(Q44578016)

4 December 2017

title

Isolation and characterisation of mutants of GroEL that are fully functional as single rings (English)

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4 December 2017

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4 December 2017

3

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4 December 2017

Zhe Sun

1

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4 December 2017

language of work or name

English

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publication date

1 September 2003

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Journal of Molecular Biology

4 December 2017

published in

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4 December 2017

volume

332

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4 December 2017

issue

3

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4 December 2017

page(s)

715-728

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The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures

4 December 2017

cites work

1 reference

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7 January 2021

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

7 January 2021

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Binding of a chaperonin to the folding intermediates of lactate dehydrogenase

7 January 2021

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GroE facilitates refolding of citrate synthase by suppressing aggregation

7 January 2021

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Substoichiometric amounts of the molecular chaperones GroEL and GroES prevent thermal denaturation and aggregation of mammalian mitochondrial malate dehydrogenase in vitro

7 January 2021

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

7 January 2021

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

7 January 2021

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

7 January 2021

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Protein folding in the central cavity of the GroEL-GroES chaperonin complex

7 January 2021

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Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes

7 January 2021

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Molecular chaperones. Opening and closing the Anfinsen cage.

7 January 2021

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Molecular chaperones in protein folding: the art of avoiding sticky situations

7 January 2021

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Dual Function of Protein Confinement in Chaperonin-Assisted Protein Folding

7 January 2021

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Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism

7 January 2021

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Chaperonin function: folding by forced unfolding

7 January 2021

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Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.

7 January 2021

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

7 January 2021

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

7 January 2021

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Structure and function in GroEL-mediated protein folding

7 January 2021

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GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings

7 January 2021

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The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding

7 January 2021

1 reference

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A single ring is sufficient for productive chaperonin-mediated folding in vivo

7 January 2021

1 reference

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From minichaperone to GroEL 3: properties of an active single-ring mutant of GroEL.

7 January 2021

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

7 January 2021

1 reference

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The effect of nucleotides and mitochondrial chaperonin 10 on the structure and chaperone activity of mitochondrial chaperonin 60.

7 January 2021

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GroE is vital for cell-wall synthesis

7 January 2021

1 reference

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Deletion of Escherichia coli groEL is complemented by a Rhizobium leguminosarum groEL homologue at 37 degrees C but not at 43 degrees C.

7 January 2021

1 reference

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Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL.

7 January 2021

1 reference

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900830-1

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900830-1

Chaperone Activity of a Chimeric GroEL Protein That Can Exist in a Single or Double Ring Form

7 January 2021

1 reference

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GroES promotes the T to R transition of the GroEL ring distal to GroES in the GroEL-GroES complex.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900830-1

The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S

7 January 2021

1 reference

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A carboxy-terminal deletion impairs the assembly of GroEL and confers a pleiotropic phenotype in Escherichia coli K-12.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900830-1

The tail of a chaperonin: the C-terminal region of Escherichia coli GroEL protein

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900830-1

Residues in chaperonin GroEL required for polypeptide binding and release

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900830-1

Effects of reduced levels of GroE chaperones on protein metabolism: enhanced synthesis of heat shock proteins during steady-state growth of Escherichia coli

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900830-1

GroEL/GroES-mediated folding of a protein too large to be encapsulated

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900830-1

Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900830-1

Criteria for assessing the purity and quality of GroEL

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900830-1

Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900830-1

A single-ring mitochondrial chaperonin (Hsp60-Hsp10) can substitute for GroEL-GroES in vivo.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900830-1

inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1016/S0022-2836(03)00830-1

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4 December 2017

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