Evidence map›Paper›PMID 29364904›Full record

ArticlePloS one2018

Development of an activity-based probe for acyl-protein thioesterases.

Megan Garland, Christopher J Schulze, Ian T Foe, Wouter A van der Linden, Matthew A Child, Matthew Bogyo

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

9 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. 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.

Megan GarlandCancer Biology Program, Stanford University School of Medicine, Stanford, California, United States of America.
Christopher J SchulzeDepartment of Pathology, Stanford University School of Medicine, Stanford, California, United States of America.
Ian T FoeDepartment of Pathology, Stanford University School of Medicine, Stanford, California, United States of America.
Wouter A van der LindenDepartment of Pathology, Stanford University School of Medicine, Stanford, California, United States of America.
Matthew A ChildDepartment of Pathology, Stanford University School of Medicine, Stanford, California, United States of America.
Matthew BogyoCancer Biology Program, Stanford University School of Medicine, Stanford, California, United States of America.ORCID 0000-0003-3753-4412
Stanford University · US

Funding

MOLECULAR BASIS OF HOST-PARASITE INTERACTIONT32AI007328 · NIAID · STANFORD UNIVERSITY · PI JUSTIN L SONNENBURG · 1987 to 2026
$11.9M
Equipment supplement for Chemical methods to study protein palmitoylation pathwaysR01GM111703 · NIGMS · STANFORD UNIVERSITY · PI BOGYO, MATTHEW · 2014 to 2017
$1.6M
NIGMS NIH HHS R01 GM111703NIH HHS R01 GM111703
6 · The paper itself

Abstract

Protein palmitoylation is a dynamic post-translational modification (PTM) important for cellular functions such as protein stability, trafficking, localization, and protein-protein interactions. S-palmitoylation occurs via the addition of palmitate to cysteine residues via a thioester linkage, catalyzed by palmitoyl acyl transferases (PATs), with removal of the palmitate catalyzed by acyl protein thioesterases (APTs) and palmitoyl-protein thioesterases (PPTs). Tools that target the regulators of palmitoylation-PATs, APTs and PPTs-will improve understanding of this essential PTM. Here, we describe the synthesis and application of a cell-permeable activity-based probe (ABP) that targets APTs in intact mammalian cells and the parasite Toxoplasma gondii. Using a focused library of substituted chloroisocoumarins, we identified a probe scaffold with nanomolar affinity for human APTs (HsAPT1 and HsAPT2) and synthesized a fluorescent ABP, JCP174-BODIPY TMR (JCP174-BT). We use JCP174-BT to profile HsAPT activity in situ in mammalian cells, to detect an APT in T. gondii (TgPPT1). We show discordance between HsAPT activity levels and total protein concentration in some cell lines, indicating that total protein levels may not be representative of APT activity in complex systems, highlighting the utility of this probe.

Indexed as

AnimalsMammalsMolecular ProbesProtein Processing, Post-TranslationalThiolester HydrolasesToxoplasmaMolecular Probespalmitoyl-protein thioesteraseThiolester Hydrolases

Identifiers

PMID29364904
PMCPMC5783350
OpenAlexW2792967544

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.