Evidence map›Paper›PMID 31772212›Full record

ArticleScientific reports2019

Functional annotation of serine hydrolases in the asexual erythrocytic stage of Plasmodium falciparum.

Rubayet Elahi, W Keith Ray, Christie Dapper, Seema Dalal, Richard F Helm, Michael Klemba

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

11 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Study of dense granule proteins inFrontiers in immunology · 2025
    Article
  3. Article
  4. Metabolism of host lysophosphatidylcholine inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Discovery ofFrontiers in pharmacology · 2022
    Article
  10. Article
  11. 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

6 authors at 1 institution in 1 country.

Rubayet ElahiDepartment of Biochemistry, Virginia Tech, Blacksburg, VA, 24061, USA.
W Keith RayDepartment of Biochemistry, Virginia Tech, Blacksburg, VA, 24061, USA.
Christie DapperDepartment of Biochemistry, Virginia Tech, Blacksburg, VA, 24061, USA.
Seema DalalDepartment of Biochemistry, Virginia Tech, Blacksburg, VA, 24061, USA.
Richard F HelmDepartment of Biochemistry, Virginia Tech, Blacksburg, VA, 24061, USA.
Michael KlembaDepartment of Biochemistry, Virginia Tech, Blacksburg, VA, 24061, USA. klemba@vt.edu.
Virginia Tech · US

Funding

Chemo-proteomic discovery of lipases in asexual and sexual erythrocytic stages of Plasmodium falciparumR21AI133136 · NIAID · VIRGINIA POLYTECHNIC INST AND ST UNIV · PI KLEMBA, MICHAEL · 2017 to 2018
$380k
National Institute of Allergy and Infectious Diseases, United States AI133136NIAID NIH HHS R21 AI133136
6 · The paper itself

Abstract

Enzymes of the serine hydrolase superfamily are ubiquitous, highly versatile catalysts that mediate a wide variety of metabolic reactions in eukaryotic cells, while also being amenable to selective inhibition. We have employed a fluorophosphonate-based affinity capture probe and mass spectrometry to explore the expression profile and metabolic roles of the 56-member P. falciparum serine hydrolase superfamily in the asexual erythrocytic stage of P. falciparum. This approach provided a detailed census of active serine hydrolases in the asexual parasite, with identification of 21 active serine hydrolases from α/β hydrolase, patatin, and rhomboid protease families. To gain insight into their functional roles and substrates, the pan-lipase inhibitor isopropyl dodecylfluorophosphonate was employed for competitive activity-based protein profiling, leading to the identification of seven serine hydrolases with potential lipolytic activity. We demonstrated how a chemoproteomic approach can provide clues to the specificity of serine hydrolases by using a panel of neutral lipase inhibitors to identify an enzyme that reacts potently with a covalent monoacylglycerol lipase inhibitor. In combination with existing phenotypic data, our studies define a set of serine hydrolases that likely mediate critical metabolic reactions in asexual parasites and enable rational prioritization of future functional characterization and inhibitor development efforts.

Indexed as

BiotinErythrocytesHumansHydrolasesLife Cycle StagesLipolysisPlasmodium falciparumProteomicsProtozoan ProteinsSerineBiotindesthiobiotinHydrolasesProtozoan ProteinsSerine

Identifiers

PMID31772212
PMCPMC6879560
OpenAlexW2990212471

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.