Evidence map›Paper›PMID 34531321›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Critical role of minor eggcase silk component in promoting spidroin chain alignment and strong fiber formation.

Tiantian Fan, Ruiqi Qin, Yan Zhang, Jingxia Wang, Jing-Song Fan, Xiangli Bai, Wensu Yuan, Weidong Huang, Shuo Shi, Xun-Cheng Su and 2 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

5 citing papers in PubMed, 21 citations in OpenAlex.

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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

12 authors at 4 institutions in 2 countries.

Tiantian FanSchool of Life Sciences, Tianjin University, Tianjin 300072, People's Republic of China.ORCID 0000-0003-4867-3856
Ruiqi QinSchool of Life Sciences, Tianjin University, Tianjin 300072, People's Republic of China.
Yan ZhangSchool of Life Sciences, Tianjin University, Tianjin 300072, People's Republic of China.ORCID 0000-0002-0207-149X
Jingxia WangSchool of Life Sciences, Tianjin University, Tianjin 300072, People's Republic of China.
Jing-Song FanDepartment of Biological Sciences, National University of Singapore, Singapore 117543, Singapore.
Xiangli BaiSchool of Life Sciences, Tianjin University, Tianjin 300072, People's Republic of China.
Wensu YuanSchool of Life Sciences, Tianjin University, Tianjin 300072, People's Republic of China.
Weidong HuangDepartment of Biochemistry and Molecular Biology, School of Basic Medicine, Ningxia Medical University, Yinchuan 750004, People's Republic of China.
Shuo ShiState Key Laboratory of Elemento-Organic Chemistry and College of Chemistry, Nankai University, Tianjin 300071, People's Republic of China.
Xun-Cheng SuState Key Laboratory of Elemento-Organic Chemistry and College of Chemistry, Nankai University, Tianjin 300071, People's Republic of China.ORCID 0000-0003-3051-0047
Daiwen YangDepartment of Biological Sciences, National University of Singapore, Singapore 117543, Singapore.
Zhi LinSchool of Life Sciences, Tianjin University, Tianjin 300072, People's Republic of China; linzhi@linzhi.net.ORCID 0000-0002-8902-4935
Tianjin University · CNNankai University · CNNational University of Singapore · SGNingxia Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Natural spider silk with extraordinary mechanical properties is typically spun from more than one type of spidroin. Although the main components of various spider silks have been widely studied, little is known about the molecular role of the minor silk components in spidroin self-assembly and fiber formation. Here, we show that the minor component of spider eggcase silk, TuSp2, not only accelerates self-assembly but remarkably promotes molecular chain alignment of spidroins upon physical shearing. NMR structure of the repetitive domain of TuSp2 reveals that its dimeric structure with unique charged surface serves as a platform to recruit different domains of the main eggcase component TuSp1. Artificial fiber spun from the complex between TuSp1 and TuSp2 minispidroins exhibits considerably higher strength and Young's modulus than its native counterpart. These results create a framework for rationally designing silk biomaterials based on distinct roles of silk components.

Indexed as

AnimalsBiocompatible MaterialsFibroinsSilkSpidersBiocompatible MaterialsFibroinsSilkspidroin 2eggcase silkminor componentNMRTuSp1TuSp2

Identifiers

PMID34531321
PMCPMC8463894
OpenAlexW3201368995

What OpenQuestion holds

Textmetadata
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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.