Evidence map›Paper›PMID 32978166›Full record

ArticleScience advances2020

Structure and sequence features of mussel adhesive protein lead to its salt-tolerant adhesion ability.

Xinwen Ou, Bin Xue, Yichong Lao, Yanee Wutthinitikornkit, Ranran Tian, Aodong Zou, Lingyun Yang, Wei Wang, Yi Cao, Jingyuan Li

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

28 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. A biofilm-derived peptide as an underwater adhesive.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Identification and characterization of a wet adhesive protein extracted fromProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Mechanochemistry: Fundamental Principles and Applications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  13. Article
  14. Mussel-InspiredACS omega · 2025
    Article
  15. Review
  16. Review
  17. Tough Hydrogels with Different Toughening Mechanisms and Applications.International journal of molecular sciences · 2024
    Review
  18. Article
  19. Enzymatic polymerization of enantiomericNature communications · 2023
    Article
  20. 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

10 authors at 3 institutions in 1 country.

Xinwen OuZhejiang Province Key Laboratory of Quantum Technology and Device, Institute of Quantitative Biology, Department of Physics, Zhejiang University, Zheda Road 38, Hangzhou 310027, China.ORCID 0000-0001-6694-7932
Bin XueCollaborative Innovation Center of Advanced Microstructures, National Laboratory of Solid State Microstructure, Department of Physics, Nanjing University, Nanjing 210093, China.ORCID 0000-0002-0822-6501
Yichong LaoZhejiang Province Key Laboratory of Quantum Technology and Device, Institute of Quantitative Biology, Department of Physics, Zhejiang University, Zheda Road 38, Hangzhou 310027, China.ORCID 0000-0002-1895-1467
Yanee WutthinitikornkitZhejiang Province Key Laboratory of Quantum Technology and Device, Institute of Quantitative Biology, Department of Physics, Zhejiang University, Zheda Road 38, Hangzhou 310027, China.ORCID 0000-0003-3153-1325
Ranran TianZhejiang Province Key Laboratory of Quantum Technology and Device, Institute of Quantitative Biology, Department of Physics, Zhejiang University, Zheda Road 38, Hangzhou 310027, China.ORCID 0000-0001-7565-1703
Aodong ZouZhejiang Province Key Laboratory of Quantum Technology and Device, Institute of Quantitative Biology, Department of Physics, Zhejiang University, Zheda Road 38, Hangzhou 310027, China.ORCID 0000-0002-9184-7658
Lingyun YangiHuman Institute, Shanghai Tech University, 393 Hua Xia Zhong Road, Shanghai 201210, China.ORCID 0000-0003-0915-7744
Wei WangCollaborative Innovation Center of Advanced Microstructures, National Laboratory of Solid State Microstructure, Department of Physics, Nanjing University, Nanjing 210093, China.ORCID 0000-0001-5441-0302
Yi CaoCollaborative Innovation Center of Advanced Microstructures, National Laboratory of Solid State Microstructure, Department of Physics, Nanjing University, Nanjing 210093, China. caoyi@nju.edu.cn jingyuanli@zju.edu.cn.ORCID 0000-0003-1493-7868
Jingyuan LiZhejiang Province Key Laboratory of Quantum Technology and Device, Institute of Quantitative Biology, Department of Physics, Zhejiang University, Zheda Road 38, Hangzhou 310027, China. caoyi@nju.edu.cn jingyuanli@zju.edu.cn.ORCID 0000-0003-2926-1864
Zhejiang University of Technology · CNCollaborative Innovation Center of Advanced Microstructures · CNShanghaiTech University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mussels can strongly adhere to hydrophilic minerals in sea habitats by secreting adhesive proteins. The adhesion ability of these proteins is often attributed to the presence of Dopa derived from posttranslational modification of Tyr, whereas the contribution of structural feature is overlooked. It remains largely unknown how adhesive proteins overcome the surface-bound water layer to establish underwater adhesion. Here, we use molecular dynamics simulations to probe the conformations of adhesive protein Pvfp-5β and its salt-tolerant underwater adhesion on superhydrophilic mica. Dopa and positively charged basic residues form pairs, in this intrinsically disordered protein, and these residue pairs can lead to firm surface binding. Our simulations further suggest that the unmodified Tyr shows similar functions on surface adhesion by forming pairing structure with a positively charged residue. We confirm the presence of these residue pairs and verify the strong binding ability of unmodified proteins using nuclear magnetic resonance spectroscopy and lap shear tests.

Identifiers

PMID32978166
PMCPMC7518861
OpenAlexW3088203618

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.