ArticleNature communications2016
Nanoscale probing of electron-regulated structural transitions in silk proteins by near-field IR imaging and nano-spectroscopy.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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
26 citing papers in PubMed.
- Infrared Near-Field Microscopy as a Platform for Nanoscale Biomedical Spectroscopy and Imaging.ACS applied materials & interfaces · 2026Review
- Nano-Infrared Imaging and Spectroscopy of Animal Cells in Liquid Environment.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Manipulating the Assembly and Architecture of Fibrillar Silk.Advanced materials (Deerfield Beach, Fla.) · 2025Article
- Scanning Probe Nano-Infrared Imaging and Spectroscopy of Biochemical and Natural Materials.Small science · 2024Article
- Two-dimensional silk.Science advances · 2024Article
- Monolithically integrated high-density vertical organic electrochemical transistor arrays and complementary circuits.Nature electronics · 2024Article
- Molecular Evidence of Structural Changes in Silk Using Unlimited Degradation Mass Spectrometry.ACS omega · 2023Article
- Construction of multifunctional hydrogel with metal-polyphenol capsules for infected full-thickness skin wound healing.Bioactive materials · 2023Article
- Determination of Secondary Structure of Proteins by Nanoinfrared Spectroscopy.Analytical chemistry · 2023Article
- 3D electron-beam writing at sub-15 nm resolution using spider silk as a resist.Nature communications · 2021Article
- A rewritable optical storage medium of silk proteins using near-field nano-optics.Nature nanotechnology · 2020Article
- Infrared and Raman chemical imaging and spectroscopy at the nanoscale.Chemical Society reviews · 2020Article
- Recent Applications of Advanced Atomic Force Microscopy in Polymer Science: A Review.Polymers · 2020Review
- Engineering Silk Materials: From Natural Spinning to Artificial Processing.Applied physics reviews · 2020Article
- Understanding the structural degradation of South American historical silk: A Focal Plane Array (FPA) FTIR and multivariate analysis.Scientific reports · 2019Article
- Design, Fabrication, and Function of Silk-Based Nanomaterials.Advanced functional materials · 2018Article
- Silkworm silk-based materials and devices generated using bio-nanotechnology.Chemical Society reviews · 2018Review
- Tomographic and multimodal scattering-type scanning near-field optical microscopy with peak force tapping mode.Nature communications · 2018Article
- Silk-Based Aqueous Microcontact Printing.ACS biomaterials science & engineering · 2018Article
- Infrared Spectroscopic Imaging Advances as an Analytical Technology for Biomedical Sciences.Analytical chemistry · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
20 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Silk protein fibres produced by silkworms and spiders are renowned for their unparalleled mechanical strength and extensibility arising from their high-β-sheet crystal contents as natural materials. Investigation of β-sheet-oriented conformational transitions in silk proteins at the nanoscale remains a challenge using conventional imaging techniques given their limitations in chemical sensitivity or limited spatial resolution. Here, we report on electron-regulated nanoscale polymorphic transitions in silk proteins revealed by near-field infrared imaging and nano-spectroscopy at resolutions approaching the molecular level. The ability to locally probe nanoscale protein structural transitions combined with nanometre-precision electron-beam lithography offers us the capability to finely control the structure of silk proteins in two and three dimensions. Our work paves the way for unlocking essential nanoscopic protein structures and critical conditions for electron-induced conformational transitions, offering new rules to design protein-based nanoarchitectures.
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.