Evidence map›Paper›PMID 35702041›Full record

ReviewJournal of enzyme inhibition and medicinal chemistry2022

Proteolysis-targeting chimaeras (PROTACs) as pharmacological tools and therapeutic agents: advances and future challenges.

Chao Wang, Yujing Zhang, Tingting Zhang, Lingyu Shi, Zhongmin Geng, Dongming Xing

Abstract readReview
In one paragraph

Review in Journal of enzyme inhibition and medicinal chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Review
  2. Article
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  6. 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

6 authors.

Chao WangThe Affiliated Hospital of Qingdao University, Qingdao University, Qingdao Cancer Institute, Qingdao, China.
Yujing ZhangThe Affiliated Cardiovascular Hospital of Qingdao University, Qingdao University, Qingdao, China.
Tingting ZhangThe Affiliated Hospital of Qingdao University, Qingdao University, Qingdao Cancer Institute, Qingdao, China.
Lingyu ShiThe Affiliated Hospital of Qingdao University, Qingdao University, Qingdao Cancer Institute, Qingdao, China.
Zhongmin GengThe Affiliated Hospital of Qingdao University, Qingdao University, Qingdao Cancer Institute, Qingdao, China.
Dongming XingThe Affiliated Hospital of Qingdao University, Qingdao University, Qingdao Cancer Institute, Qingdao, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteolysis-targeting chimaeras (PROTACs) have been developed to be an emerging technology for targeted protein degradation and attracted the favour of academic institutions, large pharmaceutical enterprises, and biotechnology companies. The mechanism is based on the inhibition of protein function by hijacking a ubiquitin E3 ligase for protein degradation. The heterobifunctional PROTACs contain a ligand for recruiting an E3 ligase, a linker, and another ligand to bind with the protein targeted for degradation. To date, PROTACs targeting ∼70 proteins, many of which are clinically validated drug targets, have been successfully developed with several in clinical trials for diseases therapy. In this review, the recent advances in PROTACs against clinically validated drug targets are summarised and the chemical structure, cellular and

Indexed as

ProteinsUbiquitin-Protein LigasesIntercellular Signaling Peptides and ProteinsLigandsProteolysisIntercellular Signaling Peptides and ProteinsLigandsProteinssnake venom protein C activatorUbiquitin-Protein Ligasesin clinicalpromising treatmentPROTACstargeted protein degradation

Identifiers

PMID35702041
PMCPMC9225776

What OpenQuestion holds

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LicenceCC BY
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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.