Redox proteomics: Methods for the identification and enrichment of redox‐modified proteins and their applications. Issue 2 (17th December 2015)
- Record Type:
- Journal Article
- Title:
- Redox proteomics: Methods for the identification and enrichment of redox‐modified proteins and their applications. Issue 2 (17th December 2015)
- Main Title:
- Redox proteomics: Methods for the identification and enrichment of redox‐modified proteins and their applications
- Authors:
- Lennicke, Claudia
Rahn, Jette
Heimer, Nadine
Lichtenfels, Rudolf
Wessjohann, Ludger A.
Seliger, Barbara - Abstract:
- Abstract : PTMs are defined as covalent additions to functional groups of amino acid residues in proteins like phosphorylation, glycosylation, S ‐nitrosylation, acetylation, methylation, lipidation, SUMOylation as well as oxidation. Oxidation of proteins has been characterized as a double‐edged sword. While oxidative modifications, in particular of cysteine residues, are widely involved in the regulation of cellular homeostasis, oxidative stress resulting in the oxidation of biomolecules along with the disruption of their biological functions can be associated with the development of diseases, such as cancer, diabetes, and neurodegenerative diseases, respectively. This is also the case for advanced glycation end products, which result from chemical reactions of keto compounds such as oxidized sugars with proteins. The role of oxidative modifications under physiological and pathophysiological conditions remains largely unknown. Recently, novel technologies have been established that allow the enrichment, identification, and characterization of specific oxidative PTMs (oxPTMs). This is essential to develop strategies to prevent and treat diseases that are associated with oxidative stress. Therefore this review will focus on (i) the methods and technologies, which are currently applied for the detection, identification, and quantification of oxPTMs including the design of high throughput approaches and (ii) the analyses of oxPTMs related to physiological and pathologicalAbstract : PTMs are defined as covalent additions to functional groups of amino acid residues in proteins like phosphorylation, glycosylation, S ‐nitrosylation, acetylation, methylation, lipidation, SUMOylation as well as oxidation. Oxidation of proteins has been characterized as a double‐edged sword. While oxidative modifications, in particular of cysteine residues, are widely involved in the regulation of cellular homeostasis, oxidative stress resulting in the oxidation of biomolecules along with the disruption of their biological functions can be associated with the development of diseases, such as cancer, diabetes, and neurodegenerative diseases, respectively. This is also the case for advanced glycation end products, which result from chemical reactions of keto compounds such as oxidized sugars with proteins. The role of oxidative modifications under physiological and pathophysiological conditions remains largely unknown. Recently, novel technologies have been established that allow the enrichment, identification, and characterization of specific oxidative PTMs (oxPTMs). This is essential to develop strategies to prevent and treat diseases that are associated with oxidative stress. Therefore this review will focus on (i) the methods and technologies, which are currently applied for the detection, identification, and quantification of oxPTMs including the design of high throughput approaches and (ii) the analyses of oxPTMs related to physiological and pathological conditions. … (more)
- Is Part Of:
- Proteomics. Volume 16:Issue 2(2016)
- Journal:
- Proteomics
- Issue:
- Volume 16:Issue 2(2016)
- Issue Display:
- Volume 16, Issue 2 (2016)
- Year:
- 2016
- Volume:
- 16
- Issue:
- 2
- Issue Sort Value:
- 2016-0016-0002-0000
- Page Start:
- 197
- Page End:
- 213
- Publication Date:
- 2015-12-17
- Subjects:
- Animal proteomics -- Mass spectrometry -- Redox modifications -- Redox proteomics
Proteins -- Separation -- Periodicals
Bioinformatics -- Periodicals
Proteomics -- Periodicals
Genomes -- Periodicals
Molecular genetics -- Periodicals
572.605 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1615-9861 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/pmic.201500268 ↗
- Languages:
- English
- ISSNs:
- 1615-9853
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6936.178000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 2450.xml