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Article summary:

1. The article discusses the development and application of serine/threonine ligation (STL) for synthetic protein chemistry.

2. STL involves the chemoselective reaction between peptide salicylaldehyde esters and peptides with N-terminal serine or threonine.

3. The method has been successfully applied to the synthesis of both linear and cyclic peptides/proteins.

Article analysis:

The article is a reliable source of information on the development and application of serine/threonine ligation (STL) for synthetic protein chemistry, as it is published in Organic & Biomolecular Chemistry (RSC Publishing), a reputable journal in the field of organic and biomolecular chemistry. The authors are affiliated with two well-known universities, The University of Hong Kong and Shenzhen Institute of Research and Innovation of the University of Hong Kong, which adds to its credibility. Furthermore, the article provides detailed information on STL, including its chemoselective reaction between peptide salicylaldehyde esters and peptides with N-terminal serine or threonine, as well as its successful application to both linear and cyclic peptides/proteins.

The article does not appear to have any biases or one-sided reporting, as it presents an objective overview of STL without making any unsupported claims or omitting any points of consideration. It also does not contain any promotional content or partiality towards any particular viewpoint. Additionally, possible risks associated with STL are noted in the article, such as potential side reactions that may occur during synthesis due to competing pathways.

In conclusion, this article is a trustworthy source on STL for synthetic protein chemistry due to its publication in a reputable journal by authors from two well-known universities, its objective overview without any unsupported claims or omissions, lack of promotional content or partiality towards any particular viewpoint, and noting possible risks associated with STL.