ArticlePloS one2013
Transiently transfected purine biosynthetic enzymes form stress bodies.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- The Purinosome: A Case Study for a Mammalian Metabolon.Annual review of biochemistry · 2022Review
- Human de novo purine biosynthesis.Critical reviews in biochemistry and molecular biology · 2021Review
- A quantitative screen for metabolic enzyme structures reveals patterns of assembly across the yeast metabolic network.Molecular biology of the cell · 2019Article
- Expression of the purine biosynthetic enzyme phosphoribosyl formylglycinamidine synthase in neurons.Journal of neurochemistry · 2018Article
- Colocalization and Sequential Enzyme Activity in Aqueous Biphasic Systems: Experiments and Modeling.Biophysical journal · 2015Article
- Dynamic architecture of the purinosome involved in human de novo purine biosynthesis.Biochemistry · 2015Article
- Enzyme clustering accelerates processing of intermediates through metabolic channeling.Nature biotechnology · 2014Article
- A proteomic survey of widespread protein aggregation in yeast.Molecular bioSystems · 2014Article
- Revisiting and revising the purinosome.Molecular bioSystems · 2014Review
- Dynamic reorganization of metabolic enzymes into intracellular bodies.Annual review of cell and developmental biology · 2012Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
It has been hypothesized that components of enzymatic pathways might organize into intracellular assemblies to improve their catalytic efficiency or lead to coordinate regulation. Accordingly, de novo purine biosynthesis enzymes may form a purinosome in the absence of purines, and a punctate intracellular body has been identified as the purinosome. We investigated the mechanism by which human de novo purine biosynthetic enzymes might be organized into purinosomes, especially under differing cellular conditions. Irregardless of the activity of bodies formed by endogenous enzymes, we demonstrate that intracellular bodies formed by transiently transfected, fluorescently tagged human purine biosynthesis proteins are best explained as protein aggregation.
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Registered trials
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