ArticleInternational journal of molecular sciences2020
Structural Basis of Oligomerization of N-Terminal Domain of Spider Aciniform Silk Protein.
Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed, 15 citations in OpenAlex.
- Ultratight Binding of a Capture Spiral Spider Silk Protein through Electrostatic Forces.ACS bio & med chem Au · 2026Article
- Intrinsically disordered linkers and terminal domains codrive aciniform spidroin self-assembly through liquid-liquid phase separation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Architectural control of rod-coil block polypeptide thermoresponsive self-assemblyJournal of materials chemistry. B · 2025Article
- Quantitative Shotgun Proteomic Analysis of Bacteria after Overexpression of Recombinant Spider Miniature Spidroin, MaSp1.International journal of molecular sciences · 2024Article
- Influence of Spider Silk Protein Structure on Mechanical and Biological Properties for Energetic Material Detection.Molecules (Basel, Switzerland) · 2024Review
- Customized Flagelliform Spidroins Form Spider Silk-like Fibers at pH 8.0 with Outstanding Tensile Strength.ACS biomaterials science & engineering · 2022Article
- Solution Structure of Tubuliform Spidroin N-Terminal Domain and Implications for pH Dependent Dimerization.Frontiers in molecular biosciences · 2022Article
- Recombinant Spider Silk: Promises and Bottlenecks.Frontiers in bioengineering and biotechnology · 2022Review
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 at 1 institution in 2 countries.
Funding
Abstract
Spider silk is self-assembled from water-soluble silk proteins through changes in the environment, including pH, salt concentrations, and shear force. The N-terminal domains of major and minor ampullate silk proteins have been found to play an important role in the assembly process through salt- and pH-dependent dimerization. Here, we identified the sequences of the N-terminal domains of aciniform silk protein (AcSpN) and major ampullate silk protein (MaSpN) from
Indexed as
Identifiers
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.