ReviewBiotechnology advances
Protein folding and assembly in confined environments: Implications for protein aggregation in hydrogels and tissues.
Review in Biotechnology advances. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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.
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Who cites it
21 citing papers in PubMed.
- A phase transition modulates the protective function of a tardigrade disordered protein during desiccation.Protein science : a publication of the Protein Society · 2025Article
- Milk protein-based hydrogels: Development and biomedical applications.Biomaterials translational · 2025Review
- Influence of device configuration and noise on a machine learning predictor for the selection of nanoparticle small-angle X-ray scattering models.Acta crystallographica. Section A, Foundations and advances · 2024Article
- Therapeutic Implications and Regulations of Protein Post-translational Modifications in Parkinsons Disease.Cellular and molecular neurobiology · 2024Review
- Tau- and α-synuclein-targeted gold nanoparticles: applications, opportunities, and future outlooks in the diagnosis and therapy of neurodegenerative diseases.Journal of nanobiotechnology · 2024Review
- Molecular Crowding: The History and Development of a Scientific Paradigm.Chemical reviews · 2024Review
- Super-resolution microscopy to study membrane nanodomains and transport mechanisms in the plasma membrane.Frontiers in molecular biosciences · 2024Review
- Diversity of Bioinspired Hydrogels: From Structure to Applications.Gels (Basel, Switzerland) · 2023Review
- Article
- Disassembly of Amyloid Fibril with Infrared Free Electron Laser.International journal of molecular sciences · 2023Review
- Biomolecular condensates can both accelerate and suppress aggregation of α-synuclein.Science advances · 2022Article
- Application study of infrared free-electron lasers towards the development of amyloidosis therapy.Journal of synchrotron radiation · 2022Article
- Hydrogels as functional components in artificial cell systems.Nature reviews. Chemistry · 2022Review
- Review
- Review
- Disordered-Ordered Protein Binary Classification by Circular Dichroism Spectroscopy.Frontiers in molecular biosciences · 2022Article
- Article
- A first-takes-all model of centriole copy number control based on cartwheel elongation.PLoS computational biology · 2021Article
- Hydrogel-Forming Algae Polysaccharides: From Seaweed to Biomedical Applications.Biomacromolecules · 2021Review
- Combined Effects of Confinement and Macromolecular Crowding on Protein Stability.International journal of molecular sciences · 2020Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
In the biological milieu of a cell, soluble crowding molecules and rigid confined environments strongly influence whether the protein is properly folded, intrinsically disordered proteins assemble into distinct phases, or a denatured or aggregated protein species is favored. Such crowding and confinement factors act to exclude solvent volume from the protein molecules, resulting in an increased local protein concentration and decreased protein entropy. A protein's structure is inherently tied to its function. Examples of processes where crowding and confinement may strongly influence protein function include transmembrane protein dimerization, enzymatic activity, assembly of supramolecular structures (e.g., microtubules), nuclear condensates containing transcriptional machinery, protein aggregation in the contexts of disease and protein therapeutics. Historically, most protein structures have been determined from pure, dilute protein solutions or pure crystals. However, these are not the environments in which these proteins function. Thus, there has been an increased emphasis on analyzing protein structure and dynamics in more "in vivo-like" environments. Complex in vitro models using hydrogel scaffolds to study proteins may better mimic features of the in vivo environment. Therefore, analytical techniques need to be optimized for real-time analysis of proteins within hydrogel scaffolds.
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What OpenQuestion 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 OpenQuestion graph.