Evidence map›Paper›PMID 42780299›Full record

ArticleResearch square2026

Engineered subtilisin protease degrades active KRAS in cancer cells leading to differential cell targeting.

Thomas Fuerst, Monty Goldstein, Betty Chu, Kathleen Carillo, John Orban, Eric Toth

Abstract readPreprint
In one paragraph

Article in Research square, 2026. 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

6 authors.

Thomas FuerstUniversity of Maryland.ORCID 0000-0002-9766-9995
Monty Goldstein
Betty Chu
Kathleen Carillo
John Orban
Eric Toth

Funding

Engineering protein-specific proteases: targeting signaling proteinsR01GM141290 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI ORBAN, JOHN, TOTH, ERIC A · 2021 to 2024
$2.3M
NIGMS NIH HHS R01 GM141290
6 · The paper itself

Abstract

Controlling aberrant RAS signaling has been the subject of intensive efforts aimed at developing specific RAS inhibitors, small molecules that promote RAS degradation, and monobodies that inhibit RAS activity. Direct proteolytic degradation of RAS by site-specific proteases has received considerably less attention. A naturally-occurring protease from

Identifiers

PMID42780299
PMCPMC13596628

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.