Evidence map›Paper›PMID 38206862›Full record

ArticleeLife2023

Binding and sequestration of poison frog alkaloids by a plasma globulin.

Aurora Alvarez-Buylla, Marie-Therese Fischer, Maria Dolores Moya Garzon, Alexandra E Rangel, Elicio E Tapia, Julia T Tanzo, H Tom Soh, Luis A Coloma, Jonathan Z Long, Lauren A O'Connell

Open access · goldAbstract read
In one paragraph

Article in eLife, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
7.5field-weighted citation impact, top 2% of its field
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

15 citing papers in PubMed, 25 citations in OpenAlex.

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  10. Review
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  13. A toxic environment selects for specialist microbiome in poison frogs.bioRxiv : the preprint server for biology · 2024
    Article
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  15. 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

10 authors at 4 institutions in 2 countries.

Aurora Alvarez-BuyllaDepartment of Biology, Stanford University, Stanford, United States.ORCID 0000-0001-6256-0300
Marie-Therese FischerDepartment of Biology, Stanford University, Stanford, United States.
Maria Dolores Moya GarzonSarafan ChEM-H, Stanford University, Stanford, United States.
Alexandra E RangelWu Tsai Human Performance Alliance, Stanford University, Stanford, United States.
Elicio E TapiaDepartment of Radiology, Stanford University, Stanford, United States.
Julia T TanzoSarafan ChEM-H, Stanford University, Stanford, United States.
H Tom SohWu Tsai Human Performance Alliance, Stanford University, Stanford, United States.
Luis A ColomaChan Zuckerberg Biohub, San Francisco, United States.
Jonathan Z LongSarafan ChEM-H, Stanford University, Stanford, United States.ORCID 0000-0003-2631-7463
Lauren A O'ConnellDepartment of Biology, Stanford University, Stanford, United States.ORCID 0000-0002-2706-4077
Neurosciences Institute · USStanford University · USChan Zuckerberg Initiative (United States) · USMorpho (United States) · US

Funding

Howard Hughes Medical Institute GT13330
6 · The paper itself

Abstract

Alkaloids are important bioactive molecules throughout the natural world, and in many animals they serve as a source of chemical defense against predation. Dendrobatid poison frogs bioaccumulate alkaloids from their diet to make themselves toxic or unpalatable to predators. Despite the proposed roles of plasma proteins as mediators of alkaloid trafficking and bioavailability, the responsible proteins have not been identified. We use chemical approaches to show that a ~50 kDa plasma protein is the principal alkaloid-binding molecule in blood of poison frogs. Proteomic and biochemical studies establish this plasma protein to be a liver-derived alkaloid-binding globulin (ABG) that is a member of the serine-protease inhibitor (serpin) family. In addition to alkaloid-binding activity, ABG sequesters and regulates the bioavailability of 'free' plasma alkaloids in vitro. Unexpectedly, ABG is not related to saxiphilin, albumin, or other known vitamin carriers, but instead exhibits sequence and structural homology to mammalian hormone carriers and amphibian biliverdin-binding proteins. ABG represents a new small molecule binding functionality in serpin proteins, a novel mechanism of plasma alkaloid transport in poison frogs, and more broadly points toward serpins acting as tunable scaffolds for small molecule binding and transport across different organisms.

Indexed as

AlkaloidsGlobulinsSerpinsAnimalsAnuraBlood ProteinsMammalsPoison FrogsProteomicsAlkaloidsBlood ProteinsGlobulinsSerpinsalkaloid bindingbiochemistrychemical biologyecologyplasma globulinpoison frogsprotein evolutionserpintoxicity

Identifiers

PMID38206862
PMCPMC10783871
OpenAlexW4390776898

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.