexts

open access: yesNew Phytologist, EarlyView.
Summary Experimental evolution under elevated temperatures has generated heat‐evolved (HE) strains of Symbiodiniaceae that enhance coral bleaching tolerance. However, the biomolecular mechanisms underlying this resilience remain poorly understood. We conducted a laboratory heat‐stress experiment and applied synchrotron‐based Fourier transform infrared (
Bede G. Johnston   +5 more
wiley   +1 more source

Facilitated release of substrate protein from prefoldin by chaperonin [PDF]

open access: yes, 2005
Prefoldin is a chaperone that captures a protein-folding intermediate and transfers it to the group II chaperonin for correct folding. However, kinetics of interactions between prefoldin and substrate proteins have not been investigated.
Masafumi Yohda   +15 more
core   +1 more source

Physiology and Transcriptomics Reveal Divergent Strategies of Mycorrhiza‐Mediated Drought Adaptation in Poplar

open access: yesPlant, Cell &Environment, EarlyView.
ABSTRACT Mycorrhizal symbiosis shapes plant growth and stress resilience. Here, we compared physiological and molecular responses of poplars (P. x canescens) colonised by Paxillus involutus (Pi) or Cenococcum geophilum (Cg) under control conditions, drought stress and recovery.
Huili Shi, Zhuchou Lu, Andrea Polle
wiley   +1 more source

Chaperonin releases the substrate protein in a form with tendency to aggregate and ability to rebind to chaperonin [PDF]

open access: yes, 1995
To know whether the protein released from chaperonin GroEL/ES is in a form committed to the native state or still an aggregatable non-native one, two experiments were carried out.
Hideki Taguchi   +3 more
core   +1 more source

Molecular Chaperone Networks in Plants: Maintaining Proteostasis and Enhancing Stress Resilience for Crop Improvement

open access: yesPlant, Cell &Environment, EarlyView.
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

Ordered biological nanostructures formed from chaperonin polypeptides [PDF]

open access: yes, 2010
The following application relates to nanotemplates, nanostructures, nanoarrays and nanodevices formed from wild-type and mutated chaperonin polypeptides, methods of producing such compositions, methods of using such compositions and particular chaperonin
Trent, Jonathan D.   +3 more
core   +1 more source

A multi‐omics investigation of sarcopenia and frailty: Integrating genomic, epigenomic and telomere length data

open access: yesExperimental Physiology, EarlyView.
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

The Cpn10(1) co-chaperonin of A. thaliana functions only as a hetero-oligomer with Cpn20. [PDF]

open access: yesPLoS ONE, 2014
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

Fungal, not insect: Revisiting a misidentified Bemisia tabaci protein interacting with a begomovirus coat protein

open access: yesInsect Molecular Biology, Volume 35, Issue 4, Page 361-363, August 2026.
A small heat‐shock protein (HSP16) previously reported as insect‐derived in Bemisia tabaci actually originates from a fungal species of the genus Wallemia. BLAST, genome survey and phylogenetic analyses support the fungal origin and clarify persistent misattribution in the literature.
Jesús Navas‐Castillo   +1 more
wiley   +1 more source

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