Tags

Type your tag names separated by a space and hit enter

Enzymatic regulation and functional relevance of NOX5.
Curr Pharm Des 2015; 21(41):5999-6008CP

Abstract

The NADPH oxidases (NOX) represent a family of 7 related transmembrane enzymes that share a basic structural paradigm and the common ability to utilize NADPH to synthesize superoxide and other reactive oxygen species (ROS). NOX isoforms are distinguished from each other by their amino acid sequences, expression levels in different cell types, the mechanisms of enzyme activation and the type of ROS that are generated. NOX5 was the last NOX family member to be identified and in the past decade and a half we have gained significant insights into how NOX5 produces ROS, the cell types where it is expressed and the functional significance of NOX5 in health and disease. The objective of this review is to highlight accumulated and recent knowledge of the genetic and enzymatic regulation of NOX5 and the importance of NOX5 in human physiology and pathophysiology.

Authors+Show Affiliations

Department of Forensic Medicine, Nanjing Medical University, Nanjing, Jiangsu, China. fchen@gru.edu.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Review

Language

eng

PubMed ID

26510438

Citation

Chen, Feng, et al. "Enzymatic Regulation and Functional Relevance of NOX5." Current Pharmaceutical Design, vol. 21, no. 41, 2015, pp. 5999-6008.
Chen F, Wang Y, Barman S, et al. Enzymatic regulation and functional relevance of NOX5. Curr Pharm Des. 2015;21(41):5999-6008.
Chen, F., Wang, Y., Barman, S., & Fulton, D. J. (2015). Enzymatic regulation and functional relevance of NOX5. Current Pharmaceutical Design, 21(41), pp. 5999-6008.
Chen F, et al. Enzymatic Regulation and Functional Relevance of NOX5. Curr Pharm Des. 2015;21(41):5999-6008. PubMed PMID: 26510438.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Enzymatic regulation and functional relevance of NOX5. AU - Chen,Feng, AU - Wang,Yusi, AU - Barman,Scott, AU - Fulton,David J R, PY - 2015/08/14/received PY - 2015/10/27/accepted PY - 2015/10/30/entrez PY - 2015/10/30/pubmed PY - 2016/9/16/medline SP - 5999 EP - 6008 JF - Current pharmaceutical design JO - Curr. Pharm. Des. VL - 21 IS - 41 N2 - The NADPH oxidases (NOX) represent a family of 7 related transmembrane enzymes that share a basic structural paradigm and the common ability to utilize NADPH to synthesize superoxide and other reactive oxygen species (ROS). NOX isoforms are distinguished from each other by their amino acid sequences, expression levels in different cell types, the mechanisms of enzyme activation and the type of ROS that are generated. NOX5 was the last NOX family member to be identified and in the past decade and a half we have gained significant insights into how NOX5 produces ROS, the cell types where it is expressed and the functional significance of NOX5 in health and disease. The objective of this review is to highlight accumulated and recent knowledge of the genetic and enzymatic regulation of NOX5 and the importance of NOX5 in human physiology and pathophysiology. SN - 1873-4286 UR - https://www.unboundmedicine.com/medline/citation/26510438/Enzymatic_regulation_and_functional_relevance_of_NOX5_ L2 - http://www.eurekaselect.com/136247/article DB - PRIME DP - Unbound Medicine ER -