Evidence map›Paper›PMID 33256092›Full record

ReviewBiology2020

Targeted Protein Degradation Tools: Overview and Future Perspectives.

Yuri Prozzillo, Gaia Fattorini, Maria Virginia Santopietro, Luigi Suglia, Alessandra Ruggiero, Diego Ferreri, Giovanni Messina

Abstract readReview
In one paragraph

Review in Biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Article
  2. Article
  3. Inhibition of mitochondrial dynamics inFrontiers in cell and developmental biology · 2026
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Degron-based bioPROTACs for controlling signaling in CAR T cells.bioRxiv : the preprint server for biology · 2024
    Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

7 authors.

Yuri ProzzilloDepartment of Biology and Biotechnology "Charles Darwin", Sapienza University of Rome, 00185 Rome, Italy.ORCID 0000-0002-6457-8552
Gaia FattoriniDepartment of Biology and Biotechnology "Charles Darwin", Sapienza University of Rome, 00185 Rome, Italy.
Maria Virginia SantopietroDepartment of Biology and Biotechnology "Charles Darwin", Sapienza University of Rome, 00185 Rome, Italy.
Luigi SugliaDepartment of Biology and Biotechnology "Charles Darwin", Sapienza University of Rome, 00185 Rome, Italy.
Alessandra RuggieroDepartment of Clinical Infection, Microbiology and Immunology, Institute of Infection and Global Health, University of Liverpool, Liverpool L69 3BX, UK.
Diego FerreriDepartment of Biology and Biotechnology "Charles Darwin", Sapienza University of Rome, 00185 Rome, Italy.ORCID 0000-0003-1756-1413
Giovanni MessinaDepartment of Biology and Biotechnology "Charles Darwin", Sapienza University of Rome, 00185 Rome, Italy.ORCID 0000-0002-7597-4972

Funding

Istituto Pasteur-Fondazione Cenci Bolognetti Teresa Ariaudo
6 · The paper itself

Abstract

Targeted protein inactivation (TPI) is an elegant approach to investigate protein function and its role in the cellular landscape, overcoming limitations of genetic perturbation strategies. These systems act in a reversible manner and reduce off-target effects exceeding the limitations of CRISPR/Cas9 and RNA interference, respectively. Several TPI have been developed and wisely improved, including compartment delocalization tools and protein degradation systems. However, unlike chemical tools such as PROTACs (PROteolysis TArgeting Chimeras), which work in a wild-type genomic background, TPI technologies require adding an aminoacidic signal sequence (tag) to the protein of interest (POI). On the other hand, the design and optimization of PROTACs are very laborious and time-consuming. In this review, we focus on anchor-away, deGradFP, auxin-inducible degron (AID) and dTAG technologies and discuss their recent applications and advances. Finally, we propose nano-grad, a novel nanobody-based protein degradation tool, which specifically proteolyzes endogenous tag-free target protein.

Indexed as

anchor-awaydeGradFPdegrondTAGFKBP12nanobodynano-gradtargeted protein degradation (TPD)targeted protein inactivation (TPI)von Hippel–Lindau (VHL)

Identifiers

PMID33256092
PMCPMC7761331

What OpenQuestion holds

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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.