ArticleACS nano2021
Control of Nanoscale
Article in ACS nano, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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
17 citing papers in PubMed, 46 citations in OpenAlex.
- Compression and Interpenetration of Ionic Microgels in Electrostatically Self-Assembled Clusters.ACS nano · 2026Article
- Viscoelastic Hydrogels Governed by Molecular Interactions and Mechanochemical Effects.Polymers · 2026Review
- HGels (Basel, Switzerland) · 2025Article
- Nanomachine Networks: Functional All-Enzyme Hydrogels from Photochemical Cross-Linking of Glucose Oxidase.Biomacromolecules · 2025Article
- Capturing Dynamic Assembly of Nanoscale Proteins During Network Formation.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Fibrinogen αC-region acts as a functional safety latch: Implications for a fibrin biomechanical behaviour model.Acta biomaterialia · 2024Article
- Design and Functionality of Trypsin-Triggered, Expandable Bovine Serum Albumin-Polyethylene Glycol Diacrylate Hydrogel Actuators.Small science · 2024Article
- Stabilization of Non-Native Folds and Programmable Protein Gelation in Compositionally Designed Deep Eutectic Solvents.ACS nano · 2024Article
- Chemical and Biological Engineering Strategies to Make and Modify Next-Generation Hydrogel Biomaterials.Matter · 2023Article
- Toward Tunable Protein-Driven Hydrogel Lens.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Visualization of Self-Assembly and Hydration of a β-Hairpin through Integrated Small and Wide-Angle Neutron Scattering.Biomacromolecules · 2023Article
- Building block aspect ratio controls assembly, architecture, and mechanics of synthetic and natural protein networks.Nature communications · 2023Article
- Structural and mechanical properties of folded protein hydrogels with embedded microbubbles.Biomaterials science · 2023Article
- Revolutionizing anti-cancer drug discovery against breast cancer and lung cancer by modification of natural genistein: an advanced computational and drug design approach.Frontiers in oncology · 2023Article
- Acetic Acid Enables Precise Tailoring of the Mechanical Behavior of Protein-Based Hydrogels.Nano letters · 2022Article
- Tuning Protein Hydrogel Mechanics through Modulation of Nanoscale Unfolding and Entanglement in Postgelation Relaxation.ACS nano · 2022Article
- Sustained Delivery of SARS-CoV-2 RBD Subunit Vaccine Using a High Affinity Injectable Hydrogel Scaffold.Advanced healthcare materials · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Hierarchical assemblies of proteins exhibit a wide-range of material properties that are exploited both in nature and by artificially by humankind. However, little is understood about the importance of protein unfolding on the network assembly, severely limiting opportunities to utilize this nanoscale transition in the development of biomimetic and bioinspired materials. Here we control the force lability of a single protein building block, bovine serum albumin (BSA), and demonstrate that protein unfolding plays a critical role in defining the architecture and mechanics of a photochemically cross-linked native protein network. The internal nanoscale structure of BSA contains "molecular reinforcement" in the form of 17 covalent disulphide "nanostaples", preventing force-induced unfolding. Upon addition of reducing agents, these nanostaples are broken rendering the protein force labile. Employing a combination of circular dichroism (CD) spectroscopy, small-angle scattering (SAS), rheology, and modeling, we show that stapled protein forms reasonably homogeneous networks of cross-linked fractal-like clusters connected by an intercluster region of folded protein. Conversely,
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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.