ReviewRSC chemical biology2026
Post-translational modifications of silk proteins.
Review in RSC chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed.
- Diverging Liquid-Liquid Phase Separation Behavior of Different Recombinant Major Ampullate Spidroins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
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
Post-translational modifications (PTMs) endow silk proteins with chemical diversity that governs their higher-order assembly, hydration, and covalent connectivity. This review highlights the principal PTMs that define silk protein function, including hydroxylation, glycosylation, phosphorylation, and covalent crosslinking. We also describe their contributions to protein structural stability and mechanical properties. Recent advances in proteomics have begun to reveal low-abundance PTMs, whereas synthetic biology and bioorthogonal chemistry enable the programmed installation of modifications to tune physicochemical properties. Understanding and harnessing these chemistries provides a foundation for the predictive design of next-generation protein-based materials at the interface of chemical biology and materials science.
Identifiers
What 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.