Results 31 to 40 of about 19,683 (209)
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
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Symmetric GroEL‐GroES complexes can contain substrate simultaneously in both GroEL rings [PDF]
FEBS Letters, 1997 © 1997 Federation of European Biochemical Societies.
Llorca, Oscar +3 more
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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
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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
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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).
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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
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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
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Proteome-Wide Analyis of Chaperonin-Dependent Protein Folding in Escherichia coli [PDF]
, 2006 In Escherichia coli, the cylindrical chaperonin GroEL and its cofactor GroES promote the folding of a fraction of newly synthesized polypeptide chains by acting as an Anfinsen cage.
Maier, Tobias
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A structural model for GroEL–polypeptide recognition [PDF]
Proceedings of the National Academy of Sciences, 1997 A monomeric peptide fragment of GroEL, consisting of residues 191–376, is a mini-chaperone with a functional chaperoning activity. We have solved the crystal structure at 1.7 Å resolution of GroEL(191–376) with a 17-residue N-terminal tag. The N-terminal tag of one molecule binds in the active site of a neighboring molecule in the crystal. This appears
A M, Buckle, R, Zahn, A R, Fersht
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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
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