(Q54631587)

1 June 2018

title

The chaperonin GroEL does not recognize apo-alpha-lactalbumin in the molten globule state. (English)

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1 June 2018

author name string

Okazaki A

1

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1 June 2018

Ikura T

2

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1 June 2018

Nikaido K

3

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1 June 2018

Kuwajima K

4

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1 June 2018

publication date

1 July 1994

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1 June 2018

Nature structural biology

published in

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1 June 2018

volume

1

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1 June 2018

page(s)

439-446

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1 June 2018

issue

7

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1 June 2018

Protein folding in the cell

cites work

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https://api.crossref.org/works/10.1038%2FNSB0794-439

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

21 January 2018

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Comparative fluorescence properties of bovine, goat, human and guinea pig alpha lactalbumin. Characterization of the environments of individual tryptophan residues in partially folded conformers

21 January 2018

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Homologous plant and bacterial proteins chaperone oligomeric protein assembly

21 January 2018

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https://api.crossref.org/works/10.1038%2FNSB0794-439

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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21 January 2018

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The aromatic amino acid content of the bacterial chaperone protein groEL (cpn60) Evidence for the presence of a single tryptophan

21 January 2018

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https://api.crossref.org/works/10.1038%2FNSB0794-439

Principles that govern the folding of protein chains

21 January 2018

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Protein folding: local structures, domains, subunits, and assemblies

31 March 2020

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Chaperonins and protein folding: unity and disunity of mechanisms

31 March 2020

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https://api.crossref.org/works/10.1038%2FNSB0794-439

The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure.

31 March 2020

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https://api.crossref.org/works/10.1038%2FNSB0794-439

alpha-Lactalbumin: a calcium metalloprotein

31 March 2020

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Absence of the thermal transition in apo-alpha-lactalbumin in the molten globule state. A study by differential scanning microcalorimetry

31 March 2020

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

31 March 2020

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

31 March 2020

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Refolding of barnase in the presence of GroE

31 March 2020

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Binding of a chaperonin to the folding intermediates of lactate dehydrogenase

31 March 2020

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Conformational states of ribulosebisphosphate carboxylase and their interaction with chaperonin 60.

31 March 2020

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GroE facilitates refolding of citrate synthase by suppressing aggregation

31 March 2020

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Renaturation of citrate synthase: influence of denaturant and folding assistants

31 March 2020

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Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase

31 March 2020

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

31 March 2020

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Primary structure of chicken liver dihydrofolate reductase

31 March 2020

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In vivoanalysis of integration of membrane proteins inEscherichia coli

31 March 2020

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

31 March 2020

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The role of alpha-lactalbumin and the A protein in lactose synthetase: a unique mechanism for the control of a biological reaction

31 March 2020

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A simple filtration assay for measuring hydrogen exchange kinetics of proteins: application to peptide and ligand binding reactions

31 March 2020

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https://api.crossref.org/works/10.1038%2FNSB0794-439

31 March 2020

Identifiers

DOI

10.1038/NSB0794-439

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1 June 2018

PubMed ID

7664062

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1 June 2018