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Solution structure of recombinant Pvfp-5β reveals insights into mussel adhesion.

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第一作者： Maria Agnese,Morando

第一单位： Structural Biology and Biophysics Unit, Fondazione Ri.MED, 90133, Palermo, Italy.

作者： Maria Agnese,Morando ^[1] ; Francesca,Venturella ^[1] ; Martina,Sollazzo ^[2] ; Elisa,Monaca ^[1] ; Raffaele,Sabbatella ^[1] ; Valeria,Vetri ^[3] ; Rosa,Passantino ^[4] ; Annalisa,Pastore ^[5] ; Caterina,Alfano ^[6]

作者单位： Structural Biology and Biophysics Unit, Fondazione Ri.MED, 90133, Palermo, Italy. ^[1] Structural Biology and Biophysics Unit, Fondazione Ri.MED, 90133, Palermo, Italy.;Department of Biological, Chemical and Pharmaceutical Sciences and Technologies (STEBICEF), University of Palermo, 90128, Palermo, Italy. ^[2] Department of Physics and Chemistry-Emilio Segrè (DiFC), University of Palermo, 90128, Palermo, Italy. ^[3] Biophysics Institute, National Research Council, 90143, Palermo, Italy. ^[4] European Synchrotron Radiation Facility, Ave des Martyrs, 38000, Grenoble, France. ^[5] Structural Biology and Biophysics Unit, Fondazione Ri.MED, 90133, Palermo, Italy. calfano@fondazionerimed.com. ^[6]

医学主题词黏着剂(Adhesives);动物(Animals);人工智能(Artificial Intelligence);生物相容性材料(Biocompatible Materials);表皮生长因子(Epidermal Growth Factor);翡翠贻贝(Perna);组织工程(Tissue Engineering)

DOI 10.1038/s42003-022-03699-w

PMID 35879391

发布时间 2025-05-30

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Communications biology

2022年5卷1期

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Communications biology

2022年5卷1期

739页

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Solution structure of recombinant Pvfp-5β reveals insights into mussel adhesion.

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Solution structure of recombinant Pvfp-5β reveals insights into mussel adhesion.

Communications biology

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Communications biology

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