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  Activation and assembly of the NADPH oxidase: a structural perspective

Groemping, Y., & Rittinger, K. (2005). Activation and assembly of the NADPH oxidase: a structural perspective. Biochemical Journal, 386(3), 401-416. doi:10.1042/BJ20041835.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-700F-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-7011-E
Genre: Journal Article
Alternative Title : Activation and assembly of the NADPH oxidase: a structural perspective

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 Creators:
Groemping, Yvonne1, Author              
Rittinger, Katrin, Author              
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: NADPH oxidase, oxidase assembly, phosphorylation, protein-protein interaction, reactive oxygen species
 Abstract: The NADPH oxidase of professional phagocytes is a crucial component of the innate immune response due to its fundamental role in the production of reactive oxygen species that act as powerful microbicidal agents. The activity of this multi−protein enzyme is dependent on the regulated assembly of the six enzyme subunits at the membrane where oxygen is reduced to superoxide anions. In the resting state, four of the enzyme subunits are maintained in the cytosol, either through auto−inhibitory interactions or through complex formation with accessory proteins that are not part of the active enzyme complex. Multiple inputs are required to disrupt these inhibitory interactions and allow translocation to the membrane and association with the integral membrane components. Protein interaction modules are key regulators of NADPH oxidase assembly and the protein−protein interactions mediated via these domains have been the target of numerous studies. Many models have been put forward to describe the intricate network of reversible protein interactions that regulate the activity of this enzyme but an all−encompassing model has so far been elusive. An important step towards an understanding of the molecular basis of NADPH oxidase assembly and activity has been the recent solution of the three−dimensional structures of some of the oxidase components. We will discuss these structures in the present review and attempt to reconcile some of the conflicting models on the basis of the structural information available

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Language(s): eng - English
 Dates: 2004-12-022004-11-032004-12-102004-12-102005-03-15
 Publication Status: Published in print
 Pages: 16
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Degree: -

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Title: Biochemical Journal
Source Genre: Journal
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Publ. Info: London : Published by Portland Press on behalf of the Biochemical Society.
Pages: - Volume / Issue: 386 (3) Sequence Number: - Start / End Page: 401 - 416 Identifier: ISSN: 0264-6021
CoNE: /journals/resource/110992357308158