(Q43559868)

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Protein compactness measured by fluorescence resonance energy transfer. Human carbonic anhydrase ii is considerably expanded by the interaction of GroEL.

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scholarly article

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Europe PubMed Central

24 November 2017

Protein compactness measured by fluorescence resonance energy transfer. Human carbonic anhydrase ii is considerably expanded by the interaction of GroEL. (English)

1 reference

Europe PubMed Central

24 November 2017

author name string

Hammarstrom P

1

1 reference

Europe PubMed Central

24 November 2017

Persson M

2

1 reference

Europe PubMed Central

24 November 2017

Carlsson U

3

1 reference

Europe PubMed Central

24 November 2017

language of work or name

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publication date

26 February 2001

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Europe PubMed Central

24 November 2017

Journal of Biological Chemistry

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Europe PubMed Central

24 November 2017

276

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Europe PubMed Central

24 November 2017

24

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Europe PubMed Central

24 November 2017

21765-21775

1 reference

Europe PubMed Central

24 November 2017

Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

Protein folding in the cell

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

Heat-shock proteins as molecular chaperones

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

Dynamics of the GroEL-protein complex: effects of nucleotides and folding mutants.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

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.M010858200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

A structural model for GroEL-polypeptide recognition

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

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.M010858200

21 January 2018

GroEL binds to and unfolds rhodanese posttranslationally

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

Refined structure of human carbonic anhydrase II at 2.0 A resolution

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

Folding of beta-sheet proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

Mapping the folding intermediate of human carbonic anhydrase II. Probing substructure by chemical reactivity and spin and fluorescence labeling of engineered cysteine residues

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

Homologous plant and bacterial proteins chaperone oligomeric protein assembly

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

Lack of correspondence between the room-temperature phosphorescence decay-components and Trp residues in a series of Trp-->Cys or Trp-->Phe mutants of human carbonic anhydrase II.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

3 The preparation of guanidine hydrochloride

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

17 The use of singlet-singlet energy transfer to study macromolecular assemblies

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

Is the unfolded state the Rosetta Stone of the protein folding problem?

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

Denatured states of proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

Refolding of barnase in the presence of GroE

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

GroEL/ES-mediated refolding of human carbonic anhydrase II: role of N-terminal helices as recognition motifs for GroEL

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

Refolding and reassociation of glycerol dehydrogenase from Bacillus stearothermophilus in the absence and presence of GroEL

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

Conformational states bound by the molecular chaperones GroEL and secB: a hidden unfolding (annealing) activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

EPR mapping of interactions between spin-labeled variants of human carbonic anhydrase II and GroEL: evidence for increased flexibility of the hydrophobic core by the interaction

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

Protein substrate binding induces conformational changes in the chaperonin GroEL. A suggested mechanism for unfoldase activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

GroEL reversibly binds to, and causes rapid inactivation of, human carbonic anhydrase II at high temperatures

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

Structural mapping of an aggregation nucleation site in a molten globule intermediate

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

Characterization of folding intermediates of human carbonic anhydrase II: probing substructure by chemical labeling of SH groups introduced by site-directed mutagenesis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

Contribution of individual tryptophan residues to the fluorescence spectrum of native and denatured forms of human carbonic anhydrase II

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

Pyrene excimer fluorescence as a proximity probe for investigation of residual structure in the unfolded state of human carbonic anhydrase II

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

Determination of protein secondary structure and solvent accessibility using site-directed fluorescence labeling. Studies of T4 lysozyme using the fluorescent probe monobromobimane

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010858200

21 January 2018

Identifiers

10.1074/JBC.M010858200

1 reference

Europe PubMed Central

24 November 2017

1 reference

Europe PubMed Central

24 November 2017

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