Evidence map›Paper›PMID 21687654›Full record

ArticleEnzyme research2011

Biosynthesis of galactofuranose in kinetoplastids: novel therapeutic targets for treating leishmaniasis and chagas' disease.

Michelle Oppenheimer, Ana L Valenciano, Pablo Sobrado

Open access · diamondAbstract read
In one paragraph

Article in Enzyme research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

25 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Galactofuranose-Related Enzymes: Challenges and Hopes.International journal of molecular sciences · 2020
    Review
  3. Article
  4. Article
  5. Article
  6. Discovery and Genetic Validation of Chemotherapeutic Targets for Chagas' Disease.Frontiers in cellular and infection microbiology · 2018
    Review
  7. Review
  8. Deciphering the sugar biosynthetic pathway and tailoring steps of nucleoside antibiotic A201A unveils a GDP-l-galactose mutase.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Structure, mechanism, and dynamics of UDP-galactopyranose mutase.Archives of biochemistry and biophysics · 2014
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Noncanonical reactions of flavoenzymes.International journal of molecular sciences · 2012
    Review
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

3 authors at 2 institutions in 2 countries.

Michelle OppenheimerDepartment of Biochemistry, Virginia Tech, Blacksburg, VA 24061, USA.
Ana L Valenciano
Pablo Sobrado
Instituto Tecnológico de Costa Rica · CRVirginia Tech · US

Funding

Drug Discovery Consortium for Chagas DiseaseR01AI082542 · NIAID · UNIVERSITY OF GEORGIA · PI TARLETON, RICK L · 2009 to 2010
$2.2M
Mechanistic and structural studies of eukaryotic UDP-galactopyranose mutasesR01GM094469 · NIGMS · VIRGINIA POLYTECHNIC INST AND ST UNIV · PI SOBRADO, PABLO, TANNER, JOHN J · 2010 to 2019
$2.0M
NIAID NIH HHS R01 AI082542NIGMS NIH HHS R01 GM094469
6 · The paper itself

Abstract

Cell surface proteins of parasites play a role in pathogenesis by modulating mammalian cell recognition and cell adhesion during infection. β-Galactofuranose (Galf) is an important component of glycoproteins and glycolipids found on the cell surface of Leishmania spp. and Trypanosoma cruzi. β-Galf-containing glycans have been shown to be important in parasite-cell interaction and protection against oxidative stress. Here, we discuss the role of β-Galf in pathogenesis and recent studies on the Galf-biosynthetic enzymes: UDP-galactose 4' epimerase (GalE), UDP-galactopyranose mutase (UGM), and UDP-galactofuranosyl transferase (GalfT). The central role in Galf formation, its unique chemical mechanism, and the absence of a homologous enzyme in humans identify UGM as the most attractive drug target in the β-Galf-biosynthetic pathway in protozoan parasites.

Identifiers

PMID21687654
PMCPMC3112513
OpenAlexW2074694172

What OpenQuestion holds

Textmetadata
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.