Post-translational modifications of circulating alpha-1-antitrypsin protein
International Journal of Molecular Sciences, ISSN: 1422-0067, Vol: 21, Issue: 23, Page: 1-18
2020
- 37Citations
- 74Captures
- 1Mentions
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations37
- Citation Indexes37
- 37
- CrossRef27
- Captures74
- Readers74
- 74
- Mentions1
- Blog Mentions1
- Blog1
Most Recent Blog
IJMS, Vol. 21, Pages 9187: Post-Translational Modifications of Circulating Alpha-1-Antitrypsin Protein
IJMS, Vol. 21, Pages 9187: Post-Translational Modifications of Circulating Alpha-1-Antitrypsin Protein International Journal of Molecular Sciences doi: 10.3390/ijms21239187 Authors: Urszula Lechowicz Stefan Rudzinski Aleksandra Jezela-Stanek
Review Description
Alpha-1-antitrypsin (AAT), an acute-phase protein encoded by the SERPINA1 gene, is a member of the serine protease inhibitor (SERPIN) superfamily. Its primary function is to protect tissues from enzymes released during inflammation, such as neutrophil elastase and proteinase 3. In addition to its antiprotease activity, AAT interacts with numerous other substances and has various functions, mainly arising from the conformational flexibility of normal variants of AAT. Therefore, AAT has diverse biological functions and plays a role in various pathophysiological processes. This review discusses major molecular forms of AAT, including complex, cleaved, glycosylated, oxidized, and S-nitrosylated forms, in terms of their origin and function.
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