1. GDF11 forms a noncovalent latent complex with its SPC-cleaved prodomain that is activated by members of the BMP1/Tolloid family of metalloproteinases.
2. This latent complex may play a general role in modulating neural differentiation.
3. Mutant GDF11 prodomains impervious to cleavage by BMP1/Tolloid proteinases are shown to be potent stimulators of neurodifferentiation, with potential for therapeutic applications.
The article is generally reliable and trustworthy, as it provides evidence for its claims and presents both sides of the argument equally. The authors provide evidence for their claims through experiments and research, which makes the article more credible and reliable. Furthermore, the authors have provided references to other studies that support their findings, which adds to the trustworthiness of the article.
The article does not appear to have any biases or one-sided reporting, as it presents both sides of the argument equally and objectively. Additionally, there are no unsupported claims or missing points of consideration in the article. All claims made are supported by evidence from experiments and research conducted by the authors or referenced from other studies.
The article does not contain any promotional content or partiality towards one side over another; instead it presents both sides objectively and fairly. Furthermore, possible risks associated with using mutant GDF11 prodomains are noted in the article, which adds to its reliability and trustworthiness.
In conclusion, this article is generally reliable and trustworthy due to its objective presentation of both sides of the argument, supported claims with evidence from experiments and research conducted by the authors or referenced from other studies, lack of bias or one-sided reporting, lack of promotional content or partiality towards one side over another, noting possible risks associated with using mutant GDF11 prodomains, and lack of unsupported claims or missing points of consideration in the article.