Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes. (Q54606460)

1 June 2018

title

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

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1 June 2018

9

Hartl FU

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Engel A

1

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Hayer-Hartl MK

2

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Goldie KN

3

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Pfeifer G

4

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Hegerl R

5

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Müller S

6

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da Silva AC

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Baumeister W

8

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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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1 June 2018

issue

5225

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page(s)

832-836

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

cites work

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

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Has negative staining still a place in biomacromolecular electron microscopy?

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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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Residues in chaperonin GroEL required for polypeptide binding and release

21 January 2018

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Protein folding in the cell

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https://api.crossref.org/works/10.1126%2FSCIENCE.7638600

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

21 January 2018

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https://api.crossref.org/works/10.1126%2FSCIENCE.7638600

Molecular chaperone functions of heat-shock proteins

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

21 January 2018

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https://api.crossref.org/works/10.1126%2FSCIENCE.7638600

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

21 January 2018

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https://api.crossref.org/works/10.1126%2FSCIENCE.7638600

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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https://api.crossref.org/works/10.1126%2FSCIENCE.7638600

Characterization of a functionally important mobile domain of GroES.

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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https://api.crossref.org/works/10.1126%2FSCIENCE.7638600

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

21 January 2018

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https://api.crossref.org/works/10.1126%2FSCIENCE.7638600

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

21 January 2018

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https://api.crossref.org/works/10.1126%2FSCIENCE.7638600

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

21 January 2018

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https://api.crossref.org/works/10.1126%2FSCIENCE.7638600

Unfolding protein folding

21 January 2018

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https://api.crossref.org/works/10.1126%2FSCIENCE.7638600

21 January 2018

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21 January 2018

Identifiers

DOI

10.1126/SCIENCE.7638600

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1 June 2018

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1 June 2018