ArticleCellular and molecular life sciences : CMLS2011
The diterpenoid alkaloid noroxoaconitine is a Mapkap kinase 5 (MK5/PRAK) inhibitor.
Article in Cellular and molecular life sciences : CMLS, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- Phytochemical study ofPharmaceutical biology · 2026Article
- Seed Dormancy Class and Ecophysiological Features ofPlants (Basel, Switzerland) · 2022Article
- Tandem mass tag labeled quantitative proteomic analysis of differential protein expression on total alkaloid ofFrontiers in veterinary science · 2022Article
- The essential role of PRAK in tumor metastasis and its therapeutic potential.Nature communications · 2021Article
- Homology modeling and ligand docking of Mitogen-activated protein kinase-activated protein kinase 5 (MK5).Theoretical biology & medical modelling · 2013Article
- The Role of Mitogen-Activated Protein Kinase-Activated Protein Kinases (MAPKAPKs) in Inflammation.Genes · 2013Article
- Tumour promoting and suppressing roles of the atypical MAP kinase signalling pathway ERK3/4-MK5.Journal of molecular signaling · 2012Article
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4 authors at 1 institution in 1 country.
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Abstract
The mitogen-activated protein kinase-activated protein kinase MK5 is ubiquitously expressed in vertebrates and is implicated in cell proliferation, cytoskeletal remodeling, and anxiety behavior. This makes MK5 an attractive drug target. We tested several diterpenoid alkaloids for their ability to suppress MK5 kinase activity. We identified noroxoaconitine as an ATP competitor that inhibited the catalytic activity of MK5 in vitro (IC₅₀ = 37.5 μM; K(i) = 0.675 μM) and prevented PKA-induced nuclear export of MK5, a process that depends on kinase active MK5. MK5 is closely related to MK2 and MK3, and noroxoaconitine inhibited MK3- and MK5- but not MK2-mediated phosphorylation of the common substrate Hsp27. Molecular docking of noroxoaconitine into the ATP binding sites indicated that noroxoaconitine binds more strongly to MK5 than to MK3. Noroxoaconitine and derivatives may help in elucidating the precise biological functions of MK5 and may prove to have therapeutic values.
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