Fluorescence-Based Assay For Measuring OMA1 Activity
Methods in Molecular Biology, ISSN: 1940-6029, Vol: 2276, Page: 325-332
2021
- 2Citations
- 2Captures
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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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- Citations2
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- Readers2
Book Chapter Description
Mitochondrial fusion depends on proteolytic processing of the dynamin-related GTPase protein, OPA1, which is regulated by the mitochondrial zinc metalloproteinase, OMA1. Last year we published a report describing a novel approach to directly measure the enzymatic activity of OMA1 in whole cell lysates. This fluorescence-based reporter assay utilizes an eight amino acid peptide sequence referred to as the S1 cleavage site where OMA1 cleaves within OPA1 and is flanked by a fluorophore and quencher. In this chapter, we provide additional insight into the OMA1 activity assay.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85107234635&origin=inward; http://dx.doi.org/10.1007/978-1-0716-1266-8_24; http://www.ncbi.nlm.nih.gov/pubmed/34060052; https://link.springer.com/10.1007/978-1-0716-1266-8_24; https://dx.doi.org/10.1007/978-1-0716-1266-8_24; https://link.springer.com/protocol/10.1007/978-1-0716-1266-8_24
Springer Science and Business Media LLC
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