Evidence map›Paper›PMID 31200855›Full record

ReviewDrug discovery today. Technologies2019

PROteolysis TArgeting Chimeras (PROTACs) - Past, present and future.

Mariell Pettersson, Craig M Crews

Abstract readReview
In one paragraph

Review in Drug discovery today. Technologies, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 355 papers.

0numbers the graph read from it
0cells of the map it votes in
355citing 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

355 citing papers in PubMed.

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295 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.

Mariell PetterssonDepartment of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06511, USA.
Craig M CrewsDepartment of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06511, 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
NCI NIH HHS R35 CA197589
6 · The paper itself

Abstract

The majority of currently used therapeutics are small molecule-based and utilize occupancy-driven pharmacology as the mode of action (MOA), in which the protein function is modulated via temporary inhibition. New modalities that operate using alternative MOAs are essential for tapping into the "undruggable" proteome. The PROteolysis Targeting Chimera (PROTAC) technology provides an attractive new approach that utilizes an event-driven MOA. Small molecule-based heterobifunctional PROTACs modulate protein target levels by hijacking the ubiquitin-proteasome system to induce degradation of the target. Here, we address important milestones in the development of the PROTAC technology, as well as emphasize key findings from this previous year and highlight future directions of this promising drug discovery modality.

Indexed as

Drug DiscoveryProteolysisAnimalsHumansProteasome Endopeptidase ComplexUbiquitin-Protein LigasesProteasome Endopeptidase ComplexUbiquitin-Protein Ligases

Identifiers

PMID31200855
PMCPMC6578591

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.