Evidence map›Paper›PMID 28221344›Full record

ArticleNature chemistry2017

Chemoproteomic profiling and discovery of protein electrophiles in human cells.

Megan L Matthews, Lin He, Benjamin D Horning, Erika J Olson, Bruno E Correia, John R Yates, Philip E Dawson, Benjamin F Cravatt

Open access · greenAbstract read
In one paragraph

Article in Nature chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

42 citing papers in PubMed, 90 citations in OpenAlex.

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  6. Covalent Proximity Inducers.Chemical reviews · 2025
    Review
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  17. Characterizing metabolic drivers ofFrontiers in pharmacology · 2023
    Article
  18. Article
  19. Advances in covalent drug discovery.Nature reviews. Drug discovery · 2022
    Review
  20. 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

8 authors at 1 institution in 3 countries.

Megan L MatthewsChemical Physiology, The Scripps Research Institute, La Jolla, California 92037, USA.ORCID 0000-0003-1178-4616
Lin HeChemical Physiology, The Scripps Research Institute, La Jolla, California 92037, USA.
Benjamin D HorningChemical Physiology, The Scripps Research Institute, La Jolla, California 92037, USA.
Erika J OlsonChemistry and Cell and Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
Bruno E CorreiaChemical Physiology, The Scripps Research Institute, La Jolla, California 92037, USA.
John R YatesChemical Physiology, The Scripps Research Institute, La Jolla, California 92037, USA.
Philip E DawsonChemistry and Cell and Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
Benjamin F CravattChemical Physiology, The Scripps Research Institute, La Jolla, California 92037, USA.
Scripps Research Institute · US

Funding

TrainingP41GM103533 · NIGMS · UNIVERSITY OF WASHINGTON · PI MACCOSS, MICHAEL · 2012 to 2021
$20.7M
TRAININGU54GM114833 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LINDSEY, MERRY L., PING, PEIPEI · 2014 to 2017
$13.8M
Chemical Probes for Metabolic Pathway Discovery in Human DiseaseR01CA132630 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI CRAVATT, BENJAMIN F · 2007 to 2018
$5.1M
NCI NIH HHS R01 CA132630NIGMS NIH HHS P41 GM103533NIGMS NIH HHS U54 GM114833
6 · The paper itself

Abstract

Activity-based protein profiling (ABPP) serves as a chemical proteomic platform to discover and characterize functional amino acids in proteins on the basis of their enhanced reactivity towards small-molecule probes. This approach, to date, has mainly targeted nucleophilic functional groups, such as the side chains of serine and cysteine, using electrophilic probes. Here we show that 'reverse-polarity' (RP)-ABPP using clickable, nucleophilic hydrazine probes can capture and identify protein-bound electrophiles in cells. Using this approach, we demonstrate that the pyruvoyl cofactor of S-adenosyl-L-methionine decarboxylase (AMD1) is dynamically controlled by intracellular methionine concentrations. We also identify a heretofore unknown modification-an N-terminally bound glyoxylyl group-in the poorly characterized protein secernin-3. RP-ABPP thus provides a versatile method to monitor the metabolic regulation of electrophilic cofactors and discover novel types of electrophilic modifications on proteins in human cells.

Indexed as

ProteomicsAdenosylmethionine DecarboxylaseAmino AcidsCell SurvivalFluorescent DyesHEK293 CellsHumansHydrazinesMethionineMolecular StructureNerve Tissue ProteinsAdenosylmethionine DecarboxylaseAMD1 protein, humanAmino AcidsFluorescent DyeshydrazineHydrazinesMethionineNerve Tissue Proteins

Identifiers

PMID28221344
PMCPMC5325178
OpenAlexW2542506435

What OpenQuestion holds

Textmetadata
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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.