Evidence map›Paper›PMID 42283365›Full record

ArticleAngewandte Chemie (International ed. in English)2026

CSAKD: Determining Absolute Ligand Affinities From

Simon H Rüdisser, Gabriela Stadler, Alvar D Gossert

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 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. A ComprehensiveAngewandte Chemie (International ed. in English) · 2026
    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

3 authors.

Simon H RüdisserDepartment of Biology, ETH Zürich, Zürich, Switzerland.ORCID 0000-0002-1107-6196
Gabriela StadlerDepartment of Biology, ETH Zürich, Zürich, Switzerland.ORCID 0000-0002-9852-6427
Alvar D GossertDepartment of Biology, ETH Zürich, Zürich, Switzerland.ORCID 0000-0001-7732-495X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small-molecule drug discovery typically begins with the screening of compound libraries to identify initial hits, which are subsequently optimized into lead compounds and, ultimately, drug candidates. Diverse screening methodologies are employed, including DNA-encoded library technology, high-throughput screening, and fragment-based drug discovery (FBDD). Among these, FBDD is particularly powerful when integrated with structure-guided drug design and biophysical affinity measurements. However, accurately quantifying the weak binding affinities of fragments remains a significant challenge. To address this, we introduce chemical shift anisotropy

Indexed as

Small Molecule LibrariesAnisotropyDrug DiscoveryFluorineLigandsMachine LearningMagnetic Resonance SpectroscopyFluorineLigandsSmall Molecule Librariesaffinity determinationchemical shielding anisotropyfragment‐based drug discoverymachine learning

Identifiers

PMID42283365
PMCPMC13452527

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.