Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space [PDF]
, 1992 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
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Applying forces to elastic network models of large biomolecules using a haptic feedback device [PDF]
, 2011 Elastic network models of biomolecules have proved to be relatively good at predicting global conformational changes particularly in large systems. Software that facilitates rapid and intuitive exploration of conformational change in elastic network ...
Hayward, Steven +2 more
core +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
A proteomic investigation of Fusobacterium nucleatum alkaline-induced biofilms [PDF]
, 2012 Background: The Gram negative anaerobe Fusobacterium nucleatum has been implicated in the aetiology of periodontal diseases. Although frequently isolated from healthy dental plaque, its numbers and proportion increase in plaque associated with disease ...
Chew, J., Fuss, J., Gully, N., Zilm, P.
core +3 more sources
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
openaire +2 more sources
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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Probing the functional mechanism of Escherichia coli GroEL using circular permutation. [PDF]
PLoS ONE, 2011 BACKGROUND: The Escherichia coli chaperonin GroEL subunit consists of three domains linked via two hinge regions, and each domain is responsible for a specific role in the functional mechanism.
Tomohiro Mizobata +5 more
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Molecules, 2023 The incorporation of photoproteins into proteins of interest allows the study of either their localization or intermolecular interactions in the cell.
Victor Marchenkov +8 more
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Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria [PDF]
, 1989 A nuclear encoded mitochondrial heat-shock protein hsp60 is required for the assembly into oligomeric complexes of proteins imported into the mitochondrial matrix.
Cheng, Ming Yuan +8 more
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