ArticleNucleic acids research2007
Flexible segments modulate co-folding of dUTPase and nucleocapsid proteins.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed, 46 citations in OpenAlex.
- dUTPase is essential in zebrafish development and possesses several single-nucleotide variants with pronounced structural and functional consequences.FEBS open bio · 2026Article
- Redox status of cysteines does not alter functional properties of human dUTPase but the Y54C mutation involved in monogenic diabetes decreases protein stability.Scientific reports · 2021Article
- Structural Insight into African Swine Fever Virus dUTPase Reveals a Novel Folding Pattern in the dUTPase Family.Journal of virology · 2020Article
- The Stl repressor fromFEBS open bio · 2018Article
- The dUTPase of white spot syndrome virus assembles its active sites in a noncanonical manner.The Journal of biological chemistry · 2018Article
- Differential control of dNTP biosynthesis and genome integrity maintenance by the dUTPase superfamily enzymes.Scientific reports · 2017Article
- A Hidden Active Site in the Potential Drug Target Mycobacterium tuberculosis dUTPase Is Accessible through Small Amplitude Protein Conformational Changes.The Journal of biological chemistry · 2016Article
- Chameleon sequences in neurodegenerative diseases.Biochemical and biophysical research communications · 2016Article
- In Vitro Analysis of Predicted DNA-Binding Sites for the Stl Repressor of the Staphylococcus aureus SaPIBov1 Pathogenicity Island.PloS one · 2016Article
- dUTPase: the frequently overlooked enzyme encoded by many retroviruses.Retrovirology · 2015Review
- Highly potent dUTPase inhibition by a bacterial repressor protein reveals a novel mechanism for gene expression control.Nucleic acids research · 2014Article
- Dynamics of re-constitution of the human nuclear proteome after cell division is regulated by NLS-adjacent phosphorylation.Cell cycle (Georgetown, Tex.) · 2014Article
- The metagenomic telescope.PloS one · 2014Article
- Catalytic mechanism of α-phosphate attack in dUTPase is revealed by X-ray crystallographic snapshots of distinct intermediates, 31P-NMR spectroscopy and reaction path modelling.Nucleic acids research · 2013Article
- Identification of diverse full-length endogenous betaretroviruses in megabats and microbats.Retrovirology · 2013Article
- Crystallization and preliminary crystallographic analysis of dUTPase from the φ11 helper phage of Staphylococcus aureus.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Nucleotide pyrophosphatase employs a P-loop-like motif to enhance catalytic power and NDP/NTP discrimination.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Evolution of the Kdo2-lipid A biosynthesis in bacteria.BMC evolutionary biology · 2010Article
- The flexible motif V of Epstein-Barr virus deoxyuridine 5'-triphosphate pyrophosphatase is essential for catalysis.The Journal of biological chemistry · 2009Article
- Crystallization and preliminary X-ray analysis of three dUTPases from Gram-positive bacteria.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
15 authors at 8 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The homotrimeric fusion protein nucleocapsid (NC)-dUTPase combines domains that participate in RNA/DNA folding, reverse transcription, and DNA repair in Mason-Pfizer monkey betaretrovirus infected cells. The structural organization of the fusion protein remained obscured by the N- and C-terminal flexible segments of dUTPase and the linker region connecting the two domains that are invisible in electron density maps. Small-angle X-ray scattering reveals that upon oligonucleotide binding the NC domains adopt the trimeric symmetry of dUTPase. High-resolution X-ray structures together with molecular modeling indicate that fusion with NC domains dramatically alters the conformation of the flexible C-terminus by perturbing the orientation of a critical beta-strand. Consequently, the C-terminal segment is capable of double backing upon the active site of its own monomer and stabilized by non-covalent interactions formed with the N-terminal segment. This co-folding of the dUTPase terminal segments, not observable in other homologous enzymes, is due to the presence of the fused NC domain. Structural and genomic advantages of fusing the NC domain to a shortened dUTPase in betaretroviruses and the possible physiological consequences are envisaged.
Indexed as
Identifiers
What 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.