ReviewInternational journal of molecular sciences2020
Structure, Folding and Stability of Nucleoside Diphosphate Kinases.
Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 34 citations in OpenAlex.
- A Modular Nucleoside Kinase Cascade for the Synthesis of Ribonucleoside Triphosphates.Biotechnology and bioengineering · 2026Article
- Functional Diversity and Emerging Roles of Human NME/NDPK Group II Proteins.International journal of molecular sciences · 2026Review
- Emerging Roles of Adenosine Metabolism in Astrocytes During Brain Injury.CNS neuroscience & therapeutics · 2026Review
- Structural and Functional Analyses ofACS omega · 2026Article
- A phosphohistidine phosphatase promotes starvation survival by dephosphorylating nucleoside diphosphate kinase.Cell reports · 2026Article
- Mechanistic Insights into Substrate Recognition of Human Nucleoside Diphosphate Kinase C Based on Nucleotide-Induced Structural Changes.International journal of molecular sciences · 2024Article
- The activation cascade of the broad-spectrum antiviral bemnifosbuvir characterized at atomic resolution.PLoS biology · 2024Article
- Review
- A ~40-kb flavi-like virus does not encode a known error-correcting mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Nucleocytoplasmic transport rates are regulated by cellular processes that modulate GTP availability.The Journal of cell biology · 2024Article
- A reanalysis and integration of transcriptomics and proteomics datasets unveil novel drug targets for Mekong schistosomiasis.Scientific reports · 2024Article
- Revisiting Exome Data Identified Missed Splice Site Variant of the Asparagine Synthetase (Journal of pediatric genetics · 2024Article
- An exonuclease-resistant chain-terminating nucleotide analogue targeting the SARS-CoV-2 replicase complex.Nucleic acids research · 2024Article
- A Non-Functional Carbon Dioxide-Mediated Post-Translational Modification on Nucleoside Diphosphate Kinase ofInternational journal of molecular sciences · 2024Article
- Redox dynamics in seeds ofFrontiers in plant science · 2024Article
- Nucleocytoplasmic transport rates are regulated by cellular processes that modulate GTP availability.bioRxiv : the preprint server for biology · 2023Article
- A nucleotide diphosphate kinase mediates tethering between mitochondria prior to fusion.The Journal of cell biology · 2023Article
- Salmonella YqiC exerts its function through an oligomeric state.Protein science : a publication of the Protein Society · 2023Article
- Fecal Proteome Profile in Dogs Suffering from Different Hepatobiliary Disorders and Comparison with Controls.Animals : an open access journal from MDPI · 2023Article
- A Unique Mode of Coenzyme A Binding to the Nucleotide Binding Pocket of Human Metastasis Suppressor NME1.International journal of molecular sciences · 2023Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nucleoside diphosphate kinases (NDPK) are oligomeric proteins involved in the synthesis of nucleoside triphosphates. Their tridimensional structure has been solved by X-ray crystallography and shows that individual subunits present a conserved ferredoxin fold of about 140 residues in prokaryotes, archaea, eukaryotes and viruses. Monomers are functionally independent from each other inside NDPK complexes and the nucleoside kinase catalytic mechanism involves transient phosphorylation of the conserved catalytic histidine. To be active, monomers must assemble into conserved head to tail dimers, which further assemble into hexamers or tetramers. The interfaces between these oligomeric states are very different but, surprisingly, the assembly structure barely affects the catalytic efficiency of the enzyme. While it has been shown that assembly into hexamers induces full formation of the catalytic site and stabilizes the complex, it is unclear why assembly into tetramers is required for function. Several additional activities have been revealed for NDPK, especially in metastasis spreading, cytoskeleton dynamics, DNA binding and membrane remodeling. However, we still lack the high resolution structural data of NDPK in complex with different partners, which is necessary for deciphering the mechanism of these diverse functions. In this review we discuss advances in the structure, folding and stability of NDPKs.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.