{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,20]],"date-time":"2026-06-20T16:51:52Z","timestamp":1781974312497,"version":"3.54.5"},"reference-count":41,"publisher":"Bentham Science Publishers Ltd.","issue":"4","content-domain":{"domain":["eurekaselect.com"],"crossmark-restriction":true},"short-container-title":["CNSNDDT"],"published-print":{"date-parts":[[2026,4]]},"abstract":"<jats:sec>\n                    <jats:title>Introduction:<\/jats:title>\n                    <jats:p>JNK3 is a specific isoform of c-Jun N-terminal kinase, mainly found in the\nbrain, and is highly sensitive to stress-associated signals in the central nervous system. It has been\nreported that JNK3 plays a crucial role in neurite formation and cognition. During pathological\nstates such as Alzheimer\u2019s disease, cerebral ischemia, Traumatic brain injury (TBI), Parkinson\u2019s\ndisease, and epilepsy, it is found to be in a hyperactivated form. Hyperphosphorylation of amyloid\nprecursor protein (APP) and tau leads to toxic A\u03b242 and neurofibrillary tangles. Excess A\u03b2 activates\nJNK3 signaling, causing neuronal loss. JNK3 also contributes to mitochondrial dysfunction, Oxidative\nstress, neuroinflammation, and apoptosis, driving AD progression.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods:<\/jats:title>\n                    <jats:p>This study aims to identify possible therapeutics based on their physicochemical, ADMET,\ntoxicity, and drug-likeness properties. Moreover, we utilized Molecular docking and Molecular\ndynamics (MD) simulation to reveal possible inhibitors against JNK3.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results:<\/jats:title>\n                    <jats:p>Based on the highest binding affinity against JNK3, the best compounds, Myricetin and\nKaempferol, were subjected to an MD simulation study. RMSD analysis indicated that the JNK3-\nKampferol complex showed more stability; at the same time, myricetin formed more hydrogen\nbonds with JNK3. Moreover, both compounds exhibited favorable ADMET properties.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Discussion:<\/jats:title>\n                    <jats:p>This study identified Kaempferol and myricetin as potential inhibitors that target JNK3\nthrough molecular docking and MD simulation studies. Both compounds demonstrated favorable\nADMET profiles, supporting their promise as safe, orally available drug candidates.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusion:<\/jats:title>\n                    <jats:p>Therefore, Kaempferol and myricetin emerge as promising candidates for further investigations\nin both in vitro and in vivo studies to treat Alzheimer\u2019s disease and other neurodegenerative\ndisorders.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.2174\/0118715273371881250723061908","type":"journal-article","created":{"date-parts":[[2025,8,22]],"date-time":"2025-08-22T09:45:45Z","timestamp":1755855945000},"page":"310-322","update-policy":"https:\/\/doi.org\/10.2174\/bsp_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Targeting JNK3: An In-silico Approach to Uncover Potential Therapeutics for Alzheimer\u2019s Disease"],"prefix":"10.2174","volume":"25","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2856-8274","authenticated-orcid":true,"given":"Mohd","family":"Kashif","sequence":"first","affiliation":[{"name":"School of Life Science, B.S. 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