(Q52511899)

2 May 2018

title

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

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2 May 2018

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5

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2 May 2018

Kurt Wüthrich

4

object named as

Wüthrich K

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2 May 2018

author name string

Zahn R

1

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2 May 2018

Spitzfaden C

2

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2 May 2018

Ottiger M

3

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2 May 2018

language of work or name

English

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publication date

1 March 1994

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2 May 2018

published in

Nature

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2 May 2018

volume

368

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2 May 2018

issue

6468

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2 May 2018

page(s)

261-265

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2 May 2018

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7 January 2021

Protein folding in the cell

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7 January 2021

Purification and properties of groE, a host protein involved in bacteriophage assembly

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7 January 2021

Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly

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7 January 2021

Homologous plant and bacterial proteins chaperone oligomeric protein assembly

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7 January 2021

Cooperativity in ATP hydrolysis by GroEL is increased by GroES

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7 January 2021

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

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7 January 2021

Two-dimensional crystals of the molecular chaperone GroEL reveal structural plasticity.

1 reference

7 January 2021

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

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7 January 2021

Binding of a chaperonin to the folding intermediates of lactate dehydrogenase

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7 January 2021

GroE facilitates refolding of citrate synthase by suppressing aggregation

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7 January 2021

Reconstitution of a heat shock effect in vitro: influence of GroE on the thermal aggregation of .alpha.-glucosidase from yeast

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7 January 2021

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

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7 January 2021

Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase

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7 January 2021

GroE prevents the accumulation of early folding intermediates of pre-beta-lactamase without changing the folding pathway.

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7 January 2021

Cyclophilin: a specific cytosolic binding protein for cyclosporin A

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7 January 2021

Chemistry and Biology of the Immunophilins and Their Immunosuppressive Ligands

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7 January 2021

Protein secondary structure determination by NMR. Application with recombinant human cyclophilin.

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7 January 2021

The chaperonin GroEL binds a polypeptide in an .alpha.-helical conformation

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7 January 2021

Different conformations for the same polypeptide bound to chaperones DnaK and GroEL.

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7 January 2021

Structure and stability of the molten globule state of guinea-pig alpha-lactalbumin: a hydrogen exchange study

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7 January 2021

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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7 January 2021

The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution

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7 January 2021

Measuring and increasing protein stability

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7 January 2021

Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity

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9 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1038/368261A0

Identifiers

DOI

10.1038/368261A0

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2 May 2018

Dimensions Publication ID

1029518150

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2 May 2018