Evidence map›Paper›PMID 33228359›Full record

ArticleACS chemical biology2020

ATE1-Mediated Post-Translational Arginylation Is an Essential Regulator of Eukaryotic Cellular Homeostasis.

Verna Van, Aaron T Smith

Open access · greenAbstract read
In one paragraph

Article in ACS chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.3field-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

21 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. N-degron pathways.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Assaying Arginylation Activity in Cell Lysates Using a Fluorescent Reporter.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  12. Reconstitution of the Arginyltransferase (ATE1) Iron-Sulfur Cluster.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Liquiritin Attenuates Angiotensin II-Induced Cardiomyocyte Hypertrophy via ATE1/TAK1-JNK1/2 Pathway.Evidence-based complementary and alternative medicine : eCAM · 2022
    Article
  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

2 authors at 1 institution in 1 country.

Verna VanDepartment of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, Maryland 21250, United States.
Aaron T SmithDepartment of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, Maryland 21250, United States.ORCID 0000-0002-9332-8683
University of Maryland, Baltimore County · US

Funding

Deciphering the Mechanisms of Pathogenic Ferrous Iron Acquisition and Eukaryotic Post-Translational ArginylationR35GM133497 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI Aaron T Smith · 2019 to 2026
$2.9M
NIGMS NIH HHS R35 GM133497
6 · The paper itself

Abstract

Arginylation is a protein post-translational modification catalyzed by arginyl-tRNA transferases (ATE1s), which are critical enzymes conserved across all eukaryotes. Arginylation is a key step in the Arg N-degron pathway, a hierarchical cellular signaling pathway that links the ubiquitin-dependent degradation of a protein to the identity of its N-terminal amino acid side chain. The fidelity of ATE1-catalyzed arginylation is imperative, as this post-translational modification regulates several essential biological processes such as cardiovascular maturation, chromosomal segregation, and even the stress response. While the process of ATE1-catalyzed arginylation has been studied in detail at the cellular level, much remains unknown about the structure of this important enzyme, its mechanism of action, and its regulation. In this work, we detail the current state of knowledge on ATE1-catalyzed arginylation, and we discuss both ongoing and future directions that will reveal the structural and mechanistic details of this essential eukaryotic cellular regulator.

Indexed as

HomeostasisAminoacyltransferasesAnimalsArginineCatalysisMiceProtein Processing, Post-TranslationalAminoacyltransferasesArginineAte1 protein, mouse

Identifiers

PMID33228359
PMCPMC7749041
OpenAlexW3107567752

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.