ReviewAdvances in experimental medicine and biology2026
Identification of Virus-Host Interactions.
Review in Advances in experimental medicine and biology, 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
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
No protein acts on its own to carry out its designated function. Proteins interact with other biomolecules to form complexes that perform a coordinated function. While proteins most often form complexes involving other proteins, they also interact with nucleic acids, lipids, carbohydrates, ions, and other small molecules and metabolites (Wang et al., Proteomics 22(15-16):e2100190, 2022; Veenstra, Proteomics 21:e2000235, 2021). While the early days of proteomics were focused on identifying and quantifying as many proteins as possible, scientists quickly recognized the power of proteomics to rapidly identify interactions between specific groups of proteins. All the necessary techniques have already been developed: methods to extract protein complexes (e.g., immunoaffinity purification under denaturing conditions), fractionate the complexes (e.g., chromatography and/or gel electrophoresis), identify the proteins that made up the complex (e.g., mass spectrometry (MS)), and validate the results (e.g., Western blotting, etc.). Indeed, one of the great accomplishments of the current proteomic era has been the speed at which protein complexes have been characterized (Labeau et al., Cell Rep 39:11074, 2022; May et al., Viruses 14:611, 2022; Havugimana et al., Nat Commun 13:4043, 2022), for example, as of 2022, the CORUM database (CORUM 3.1) contains data on 5134 mammalian protein complexes (Giurgiu et al., Nucleic Acids Res 47:D559-D563, 2019). The latest version of the Human Protein Complex Map (hu.MAP 2.0) contains information on over 7000 protein complexes (Drew et al., Mol Syst Biol 17:e10016, 2021). The IntAct Molecular Interaction Database contains over 700,000 binary molecular interactions curated from approximately 74,000 published experiments (Orchard et al., Nucleic Acids Res 42(Database issue):D358-D363, 2014). These databases show the amount of effort that continues to be expended in identifying biomolecular interactions, which demonstrates their importance in understanding how they affect cell function.
Indexed as
Identifiers
42129073What Socratic 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 Socratic graph.