Evidence map›Paper›PMID 41147131›Full record

ReviewChembiochem : a European journal of chemical biology2025

Method Overview for Discovering ATE1 Substrates and their Arginylation Sites.

Richard M Searfoss, Benjamin A Garcia, Zongtao Lin

Abstract readReview
In one paragraph

Review in Chembiochem : a European journal of chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Review
  2. Method Overview for Discovering ATE1 Substrates and their Arginylation Sites.Chembiochem : a European journal of chemical biology · 2025
    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

3 authors.

Richard M SearfossDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, 63110, USA.
Benjamin A GarciaDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, 63110, USA.
Zongtao LinDepartment of Medicinal Chemistry, Rutgers University, Piscataway, NJ, 08854, USA.ORCID https://orcid.org/0000-0002-6017-338X

Funding

Research Education ComponentP30AG066444 · NIA · WASHINGTON UNIVERSITY · PI Susan Lynn Stark · 2020 to 2026
$28.7M
Development and Application of Chemical Biology Approaches for Understanding Protein ArginylationR01HL177113 · NHLBI · WASHINGTON UNIVERSITY · PI Benjamin A Garcia, Zongtao Lin · 2025 to 2026
$1.2M
Hijacking Post-translational Arginylation for Targeted Protein DegradationR21CA292191 · NCI · WASHINGTON UNIVERSITY · PI LIN, ZONGTAO, LYU, DONGWEN · 2024 to 2024
$426k
MilliporeSigmaNCI NIH HHS R21 CA292191NHLBI NIH HHS R01 HL177113NIA NIH HHS P30 AG066444NIH HHS P30AG066444NIH HHS R01HL177113NIH HHS R21CA292191
6 · The paper itself

Abstract

Arginylation is a protein modification event in which cellular machinery recognizes a conserved N-terminal or side-chain motif and post-translationally installs an arginine residue to signal a protein for degradation. This modification affects protein function, stability, and half-life and is essential to proper functions in mammalian systems. Since its discovery in the early 1960s, scientists have struggled to broadly characterize this modification in its canonical function outside of a handful of specific cases. It is known to be an essential cellular mark, as loss of the installation enzyme is embryonically lethal. However, the discovery of the substrates regulated by this mark has been slow and has required some creativity by the scientists who have chased it. Over the course of roughly six decades, the library of substrates has consistently grown through various applications. Here, we seek to summarize all approaches that have been applied to discovering and studying arginylation.

Indexed as

AminoacyltransferasesArginineAnimalsHumansProtein Processing, Post-TranslationalSubstrate SpecificityAminoacyltransferasesArgininearginyltransferasearginylationATE1cDNA screeningproteomicsradiolabeling

Identifiers

PMID41147131
PMCPMC12666246

What OpenQuestion holds

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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.