Evidence map›Paper›PMID 39026646›Full record

ReviewRSC medicinal chemistry2024

Fragment-based drug discovery campaigns guided by native mass spectrometry.

Louise M Sternicki, Sally-Ann Poulsen

Abstract readReview
In one paragraph

Review in RSC medicinal chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Target Engagement Assays in Early Drug Discovery.Journal of medicinal chemistry · 2025
    Review
  6. Review
  7. Review
  8. Fragment-based drug discovery: A graphical review.Current research in pharmacology and drug discovery · 2025
    Review
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

2 authors.

Louise M SternickiGriffith Institute for Drug Discovery, Griffith University Nathan Brisbane Queensland 4111 Australia s.poulsen@griffith.edu.au.ORCID https://orcid.org/0000-0001-6158-663X
Sally-Ann PoulsenGriffith Institute for Drug Discovery, Griffith University Nathan Brisbane Queensland 4111 Australia s.poulsen@griffith.edu.au.ORCID https://orcid.org/0000-0003-4494-3687

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Native mass spectrometry (nMS) is well established as a biophysical technique for characterising biomolecules and their interactions with endogenous or investigational small molecule ligands. The high sensitivity mass measurements make nMS particularly well suited for applications in fragment-based drug discovery (FBDD) screening campaigns where the detection of weakly binding ligands to a target biomolecule is crucial. We first reviewed the contributions of nMS to guiding FBDD hit identification in 2013, providing a comprehensive perspective on the early adoption of nMS for fragment screening. Here we update this initial progress with a focus on contributions of nMS that have guided FBDD for the period 2014 until end of 2023. We highlight the development of nMS adoption in FBDD in the context of other biophysical fragment screening techniques. We also discuss the roadmap for increased adoption of nMS for fragment screening beyond soluble proteins, including for guiding the discovery of fragments supporting advances in PROTAC discovery, RNA-binding small molecules and covalent therapeutic drug discovery.

Identifiers

PMID39026646
PMCPMC11253872

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.