Myxococcus xanthus DK1622 Coordinates Expressions of the Duplicate groEL and Single groES Genes for Synergistic Functions of GroELs and GroES [PDF]
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
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Chaperonin GroEL/GroES over-expression promotes multi-drug resistance in E. coli following exposure to aminoglycoside antibiotics [PDF]
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
The GroES/GroEL chaperonin from E ...
Jared Sivinski +2 more
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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
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Multi-scale simulations provide supporting evidence for the hypothesis of intramolecular protein translocation in GroEL/GroES complexes. [PDF]
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]
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]
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
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
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The trajectory of conditional, recurrence-free, and long-term survival in a complete 10-year cohort of patients with advanced ovarian cancer [PDF]
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
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

