Evidence map›Paper›PMID 35311258›Full record

ArticleJournal of the American Chemical Society2022

Hijacking Methyl Reader Proteins for Nuclear-Specific Protein Degradation.

Dhanusha A Nalawansha, Ke Li, John Hines, Craig M Crews

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

17 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Article
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  5. Article
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  7. Article
  8. Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Chemical tools targeting readers of lysine methylation.Current opinion in chemical biology · 2023
    Review
  15. Article
  16. Review
  17. PROTACs: past, present and future.Chemical Society reviews · 2022
    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

4 authors at 1 institution in 1 country.

Dhanusha A NalawanshaDepartment of Molecular, Cellular and Developmental Biology, Yale University, New Haven, Connecticut 06511, United States.
Ke LiDepartment of Molecular, Cellular and Developmental Biology, Yale University, New Haven, Connecticut 06511, United States.
John HinesDepartment of Molecular, Cellular and Developmental Biology, Yale University, New Haven, Connecticut 06511, United States.
Craig M CrewsDepartment of Molecular, Cellular and Developmental Biology, Yale University, New Haven, Connecticut 06511, United States.ORCID 0000-0002-8456-2005
Yale University · US

Funding

Inducing Proximity: An Emerging Paradigm for New Therapeutic ModalitiesR35CA197589 · NCI · YALE UNIVERSITY · PI CRAIG M CREWS · 2015 to 2026
$10.7M
Developing Tumor-specific PROTACsR01CA238570 · NCI · YALE UNIVERSITY · PI CREWS, CRAIG M · 2019 to 2023
$1.9M
NCI NIH HHS R01 CA238570NCI NIH HHS R35 CA197589
6 · The paper itself

Abstract

Targeted protein degradation (TPD) by PROTACs is a promising strategy to control disease-causing protein levels within the cell. While TPD is emerging as an innovative drug discovery paradigm, there are currently only a limited number of E3 ligase:ligand pairs that are employed to induce protein degradation. Herein, we report a novel approach to induce protein degradation by hijacking a methyl reader:E3 ligase complex. L3MBTL3 is a methyl-lysine reader protein that binds to the Cul4

Indexed as

Nuclear ProteinsUbiquitin-Protein LigasesDrug DiscoveryLigandsProteolysisLigandsNuclear ProteinsUbiquitin-Protein Ligases

Identifiers

PMID35311258
PMCPMC10331457
OpenAlexW4220821279

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.