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 ） 。
謝孟穎 , Masters Advisor：邱式鴻
繁體中文 DOI： 10.6342/NTU.2004.02518
- Andley, U.P., Mathur, S., Griest, T.A., Petrash, J.M. (1996) Cloning, expression, and chaperone-like activity of human alphaA-crystallin. J Biol Chem, 271, 31973-31980.
- Berengian, A.R., Parfenova, M., Mchaourab, H.S. (1999) Site-directed spin labeling study of subunit interactions in the alpha-crystallin domain of small heat-shock proteins. Comparison of the oligomer symmetry in alphaA-crystallin, HSP 27, and HSP 16.3. J Biol Chem, 274, 6305-6314.
- Buchner, J. (1996) Supervising the fold: functional principles of molecular chaperones. FASEB J., 10, 10-19.
- Candido, E.P., Ding, L. (2000) HSP25, a small heat shock protein associated with dense bodies and M-lines of body wall muscle in Caenorhabditis elegans. J Biol Chem, 275, 9510-517.
- Chang, Z., Primm, T.P., Jakana, J., Lee, I.H., Serysheva, I., Chiu, W., Gilbert, H.F., Quiocho, F.A. (1996) Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation. J Biol Chem, 271, 7218-7223.
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