ArticleMolecular diversity2026
Identification of an SFRP1 inhibitor as a potential therapeutic strategy for cancers using dry-wet combined drug discovery strategy.
Article in Molecular diversity, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Secreted frizzled-related protein 1 (SFRP1) exerts a context-dependent dual role in cancer, and its epigenetic silencing drives pro-tumorigenic non-canonical Wnt activation, a potentially promising therapeutic target for advanced malignancies. In this study, a preliminarily validated 3D SFRP1 model was built by comprehensive computational approach. High-throughput virtual screening of a commercial compound library identified a common core scaffold, which was rationally design to synthesize lead compound. The target molecule was synthesized via organic synthetic approaches. Surface plasmon resonance (SPR) assays indicated concentration-dependent and specific binding of compound L1 to SFRP1 with a dissociation constant (KD) of 79.1 nM. Furthermore, molecular docking and molecular dynamics (MD) simulation provided insights into the interaction between compound L1 and SFRP1 at the molecular level and in simulated physiological conditions.
Indexed as
Identifiers
42201537What 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.