Evidence map›Paper›PMID 30486612›Full record

ReviewMolecules and cells2018

Chemically Induced Cellular Proteolysis: An Emerging Therapeutic Strategy for Undruggable Targets.

Seonghyeon Moon, Byung-Hoon Lee

Open access · greenAbstract readReview
In one paragraph

Review in Molecules and cells, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

29 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Exploration of the Tunability of BRD4 Degradation by DCAF16bioRxiv : the preprint server for biology · 2023
    Article
  6. Facile Synthesis of Homodimeric Protein Ligands.Chembiochem : a European journal of chemical biology · 2023
    Article
  7. Article
  8. E3 ubiquitin ligase on the biological properties of hematopoietic stem cell.Journal of molecular medicine (Berlin, Germany) · 2023
    Review
  9. Article
  10. Review
  11. Review
  12. Review
  13. Applications and Limitations of Oxime-Linked "Split PROTACs".Chembiochem : a European journal of chemical biology · 2022
    Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Small-Molecule Inhibitors Targeting Proteasome-Associated Deubiquitinases.International journal of molecular sciences · 2021
    Review
  19. Review
  20. Chronic lung diseases: prospects for regeneration and repair.European respiratory review : an official journal of the European Respiratory Society · 2021
    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

2 authors at 1 institution in 1 country.

Seonghyeon MoonDepartment of New Biology, DGIST, Daegu 42988, Korea.
Byung-Hoon LeeDepartment of New Biology, DGIST, Daegu 42988, Korea.
Daegu Gyeongbuk Institute of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Traditionally, small-molecule or antibody-based therapies against human diseases have been designed to inhibit the enzymatic activity or compete for the ligand binding sites of pathological target proteins. Despite its demonstrated effectiveness, such as in cancer treatment, this approach is often limited by recurring drug resistance. More importantly, not all molecular targets are enzymes or receptors with druggable 'hot spots' that can be directly occupied by active site-directed inhibitors. Recently, a promising new paradigm has been created, in which small-molecule chemicals harness the naturally occurring protein quality control machinery of the ubiquitin-proteasome system to specifically eradicate disease-causing proteins in cells. Such 'chemically induced protein degradation' may provide unprecedented opportunities for targeting proteins that are inherently undruggable, such as structural scaffolds and other non-enzymatic molecules, for therapeutic purposes. This review focuses on surveying recent progress in developing E3-guided proteolysis-targeting chimeras (PROTACs) and small-molecule chemical modulators of deubiquitinating enzymes upstream of or on the proteasome.

Indexed as

ProteolysisAnimalsDrug DesignHumansMolecular Targeted TherapyProteasome Endopeptidase ComplexSmall Molecule LibrariesUbiquitinUbiquitinationUbiquitin-Protein LigasesProteasome Endopeptidase ComplexSmall Molecule LibrariesUbiquitinUbiquitin-Protein Ligasesdeubiquitinating enzymeinduced proteolysisPROTACsmall-moleculesubiquitin-proteasome systemundruggable target

Identifiers

PMID30486612
PMCPMC6277563
OpenAlexW2987737568

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.