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.Wickner, S., Maurizi, M. R., & Gottesman, S. (1999). Posttranslational quality control: folding, refolding, and degrading proteins. Science, 286(5446), 1888-1893.
- 2.Bukau, B., & Horwich, A. L. (1998). The Hsp70 and Hsp60 chaperone machines. Cell, 92(3), 351-366.
- 3.Gassler, C. S., Buchberger, A., Laufen, T., Mayer, M. P., Schroder, H., Valencia, A., & Bukau, B. (1998). Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone. Proc Natl Acad Sci USA, 95(26), 15229-15234.
- 4.Goloubinoff, P., Mogk, A., Zvi, A. P., Tomoyasu, T., & Bukau, B. (1999). Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc Natl Acad Sci USA, 96(24), 13732-13737.
- 5.Marchenko, N., Marchenkov, V. V., Kaisheva, A. L., Kashparov, I. A., Kotova, N. V., Kaliman, P. A., & Semisotnov, G. V. (2006). Affinity chromatography of GroEL chaperonin based on denatured proteins: role of electrostatic interactions in regulation of GroEL affinity for protein substrates. 71(12), 1357-1364.
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