(Q28239314)

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Residues in chaperonin GroEL required for polypeptide binding and release

scientific article (publication date: 13 October 1994)

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Residues in chaperonin GroEL required for polypeptide binding and release (English)

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A L Horwich

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W A Fenton

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Y Kashi

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K Furtak

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English

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publication date

13 October 1994

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published in

Nature

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volume

371

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issue

6498

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page(s)

614-9

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cites work

Protein folding in the cell

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7 January 2021

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Molecular chaperone functions of heat-shock proteins

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7 January 2021

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Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1

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Crossref

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7 January 2021

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

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7 January 2021

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A novel cochaperonin that modulates the ATPase activity of cytoplasmic chaperonin

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7 January 2021

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

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Crossref

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7 January 2021

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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7 January 2021

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

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Crossref

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7 January 2021

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

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https://api.crossref.org/works/10.1038%2F371614A0

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7 January 2021

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

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7 January 2021

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

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Crossref

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https://api.crossref.org/works/10.1038%2F371614A0

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7 January 2021

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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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https://api.crossref.org/works/10.1038%2F371614A0

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7 January 2021

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Characterization of a functionally important mobile domain of GroES.

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7 January 2021

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ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis.

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7 January 2021

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Cooperativity in ATP hydrolysis by GroEL is increased by GroES

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7 January 2021

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

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https://api.crossref.org/works/10.1038%2F371614A0

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7 January 2021

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Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer

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https://api.crossref.org/works/10.1038%2F371614A0

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7 January 2021

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Symmetric complexes of GroE chaperonins as part of the functional cycle

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https://api.crossref.org/works/10.1038%2F371614A0

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7 January 2021

based on heuristic

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A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1.

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7 January 2021

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