ArticleCell death & disease2014
Cancer cell death induced by novel small molecules degrading the TACC3 protein via the ubiquitin-proteasome pathway.
Article in Cell death & disease, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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.
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.
Who cites it
42 citing papers in PubMed, 99 citations in OpenAlex.
- The Progress of Small Molecule Targeting BCR-ABL in the Treatment of Chronic Myeloid Leukemia.Mini reviews in medicinal chemistry · 2024Review
- Ligandability of E3 Ligases for Targeted Protein Degradation Applications.Biochemistry · 2023Review
- Molecular Glues: The Adhesive Connecting Targeted Protein Degradation to the Clinic.Biochemistry · 2023Review
- Recent advances in IAP-based PROTACs (SNIPERs) as potential therapeutic agents.Journal of enzyme inhibition and medicinal chemistry · 2022Review
- Proteolysis-targeting chimeras (PROTACs) in cancer therapy.Molecular cancer · 2022Review
- Advancing targeted protein degradation for cancer therapy.Nature reviews. Cancer · 2021Review
- A narrative review of proteolytic targeting chimeras (PROTACs): future perspective for prostate cancer therapy.Translational andrology and urology · 2021Review
- Light-Controllable PROTACs for Temporospatial Control of Protein Degradation.Frontiers in cell and developmental biology · 2021Review
- E3 Ligase Ligands in Successful PROTACs: An Overview of Syntheses and Linker Attachment Points.Frontiers in chemistry · 2021Review
- The Potential of Proteolytic Chimeras as Pharmacological Tools and Therapeutic Agents.Molecules (Basel, Switzerland) · 2020Review
- First small-molecule PROTACs for G protein-coupled receptors: inducingActa pharmaceutica Sinica. B · 2020Article
- PROTACs: An Emerging Therapeutic Modality in Precision Medicine.Cell chemical biology · 2020Review
- Review
- Degradation of proteins by PROTACs and other strategies.Acta pharmaceutica Sinica. B · 2020Review
- PROTACs- a game-changing technology.Expert opinion on drug discovery · 2019Review
- Inducing the Degradation of Disease-Related Proteins Using Heterobifunctional Molecules.Molecules (Basel, Switzerland) · 2019Review
- Advances in targeted degradation of endogenous proteins.Cellular and molecular life sciences : CMLS · 2019Review
- Small molecule PROTACs: an emerging technology for targeted therapy in drug discovery.RSC advances · 2019Review
- The PROTAC technology in drug development.Cell biochemistry and function · 2019Review
- The emerging role for Cullin 4 family of E3 ligases in tumorigenesis.Biochimica et biophysica acta. Reviews on cancer · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The selective degradation of target proteins with small molecules is a novel approach to the treatment of various diseases, including cancer. We have developed a protein knockdown system with a series of hybrid small compounds that induce the selective degradation of target proteins via the ubiquitin-proteasome pathway. In this study, we designed and synthesized novel small molecules called SNIPER(TACC3)s, which target the spindle regulatory protein transforming acidic coiled-coil-3 (TACC3). SNIPER(TACC3)s induce poly-ubiquitylation and proteasomal degradation of TACC3 and reduce the TACC3 protein level in cells. Mechanistic analysis indicated that the ubiquitin ligase APC/C(CDH1) mediates the SNIPER(TACC3)-induced degradation of TACC3. Intriguingly, SNIPER(TACC3) selectively induced cell death in cancer cells expressing a larger amount of TACC3 protein than normal cells. These results suggest that protein knockdown of TACC3 by SNIPER(TACC3) is a potential strategy for treating cancers overexpressing the TACC3 protein.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.