ArticleiScience2026
Amino acid repeat signatures underlying human-pathogen interactions.
Article in iScience, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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.
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Authors and funding
7 authors.
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Abstract
Emerging evidence suggests that amino acid homorepeats (HRs) in proteins (HRPs) contribute to protein interactability. What is the role of HRs in HPIs? We found that pathogens engage physiologically important human HRPs, thereby affecting diverse host physiological processes. From the pathogen standpoint, (1) eukaryotic pathogens engage more HRPs but with host-sparse HRs (HR types that are rare in the host), leading to disparate and discriminate interactions, (2) prokaryotic pathogens engage less HRPs but with host-abundant non-polar HRs via host-protein proxies, bringing about discriminate or promiscuous interactions, and (3) viral pathogens engage more HRPs with host-abundant polar uncharged HRs, affecting promiscuous interactions using host-partner HR tract mimicry. To propel further research, we introduce a resource Hi-PHI (http://hiphi.iisertirupati.ac.in/), cataloging critical information about human and pathogen HRPs and HRs. We propose mechanisms to (1) repurpose drugs targeting human HRPs engaged by pathogens for treating different infections, and (2) exploit HRs and their flanks as targets for pathogen-targeted anti-infectives.
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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 Socratic graph.