In silico Screening and Molecular Interaction Studies of Tetrahydrocannabinol and its Derivatives with Acetylcholine Binding Protein

Panigrahi, Priya P.; Singla, Ramit; Bansal, Ankush; Comar, Moacyr; Jaitak, Vikas; Yennamalli, Ragothaman M.; Singh, Tiratha Raj

doi:10.2174/2212796812666180416145232

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Roles Of Hsp70 and Hsp90 In Neurogenerative Diseases1

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“…AD is the most common type of dementia, mainly afflicting aging population [56][57][58]. A major hypothesis for the disease pathology posits the accumulation of misfolded proteins, Amyloid β and Tau in the forebrain [59,60].…”

Section: Roles Of Hsp70 and Hsp90 In Neurogenerative Diseasesmentioning

confidence: 99%

HSP70 and HSP90 in neurodegenerative diseases

Gupta

Bansal

Hashimoto-Torii

2020

Neuroscience Letters

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Molecular chaperones have a role to stabilize proteins or assist them in reaching their native fold. Heat shock proteins (HSPs) are a family of molecular chaperons that protect proteins from cellular stress during the assembly of protein complexes and also prevent the proteins from aggregation and disassembly. The immediate increase of HSPs is crucial for cellular adaptation to environmental changes and protection of other proteins from denaturation, thereby maintaining the cellular homeostasis and increasing the longevity of an organism. HSP70 and HSP90 are the most studied HSPs in this very large HSP family. Notably, HSP90 also stabilizes the disease-related proteins in neurodegenerative disorders. Therefore, small molecules that inhibit the HSP90 but also increase the HSP70 has been tested as potential drugs for neurodegenerative disorders.

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