Evidence map›Paper›PMID 34381032›Full record

ArticleNature communications2021

Protein interface redesign facilitates the transformation of nanocage building blocks to 1D and 2D nanomaterials.

Xiaorong Zhang, Yu Liu, Bowen Zheng, Jiachen Zang, Chenyan Lv, Tuo Zhang, Hongfei Wang, Guanghua Zhao

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.4field-weighted citation impact, top 12% of its field
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

8 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Assembly and Functionality of 2D Protein Arrays.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  6. Article
  7. Article
  8. Article
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

8 authors at 2 institutions in 1 country.

Xiaorong ZhangCollege of Food Science & Nutritional Engineering, China Agricultural University, Beijing Key Laboratory of Functional Food from Plant Resources, Beijing, 100083, China.
Yu LiuCollege of Food Science & Nutritional Engineering, China Agricultural University, Beijing Key Laboratory of Functional Food from Plant Resources, Beijing, 100083, China.
Bowen ZhengCollege of Food Science & Nutritional Engineering, China Agricultural University, Beijing Key Laboratory of Functional Food from Plant Resources, Beijing, 100083, China.
Jiachen ZangCollege of Food Science & Nutritional Engineering, China Agricultural University, Beijing Key Laboratory of Functional Food from Plant Resources, Beijing, 100083, China.
Chenyan LvCollege of Food Science & Nutritional Engineering, China Agricultural University, Beijing Key Laboratory of Functional Food from Plant Resources, Beijing, 100083, China.
Tuo ZhangCollege of Food Science & Nutritional Engineering, China Agricultural University, Beijing Key Laboratory of Functional Food from Plant Resources, Beijing, 100083, China. zhangtuo@cau.edu.cn.ORCID 0000-0002-0900-9285
Hongfei WangKey Laboratory of Chemical Biology and Molecular Engineering of Education Ministry, Key Laboratory of Energy Conversion and Storage Materials of Shanxi Province, Institute of Molecular Science, Shanxi University, Taiyuan, China.
Guanghua ZhaoCollege of Food Science & Nutritional Engineering, China Agricultural University, Beijing Key Laboratory of Functional Food from Plant Resources, Beijing, 100083, China. gzhao@cau.edu.cn.ORCID 0000-0001-8587-9680
China Agricultural University · CNShanxi University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although various artificial protein nanoarchitectures have been constructed, controlling the transformation between different protein assemblies has largely been unexplored. Here, we describe an approach to realize the self-assembly transformation of dimeric building blocks by adjusting their geometric arrangement. Thermotoga maritima ferritin (TmFtn) naturally occurs as a dimer; twelve of these dimers interact with each other in a head-to-side manner to generate 24-meric hollow protein nanocage in the presence of Ca

Indexed as

CalciumFerritinsNanostructuresNanotechnologyPolyethylene GlycolsProtein MultimerizationProteinsThermotoga maritimaCalciumFerritinsPolyethylene GlycolsProteins

Identifiers

PMID34381032
PMCPMC8357837
OpenAlexW3187887373

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.