Evidence map›Paper›PMID 41256625›Full record

ArticlebioRxiv : the preprint server for biology2025

Epistasis among clustered lineage-specific adaptive amino acid substitutions in the Drosophila Trio protein.

Flora Borne, Andrew M Taverner, Peter Andolfatto

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2025. 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

5 · Who and what money

Authors and funding

3 authors.

Flora BorneDepartment of Biological Sciences, Columbia University; 1212 Amsterdam Avenue, New York, New York, 10027.ORCID 0000-0002-6660-8559
Andrew M TavernerThe Lewis-Sigler Institute, Princeton University; Princeton, New Jersey, 08544.
Peter AndolfattoDepartment of Biological Sciences, Columbia University; 1212 Amsterdam Avenue, New York, New York, 10027.ORCID 0000-0003-3393-4574

Funding

Parallel evolution at Na,K-ATPase: a model system for understanding constraints on the evolution of novel protein functions.R01GM115523 · NIGMS · PRINCETON UNIVERSITY · PI ANDOLFATTO, PETER · 2015 to 2024
$2.8M
NIGMS NIH HHS R01 GM115523
6 · The paper itself

Abstract

Intramolecular epistasis is increasingly recognized as a key factor shaping patterns of evolutionary rate variation among protein sites and constraining adaptive evolution. While genome-wide analyses have revealed that intramolecular epistatic interactions can drive the spatial clustering of amino acid substitutions, direct empirical evidence for such interactions and their evolutionary consequences remains limited. Using a population genetic screen for spatially-clustered and lineage-specific adaptive amino acid substitutions in

Identifiers

PMID41256625
PMCPMC12621854

What OpenQuestion 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 OpenQuestion graph.