Evidence map›Paper›PMID 27713412›Full record

ArticleNature communications2016

Nanoscale probing of electron-regulated structural transitions in silk proteins by near-field IR imaging and nano-spectroscopy.

Nan Qin, Shaoqing Zhang, Jianjuan Jiang, Stephanie Gilbert Corder, Zhigang Qian, Zhitao Zhou, Woonsoo Lee, Keyin Liu, Xiaohan Wang, Xinxin Li and 10 more

Abstract read
In one paragraph

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.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

26 citing papers in PubMed.

  1. Review
  2. Nano-Infrared Imaging and Spectroscopy of Animal Cells in Liquid Environment.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  3. Manipulating the Assembly and Architecture of Fibrillar Silk.Advanced materials (Deerfield Beach, Fla.) · 2025
    Article
  4. Article
  5. Two-dimensional silk.Science advances · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Silk-Based Aqueous Microcontact Printing.ACS biomaterials science & engineering · 2018
    Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

20 authors.

Nan QinState Key Laboratory of Transducer Technology, Shanghai Institute of Microsystem and Information Technology, Chinese Academy of Sciences, Shanghai 200050, China.
Shaoqing ZhangDepartment of Mechanical Engineering, the University of Texas at Austin, Austin, Texas 78712, USA.
Jianjuan JiangState Key Laboratory of Transducer Technology, Shanghai Institute of Microsystem and Information Technology, Chinese Academy of Sciences, Shanghai 200050, China.
Stephanie Gilbert CorderDepartment of Physics and Astronomy, Stony Brook University, Stony Brook, New York 11794, USA.ORCID 0000-0002-5041-8670
Zhigang QianState Key Laboratory of Microbial Metabolism, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, China.
Zhitao ZhouState Key Laboratory of Transducer Technology, Shanghai Institute of Microsystem and Information Technology, Chinese Academy of Sciences, Shanghai 200050, China.
Woonsoo LeeDepartment of Mechanical Engineering, the University of Texas at Austin, Austin, Texas 78712, USA.
Keyin LiuState Key Laboratory of Transducer Technology, Shanghai Institute of Microsystem and Information Technology, Chinese Academy of Sciences, Shanghai 200050, China.
Xiaohan WangDepartment of Mechanical Engineering, the University of Texas at Austin, Austin, Texas 78712, USA.
Xinxin LiState Key Laboratory of Transducer Technology, Shanghai Institute of Microsystem and Information Technology, Chinese Academy of Sciences, Shanghai 200050, China.
Zhifeng ShiDepartment of Neurosurgery, Huashan Hospital of Fudan University, Wulumuqi Zhong Road 12, Shanghai, 200040, China.
Ying MaoDepartment of Neurosurgery, Huashan Hospital of Fudan University, Wulumuqi Zhong Road 12, Shanghai, 200040, China.
Hans A BechtelNano-FTIR, Advanced Light Source Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
Michael C MartinNano-FTIR, Advanced Light Source Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.ORCID 0000-0002-6611-070X
Xiaoxia XiaState Key Laboratory of Microbial Metabolism, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, China.
Benedetto MarelliDepartment of Civil and Environmental Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
David L KaplanDepartment of Biomedical Engineering, Tufts University, Medford, Massachusetts 02155, USA.
Fiorenzo G OmenettoDepartment of Biomedical Engineering, Tufts University, Medford, Massachusetts 02155, USA.
Mengkun LiuDepartment of Physics and Astronomy, Stony Brook University, Stony Brook, New York 11794, USA.
Tiger H TaoState Key Laboratory of Transducer Technology, Shanghai Institute of Microsystem and Information Technology, Chinese Academy of Sciences, Shanghai 200050, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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

AnimalsBombyxFibroinsImaging, Three-DimensionalMolecular ConformationSilkSpectroscopy, Fourier Transform InfraredSpidersFibroinsSilk

Identifiers

PMID27713412
PMCPMC5059764

What OpenQuestion holds

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Registered trials

None linked

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.