Exposure of Bifidobacterium longum subsp. infantis to Milk Oligosaccharides Increases Adhesion to Epithelial Cells and Induces a Substantial Transcriptional Response [PDF]
, 2013 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 +10 more sources
Probing the dynamic process of encapsulation in Escherichia coli GroEL. [PDF]
PLoS ONE, 2013 Kinetic analyses of GroE-assisted folding provide a dynamic sequence of molecular events that underlie chaperonin function. We used stopped-flow analysis of various fluorescent GroEL mutants to obtain details regarding the sequence of events that ...
Toshifumi Mizuta +4 more
doaj +1 more source
Foods, 2023 The molecular chaperone GroEL of C. sakazakii, a highly conserved protein encoded by the gene grol, has the basic function of responding to heat shock, thus enhancing the bacterium’s adaptation to dry and high-temperature environments, which poses a ...
Dongdong Zhu +9 more
doaj +1 more source
Journal of the Formosan Medical Association, 2021 Background/Purpose: Porphyromonas gingivalis is an oral pathogen associated with periodontal diseases. P. gingivalis GroEL protein is a stimulator of inflammatory cytokines in macrophages. This study inspected effects of P.
Hsiu-Hui Lin +5 more
doaj +1 more source
Structural and Computational Study of the GroEL–Prion Protein Complex
Biomedicines, 2021 The molecular chaperone GroEL is designed to promote protein folding and prevent aggregation. However, the interaction between GroEL and the prion protein, PrPC, could lead to pathogenic transformation of the latter to the aggregation-prone PrPSc form ...
Aleksandra A. Mamchur +8 more
doaj +1 more source
Porphyromonas gingivalis GroEL induces osteoclastogenesis of periodontal ligament cells and enhances alveolar bone resorption in rats. [PDF]
PLoS ONE, 2014 Porphyromonas gingivalis is a major periodontal pathogen that contains a variety of virulence factors. The antibody titer to P. gingivalis GroEL, a homologue of HSP60, is significantly higher in periodontitis patients than in healthy control subjects ...
Feng-Yen Lin +9 more
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]
, 2002 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
Borrelia burgdorferi Surface Exposed GroEL Is a Multifunctional Protein
Pathogens, 2021 The spirochete, Borrelia burgdorferi, has a large number of membrane proteins involved in a complex life cycle, that includes a tick vector and a vertebrate host.
Thomas Cafiero, Alvaro Toledo
doaj +1 more source
Cryo-EM map interpretation and protein model-building using iterative map segmentation. [PDF]
, 2020 A procedure for building protein chains into maps produced by single-particle electron cryo-microscopy (cryo-EM) is described. The procedure is similar to the way an experienced structural biologist might analyze a map, focusing first on secondary ...
Afonine PV +9 more
core +2 more sources
Ligands regulate GroEL thermostability
FEBS Letters, 1997 Escherichia coli heat‐shock proteins GroEL and GroES stimulate (in an ATP‐dependent manner) the folding of various proteins. In this study scanning microcalorimetry was applied to investigate GroEL thermostability in the presence of its ligands. Mg2+ and K+ ions stabilize while ADP destabilizes the GroEL molecule against the action of temperature ...
Surin, A.K +5 more
openaire +2 more sources