Results 21 to 30 of about 18,538 (219)
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
A structural model for the GroEL chaperonin [PDF]
FEMS Microbiology Letters, 1993 Individual particle analysis of end views from negatively stained specimens of purified GroEL from Escherichia coli showed the presence of two different particle populations, those with a six-fold symmetry and those with a seven-fold symmetry, when studied at pH 7.7 and 5.0.
S, Marco +5 more
openaire +2 more sources
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
Putting handcuffs on the chaperonin GroEL [PDF]
Proceedings of the National Academy of Sciences, 2013 Oligomeric, ring-shaped nano-machines that are fueled by ATP are ubiquitous in all three kingdoms of life and are involved in a wide range of processes that include, for example, protein folding, protein degradation, DNA and RNA remodeling, and protein insertion into membranes (for review, see ref. 1).
openaire +2 more sources
ATP‐Responsive Nanoparticles Covered with Biomolecular Machine “Chaperonin GroEL”
, 2023 Herein, we report an ATP-responsive nanoparticle ((NP)-N-GroEL) whose surface is fully covered with the biomolecular machine "chaperonin protein GroEL".
Kikkawa, M +21 more
core +1 more source
Structural biology of GroEL assisted protein folding [PDF]
, 2014 GroEL/ES is the classical example of molecular chaperone that assists the re-folding of many misfolded proteins (SP). Recent kinetic analyses revealed a new paradigm of how GroEL/ES uses ATP to assist protein folding.
Fei, Xue
core +1 more source
BMC Evolutionary Biology, 2007 Background Heat-shock proteins are specialized molecules performing different and essential roles in the cell including protein degradation, folding and trafficking.
Fares Mario A, McNally David
doaj +1 more source
Chaperonin GroEL Reassembly: An Effect of Protein Ligands and Solvent Composition
Biomolecules, 2014 Chaperonin GroEL is a complex oligomeric heat shock protein (Hsp60) assisting the correct folding and assembly of other proteins in the cell. An intriguing question is how GroEL folds itself.
Nataliya Ryabova +3 more
doaj +1 more source
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 +6 more
doaj +1 more source
Design and analytical validation of a duplex PCR for Ehrlichia and Rickettsia detection in ticks
Revista Colombiana de Ciencias Pecuarias, 2018 Background: Ehrlichia and Rickettsia are two major rickettsial genera transmitted by ticks that affect a number of wild and domestic animal species and human populations around the world.
Juan C. Pérez Pérez +4 more
doaj +1 more source