Evidence map›Paper›PMID 29562352›Full record

ArticleNucleic acids research2018

Structural basis for LeishIF4E-1 modulation by an interacting protein in the human parasite Leishmania major.

Shimi Meleppattu, Haribabu Arthanari, Alexandra Zinoviev, Andras Boeszoermenyi, Gerhard Wagner, Michal Shapira, Mélissa Léger-Abraham

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

17 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. LeishIF3d is a non-canonical cap-binding protein inFrontiers in molecular biosciences · 2023
    Article
  4. Article
  5. Characterization of an Atypical eIF4E Ortholog inInternational journal of molecular sciences · 2021
    Article
  6. Article
  7. LeishIF4E-5 Is a Promastigote-Specific Cap-Binding Protein inInternational journal of molecular sciences · 2021
    Article
  8. Review
  9. Computational study on the allosteric mechanism ofComputational and structural biotechnology journal · 2021
    Article
  10. Article
  11. Biomolecular NMR assignments · 2020
    Article
  12. Article
  13. eIF4E and Interactors from Unicellular Eukaryotes.International journal of molecular sciences · 2020
    Review
  14. Article
  15. Article
  16. Article
  17. 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

7 authors at 2 institutions in 2 countries.

Shimi MeleppattuDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115, USA.
Haribabu ArthanariDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Alexandra ZinovievDepartment of Life Sciences, Ben-Gurion University of the Negev, Beer Sheva 84105, Israel.
Andras BoeszoermenyiDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Gerhard WagnerDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Michal ShapiraDepartment of Life Sciences, Ben-Gurion University of the Negev, Beer Sheva 84105, Israel.
Mélissa Léger-AbrahamDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115, USA.
Harvard University · USBen-Gurion University of the Negev · IL

Funding

Harvard Clinical and Translational Science CenterUL1TR001102 · NCATS · HARVARD MEDICAL SCHOOL · PI NADLER, LEE MARSHALL · 2013 to 2017
$106.2M
Roles of Eukaryotic Translation Initiation Factors in Gene ExpressionR01CA200913 · NCI · HARVARD MEDICAL SCHOOL · PI WAGNER, GERHARD · 2016 to 2020
$2.3M
The translation apparatus of Leishmania: from basic analysis to pursuit of novelR01AI108718 · NIAID · HARVARD MEDICAL SCHOOL · PI WAGNER, GERHARD · 2014 to 2017
$1.4M
Structural Basis for Translation Initiation in Leishmania MajorR21AI156087 · NIAID · HARVARD MEDICAL SCHOOL · PI LEGER-ABRAHAM, MELISSA · 2021 to 2022
$465k
NCATS NIH HHS UL1 TR001102NCI NIH HHS R01 CA200913NIAID NIH HHS R01 AI108718NIAID NIH HHS R21 AI156087
6 · The paper itself

Abstract

Leishmania parasites are unicellular pathogens that are transmitted to humans through the bite of infected sandflies. Most of the regulation of their gene expression occurs post-transcriptionally, and the different patterns of gene expression required throughout the parasites' life cycle are regulated at the level of translation. Here, we report the X-ray crystal structure of the Leishmania cap-binding isoform 1, LeishIF4E-1, bound to a protein fragment of previously unknown function, Leish4E-IP1, that binds tightly to LeishIF4E-1. The molecular structure, coupled to NMR spectroscopy experiments and in vitro cap-binding assays, reveal that Leish4E-IP1 allosterically destabilizes the binding of LeishIF4E-1 to the 5' mRNA cap. We propose mechanisms through which Leish4E-IP1-mediated LeishIF4E-1 inhibition could regulate translation initiation in the human parasite.

Indexed as

Protein BiosynthesisCrystallography, X-RayEukaryotic Initiation Factor-4EGene Expression RegulationHumansLeishmania majorLeishmaniasis, CutaneousStructure-Activity RelationshipEukaryotic Initiation Factor-4E

Identifiers

PMID29562352
PMCPMC5909430
OpenAlexW2789930720

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.