Evidence map›Paper›PMID 38990186›Full record

ReviewBioconjugate chemistry2024

Targeted Protein Degradation (TPD) for Immunotherapy: Understanding Proteolysis Targeting Chimera-Driven Ubiquitin-Proteasome Interactions.

Rajamanikkam Kamaraj, Subhrojyoti Ghosh, Souvadra Das, Shinjini Sen, Priyanka Kumar, Madhurima Majumdar, Renesa Dasgupta, Sampurna Mukherjee, Shrimanti Das, Indrilla Ghose and 4 more

Abstract readReview
In one paragraph

Review in Bioconjugate chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Review
  2. Article
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  9. Review
  10. Review
  11. A novel HPβCD-Cu(DDC)Scientific reports · 2025
    Article
  12. Article
  13. Review
  14. Article
  15. 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

14 authors.

Rajamanikkam KamarajDepartment of Pharmacology and Toxicology, Faculty of Pharmacy, Charles University in Prague, Heyrovskeho 1203, 50005 Hradec Kralove, Czech Republic.ORCID 0000-0001-7115-0178
Subhrojyoti GhoshDepartment of Biotechnology, Indian Institute of Technology Madras, Chennai 600036, India.ORCID 0000-0003-1528-423X
Souvadra DasDepartment of Biotechnology, Heritage Institute of Technology, Kolkata 700107, India.
Shinjini SenDepartment of Biotechnology, Heritage Institute of Technology, Kolkata 700107, India.
Priyanka KumarDepartment of Biotechnology, Heritage Institute of Technology, Kolkata 700107, India.
Madhurima MajumdarDepartment of Biotechnology, Heritage Institute of Technology, Kolkata 700107, India.
Renesa DasguptaDepartment of Biotechnology, Heritage Institute of Technology, Kolkata 700107, India.
Sampurna MukherjeeDepartment of Biotechnology, Heritage Institute of Technology, Kolkata 700107, India.
Shrimanti DasDepartment of Biotechnology, Heritage Institute of Technology, Kolkata 700107, India.
Indrilla GhoseDepartment of Biotechnology, Heritage Institute of Technology, Kolkata 700107, India.
Petr PavekDepartment of Pharmacology and Toxicology, Faculty of Pharmacy, Charles University in Prague, Heyrovskeho 1203, 50005 Hradec Kralove, Czech Republic.
Muruga Poopathi Raja KaruppiahDepartment of Chemistry, School of Physical Sciences, Central University of Kerala, Tejaswini Hills, Periye, Kasaragod District, Kerala 671320, India.
Anil A ChuturgoonDiscipline of Medical Biochemistry, School of Laboratory Medicine and Medical Sciences, College of Health Sciences, Howard College Campus, University of KwaZulu-Natal, Durban 4041, South Africa.ORCID 0000-0003-4649-4133
Krishnan AnandDepartment of Chemical Pathology, School of Pathology, Faculty of Health Sciences, University of the Free State, Bloemfontein, Free State 9300, South Africa.ORCID 0000-0002-8886-8482

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Targeted protein degradation or TPD, is rapidly emerging as a treatment that utilizes small molecules to degrade proteins that cause diseases. TPD allows for the selective removal of disease-causing proteins, including proteasome-mediated degradation, lysosome-mediated degradation, and autophagy-mediated degradation. This approach has shown great promise in preclinical studies and is now being translated to treat numerous diseases, including neurodegenerative diseases, infectious diseases, and cancer. This review discusses the latest advances in TPD and its potential as a new chemical modality for immunotherapy, with a special focus on the innovative applications and cutting-edge research of PROTACs (Proteolysis TArgeting Chimeras) and their efficient translation from scientific discovery to technological achievements. Our review also addresses the significant obstacles and potential prospects in this domain, while also offering insights into the future of TPD for immunotherapeutic applications.

Indexed as

ImmunotherapyProteasome Endopeptidase ComplexProteolysisUbiquitinAnimalsHumansNeoplasmsProteolysis Targeting ChimeraProteasome Endopeptidase ComplexProteolysis Targeting ChimeraUbiquitin

Identifiers

PMID38990186
PMCPMC11342303

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.