Evidence map›Paper›PMID 42745536›Full record

ArticleChemMedChem2026

Linker Optimization of cMYC RIBOTAC for Efficient cMYC Modulation.

Sivakumar Komachankandy, Jinseo Heo, Yerin Kim, Wonpil Im, Yeongju Lee

Abstract read
In one paragraph

Article in ChemMedChem, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

5 authors.

Sivakumar KomachankandyDepartment of Chemistry, Pusan National University, Busan, Republic of Korea.ORCID https://orcid.org/0009-0003-0013-9512
Jinseo HeoDepartment of Chemistry, Pusan National University, Busan, Republic of Korea.ORCID https://orcid.org/0009-0002-7481-9839
Yerin KimDepartment of Chemistry, Pusan National University, Busan, Republic of Korea.
Wonpil ImDepartment of Biological Sciences, Lehigh University, Bethlehem, Pennsylvania, United States.
Yeongju LeeDepartment of Chemistry, Pusan National University, Busan, Republic of Korea.ORCID https://orcid.org/0000-0003-4220-3028

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribonuclease-targeting chimeras (RIBOTACs) are heterobifunctional molecules composed of an RNA-binding motif and an RNase L-recruiting module, enabling selective RNA cleavage by recruited RNase L. While optimization efforts have primarily focused on RNA-binding ligands and RNase L-recruiting motifs, the linker design remains poorly understood. Here, we systematically evaluated the impact of linker length and rigidity in a cMYC-targeting RIBOTAC system. A series of PEG-based linkers (PEG2-PEG7) was employed while maintaining identical RNA-binding and RNase L-recruiting modules. Functional evaluation through in vitro cleavage, RT-qPCR, and Western blot analysis established PEG3 and PEG4 as the optimal linkers, whereas further elongation to PEG5-7 or substitution with a rigid triazole-based linker resulted in complete loss of activity. These findings demonstrate that precise linker design is essential for effective RNA degradation.

Indexed as

EndoribonucleasesHumansMolecular StructurePolyethylene Glycols2-5A-dependent ribonucleaseEndoribonucleasesPolyethylene GlycolscMYC modulationlinker optimizationRIBOTACRNA degradationRNase L

Identifiers

PMID42745536
PMCPMC13579077

What Socratic 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 Socratic graph.