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Research Paper on Structural insights and a therapeutic perspective on taurine in neurodegenerative diseases from the expedition into taurine biology

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Research Paper on Structural insights and a therapeutic perspective on taurine in neurodegenerative diseases from the expedition into taurine biology

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Title: Structural insights and a therapeutic perspective on taurine in neurodegenerative diseases from the expedition into taurine biology

Abstract: Proteins that are misfolded tend to accumulate in neurodegenerative diseases (NDs). The hallmarks of protein aggregation in NDs include mitochondrial dysfunction in addition to causing an increase in ER stress, neuroinflammation, and synaptic loss. Since the buildup of misfolded proteins impairs normal neuronal function, it causes ER stress, which in turn activates downstream effectors to form the unfolded protein response (UPRER), which regulates cellular gene expression. It is crucial to investigate new methods of treating these debilitating diseases due to the absence of disease-modifying therapeutic targets in various NDs and the exponential rise in the number of cases. In one such method, it has been discovered that osmolytes (low molecular weight substances), such as taurine, encourage protein folding under stress, preventing the aggregation of the misfolded proteins. Taurine-mediated resumption of protein folding causes a shift in folding homeostasis more towards functionality than towards aggregation and degradation, maintaining the structural integrity of the protein. Together, taurine and NDs work to protect against damage by refolding misfolded proteins to restore their stability and functionality. The current study summarizes the genetics of NDs in relation to mitochondrial dysfunction, ER stress, neuroinflammation, and synaptic loss, as well as offers recent and helpful insights into understanding the progression of NDs. It also draws attention to the structural and functional roles that taurine plays in protecting against protein aggregation and misfolding, refocusing attention more on the creation of potent therapeutic components that could prevent the emergence of NDs.

Keywords: aggregation; neurodegenerative diseases; osmolytes; protein folding; therapeutics; unfolded protein response

Paper Quality: SCOPUS / Web of Science Level Research Paper

Subject: Biomolecules

Writer Experience: 20+ Years

Plagiarism Report: Turnitin Plagiarism Report will be less than 10%

Restriction: Only one author may purchase a single paper. The paper will then indicate that it is out of stock.

What will I get after the purchase?

A turnitin plagiarism report of less than 10% in a pdf file and a full research paper in a word document.

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