The importance of being knotted: effects of the C-terminal knot structure on enzymatic and mechanical properties of bovine carbonic anhydrase II (Q74144055)

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scientific article published on 01 May 2002

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English	The importance of being knotted: effects of the C-terminal knot structure on enzymatic and mechanical properties of bovine carbonic anhydrase II	scientific article published on 01 May 2002

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scholarly article

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12023014%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

The importance of being knotted: effects of the C-terminal knot structure on enzymatic and mechanical properties of bovine carbonic anhydrase II (English)

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12023014%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

molecular knots

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author name string

Mohammad Taufiq Alam

1

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9 November 2019

Takafumi Yamada

2

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12023014%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

Uno Carlsson

3

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12023014%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

Atsushi Ikai

4

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9 November 2019

publication date

1 May 2002

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9 November 2019

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6

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9 November 2019

519

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9 November 2019

1-3

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9 November 2019

35-40

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9 November 2019

A deeply knotted protein structure and how it might fold.

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902693-5

7 January 2021

A comparative CD study of carbonic anhydrase isoenzymes with different number of tryptophans: impact on calculation of secondary structure content

1 reference

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7 January 2021

Folding around the C-terminus of human carbonic anhydrase II. Kinetic characterization by use of a chemically reactive SH-group introduced by protein engineering

1 reference

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7 January 2021

Refined structure of human carbonic anhydrase II at 2.0 A resolution

1 reference

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7 January 2021

Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-A resolution

1 reference

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7 January 2021

Cis-transisomerization is rate-determining in the reactivation of denatured human carbonic anhydrase II as evidenced by proline isomerase

1 reference

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7 January 2021

Studies on the influence of carboxyl-terminal amino acid residues on the activity and stability of human erythrocyte carbonic anhydrase B.

1 reference

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7 January 2021

Mechanical unfolding of alpha2-macroglobulin molecules with atomic force microscope

1 reference

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7 January 2021

Reversible unfolding of individual titin immunoglobulin domains by AFM

1 reference

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7 January 2021

The molecular elasticity of the extracellular matrix protein tenascin

1 reference

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7 January 2021

Two slow stages in refolding of bovine carbonic anhydrase B are due to proline isomerization.

1 reference

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7 January 2021

Detection and characterization using circular dichroism and fluorescence spectroscopy of a stable intermediate conformation formed in the denaturation of bovine carbonic anhydrase with guanidinium chloride

1 reference

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7 January 2021

Force measurement and inhibitor binding assay of monomer and engineered dimer of bovine carbonic anhydrase B.

1 reference

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7 January 2021

Spring mechanics of alpha-helical polypeptide

1 reference

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7 January 2021

The Catalytic Versatility of Erythrocyte Carbonic Anhydrase. III. Kinetic Studies of the Enzyme-Catalyzed Hydrolysis of p-Nitrophenyl Acetate*

1 reference

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7 January 2021

Carbon-13 nuclear magnetic resonance probe of active-site ionizations in human carbonic anhydrase B

1 reference

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7 January 2021

Estimation of globular protein secondary structure from circular dichroism.

1 reference

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7 January 2021

Calibration of atomic‐force microscope tips

1 reference

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7 January 2021

Dynamic measurement of single protein's mechanical properties

1 reference

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7 January 2021

GroEL provides a folding pathway with lower apparent activation energy compared to spontaneous refolding of human carbonic anhydrase II.

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902693-5

7 January 2021

Effect of experimental conditions on the analysis of sodium dodecyl sulphate polyacrylamide gel electrophoresis separated proteins by matrix-assisted laser desorption/ ionisation mass spectrometry

1 reference

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7 January 2021

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

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7 January 2021

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

1 reference

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7 January 2021

Secondary Interactions Significantly Removed from the Sulfonamide Binding Pocket of Carbonic Anhydrase II Influence Inhibitor Binding Constants

1 reference

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7 January 2021

Carboxyl-Terminal Region of Human and Bovine Erythrocyte Carbonic Anhydrases. 1. Amino Acid Sequences of Terminal Cyanogen Bromide Fragments

1 reference

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7 January 2021

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

1 reference

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7 January 2021

Identifiers

10.1016/S0014-5793(02)02693-5

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12023014%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12023014%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

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