ArticleProteoglycan research
High-fidelity and iterative affinity extraction of hyaluronan.
Article in Proteoglycan research. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed.
- Hyaluronan Signaling Ameliorates the Epithelial Injury Response and Barrier Disruption After Ozone Exposure.Biomolecules · 2026Article
- Hyaluronan Underlies the Emergence of Form, Fate, and Function in Human Cardioids.bioRxiv : the preprint server for biology · 2026Article
- Analytical Assessment of Hyaluronan and Its Heavy Chain Modification with Solid-State Nanopore Sensors.Annual review of analytical chemistry (Palo Alto, Calif.) · 2026Review
- Co-purification of the GroEL chaperone during outer membrane vesicle purification: insights fromMicrobiology (Reading, England) · 2025Article
- High-fidelity and iterative affinity extraction of hyaluronan.Proteoglycan researchArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
The glycosaminoglycan hyaluronan (HA) serves a variety of crucial physiological functions in vertebrates. Synthesized at the plasma membrane and secreted into the extracellular environment, HA polymers span a wide range of molecular weights (MW) that define their activity through a notable size-function relationship. Analytical technologies for determining HA MW distributions typically require selective extraction from complex biofluids or tissues. A common method for achieving this is immunoprecipitation-like pull-down using specific HA-binding proteins bound to magnetic beads. Here, we present a systematic investigation of experimental variables involved in this process, leading to an affinity extraction protocol that enables iterative bead reuse and reagent lifetime maximization, thereby enhancing the efficiency of the HA extraction process. Our methods provide a framework for general optimization of immunoprecipitation in other contexts with heterogenous analyte sizes.
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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 OpenQuestion graph.