ArticleBiochemistry2011
Structural basis of the substrate specificity of bifunctional isocitrate dehydrogenase kinase/phosphatase.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- Study on the phosphorylation of NADJournal of enzyme inhibition and medicinal chemistry · 2025Article
- Kinases on Double Duty: A Review of UniProtKB Annotated Bifunctionality within the Kinome.Biomolecules · 2022Review
- Engineering the glyoxylate cycle for chemical bioproduction.Frontiers in bioengineering and biotechnology · 2022Review
- Crystal Structures of the Putative Isocitrate Dehydrogenase fromArchaea (Vancouver, B.C.) · 2018Article
- A rheostat mechanism governs the bifurcation of carbon flux in mycobacteria.Nature communications · 2016Article
- Dimerization and bifunctionality confer robustness to the isocitrate dehydrogenase regulatory system in Escherichia coli.The Journal of biological chemistry · 2013Article
- Design principles underpinning the regulatory diversity of protein kinases.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Structural and mechanistic insights into the bifunctional enzyme isocitrate dehydrogenase kinase/phosphatase AceK.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Induced fit and the catalytic mechanism of isocitrate dehydrogenase.Biochemistry · 2012Article
- Functional relevance of dynamic properties of Dimeric NADP-dependent Isocitrate Dehydrogenases.BMC bioinformatics · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
Abstract
Isocitrate dehydrogenase kinase/phosphatase (AceK) regulates entry into the glyoxylate bypass by reversibly phosphorylating isocitrate dehydrogenase (ICDH). On the basis of the recently determined structure of the AceK-ICDH complex from Escherichia coli, we have classified the structures of homodimeric NADP(+)-ICDHs to rationalize and predict which organisms likely contain substrates for AceK. One example is Burkholderia pseudomallei (Bp). Here we report a crystal structure of Bp-ICDH that exhibits the necessary structural elements required for AceK recognition. Kinetic analyses provided further confirmation that Bp-ICDH is a substrate for AceK. We conclude that the highly stringent AceK binding sites on ICDH are maintained only in Gram-negative bacteria.
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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.