ArticleProceedings of the National Academy of Sciences of the United States of America2022
Structure of human NADK2 reveals atypical assembly and regulation of NAD kinases from animal mitochondria.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Mitochondrial NADP(H)-dependent de novo dTMP biosynthesis counteracts the cytotoxicity of PARP inhibitors.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- NADK tetramer defective mutants affect lung cancer response to chemotherapy via controlling NADK activity.Genes & diseases · 2025Article
- Cytosolic NADK is conditionally essential for folate-dependent nucleotide synthesis.Nature metabolism · 2025Article
- Cryo-EM structure and regulation of human NAD kinase.Science advances · 2025Article
- Metabolic control of collagen synthesis.Matrix biology : journal of the International Society for Matrix Biology · 2024Review
- Homeostatic regulation of NAD(H) and NADP(H) in cells.Genes & diseases · 2024Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
All kingdoms of life produce essential nicotinamide dinucleotide NADP(H) using NAD kinases (NADKs). A panel of published NADK structures from bacteria, eukaryotic cytosol, and yeast mitochondria revealed similar tetrameric enzymes. Here, we present the 2.8-Å structure of the human mitochondrial kinase NADK2 with a bound substrate, which is an exception to this uniformity, diverging both structurally and biochemically from NADKs. We show that NADK2 harbors a unique tetramer disruptor/dimerization
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Registered trials
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