(Q71137935)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6651842%20AND%20SRC:MED&resulttype=core&format=json

16 October 2019

title

Affinity inactivation of bovine Cu,Zn superoxide dismutase by hydroperoxide anion, HO2- (English)

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6651842%20AND%20SRC:MED&resulttype=core&format=json

16 October 2019

author name string

H J Fuchs

series ordinal

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6651842%20AND%20SRC:MED&resulttype=core&format=json

16 October 2019

C L Borders

series ordinal

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6651842%20AND%20SRC:MED&resulttype=core&format=json

16 October 2019

publication date

1 November 1983

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6651842%20AND%20SRC:MED&resulttype=core&format=json

Biochemical and Biophysical Research Communications

16 October 2019

number of pages

7

1 reference

based on heuristic

inferred from page(s)

published in

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6651842%20AND%20SRC:MED&resulttype=core&format=json

16 October 2019

volume

116

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6651842%20AND%20SRC:MED&resulttype=core&format=json

16 October 2019

issue

3

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6651842%20AND%20SRC:MED&resulttype=core&format=json

16 October 2019

page(s)

1107-1113

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6651842%20AND%20SRC:MED&resulttype=core&format=json

16 October 2019

cites work

Superoxide dismutases

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2883%2980256-3

Some sulfhydryl properties and primary structure of human erythrocyte superoxide dismutase

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2883%2980256-3

Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2883%2980256-3

Identification of Arg-143 as the essential arginyl residue in yeast Cu,Zn superoxide dismutase by use of a chromophoric arginine reagent

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2883%2980256-3

Chemical modification of arginine at the active site of the bovine erythrocyte superoxide dismutase

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2883%2980256-3

Hydroperoxide anion, HO2−, is an affinity reagent for the inactivation of yeast Cu,Zn superoxide dismutase: Modification of one histidine per subunit

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2883%2980256-3

Reduction and inactivation of superoxide dismutase by hydrogen peroxide

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2883%2980256-3

Interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide. Inactivation of the enzyme

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2883%2980256-3

Reversal of the superoxide dismutase reaction

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2883%2980256-3

Interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide. Chemiluminescence and peroxidation

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2883%2980256-3

Studies of the metal sites of copper proteins. Symmetry of copper in bovine superoxide dismutase and its functional significance

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2883%2980256-3

Competitive inhibition of Cu, Zn superoxide dismutase by monovalent anions

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2883%2980256-3

Pulse radiolytic investigations of superoxide catalyzed disproportionation. Mechanism for bovine superoxide dismutase

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2883%2980256-3

Reduced anion-binding affinity of Cu,Zn superoxide dismutases chemically modified at arginine

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2883%2980256-3

Kinetic study of O-2 DISMUTATION BY BOVINE SUPEROXIDE DISMUTASE. Evidence for saturation of the catalytic sites by O-2.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2883%2980256-3

Properties of the cupric sites in bovine superoxide dismutase studied by nuclear-magnetic-relaxation measurements

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2883%2980256-3

A water 17O NMR study of the pH dependent properties of superoxide dismutase

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2883%2980256-3

10.1016/S0006-291X(83)80256-3

7 January 2021

Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6651842%20AND%20SRC:MED&resulttype=core&format=json

16 October 2019

1 reference