(Q27742747)

7 January 2021

GroEL-mediated protein folding

1 reference

7 January 2021

Principles that govern the folding of protein chains

1 reference

7 January 2021

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

1 reference

7 January 2021

GroE facilitates refolding of citrate synthase by suppressing aggregation

1 reference

7 January 2021

Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

1 reference

7 January 2021

Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria

1 reference

7 January 2021

The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures

1 reference

7 January 2021

Folding in vivo of bacterial cytoplasmic proteins: role of GroEL.

1 reference

7 January 2021

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

7 January 2021

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

7 January 2021

Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding

1 reference

7 January 2021

The hydrophobic nature of GroEL-substrate binding

1 reference

7 January 2021

Nature and consequences of GroEL-protein interactions.

1 reference

7 January 2021

GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms

1 reference

7 January 2021

Chaperonins can Catalyse the Reversal of Early Aggregation Steps when a Protein Misfolds

1 reference

7 January 2021

Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB

1 reference

7 January 2021

A thermodynamic coupling mechanism for GroEL-mediated unfolding

1 reference

7 January 2021

Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes

1 reference

7 January 2021

Protein folding in the central cavity of the GroEL-GroES chaperonin complex

1 reference

7 January 2021

Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction

1 reference

7 January 2021

The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL.

1 reference

7 January 2021

Allosteric control by ATP of non-folded protein binding to GroEL

1 reference

7 January 2021

Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL.

1 reference

7 January 2021

The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S

1 reference

7 January 2021

Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.

1 reference

7 January 2021

Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding

1 reference

7 January 2021

Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism

1 reference

7 January 2021

Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction

1 reference

7 January 2021

Chaperonin releases the substrate protein in a form with tendency to aggregate and ability to rebind to chaperonin

1 reference

7 January 2021

Interactions between the GroE chaperonins and rhodanese. Multiple intermediates and release and rebinding

1 reference

7 January 2021

Release of both native and non-native proteins from a cis-only GroEL ternary complex

1 reference

7 January 2021

Binding of chaperonins.

1 reference

7 January 2021

Structure of holo-chaperonin studied with electron microscopy. Oligomeric cpn10 on top of two layers of cpn60 rings with two stripes each

1 reference

7 January 2021

Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.

1 reference

7 January 2021

The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

1 reference

7 January 2021

A structural model for GroEL-polypeptide recognition

1 reference

7 January 2021

Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL.

1 reference

7 January 2021

Characterization of a functionally important mobile domain of GroES.

1 reference

7 January 2021

Interplay of structure and disorder in cochaperonin mobile loops

1 reference

7 January 2021

Two classes of extragenic suppressor mutations identify functionally distinct regions of the GroEL chaperone of Escherichia coli

1 reference

7 January 2021

GroEL locked in a closed conformation by an interdomain cross-link can bind ATP and polypeptide but cannot process further reaction steps

1 reference

7 January 2021

Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering.

1 reference

7 January 2021

Structural determinants for activation of the alpha-subunit of a heterotrimeric G protein

1 reference

7 January 2021

Processing of X-ray diffraction data collected in oscillation mode

1 reference

7 January 2021

Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution

1 reference

7 January 2021

Improved methods for building protein models in electron density maps and the location of errors in these models

1 reference

7 January 2021

Torsion angle dynamics: reduced variable conformational sampling enhances crystallographic structure refinement

1 reference

7 January 2021

Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement

1 reference

7 January 2021

Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

1 reference

7 January 2021