Evidence map›Paper›PMID 37312850›Full record

ArticleACS medicinal chemistry letters2023

Potent and Selective BCL-XL Inhibitors and PROTAC Compounds as Potential Cancer Treatment and Immunotherapy.

Robert B Kargbo

Abstract readEditorial
In one paragraph

Article in ACS medicinal chemistry letters, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

1 author.

Robert B KargboUsona Institute, Fitchburg, Wisconsin 53711-5300, United States.ORCID https://orcid.org/0000-0002-5539-6343

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The B-cell lymphoma 2 (BCL-2) protein is the most extensively studied anti-apoptotic member within the BCL-2 protein family. It functions to inhibit programmed cell death by forming a heterodimer with BAX, thereby promoting cellular survival through the extension of tumor cell lifespan and facilitating malignant transformation. This Patent Highlight reveals the development of small molecule degraders that consist of a ligand targeting the protein of interest, BCL-2, an E3 ubiquitin ligase recruitment ligand (such as Cereblon or Von Hippel-Lindau ligands), and a chemical linker that connects the two ligands. The proteolysis-targeting chimera (PROTAC)-mediated heterodimerization of the bound proteins leads to the ubiquitination of the target protein, which is subsequently degraded by the proteasome. This strategy offers innovative therapeutic options for cancer, immunology, and autoimmune disease management.

Identifiers

PMID37312850
PMCPMC10258826

What OpenQuestion holds

Textmetadata
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.