(Q30176259)

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Role of the dimeric structure in Cu,Zn superoxide dismutase. pH-dependent, reversible denaturation of the monomeric enzyme from Escherichia coli

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scholarly article

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Europe PubMed Central

PubMed publication ID

9 June 2017

Role of the dimeric structure in Cu,Zn superoxide dismutase. pH-dependent, reversible denaturation of the monomeric enzyme from Escherichia coli (English)

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

1 reference

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Escherichia coli

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author name string

Battistoni A

1

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Europe PubMed Central

PubMed publication ID

9 June 2017

Folcarelli S

2

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

Cervoni L

3

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

Polizio F

4

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

Desideri A

5

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

Giartosio A

6

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

Rotilio G

7

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

language of work or name

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publication date

1 March 1998

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9 June 2017

Journal of Biological Chemistry

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9 June 2017

273

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Europe PubMed Central

PubMed publication ID

9 June 2017

10

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Europe PubMed Central

PubMed publication ID

9 June 2017

5655-5661

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

Aspects of the Structure, Function, and Applications of Superoxide Dismutas

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5655

21 January 2018

Bacterial [Cu,Zn]-superoxide dismutase: phylogenetically distinct from the eukaryotic enzyme, and not so rare after all!

1 reference

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21 January 2018

Evolutionary conservativeness of electric field in the Cu,Zn superoxide dismutase active site. Evidence for co-ordinated mutation of charged amino acid residues.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5655

21 January 2018

Evolution of CuZn superoxide dismutase and the Greek key beta-barrel structural motif

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5655

21 January 2018

Conserved patterns in the Cu,Zn superoxide dismutase family.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5655

21 January 2018

Cloning and analysis of sodC, encoding the copper-zinc superoxide dismutase of Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5655

21 January 2018

The Cu,Zn superoxide dismutase from Escherichia coli retains monomeric structure at high protein concentration. Evidence for altered subunit interaction in all the bacteriocupreins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5655

21 January 2018

Novel dimeric interface and electrostatic recognition in bacterial Cu,Zn superoxide dismutase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5655

21 January 2018

On the quaternary structure of copper-zinc superoxide dismutases. Reversible dissociation into protomers of the isozyme I from wheat germ

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5655

21 January 2018

Crystallization and preliminary X-ray analysis of the monomeric Cu,Zn superoxide dismutase from Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5655

21 January 2018

Purification and characterization of the Cu,Zn SOD from Escherichia coli.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5655

21 January 2018

Differential scanning calorimetry of Cu,Zn-superoxide dismutase, the apoprotein, and its zinc-substituted derivatives

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5655

21 January 2018

Metal sites of copper proteins. Ligands of copper in hemocuprein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5655

21 January 2018

Subunit association and side-chain reactivities of bovine erythrocyte superoxide dismutase in denaturing solvents

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5655

21 January 2018

The copper- and zinc-containing superoxide dismutase from Escherichia coli: molecular weight and stability

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5655

21 January 2018

The effects of pH and various salts upon the activity of a series of superoxide dismutases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5655

21 January 2018

Identification of the residues responsible for the alkaline inhibition of Cu,Zn superoxide dismutase: a site-directed mutagenesis approach

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5655

21 January 2018

Thermostabilization of recombinant human and bovine CuZn superoxide dismutases by replacement of free cysteines

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5655

21 January 2018

A spectroscopic characterization of a monomeric analog of copper, zinc superoxide dismutase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5655

21 January 2018

Isolation of an active and heat-stable monomeric form of Cu,Zn superoxide dismutase from the periplasmic space of Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5655

21 January 2018

Structural analyses of various Cu2+, Zn2+-superoxide dismutases by differential scanning calorimetry and Raman spectroscopy

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5655

21 January 2018

Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5655

21 January 2018

Spectroscopic characterization of recombinant Cu,Zn superoxide dismutase from Photobacterium leiognathi expressed in Escherichia coli: evidence for a novel catalytic copper binding site

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5655

21 January 2018

The role of cysteine oxidation in the thermal inactivation of T4 lysozyme

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5655

21 January 2018

Identifiers

10.1074/JBC.273.10.5655

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

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