Chaperonin releases the substrate protein in a form with tendency to aggregate and ability to rebind to chaperonin (Q72572687)

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27 October 2019

title

Chaperonin releases the substrate protein in a form with tendency to aggregate and ability to rebind to chaperonin (English)

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27 October 2019

author name string

Taguchi H

series ordinal

1

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27 October 2019

Yoshida M

series ordinal

2

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27 October 2019

publication date

1 February 1995

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27 October 2019

language of work or name

0 references

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27 October 2019

volume

359

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27 October 2019

issue

2-3

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27 October 2019

page(s)

195-198

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Homologous plant and bacterial proteins chaperone oligomeric protein assembly

27 October 2019

cites work

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Protein folding in the cell

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Role of the major heat shock proteins as molecular chaperones

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

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

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

21 January 2018

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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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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

21 January 2018

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Truncated GroEL monomer has the ability to promote folding of rhodanese without GroES and ATP.

21 January 2018

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Molecular chaperone functions of heat-shock proteins

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Polypeptide interactions with molecular chaperones and their relationship to in vivo protein folding.

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GroE facilitates refolding of citrate synthase by suppressing aggregation

21 January 2018

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A chaperonin from a thermophilic bacterium, Thermus thermophilus

21 January 2018

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Theory of chaperonin action: inertial model for enhancement of prokaryotic Rubisco assembly

21 January 2018

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

21 January 2018

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The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding

21 January 2018

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To fold or not to fold....

21 January 2018

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

21 January 2018

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

21 January 2018

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Sulfhydryl modification of E. coli Cpn60 leads to loss of its ability to support refolding of rhodanese but not to form a binary complex

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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Renaturation of citrate synthase: influence of denaturant and folding assistants

21 January 2018

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Residues in chaperonin GroEL required for polypeptide binding and release

21 January 2018

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A novel cochaperonin that modulates the ATPase activity of cytoplasmic chaperonin

21 January 2018

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10.1016/0014-5793(95)00041-7

21 January 2018

Identifiers

DOI

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27 October 2019

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