The stability and hydrophobicity of cytosolic and mitochondrial malate dehydrogenases and their relation to chaperonin-assisted folding. (Q54633348)

1 June 2018

title

The stability and hydrophobicity of cytosolic and mitochondrial malate dehydrogenases and their relation to chaperonin-assisted folding. (English)

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1 June 2018

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R A Staniforth

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1 June 2018

A Cortés

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1 June 2018

S G Burston

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1 June 2018

T Atkinson

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J J Holbrook

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A R Clarke

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1 June 2018

language of work or name

English

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publication date

1 May 1994

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1 June 2018

published in

FEBS Letters

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volume

344

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issue

2-3

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1 June 2018

page(s)

129-135

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1 June 2018

Binding of a chaperonin to the folding intermediates of lactate dehydrogenase

cites work

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

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

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Structure of holo-chaperonin studied with electron microscopy. Oligomeric cpn10 on top of two layers of cpn60 rings with two stripes each

21 January 2018

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

21 January 2018

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

21 January 2018

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The influence of chaperonins on protein folding. A mechanism for increasing the yield of the native form

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

21 January 2018

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Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-A resolution

21 January 2018

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Kinetic studies of the regulation of mitochondrial malate dehydrogenase by citrate

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The energetics and cooperativity of protein folding: a simple experimental analysis based upon the solvation of internal residues.

21 January 2018

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

21 January 2018

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Folding and association of proteins

21 January 2018

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

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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The folding of hen lysozyme involves partially structured intermediates and multiple pathways

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GroE facilitates refolding of citrate synthase by suppressing aggregation

21 January 2018

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Refolding of barnase in the presence of GroE

21 January 2018

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Comparison of the molecular structures of cytoplasmic and mitochondrial malate dehydrogenase

21 January 2018

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A DNA fragment containing the groE genes can suppress mutations in the Escherichia coli dnaA gene

21 January 2018

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Quaternary structure, subunit activity, and in vitro association of porcine mitochondrial malic dehydrogenase

21 January 2018

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Reassociation of dimeric cytoplasmic malate dehydrogenase is determined by slow and very slow folding reactions

21 January 2018

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The barriers in protein folding

21 January 2018

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10.1016/0014-5793(94)00348-3

21 January 2018

Identifiers

DOI

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1 June 2018

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1 June 2018