(Q63363490)

English

Intrinsic Fluorescence Studies of the Chaperonin GroEL Containing Single Tyr → Trp Replacements Reveal Ligand-induced Conformational Changes

scientific article published on 01 December 1996

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scholarly article

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21 October 2019

Intrinsic fluorescence studies of the chaperonin GroEL containing single Tyr --> Trp replacements reveal ligand-induced conformational changes (English)

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21 October 2019

4

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21 October 2019

author name string

D L Gibbons

1

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21 October 2019

J D Hixson

2

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21 October 2019

N Hay

3

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21 October 2019

B M Gorovits

5

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21 October 2019

J Ybarra

6

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21 October 2019

P M Horowitz

7

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21 October 2019

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publication date

1 December 1996

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21 October 2019

number of pages

7

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inferred from page(s)

Journal of Biological Chemistry

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21 October 2019

271

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21 October 2019

50

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21 October 2019

31989-31995

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21 October 2019

Protein folding in the cell

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

Homologous plant and bacterial proteins chaperone oligomeric protein assembly

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

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.271.50.31989

21 January 2018

Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

The hydrophobic nature of GroEL-substrate binding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

Photoincorporation of 4,4'-bis(1-anilino-8-naphthalenesulfonic acid) into the apical domain of GroEL: specific information from a nonspecific probe

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

Ligand-induced conformational changes in the apical domain of the chaperonin GroEL

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

Neurodegeneration: great minds think alike

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

Efficient oligonucleotide-directed construction of mutations in expression vectors by the gapped duplex DNA method using alternating selectable markers.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

Inactive GroEL monomers can be isolated and reassembled to functional tetradecamers that contain few bound peptides

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

The guanidine-induced conformational changes of the chaperonin GroEL from Escherichia coli. Evidence for the existence of an unfolding intermediate state.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

Refolding and reassembly of active chaperonin GroEL after denaturation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

The chaperonin GroEL is destabilized by binding of ADP

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

A physical characterization of sulfane sulfurtransferase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

Effect of divalent cations on the molecular structure of the GroEL oligomer.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

Refolding of barnase in the presence of GroE

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

Allosteric control by ATP of non-folded protein binding to GroEL

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.50.31989

21 January 2018

Identifiers

10.1074/JBC.271.50.31989

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8943246%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8943246%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

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