ArticleBiomolecules2026
A Novel Mechanism for Autoantigenicity: Condensate Conformational Change.
Article in Biomolecules, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Autoantigens, targets of B cell antibodies, account for ~10% of the human proteome. It is not well understood why or how particular self-proteins become autoantigens. Prominent theories posit that failures of the immune system at various levels or exposure of aberrant proteins to the immune system are responsible for autoantigenicity. In contrast, we propose a completely unrelated mechanism of autoantigenicity that is based on normal cell functioning. We suggest that, when a protein associates with one of the ~100 types of biomolecular condensates, protein-protein interaction therein causes changes in protein structure or conformation that signal an untolerized state to the immune system. This proposal is derived from the fact that many macromolecules are more concentrated within condensates than in the extra-condensate environment. Thus, the propensity for macromolecular interaction may be greater in condensates compared with the non-condensate environment. In support of this proposal, we present examples of predicted conformational differences, with and without accompanying secondary structure differences, between proteins in known condensate heteromeric complexes and in their free monomer forms. In each case, the differences correlated with predicted B-cell binding, supporting our model. Further, from a compilation of ~1900 autoantigens, we estimate that autoantigens are twice as prevalent in condensates compared with the entire human proteome (Chi squared
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.