Results 1 to 10 of about 24,615 (247)

Myxococcus xanthus DK1622 Coordinates Expressions of the Duplicate groEL and Single groES Genes for Synergistic Functions of GroELs and GroES [PDF]

open access: goldFrontiers in Microbiology, 2017
Chaperonin GroEL (Cpn60) requires cofactor GroES (Cpn10) for protein refolding in bacteria that possess single groEL and groES genes in a bicistronic groESL operon.
Yan Wang, Zheng Zhang, Yue-zhong Li
exaly   +4 more sources

Chaperonin GroEL/GroES over-expression promotes multi-drug resistance in E. coli following exposure to aminoglycoside antibiotics [PDF]

open access: yesFrontiers in Microbiology, 2016
Antibiotic resistance is an increasing challenge to modern healthcare. Aminoglycoside antiobiotics cause translation corruption and protein misfolding and aggregation in Escherichia coli.
Lise eGoltermann   +2 more
doaj   +5 more sources

Functional Differences between E. coli and ESKAPE Pathogen GroES/GroEL

open access: yesMBio, 2021
The GroES/GroEL chaperonin from E ...
Jared Sivinski   +2 more
exaly   +3 more sources

Refolding of yeast enolase in the presence of the chaperonin GroE. The nucleotide specificity of GroE and the role of GroES.

open access: hybridJournal of Biological Chemistry, 1993
GroE, a chaperonin protein from Escherichia coli, facilitates the folding of numerous proteins by binding to protein-folding intermediates and suppressing aggregation (Gething, M., and Sambrook, J. (1992) Nature 355, 33-45). The specific mechanism of GroE-facilitated folding involves numerous interactions between GroEL, GroES, the refolding protein ...
Tomoko Kubo   +2 more
openalex   +3 more sources

Multi-scale simulations provide supporting evidence for the hypothesis of intramolecular protein translocation in GroEL/GroES complexes. [PDF]

open access: goldPLoS Computational Biology, 2008
The biological function of chaperone complexes is to assist the folding of non-native proteins. The widely studied GroEL chaperonin is a double-barreled complex that can trap non-native proteins in one of its two barrels.
Ivan Coluzza   +3 more
doaj   +3 more sources

Bone morphology and alignment features are associated with knee kinematics in healthy individuals: A scoping review [PDF]

open access: yesJournal of Experimental Orthopaedics
Purpose The aim of this scoping review was to compose an overview of existing literature on the influence of knee bone morphology and alignment on knee kinematics in healthy individuals.
Erin Teule   +3 more
doaj   +2 more sources

Triggering Protein Folding within the GroEL-GroES Complex [PDF]

open access: hybridJournal of Biological Chemistry, 2008
The folding of many proteins depends on the assistance of chaperonins like GroEL and GroES and involves the enclosure of substrate proteins inside an internal cavity that is formed when GroES binds to GroEL in the presence of ATP. Precisely how assembly of the GroEL-GroES complex leads to substrate protein encapsulation and folding remains poorly ...
Damian Madan, Zong Lin, Hays S. Rye
openalex   +4 more sources

Conversion of an inactive xylose isomerase into a functional enzyme by co-expression of GroEL-GroES chaperonins in Saccharomyces cerevisiae

open access: goldBMC Biotechnology, 2017
Background Second-generation ethanol production is a clean bioenergy source with potential to mitigate fossil fuel emissions. The engineering of Saccharomyces cerevisiae for xylose utilization is an essential step towards the production of this biofuel ...
Beatriz Temer   +9 more
doaj   +2 more sources

The trajectory of conditional, recurrence-free, and long-term survival in a complete 10-year cohort of patients with advanced ovarian cancer [PDF]

open access: yesActa Oncologica
Background: The prognosis in advanced ovarian cancer is generally poor since the majority experience recurrence. Nevertheless, there is a chance of cure and very long-term survival may be achieved. However, traditional survival metrics do not account for
Nina Groes Kofoed   +3 more
doaj   +2 more sources

The structural stability of the co-chaperonin GroES

open access: yesJournal of Molecular Biology, 1997
The structural stability of the co-chaperonin GroES has been studied by high sensitivity differential scanning calorimetry and circular dichroism under different solvent conditions. The thermal folding/unfolding of GroES is a spontaneous reversible process involving a highly cooperative transition between folded heptamers and unfolded monomers.
Ernesto Freire
exaly   +3 more sources

Home - About - Disclaimer - Privacy