Landmarks to guide femoral insertion in lateral patellofemoral ligament reconstruction: An in vivo assessment of isometry. [PDF]
Abstract Purpose Lateral patellofemoral ligament (LPFL) reconstruction addresses medial patellar instability, but uncertainty regarding the optimal femoral attachment site may affect isometry and increase complication rates. This study aimed to establish landmarks for the femoral attachment of the LPFL graft based on in vivo isometry during active knee
Boot MR +3 more
europepmc +2 more sources
The Cowdria ruminantium groE operon [PDF]
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 +4 more
openaire +2 more sources
GroES and the chaperonin‐assisted protein folding cycle: GroES has no affinity for nucleotides [PDF]
The E. coli chaperonin proteins, GroEL and GroES, assist in folding newly synthesized proteins. GroES is necessary for GroEL‐assisted folding under conditions where the substrate protein cannot spontaneously fold. On the basis of photolabelling of GroES with 8‐azido‐ATP, a role for nucleotide binding to GroES in chaperonin function was suggested ...
Todd, Matthew J. +3 more
openaire +2 more sources
Gold nanoparticles have gained interest in biomedical sciences in the areas of nano-diagnostics, bio-labeling, drug delivery, and bacterial infection.
Rihab Lagha +3 more
doaj +1 more source
Creating the Functional Single-Ring GroEL-GroES Chaperonin Systems via Modulating GroEL-GroES Interaction [PDF]
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 +2 more
openaire +2 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.
Yue-zhong Li +6 more
doaj +1 more source
Ligand Binding Introduces Significant Allosteric Shifts in the Locations of Protein Fluctuations
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
Structural Plasticity and Noncovalent Substrate Binding in the GroEL Apical Domain. A study using electrospray ionization mass spectrometry and fluorescence binding studies [PDF]
Advances in understanding how GroEL binds to non-native proteins are reported. Conformational flexibility in the GroEL apical domain, which could account for the variety of substrates that GroEL binds, is illustrated by comparison of several independent ...
Adams +62 more
core +1 more source
Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space [PDF]
Cytochrome b2 reaches the intermembrane space of mitochondria by transport into the matrix followed by export across the inner membrane. While in the matrix, the protein interacts with hsp60, which arrests its folding prior to export.
Guiard, Bernard +6 more
core +1 more source
Exposure of Bifidobacterium longum subsp. infantis to Milk Oligosaccharides Increases Adhesion to Epithelial Cells and Induces a Substantial Transcriptional Response [PDF]
Devon Kavanaugh is in receipt of a Teagasc Walsh Fellowship. The authors would also like to acknowledge the support of Science Foundation Ireland under Grant No.
Butto, Ludovica F. +8 more
core +7 more sources

