Evidence map›Paper›PMID 35101210›Full record

ArticleMethods in enzymology2022

Chemoproteomic interrogation of selenocysteine by low-pH isoTOP-ABPP.

Daniel W Bak, Eranthie Weerapana

Open access · greenAbstract read
In one paragraph

Article in Methods in enzymology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
1.3field-weighted citation impact, top 26% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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

2 authors at 1 institution in 1 country.

Daniel W BakDepartment of Chemistry, Boston College, Chestnut Hill, MA, United States. Electronic address: bakd@bc.edu.
Eranthie WeerapanaDepartment of Chemistry, Boston College, Chestnut Hill, MA, United States. Electronic address: eranthie@bc.edu.
Boston College · US

Funding

Developing chemical-proteomic tools to investigate cysteine oxidationR35GM134964 · NIGMS · BOSTON COLLEGE · PI WEERAPANA, ERANTHIE · 2020 to 2024
$3.1M
NIGMS NIH HHS R35 GM134964
6 · The paper itself

Abstract

Selenoproteins comprise a small group of selenocysteine (Sec) containing proteins, often involved in redox homeostasis. While Sec is functionally similar to cysteine (Cys), with both acting as protein-centered nucleophiles, chemoproteomic strategies employing electrophilic probes have often failed to rigorously identify Sec residues, due to their relatively low abundance with respect to Cys across a proteome. To improve the enrichment and detection of selenoproteins, herein we describe a chemoproteomic strategy that relies on the unique properties of Sec as compared to Cys, such as reduced pK

Indexed as

SeleniumSelenocysteineAnimalsCysteineHydrogen-Ion ConcentrationMiceProteomeSelenoproteinsCysteineProteomeSeleniumSelenocysteineSelenoproteinsChemoproteomicsIodoacetamide-alkyneIsoTOP-ABPPSelenocysteineSelenoproteins

Identifiers

PMID35101210
PMCPMC9558968
OpenAlexW4210602229

What OpenQuestion holds

Textmetadata
LicenceTDM
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.