Evidence map›Paper›PMID 40949976›Full record

ArticlebioRxiv : the preprint server for biology2025

The

Raymondo Lopez-Magaña, Karen M Ottemann

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

  • Updated by
    The2026
5 · Who and what money

Authors and funding

2 authors.

Raymondo Lopez-Magaña

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacteria localize proteins to distinct subcellular locations, including chemoreceptors, which frequently localize to the bacterial pole. Although some polarity-promoting mechanisms have been described, many chemoreceptors lack clear routes to becoming polar. TlpD of the bacterial pathogen Importance: Bacteria place their proteins in specific locations that are required for the proteins to function including the bacterial pole. How the bacterial cell identifies which proteins go to the pole is not fully understood. In this work, we dissect parts of a protein called TlpD that naturally goes to the pole. We find that mutants lacking one end of TlpD lose their polar placement, but retain other abilities. TlpD allows directed motility known as chemotaxis. This ability is critical for infection in

Identifiers

PMID40949976
PMCPMC12424713

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.