PNPLA-mediated lipid hydrolysis and transacylation – At the intersection of catabolism and anabolism
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, ISSN: 1388-1981, Vol: 1869, Issue: 2, Page: 159410
2024
- 5Citations
- 14Captures
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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.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations5
- Citation Indexes5
- CrossRef1
- Captures14
- Readers14
- 14
Article Description
Patatin-like phospholipase domain containing proteins (PNPLAs) play diverse roles in lipid metabolism. In this review, we focus on the enzymatic properties and predicted 3D structures of PNPLA1-5. PNPLA2-4 exert both catabolic and anabolic functions. Whereas PNPLA1 is predominantly expressed in the epidermis and involved in sphingolipid biosynthesis, PNPLA2 and 4 are ubiquitously expressed and exhibit several enzymatic activities, including hydrolysis and transacylation of various (glycero-)lipid species. This review summarizes known biological roles for PNPLA-mediated hydrolysis and transacylation reactions and highlights open questions concerning their physiological function.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S1388198123001348; http://dx.doi.org/10.1016/j.bbalip.2023.159410; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85179151995&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/37951382; https://linkinghub.elsevier.com/retrieve/pii/S1388198123001348; https://dx.doi.org/10.1016/j.bbalip.2023.159410
Elsevier BV
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