Denaturation and reassembly of chaperonin GroEL studied by solution X-ray scattering (Q36571942)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12649424%20AND%20SRC:MED&resulttype=core&format=json

1 November 2019

title

Denaturation and reassembly of chaperonin GroEL studied by solution X-ray scattering (English)

1 reference

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X-ray scattering techniques

1 November 2019

main subject

1 reference

1

1 reference

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1 November 2019

Tomonao Inobe

2

1 reference

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1 November 2019

Yoshiyuki Amemiya

6

1 reference

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1 November 2019

author name string

Kosuke Maki

3

1 reference

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1 November 2019

Teikichi Ikura

4

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1 November 2019

Hiroshi Kihara

5

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1 November 2019

Kunihiro Kuwajima

7

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1 November 2019

publication date

1 April 2003

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1 November 2019

1 reference

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1 November 2019

volume

12

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1 November 2019

issue

4

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1 November 2019

page(s)

672-680

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Molecular chaperones in the cytosol: from nascent chain to folded protein

1 November 2019

cites work

1 reference

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Assembly of chaperonin complexes

30 September 2017

1 reference

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Changes in biomolecular conformation seen by small angle X-ray scattering

30 September 2017

1 reference

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Folding of newly translated proteins in vivo: the role of molecular chaperones

30 September 2017

1 reference

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Reversible denaturation of oligomeric human chaperonin 10: denatured state depends on chemical denaturant

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2323844

Excluded volume effects on the refolding and assembly of an oligomeric protein. GroEL, a case study

30 September 2017

1 reference

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Folding and association of oligomeric and multimeric proteins

30 September 2017

1 reference

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Role of the molten globule state in protein folding.

30 September 2017

1 reference

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Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10.

30 September 2017

1 reference

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The Hsp70 and Hsp60 chaperone machines

30 September 2017

1 reference

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

30 September 2017

1 reference

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MOLMOL: a program for display and analysis of macromolecular structures

30 September 2017

1 reference

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

30 September 2017

1 reference

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Molten globule of cytochrome c studied by small angle X-ray scattering.

30 September 2017

1 reference

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Residues in chaperonin GroEL required for polypeptide binding and release

30 September 2017

1 reference

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

30 September 2017

1 reference

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30 September 2017

1 reference

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Determination and analysis of urea and guanidine hydrochloride denaturation curves

30 September 2017

1 reference

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The mitochondrial chaperonin hsp60 is required for its own assembly

30 September 2017

1 reference

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GroEL-mediated protein folding

30 September 2017

1 reference

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X-ray solution scattering studies of protein folding

30 September 2017

1 reference

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Synchronized domain-opening motion of GroEL is essential for communication between the two rings.

30 September 2017

1 reference

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(Mg-ATP)-dependent self-assembly of molecular chaperone GroEL.

28 June 2018

1 reference

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In vivoanalysis of integration of membrane proteins inEscherichia coli

28 June 2018

1 reference

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Equilibrium and kinetics of the allosteric transition of GroEL studied by solution X-ray scattering and fluorescence spectroscopy

28 June 2018

1 reference

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Nucleotide binding to the chaperonin GroEL: non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATP.

21 September 2018

1 reference

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Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.

21 September 2018

1 reference

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GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism.

21 September 2018

1 reference

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

21 September 2018

1 reference

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Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering.

21 September 2018

1 reference

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Stabilization of a compact conformation of monomeric GroEL at low temperature by adenine nucleotides.

21 September 2018

1 reference

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Solution X-ray scattering study on the chaperonin GroEL from Escherichia coli.

21 September 2018

1 reference

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Residual Structure in Urea-Denatured Chaperonin GroEL

21 September 2018

1 reference

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Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent

21 September 2018

1 reference

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Fast compaction of alpha-lactalbumin during folding studied by stopped-flow X-ray scattering

21 September 2018

1 reference

https://pubmed.ncbi.nlm.nih.gov/12649424

12 December 2020

Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering

1 reference

https://pubmed.ncbi.nlm.nih.gov/12649424

12 December 2020

Refolding and Reassembly of Active Chaperonin GroEL After Denaturation

1 reference

https://pubmed.ncbi.nlm.nih.gov/12649424

12 December 2020

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/12649424

12 December 2020

Reversible oligomerization and denaturation of the chaperonin GroES

1 reference

https://pubmed.ncbi.nlm.nih.gov/12649424

12 December 2020

Protein globularization during folding. A study by synchrotron small-angle X-ray scattering

1 reference

https://pubmed.ncbi.nlm.nih.gov/12649424

12 December 2020

Dominant forces in the recognition of a transient folding intermediate of alpha-lactalbumin by GroEL

1 reference

https://pubmed.ncbi.nlm.nih.gov/12649424

12 December 2020

The structural stability of the co-chaperonin GroES

1 reference

https://pubmed.ncbi.nlm.nih.gov/12649424

12 December 2020

Kinetic refolding of beta-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy

1 reference

https://pubmed.ncbi.nlm.nih.gov/12649424

12 December 2020

Structural Changes of theEscherichia coliGroEL–GroES Chaperonins upon Complex Formation in Solution: A Neutron Small Angle Scattering Study

1 reference

https://pubmed.ncbi.nlm.nih.gov/12649424

12 December 2020

Structure and function in GroEL-mediated protein folding

1 reference

https://pubmed.ncbi.nlm.nih.gov/12649424

12 December 2020

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/12649424

12 December 2020

Thermodynamics of nucleotide binding to the chaperonin GroEL studied by isothermal titration calorimetry: evidence for noncooperative nucleotide binding

1 reference

https://pubmed.ncbi.nlm.nih.gov/12649424

12 December 2020

Unfolding and refolding of Escherichia coli chaperonin GroES is expressed by a three-state model

1 reference

https://pubmed.ncbi.nlm.nih.gov/12649424

12 December 2020

Chaperonin-affected refolding of alpha-lactalbumin: effects of nucleotides and the co-chaperonin GroES

1 reference

https://pubmed.ncbi.nlm.nih.gov/12649424

12 December 2020

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/12649424

12 December 2020

Identification of in vivo substrates of the chaperonin GroEL

1 reference

https://pubmed.ncbi.nlm.nih.gov/12649424

12 December 2020

The unfolding and attempted refolding of the bacterial chaperone protein groEL (cpn60)

1 reference

https://pubmed.ncbi.nlm.nih.gov/12649424

12 December 2020

In vitro dissociation of self-assembly of three chaperonin 60s: the role of ATP

1 reference

https://pubmed.ncbi.nlm.nih.gov/12649424

12 December 2020

Tetradecameric chaperonin 60 can be assembled in vitro from monomers in a process that is ATP independent

1 reference

https://pubmed.ncbi.nlm.nih.gov/12649424

12 December 2020

Identifiers

DOI

10.1110/PS.0233603

1 reference

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1 November 2019

1 reference

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1 November 2019

PubMed publication ID

12649424

1 reference

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