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Article summary:
1. Abnormal phosphorylation of amyloid-beta precursor protein (APP) is a pathologic feature of Alzheimer's disease.
2. c-Jun NH2-terminal kinase (JNK), not cyclin-dependent kinase 5, is required for APP phosphorylation, leading to localized accumulation of phosphorylated APP (pAPP) in neurites.
3. JNK-interacting protein-3 (JIP-3) selectively increases APP phosphorylation, accumulation of pAPP into processes, and stimulates process extension in both neurons and COS-1 cells.
Article analysis:
The article “c-Jun NH2-terminal kinase-interacting protein-3 facilitates phosphorylation and controls localization of amyloid-beta precursor protein” is a well written and comprehensive study on the role of JNK interacting proteins in the regulation of APP phosphorylation and localization. The authors provide evidence that JIP-3 selectively increases APP phosphorylation, accumulation of pAPP into processes, and stimulates process extension in both neurons and COS-1 cells. The article is reliable as it provides detailed information on the methods used to conduct the experiments as well as clear results from each experiment which are supported by figures.
The article does not appear to be biased or one sided as it presents both sides equally with no promotional content or partiality towards any particular point of view. The authors also note possible risks associated with their findings such as abnormal APP phosphorylation being a pathologic feature of Alzheimer's disease.
The only potential issue with the article is that it does not explore counterarguments or present any missing points of consideration which could have been beneficial for readers to gain a more comprehensive understanding on the topic discussed in the article.