ArticleMethods in molecular biology (Clifton, N.J.)2026
Allosteric Network Analysis Toolkit for Single-Domain Phosphoproteins.
Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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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.
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
2 citing papers in PubMed.
- The protein-water H-bond network for bacterial response regulator REC domain activation.Journal of structural biology: X · 2026Article
- The Enigmatic Conserved Q134-F135-N137 Triad in SARS-CoV-2 Spike Protein: A Conformational Transducer?Biomolecules · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Single-domain protein superfamilies mediate essential signaling functions in both prokaryotes and eukaryotes. Signal transduction mediated by single-residue phosphorylation involves subtle secondary structure, side chain rotamer, and hydrogen-bond fluctuations for transitions between active and inactive conformational states, rather than large fold variations. Its study requires molecular dynamics simulations for adequate sampling of the conformational landscape. Discrimination between functional states and subfamilies is achieved by subsequent network analysis designed to couple variations at the local residue or fragment levels to functional collective motions. We describe an integrated protocol for quantitative measurement of local fluctuations and their coupling to functional motions with phosphorylation of the CheY bacterial chemotaxis signal protein as a case study.
Indexed as
Identifiers
41174311What 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.