stands for Digital Object Identifier
and is the unique identifier for objects on the internet. It can be used to create persistent link and to cite articles.
Using DOI as a persistent link
To create a persistent link, add「http://dx.doi.org/」
before a DOI.
For instance, if the DOI of an article is 10.5297/ser.1201.002 , you can link persistently to the article by entering the following link in your browser: http://dx.doi.org/ 10.5297/ser.1201.002 。
The DOI link will always direct you to the most updated article page no matter how the publisher changes the document's position, avoiding errors when engaging in important research.
Cite a document with DOI
When citing references, you should also cite the DOI if the article has one. If your citation guideline does not include DOIs, you may cite the DOI link.
DOIs allow accurate citations, improve academic contents connections, and allow users to gain better experience across different platforms. Currently, there are more than 70 million DOIs registered for academic contents. If you want to understand more about DOI, please visit airiti DOI Registration （ doi.airiti.com ） 。
- 1. Arold ST. (2011). How focal adhesion kinase achieves regulation by linking ligand binding, localization and action. Curr. Opin. Struct. Biol. 21: 808-813.
- 2. Barret C, Roy C, Montcourrier P, Mangeat P, Niggli V. (2000). Mutagenesis of the Phosphatidylinositol 4,5-Bisphosphate (PIP2) Binding Site in the NH2-Terminal Domain of Ezrin Correlates with Its Altered Cellular Distribution. J. Cell Biol. 151: 1067–1079.
- 3. Bompard G, Martin M, Roy C, Vignon F, Friess G. (2003). Membrane targeting of protein tyrosine phosphatase PTPL1 through its FERM domain via binding to phosphatidylinositol 4,5-biphosphate. J. Cell Sci. 116: 2519–2530.
- 4. Cai X, Lietha D, Ceccarelli DF, Karginov AV, Rajfur Z, Jacobson K et al.(2008). Spatial and temporal regulation of focal adhesion kinase activity in living cells. Mol. Cell. Biol. 28: 201-214.
- 5. Calalb MB, Polte TR, Hanks SK. (1995). Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases. Mol. Cell. Biol. 15: 954-963.
The cart has had several articles, so do you want to clear it, or add together to the cart?