Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Combined Automated Annotation using Multiple IEA Methods
GroES in the asymmetric GroEL14-GroES7 complex exchanges via an associative mechanism.
ATP-bound states of GroEL captured by cryo-electron microscopy.
Identification and characterization of the Escherichia coli stress protein UP12, a putative in vivo substrate of GroEL.
Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics.
Exploring the structural dynamics of the E.coli chaperonin GroEL using translation-libration-screw crystallographic refinement of intermediate states.
Interaction network containing conserved and essential protein complexes in Escherichia coli.
Leu309 plays a critical role in the encapsulation of substrate protein into the internal cavity of GroEL.
Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes.
Large-scale identification of protein-protein interaction of Escherichia coli K-12.
A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis.
Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational changes of GroEL.
Proton-proton Overhauser NMR spectroscopy with polypeptide chains in large structures.
An expanded conformation of single-ring GroEL-GroES complex encapsulates an 86 kDa substrate.
Analysis of sigma32 mutants defective in chaperone-mediated feedback control reveals unexpected complexity of the heat shock response.
Protein abundance profiling of the Escherichia coli cytosol.
De novo backbone trace of GroEL from single particle electron cryomicroscopy.
Monitoring protein conformation along the pathway of chaperonin-assisted folding.
Essential role of the chaperonin folding compartment in vivo.
GroEL as a molecular scaffold for structural analysis of the anthrax toxin pore.
Out-of-equilibrium conformational cycling of GroEL under saturating ATP concentrations.
Polypeptide in the chaperonin cage partly protrudes out and then folds inside or escapes outside.
Fibrillogenic propensity of the GroEL apical domain: a Janus-faced minichaperone.
Visualizing GroEL/ES in the act of encapsulating a folding protein.
The binary protein-protein interaction landscape of Escherichia coli.
Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli.
GroEL to DnaK chaperone network behind the stability modulation of σ(32) at physiological temperature in Escherichia coli.
Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database.
Purification and properties of groE, a host protein involved in bacteriophage assembly.
Identification of a second Escherichia coli groE gene whose product is necessary for bacteriophage morphogenesis.
The crystal structure of the bacterial chaperonin GroEL at 2.8 A.
Residues in chaperonin GroEL required for polypeptide binding and release.
A polypeptide bound by the chaperonin groEL is localized within a central cavity.
Characterization of twenty-six new heat shock genes of Escherichia coli.
The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S.
The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer.
The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex.
Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL.
Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system.
Deep research synthesis for Escherichia coli GroEL
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Corroborating synthesis of GroEL architecture, ATP-dependent folding, cytosolic localization, and current client-repertoire literature.
"GroEL is the archetypal bacterial **chaperonin**"
Unfolded protein binding annotation review project