Interactions of GroEL/GroES with a heterodimeric intermediate during alpha 2beta 2 assembly of mitochondrial branched-chain alpha-ketoacid dehydrogenase. cis capping of the native-like 86-kDa intermediate by GroES (Q73675908)

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scientific article published on 01 July 2000

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English	Interactions of GroEL/GroES with a heterodimeric intermediate during alpha 2beta 2 assembly of mitochondrial branched-chain alpha-ketoacid dehydrogenase. cis capping of the native-like 86-kDa intermediate by GroES	scientific article published on 01 July 2000

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5 November 2019

Interactions of GroEL/GroES with a heterodimeric intermediate during alpha 2beta 2 assembly of mitochondrial branched-chain alpha-ketoacid dehydrogenase. cis capping of the native-like 86-kDa intermediate by GroES (English)

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Song JL

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Chuang DT

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1 July 2000

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Journal of Biological Chemistry

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22305-22312

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5 November 2019

Structure and function in GroEL-mediated protein folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002038200

21 January 2018

Molecular chaperones in cellular protein folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002038200

21 January 2018

GroEL-mediated protein folding

1 reference

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21 January 2018

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

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21 January 2018

The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002038200

21 January 2018

Pass the butter...

1 reference

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21 January 2018

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

1 reference

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21 January 2018

The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL.

1 reference

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21 January 2018

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

1 reference

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21 January 2018

On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES.

1 reference

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21 January 2018

Mechanisms for GroEL/GroES-mediated folding of a large 86-kDa fusion polypeptide in vitro

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002038200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002038200

21 January 2018

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

1 reference

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21 January 2018

Protein folding Folding with a two-stroke motor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002038200

21 January 2018

GroEL/GroES: structure and function of a two-stroke folding machine

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002038200

21 January 2018

Functional communications between the apical and equatorial domains of GroEL through the intermediate domain.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002038200

21 January 2018

GroEL recognises sequential and non-sequential linear structural motifs compatible with extended beta-strands and alpha-helices

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002038200

21 January 2018

Identification of substrate binding site of GroEL minichaperone in solution

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002038200

21 January 2018

NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002038200

21 January 2018

The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002038200

21 January 2018

GroEL-substrate interactions: molding the fold, or folding the mold?

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002038200

21 January 2018

Basis of Substrate Binding by the Chaperonin GroEL†

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002038200

21 January 2018

GroE modulates kinetic partitioning of folding intermediates between alternative states to maximize the yield of biologically active protein.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002038200

21 January 2018

Crystal structure of human branched-chain alpha-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease

1 reference

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21 January 2018

Impaired assembly of E1 decarboxylase of the branched-chain alpha-ketoacid dehydrogenase complex in type IA maple syrup urine disease

1 reference

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21 January 2018

GroEL/GroES-dependent reconstitution of alpha2 beta2 tetramers of humanmitochondrial branched chain alpha-ketoacid decarboxylase. Obligatory interaction of chaperonins with an alpha beta dimeric intermediate

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002038200

21 January 2018

GroEL/GroES promote dissociation/reassociation cycles of a heterodimeric intermediate during alpha(2)beta(2) protein assembly. Iterative annealing at the quaternary structure level

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002038200

21 January 2018

Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase

1 reference

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21 January 2018

The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

1 reference

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21 January 2018

Promotion of the in vitro renaturation of dodecameric glutamine synthetase from Escherichia coli in the presence of GroEL (chaperonin-60) and ATP.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002038200

21 January 2018

Kinetic analysis of interactions between GroEL and reduced alpha-lactalbumin. Effect of GroES and nucleotides.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002038200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002038200

21 January 2018

Chaperonins can Catalyse the Reversal of Early Aggregation Steps when a Protein Misfolds

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002038200

21 January 2018

"Half of the sites" binding of D-glyceraldehyde-3-phosphate dehydrogenase folding intermediate with GroEL

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002038200

21 January 2018

Chaperonin function: folding by forced unfolding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002038200

21 January 2018

Identification of in vivo substrates of the chaperonin GroEL

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002038200

21 January 2018

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

1 reference

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21 January 2018

Identifiers

10.1074/JBC.M002038200

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10764784%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10764784%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

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