Evidence map›Paper›PMID 39693348›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2024

Proteomic analysis of the sponge Aggregation Factor implicates an ancient toolkit for allorecognition and adhesion in animals.

Fabian Ruperti, Monika Dzieciatkowska, M Sabrina Pankey, Cedric S Asensio, Dario Anselmetti, Xavier Fernàndez-Busquets, Scott A Nichols

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. An abundant membrane protein in the NCAM superfamily is required for epithelial organization in sea anemone embryos.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Proteomic analysis of the sponge Aggregation Factor implicates an ancient toolkit for allorecognition and adhesion in animals.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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

7 authors.

Fabian RupertiDevelopmental Biology Unit, European Molecular Biology Laboratory, Heidelberg 69117, Germany.ORCID 0000-0002-0724-3262
Monika DzieciatkowskaDepartment of Biochemistry and Molecular Genetics, Anschutz Medical Campus, University of Colorado, Aurora, CO 80045.ORCID 0000-0002-9947-2520
M Sabrina PankeyDepartment of Molecular, Cellular and Biomedical Science, University of New Hampshire, Durham, NH 03824.ORCID 0000-0002-7061-9613
Cedric S AsensioDepartment of Biological Sciences, University of Denver, Denver, CO 80208.ORCID 0000-0002-2284-0217
Dario AnselmettiNanomalaria Group, Faculty of Physics, Experimental Biophysics, Bielefeld University, Bielefeld 33501, Germany.ORCID 0000-0002-8720-4369
Xavier Fernàndez-BusquetsNanomalaria Group, Barcelona Institute for Global Health, Hospital Clínic Universitat de Barcelona, Barcelona 08036, Spain.ORCID 0000-0002-4622-9631
Scott A NicholsDepartment of Biological Sciences, University of Denver, Denver, CO 80208.ORCID 0000-0002-4765-754X

Funding

NSF | BIO | Division of Integrative Organismal Systems (IOS) 2015608
6 · The paper itself

Abstract

The discovery that sponges (Porifera) can fully regenerate from aggregates of dissociated cells launched them as one of the earliest experimental models to study the evolution of cell adhesion and allorecognition in animals. This process depends on an extracellular glycoprotein complex called the Aggregation Factor (AF), which is composed of proteins thought to be unique to sponges. We used quantitative proteomics to identify additional AF components and interacting proteins in the classical model,

Indexed as

Cell AdhesionPoriferaProteomicsAnimalsGlycoproteinsProtein DomainsGlycoproteinsadhesionallorecognitionevolutionPoriferaproteomics

Identifiers

PMID39693348
PMCPMC11670116

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.