Evidence map›Paper›PMID 33839157›Full record

ReviewThe Journal of biological chemistry

Major advances in targeted protein degradation: PROTACs, LYTACs, and MADTACs.

Shanique B Alabi, Craig M Crews

Abstract readReview
In one paragraph

Review in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 119 papers.

0numbers the graph read from it
0cells of the map it votes in
119citing 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

119 citing papers in PubMed.

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  7. AbioRxiv : the preprint server for biology · 2026
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59 more citing papers are in PubMed but not listed here.

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.

Shanique B AlabiDepartment of Pharmacology, Yale University, New Haven, Connecticut, USA.
Craig M CrewsDepartment of Pharmacology, Yale University, New Haven, Connecticut, USA; Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut, USA; Department of Chemistry, Yale University, New Haven, Connecticut, USA. Electronic address: craig.crews@yale.edu.

Funding

Inducing Proximity: An Emerging Paradigm for New Therapeutic ModalitiesR35CA197589 · NCI · YALE UNIVERSITY · PI CRAIG M CREWS · 2015 to 2026
$10.7M
Howard Hughes Medical InstituteNCI NIH HHS R35 CA197589
6 · The paper itself

Abstract

Of late, targeted protein degradation (TPD) has surfaced as a novel and innovative chemical tool and therapeutic modality. By co-opting protein degradation pathways, TPD facilitates complete removal of the protein molecules from within or outside the cell. While the pioneering Proteolysis-Targeting Chimera (PROTAC) technology and molecular glues hijack the ubiquitin-proteasome system, newer modalities co-opt autophagy or the endo-lysosomal pathway. Using this mechanism, TPD is posited to largely expand the druggable space far beyond small-molecule inhibitors. In this review, we discuss the major advances in TPD, highlight our current understanding, and explore outstanding questions in the field.

Indexed as

LysosomesProteasome Endopeptidase ComplexProteinsProteolysisUbiquitinationProteasome Endopeptidase ComplexProteinsAUTACschemical biologydrug actionlysosomeLYTACsmolecular gluesPROTACsprotein degradationubiquitination

Identifiers

PMID33839157
PMCPMC8131913

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.