Evidence map›Paper›PMID 24817714›Full record

ArticleActa crystallographica. Section F, Structural biology communications2014

Structure of tyrosine aminotransferase from Leishmania infantum.

M A Moreno, A Abramov, J Abendroth, A Alonso, S Zhang, P J Alcolea, T Edwards, D Lorimer, P J Myler, V Larraga

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

12 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. L-Asparaginase of Leishmania donovani: Metabolic target and its role in Amphotericin B resistance.International journal for parasitology. Drugs and drug resistance · 2017
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Tyrosine aminotransferase from Leishmania infantum: A new drug target candidate.International journal for parasitology. Drugs and drug resistance · 2014
    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

10 authors at 5 institutions in 2 countries.

M A MorenoDepartamento de Microbiología Molecular, Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC), Calle Ramiro de Maeztu 9, 28040 Madrid, Spain.
A AbramovSeattle Structural Genomics Center for Infectious Disease (SSGCID), USA.
J AbendrothSeattle Structural Genomics Center for Infectious Disease (SSGCID), USA.
A AlonsoDepartamento de Microbiología Molecular, Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC), Calle Ramiro de Maeztu 9, 28040 Madrid, Spain.
S ZhangSeattle Structural Genomics Center for Infectious Disease (SSGCID), USA.
P J AlcoleaDepartamento de Microbiología Molecular, Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC), Calle Ramiro de Maeztu 9, 28040 Madrid, Spain.
T EdwardsSeattle Structural Genomics Center for Infectious Disease (SSGCID), USA.
D LorimerSeattle Structural Genomics Center for Infectious Disease (SSGCID), USA.
P J MylerSeattle Structural Genomics Center for Infectious Disease (SSGCID), USA.
V LarragaDepartamento de Microbiología Molecular, Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC), Calle Ramiro de Maeztu 9, 28040 Madrid, Spain.
Centro de Investigaciones Biológicas Margarita Salas · ESJoint Center for Structural Genomics · USNorth Seattle College · USCenter for Infectious Disease Research · USConsejo Superior de Investigaciones Científicas · ES

Funding

NIAID NIH HHS HHSN272201200025C
6 · The paper itself

Abstract

The trypanosomatid parasite Leishmania infantum is the causative agent of visceral leishmaniasis (VL), which is usually fatal unless treated. VL has an incidence of 0.5 million cases every year and is an important opportunistic co-infection in HIV/AIDS. Tyrosine aminotransferase (TAT) has an important role in the metabolism of trypanosomatids, catalyzing the first step in the degradation pathway of aromatic amino acids, which are ultimately converted into their corresponding L-2-oxoacids. Unlike the enzyme in Trypanosoma cruzi and mammals, L. infantum TAT (LiTAT) is not able to transaminate ketoglutarate. Here, the structure of LiTAT at 2.35 Å resolution is reported, and it is confirmed that the presence of two Leishmania-specific residues (Gln55 and Asn58) explains, at least in part, this specific reactivity. The difference in substrate specificity between leishmanial and mammalian TAT and the importance of this enzyme in parasite metabolism suggest that it may be a useful target in the development of new drugs against leishmaniasis.

Indexed as

Leishmania infantumProtein Structure, SecondaryProtein Structure, TertiaryTyrosine TransaminaseX-Ray DiffractionTyrosine TransaminaseLeishmania infantumtyrosine aminotransferase

Identifiers

PMID24817714
PMCPMC4014323
OpenAlexW2082383834

What OpenQuestion holds

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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.