Extracellular superoxide dismutase exists as an octamer (original) (raw)

Characterization of the heparin-binding domain of human extracellular superoxide dismutase

Alexei Buevich

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1997

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The Folding of Human Active and Inactive Extracellular Superoxide Dismutases Is an Intracellular Event

Torsten Kristensen

Journal of Biological Chemistry, 2008

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Extracellular superoxide dismutase: structural and functional considerations of a protein shaped by two different disulfide bridge patterns

Jan Enghild

2005

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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

Jan Enghild

Biochemical Journal, 1996

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

Peter Stenlund

Protein Engineering Design and Selection, 1999

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The Heparin-binding Domain of Extracellular Superoxide Dismutase Is Proteolytically Processed Intracellularly during Biosynthesis

Jan Enghild

Journal of Biological Chemistry, 1999

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The subunit composition of human extracellular superoxide dismutase (EC-SOD) regulate enzymatic activity

Jan Enghild

2007

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The Intracellular Proteolytic Processing of Extracellular Superoxide Dismutase (EC-SOD) is a Two-step Event

Jan Enghild

Journal of Biological Chemistry, 2004

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Characterization of Heparin Binding of Human Extracellular Superoxide Dismutase

Peter Stenlund

Biochemistry, 2000

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

Peter Stenlund

Protein Science, 2008

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Determination of the structural role of the N-terminal domain of human extracellular superoxide dismutase by use of protein fusions

Bengt-harald Jonsson

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1996

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The dual nature of human extracellular superoxide dismutase: One sequence and two structures

Jan Enghild

Proceedings of the National Academy of Sciences, 2003

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Extracellular Superoxide Dismutase (EC-SOD) Binds to Type I Collagen and Protects Against Oxidative Fragmentation

joanna wegrzyn

Journal of Biological Chemistry, 2004

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Structural Requirements for High-Affinity Heparin Binding: Alanine Scanning Analysis of Charged Residues in the C-Terminal Domain of Human Extracellular Superoxide Dismutase †

Peter Stenlund

Biochemistry, 2002

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On the selectivity of superoxide dismutase mimetics and its importance in pharmacological studies

Daniela Salvemini

British Journal of Pharmacology, 2003

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The Structure of Human M Superoxide Dismutase Irrteti of Two LGHdix Bundles

John Tainer

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A non-glycosylated extracellular superoxide dismutase variant

Thomas Edlund

The Biochemical journal, 1992

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The Structure of Human Extracellular Copper–Zinc Superoxide Dismutase at 1.7 Å Resolution: Insights into Heparin and Collagen Binding

Svetlana Antonyuk

Journal of Molecular Biology, 2009

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The C-terminal proteolytic processing of extracellular superoxide dismutase is redox regulated

Jan Enghild

Free Radical Biology and Medicine, 2012

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The high concentration of Arg213→Gly extracellular superoxide dismutase (EC-SOD) in plasma is caused by a reduction of both heparin and collagen affinities

Jan Enghild

Biochemical Journal, 2005

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The basic and applied aspects of superoxide dismutase

Sanjay Kumar

Journal of Molecular Catalysis B: Enzymatic, 2011

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Rational design of a secreted enzymatically inactive mutant of extracellular superoxide dismutase

Adam Case

Redox Report, 2012

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Superoxide Dismutase: Therapeutic Targets in SOD Related Pathology

Zamosteanu Nina

Health, 2014

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The structural biochemistry of the superoxide dismutases

J. Perry, John Tainer

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2010

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Endocytosis of Extracellular Superoxide Dismutase Into Endothelial Cells: Role of the Heparin-Binding Domain

ROBERT-GENE PIPER

Arteriosclerosis, Thrombosis, and Vascular Biology, 2006

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Superoxide Dismutase (SOD): A Promising Enzyme in the Area of Biopharmaceuticals in Its Native and Immobilized Form: A Review

IJRASET Publication

International Journal for Research in Applied Science & Engineering Technology (IJRASET), 2022

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Hydrogen peroxide induce modifications of human extracellular superoxide dismutase that results in enzyme inhibition

Jan Enghild

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Furin Proteolytically Processes the Heparin-binding Region of Extracellular Superoxide Dismutase

Jan Enghild

Journal of Biological Chemistry, 2002

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The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles

John Tainer

Cell, 1992

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