Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding. (Q54606454)

1 June 2018

title

Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding. (English)

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1 June 2018

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3

Hartl FU

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1 June 2018

Hayer-Hartl MK

1

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1 June 2018

Martin J

series ordinal

2

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1 June 2018

language of work or name

English

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publication date

1 August 1995

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1 June 2018

published in

Science

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1 June 2018

volume

269

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issue

5225

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1 June 2018

page(s)

836-841

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1 June 2018

Effect of divalent cations on the molecular structure of the GroEL oligomer.

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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A polypeptide bound by the chaperonin groEL is localized within a central cavity

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

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

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Proteins as molecular chaperones.

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Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes.

21 January 2018

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

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Protein folding. Secrets of a double-doughnut.

21 January 2018

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Homologous plant and bacterial proteins chaperone oligomeric protein assembly

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Molecular chaperone functions of heat-shock proteins

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

21 January 2018

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The formation of symmetrical GroEL-GroES complexes in the presence of ATP.

21 January 2018

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

21 January 2018

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The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.

21 January 2018

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Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES.

21 January 2018

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Determination of rate and equilibrium binding constants for macromolecular interactions using surface plasmon resonance: use of nonlinear least squares analysis methods.

21 January 2018

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Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis

21 January 2018

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Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry.

21 January 2018

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ATP induces large quaternary rearrangements in a cage-like chaperonin structure.

21 January 2018

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Assembly and function of a quaternary signal transduction complex monitored by surface plasmon resonance

21 January 2018

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Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion.

21 January 2018

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

21 January 2018

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Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. II. GroEL recognizes thermally unfolded mature beta-lactamase.

21 January 2018

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Destabilization of the complete protein secondary structure on binding to the chaperone GroEL.

21 January 2018

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Biospecific interaction analysis using surface plasmon resonance detection applied to kinetic, binding site and concentration analysis

21 January 2018

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21 January 2018

Identifiers

DOI

10.1126/SCIENCE.7638601

1 reference

1 June 2018

PubMed ID

7638601

1 reference

1 June 2018