Evidence map›Paper›PMID 21904052›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2011

Inhibitor-bound complexes of dihydrofolate reductase-thymidylate synthase from Babesia bovis.

Darren W Begley, Thomas E Edwards, Amy C Raymond, Eric R Smith, Robert C Hartley, Jan Abendroth, Banumathi Sankaran, Donald D Lorimer, Peter J Myler, Bart L Staker and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.5field-weighted citation impact, top 34% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

9 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Antimicrobial agents and chemotherapy · 2024
    Article
  3. Article
  4. Screening the Medicines for Malaria Venture Pathogen Box against piroplasm parasites.International journal for parasitology. Drugs and drug resistance · 2019
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. The Protein Maker: an automated system for high-throughput parallel purification.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 2 institutions in 1 country.

Darren W BegleySeattle Structural Genomics Center for Infectious Disease (http://www.ssgcid.org), USA. dbegley@embios.com
Thomas E Edwards
Amy C Raymond
Eric R Smith
Robert C Hartley
Jan Abendroth
Banumathi Sankaran
Donald D Lorimer
Peter J Myler
Bart L Staker
Lance J Stewart
Joint Center for Structural Genomics · USCenter for Infectious Disease Research · US

Funding

Howard Hughes Medical InstituteNIAID NIH HHS HHSN272200700057C
6 · The paper itself

Abstract

Babesiosis is a tick-borne disease caused by eukaryotic Babesia parasites which are morphologically similar to Plasmodium falciparum, the causative agent of malaria in humans. Like Plasmodium, different species of Babesia are tuned to infect different mammalian hosts, including rats, dogs, horses and cattle. Most species of Plasmodium and Babesia possess an essential bifunctional enzyme for nucleotide synthesis and folate metabolism: dihydrofolate reductase-thymidylate synthase. Although thymidylate synthase is highly conserved across organisms, the bifunctional form of this enzyme is relatively uncommon in nature. The structural characterization of dihydrofolate reductase-thymidylate synthase in Babesia bovis, the causative agent of babesiosis in livestock cattle, is reported here. The apo state is compared with structures that contain dUMP, NADP and two different antifolate inhibitors: pemetrexed and raltitrexed. The complexes reveal modes of binding similar to that seen in drug-resistant malaria strains and point to the utility of applying structural studies with proven cancer chemotherapies towards infectious disease research.

Indexed as

ApoproteinsBabesia bovisCrystallography, X-RayEnzyme InhibitorsLigandsModels, MolecularMultienzyme ComplexesProtein BindingProtein Structure, QuaternaryProtein Structure, TertiaryStructural Homology, ProteinSubstrate SpecificityTetrahydrofolate DehydrogenaseThymidylate SynthaseApoproteinsEnzyme InhibitorsLigandsMultienzyme ComplexesTetrahydrofolate DehydrogenaseThymidylate Synthasethymidylate synthase-dihydrofolate reductase

Identifiers

PMID21904052
PMCPMC3169404
OpenAlexW2044926508

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.