Functional Differences between E. coli and ESKAPE Pathogen GroES/GroEL
The GroES/GroEL chaperonin from E ...
Jared Sivinski +2 more
exaly +3 more sources
Chaperonin GroEL (Cpn60) requires cofactor GroES (Cpn10) for protein refolding in bacteria that possess single groEL and groES genes in a bicistronic groESL operon.
Li Zhuo, Zheng Zhang, Xiao-Hua Zhang
exaly +3 more sources
Dual-calibration RT-qPCR reveals distinct dnaK1/2/3 and groEL1/2 expression dynamics under heat and acid stress in the sinefungin producer Streptomyces incarnatus [PDF]
Streptomyces incarnatus NRRL8089 produces sinefungin, a nucleoside antibiotic whose yield is enhanced under defined environmental stresses. Here, dual-calibration RT-qPCR was used to resolve paralogue-specific expression dynamics of the dnaK and groE ...
Zhao Xiao-Hui +6 more
doaj +2 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
Screening of molecular elements and improvement of heat resistance in a thermophilic bacterium [PDF]
Engineering microorganisms to withstand extreme temperatures (>80 °C) remains a critical challenge in industrial biotechnology owing to limited genetic tools and poor mechanistic understanding of microbial thermoadaptation.
Jie Cui +8 more
doaj +2 more sources
Formation of the chaperonin complex studied by 2D NMR spectroscopy. [PDF]
We studied the interaction between GroES and a single-ring mutant (SR1) of GroEL by the NMR titration of 15N-labeled GroES with SR1 at three different temperatures (20, 25 and 30°C) in the presence of 3 mM ADP in 100 mM KCl and 10 mM MgCl2 at pH 7.5.
Toshio Takenaka +10 more
doaj +1 more source
Protein folding is often hampered by intermolecular protein aggregation, which can be prevented by a variety of chaperones in the cell. Bacterial chaperonin GroEL is a ring-shaped chaperone that forms complexes with its cochaperonin GroES, creating ...
Hideki Taguchi, Ayumi Koike-Takeshita
doaj +1 more source
Identification of elements that dictate the specificity of mitochondrial Hsp60 for its co-chaperonin. [PDF]
Type I chaperonins (cpn60/Hsp60) are essential proteins that mediate the folding of proteins in bacteria, chloroplast and mitochondria. Despite the high sequence homology among chaperonins, the mitochondrial chaperonin system has developed unique ...
Avital Parnas +8 more
doaj +1 more source
The main events in chaperone-assisted protein folding are the binding and ligand-induced release of substrate proteins. Here, we studied the location of denatured proteins previously bound to the GroEL chaperonin resulting from the action of the GroES co-
Victor Marchenkov +4 more
doaj +1 more source
Exploração ou gratidão? Patronagem íntima e a gramática moral das trocas sexuais econômicas entre jovens curtidoras e europeus mais velhos, expatriados, em Maputo – Moçambique [PDF]
Resumo Neste artigo exploro uma categoria particular de mulheres inserida em sistemas de intercâmbio locais assim como na paisagem urbana transnacional de trocas íntimas.
Christian Groes-Green
doaj +3 more sources

