Evidence mapPaperPMID 35036934Full record

ArticleCurrent research in structural biology2022

Fragment-based exploration of the 14-3-3/Amot-p130 interface.

Federica Centorrino, Blaž Andlovic, Peter Cossar, Luc Brunsveld, Christian Ottmann

Abstract read
In one paragraph

Article in Current research in structural biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Role of angiomotin family members in human diseases (Review).Experimental and therapeutic medicine · 2024
    Review
  5. Review
  6. Article
  7. 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

5 authors.

Federica CentorrinoLaboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology, P. O. Box 513, 5600 MB, Eindhoven, the Netherlands.
Blaž AndlovicLaboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology, P. O. Box 513, 5600 MB, Eindhoven, the Netherlands.
Peter CossarLaboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology, P. O. Box 513, 5600 MB, Eindhoven, the Netherlands.
Luc BrunsveldLaboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology, P. O. Box 513, 5600 MB, Eindhoven, the Netherlands.
Christian OttmannLaboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology, P. O. Box 513, 5600 MB, Eindhoven, the Netherlands.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The modulation of protein-protein interactions (PPIs) has developed into a well-established field of drug discovery. Despite the advances achieved in the field, many PPIs are still deemed as '

Indexed as

14-3-3 /protein-protein interactions stabilizersAIP4, Atrophin-1 interacting protein 4Amot, AngiomotinAmotL1/2, Angiomotin-like 1/2Amot-p130FBDD, Fragment-based drug discoveryFP, Fluorescence polarizationFragment-based drug discoveryLats 1/2, Large tumor suppressor 1/2LigandabilityMST, Microscale thermophoresisPPI, Protein-protein interactionPTMs, post-translational modificationsX-ray crystallographyYAP1, Yes-associated protein 1

Identifiers

PMID35036934
PMCPMC8743172

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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.