Results 11 to 20 of about 9,153 (190)

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

Frontiers 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.
Yue-zhong Li, Li Zhuo, Yan Wang, Yan Wang, Zheng Zhang, Jian Li, Xiao-Hua Zhang   +6 more
doaj   +5 more sources

Creating the Functional Single-Ring GroEL-GroES Chaperonin Systems via Modulating GroEL-GroES Interaction [PDF]

Scientific Reports, 2017
AbstractChaperonin and cochaperonin, represented by E. coli GroEL and GroES, are essential molecular chaperones for protein folding. The double-ring assembly of GroEL is required to function with GroES, and a single-ring GroEL variant GroELSR forms a stable complex with GroES, arresting the chaperoning reaction cycle.
Illingworth, Melissa, Ellis, Holly, Chen, Lingling   +2 more
openaire   +3 more sources

Role of the amino terminal domain in GroES oligomerization

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1997
Digestions of the GroES oligomer with trypsin, chymotrypsin and Glu-C protease from Staphylococcus aureus V8 (V8) have helped to locate three regions in the GroES sequence that are sensitive to limited proteolysis and have provided information of the GroES domains involved in monomer-monomer and GroEL interaction.
Llorca, Óscar, Schneider, Klaus, Carrascosa, José L., Méndez, Enrique, Valpuesta, José M.   +4 more
openaire   +4 more sources

Dynamic computed tomography assessment of patellofemoral and tibiofemoral kinematics before and after total knee arthroplasty: A pilot study. [PDF]

Knee Surg Sports Traumatol Arthrosc
Abstract Purpose To develop and evaluate the clinical feasibility of a dynamic computed tomography (CT) protocol for assessing patellofemoral (PF) and tibiofemoral (TF) kinematics before and after total knee arthroplasty (TKA), and to quantify postoperative kinematic changes in a pilot study.
Boot MR, van de Groes SAW, Tanck E, Janssen D.   +3 more
europepmc   +2 more sources

The Cowdria ruminantium groE operon [PDF]

Microbiology, 1995
A Cowdria ruminantium genomic DNA library was constructed in the expression vector lambda ZAPII, and an immunoreactive clone, designated lambda Cr9.4, was isolated by screening with serum from a C. ruminantium-infected goat. Sequencing of the insert from this clone revealed two open reading frames, encoding peptides of 10462 and 58697 kDa respectively.
N C, Lally, S, Nicoll, E A, Paxton, C M, Cary, K J, Sumption   +4 more
openaire   +2 more sources

Effect of Plasmonic Gold Nanoprisms on Biofilm Formation and Heat Shock Proteins Expression in Human Pathogenic Bacteria

Pharmaceuticals, 2021
Gold nanoparticles have gained interest in biomedical sciences in the areas of nano-diagnostics, bio-labeling, drug delivery, and bacterial infection.
Rihab Lagha, Fethi Ben Abdallah, Amine Mezni, Othman M. Alzahrani   +3 more
doaj   +1 more source

Determination of the Number of Active GroES Subunits in the Fused Heptamer GroES Required for Interactions with GroEL [PDF]

Journal of Biological Chemistry, 2008
A double-heptamer ring chaperonin GroEL binds denatured substrate protein, ATP, and GroES to the same heptamer ring and encapsulates substrate into the central cavity underneath GroES where productive folding occurs. GroES is a disk-shaped heptamer, and each subunit has a GroEL-binding loop.
T. Nojima, S. Murayama, MASASUKE YOSHIDA, F. Motojima   +3 more
openaire   +2 more sources

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

Journal 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 ...
T, Kubo, T, Mizobata, Y, Kawata
openaire   +2 more sources

Ligand Binding Introduces Significant Allosteric Shifts in the Locations of Protein Fluctuations

Frontiers in Molecular Biosciences, 2021
Allostery is usually considered to be a mechanism for transmission of signals associated with physical or dynamic changes in some part of a protein. Here, we investigate the changes in fluctuations across the protein upon ligand binding based on the ...
Ambuj Kumar, Robert L. Jernigan
doaj   +1 more source

HSP10 as a Chaperone for Neurodegenerative Amyloid Fibrils

Frontiers in Neuroscience, 2022
Neurodegenerative diseases (NDs) are associated with accumulated misfolded proteins (MPs). MPs oligomerize and form multiple forms of amyloid fibril polymorphs that dictate fibril propagation and cellular dysfunction.
Johan N. K. Larsson, Sofie Nyström, Per Hammarström   +2 more
doaj   +1 more source