The dual nature of human extracellular superoxide dismutase: one sequence and two structures. (Q33713531)

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21 December 2019

title

The dual nature of human extracellular superoxide dismutase: one sequence and two structures (English)

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21 December 2019

7

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21 December 2019

author name string

Steen V Petersen

1

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21 December 2019

Tim D Oury

2

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21 December 2019

Zuzana Valnickova

3

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21 December 2019

Ida B Thøgersen

4

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21 December 2019

Peter Højrup

5

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21 December 2019

James D Crapo

6

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21 December 2019

publication date

13 November 2003

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Proceedings of the National Academy of Sciences of the United States of America

21 December 2019

published in

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21 December 2019

volume

100

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21 December 2019

issue

24

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21 December 2019

page(s)

13875-13880

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Extracellular superoxide dismutase in biology and medicine

21 December 2019

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Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression

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Furin proteolytically processes the heparin-binding region of extracellular superoxide dismutase

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Heterodimeric structure of superoxide dismutase in complex with its metallochaperone

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The heparin-binding domain of extracellular superoxide dismutase is proteolytically processed intracellularly during biosynthesis.

28 July 2018

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Bridge over troubled waters: sensing stress by disulfide bond formation

28 July 2018

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Posttranslational modifications of human inter-alpha-inhibitor: identification of glycans and disulfide bridges in heavy chains 1 and 2

28 July 2018

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Subunit interaction in extracellular superoxide dismutase: effects of mutations in the N-terminal domain

28 July 2018

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Mouse extracellular superoxide dismutase: primary structure, tissue-specific gene expression, chromosomal localization, and lung in situ hybridization

28 July 2018

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Function of the Greek key connection analysed using circular permutants of superoxide dismutase.

28 July 2018

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Human extracellular superoxide dismutase is a tetramer composed of two disulphide-linked dimers: a simplified, high-yield purification of extracellular superoxide dismutase

28 July 2018

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The rat extracellular superoxide dismutase dimer is converted to a tetramer by the exchange of a single amino acid

28 July 2018

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Purification and sequence of rat extracellular superoxide dismutase B secreted by C6 glioma

28 July 2018

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Prompt fragmentation of disulfide-linked peptides during matrix-assisted laser desorption ionization mass spectrometry

28 July 2018

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28 July 2018

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28 July 2018

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28 July 2018

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28 July 2018

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28 July 2018

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28 July 2018

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28 July 2018

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28 July 2018

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12 December 2020

The heparin binding site of human extracellular-superoxide dismutase

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12 December 2020

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12 December 2020

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12 December 2020

Chimeras of human extracellular and intracellular superoxide dismutases. Analysis of structure and function of the individual domains

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12 December 2020

Identifiers

DOI

10.1073/PNAS.2436143100

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21 December 2019

0 references

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21 December 2019

PubMed publication ID

14615576

1 reference