(Q47693862)

4 February 2018

title

A single ring is sufficient for productive chaperonin-mediated folding in vivo. (English)

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4 February 2018

author name string

Nielsen KL

series ordinal

1

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4 February 2018

Cowan NJ

series ordinal

2

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4 February 2018

publication date

1 July 1998

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4 February 2018

published in

Molecular Cell

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4 February 2018

volume

2

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4 February 2018

issue

1

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4 February 2018

page(s)

93-99

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4 February 2018

Formation of the LuxR protein in the Vibrio fischeri lux system is controlled by HtpR through the GroESL proteins

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Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.

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DMA mutagenesis and recombination

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Protein folding Folding with a two-stroke motor

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Escherichia coli chaperonins cpn60 (groEL) and cpn10 (groES) do not catalyse the refolding of mitochondrial malate dehydrogenase

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

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Use of T7 RNA polymerase to direct expression of cloned genes

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

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The Single-Ring Thermoanaerobacter brockii Chaperonin 60 (Tbr-EL7) Dimerizes to Tbr-EL14.cntdot.Tbr-ES7 under Protein Folding Conditions

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7 January 2021

Nucleotide sequences and novel structural features of human and Chinese hamster hsp60 (chaperonin) gene families

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Purification of mammalian mitochondrial chaperonin 60 through in vitro reconstitution of active oligomers

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7 January 2021

Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES.

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7 January 2021

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

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7 January 2021

The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex

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7 January 2021

10.1016/S1097-2765(00)80117-3

Identifiers

DOI

1 reference

4 February 2018

PubMed ID

9702195

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4 February 2018