ArticleActa naturae2009
D-Arabinose Methabolism: Characterization of Bifunctional Arabinokinase/Pyrophosphorylase of Leishmania major.
Article in Acta naturae, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed, 11 citations in OpenAlex.
- Dual cytosine modification through hydroxylation and arabinofuranosylation in phages.Nature chemical biology · 2026Article
- Use of Crithidia fasciculata extract for the facile enzymatic synthesis of GDP-L-[3H]Fucose.Glycobiology · 2025Article
- Article
- D-arabinose induces cell cycle arrest by promoting autophagy via p38 MAPK signaling pathway in breast cancer.Scientific reports · 2024Article
- Genetic metabolic complementation establishes a requirement for GDP-fucose inThe Journal of biological chemistry · 2017Article
- Influence of the Microenvironment in the Transcriptome of Leishmania infantum Promastigotes: Sand Fly versus Culture.PLoS neglected tropical diseases · 2016Article
- Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this work we describe an unusual enzyme from Leishmania major (Arabinokinase/Pyrophosphorylase) that catalyzes the synthesis of GDP-D-arabinopyranose (GDP-D-Arap) via a D-arabinose-1-phosphate intermediate in the presence of ATP and GTP. Our data indicate GDP-D-Arap transport in vivo by the LPG2 multispecific nucleotide sugar transporter into the Leishmania Golgi apparatus, in which it can be used by glycosyltransferases as a donor substrate for glycosylation.
Identifiers
22649617PMC3347535W163716851What OpenQuestion holds
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.