Evidence map›Paper›PMID 28815215›Full record

ArticlemSphere

Structural Characterization of Acidic M17 Leucine Aminopeptidases from the TriTryps and Evaluation of Their Role in Nutrient Starvation in

Jennifer Timm, Maria Valente, Daniel García-Caballero, Keith S Wilson, Dolores González-Pacanowska

Open access · goldAbstract read
In one paragraph

Article in mSphere. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.1field-weighted citation impact, top 21% 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

8 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. KBE009: A Bestatin-Like Inhibitor of theLife (Basel, Switzerland) · 2021
    Article
  5. Article
  6. Article
  7. Article
  8. 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

5 authors at 3 institutions in 2 countries.

Jennifer TimmStructural Biology Laboratory, Department of Chemistry, University of York, York, United Kingdom.
Maria ValenteInstituto de Parasitología y Biomedicina López-Neyra, Consejo Superior de Investigaciones Científicas, Parque Tecnológico de Ciencias de la Salud, Armilla, Granada, Spain.
Daniel García-CaballeroInstituto de Parasitología y Biomedicina López-Neyra, Consejo Superior de Investigaciones Científicas, Parque Tecnológico de Ciencias de la Salud, Armilla, Granada, Spain.
Keith S WilsonStructural Biology Laboratory, Department of Chemistry, University of York, York, United Kingdom.
Dolores González-PacanowskaInstituto de Parasitología y Biomedicina López-Neyra, Consejo Superior de Investigaciones Científicas, Parque Tecnológico de Ciencias de la Salud, Armilla, Granada, Spain.
Consejo Superior de Investigaciones Científicas · ESUniversity of York · GBInstituto de Parasitología y Biomedicina "López - Neyra" · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Leucine aminopeptidase (LAP) is found in all kingdoms of life and catalyzes the metal-dependent hydrolysis of the N-terminal amino acid residue of peptide or amino acyl substrates. LAPs have been shown to participate in the N-terminal processing of certain proteins in mammalian cells and in homologous recombination and transcription regulation in bacteria, while in parasites, they are involved in host cell invasion and provision of essential amino acids for growth. The enzyme is essential for survival in

Indexed as

crystallographyknockoutLeishmania majorleucine aminopeptidaseTrypanosoma bruceiTrypanosoma cruzi

Identifiers

PMID28815215
PMCPMC5557676
OpenAlexW2747588301

What Socratic 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 Socratic graph.