{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,10]],"date-time":"2026-10-10T00:53:02Z","timestamp":1791593582318,"version":"4.3.4"},"reference-count":58,"publisher":"Springer Science and Business Media LLC","issue":"8","license":[{"start":{"date-parts":[[2018,1,2]],"date-time":"2018-01-02T00:00:00Z","timestamp":1514851200000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"funder":[{"DOI":"10.13039\/501100001407","name":"Department of Biotechnology , Ministry of Science and Technology","doi-asserted-by":"publisher","award":["BT\/HRD\/35\/01\/03\/2013"],"award-info":[{"award-number":["BT\/HRD\/35\/01\/03\/2013"]}],"id":[{"id":"10.13039\/501100001407","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Mol Neurobiol"],"published-print":{"date-parts":[[2018,8]]},"DOI":"10.1007\/s12035-017-0853-3","type":"journal-article","created":{"date-parts":[[2018,1,2]],"date-time":"2018-01-02T02:34:06Z","timestamp":1514860446000},"page":"6337-6346","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":39,"title":["Azadiradione Restores Protein Quality Control and Ameliorates the Disease Pathogenesis in a Mouse Model of Huntington\u2019s Disease"],"prefix":"10.1007","volume":"55","author":[{"given":"Brijesh Kumar","family":"Singh","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Naman","family":"Vatsa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vinod K.","family":"Nelson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vipendra","family":"Kumar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shashi Shekhar","family":"Kumar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Subhash C.","family":"Mandal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mahadeb","family":"Pal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nihar Ranjan","family":"Jana","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2018,1,2]]},"reference":[{"issue":"3","key":"853_CR1","doi-asserted-by":"publisher","first-page":"189","DOI":"10.2190\/HU6W-3K7Q-NAEL-XU6K","volume":"24","author":"MF Mendez","year":"1994","unstructured":"Mendez MF (1994) Huntington\u2019s disease: update and review of neuropsychiatric aspects. Int J Psychiatry Med 24(3):189\u2013208. \nhttps:\/\/doi.org\/10.2190\/HU6W-3K7Q-NAEL-XU6K","journal-title":"Int J Psychiatry Med"},{"issue":"6","key":"853_CR2","doi-asserted-by":"publisher","first-page":"559","DOI":"10.1097\/00005072-198511000-00003","volume":"44","author":"JP Vonsattel","year":"1985","unstructured":"Vonsattel JP, Myers RH, Stevens TJ, Ferrante RJ, Bird ED, Richardson EP Jr (1985) Neuropathological classification of Huntington\u2019s disease. J Neuropathol Exp Neurol 44(6):559\u2013577. \nhttps:\/\/doi.org\/10.1097\/00005072-198511000-00003","journal-title":"J Neuropathol Exp Neurol"},{"issue":"1","key":"853_CR3","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1097\/00005072-199501000-00013","volume":"54","author":"JC Hedreen","year":"1995","unstructured":"Hedreen JC, Folstein SE (1995) Early loss of neostriatal striosome neurons in Huntington\u2019s disease. J Neuropathol Exp Neurol 54(1):105\u2013120. \nhttps:\/\/doi.org\/10.1097\/00005072-199501000-00013","journal-title":"J Neuropathol Exp Neurol"},{"issue":"4688","key":"853_CR4","doi-asserted-by":"publisher","first-page":"770","DOI":"10.1126\/science.3155875","volume":"227","author":"GA Graveland","year":"1985","unstructured":"Graveland GA, Williams RS, DiFiglia M (1985) Evidence for degenerative and regenerative changes in neostriatal spiny neurons in Huntington\u2019s disease. Science 227(4688):770\u2013773. \nhttps:\/\/doi.org\/10.1126\/science.3155875","journal-title":"Science"},{"key":"853_CR5","doi-asserted-by":"publisher","unstructured":"The Huntington\u2019s Disease Collaborative Research Group (1993) A novel gene containing trinucleotide repeat that is expanded and unstable on Huntington\u2019s disease chromosomes. Cell 72(6):971\u2013983. \nhttps:\/\/doi.org\/10.1016\/0092-8674(93)90585-E","DOI":"10.1016\/0092-8674(93)90585-E"},{"issue":"4","key":"853_CR6","doi-asserted-by":"publisher","first-page":"442","DOI":"10.1038\/ng0896-442","volume":"13","author":"YP Goldberg","year":"1996","unstructured":"Goldberg YP, Nicholson DW, Rasper DM, Kalchman MA, Koide HB, Graham RK, Bromm M, Kazemi-Esfarjani P et al (1996) Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract. Nat Genet 13(4):442\u2013449. \nhttps:\/\/doi.org\/10.1038\/ng0896-442","journal-title":"Nat Genet"},{"issue":"10","key":"853_CR7","doi-asserted-by":"publisher","first-page":"958","DOI":"10.1038\/sj.embor.7400250","volume":"5","author":"C Landles","year":"2004","unstructured":"Landles C, Bates GP (2004) Huntingtin and the molecular pathogenesis of Huntington\u2019s disease. Fourth in molecular medicine review series. EMBO Rep 5(10):958\u2013963. \nhttps:\/\/doi.org\/10.1038\/sj.embor.7400250","journal-title":"EMBO Rep"},{"key":"853_CR8","doi-asserted-by":"publisher","first-page":"373","DOI":"10.1016\/B978-0-12-381328-2.00015-8","volume":"98","author":"L Jones","year":"2011","unstructured":"Jones L, Hughes A (2011) Pathogenic mechanisms in Huntington\u2019s disease. Int Rev Neurobiol 98:373\u2013418. \nhttps:\/\/doi.org\/10.1016\/B978-0-12-381328-2.00015-8","journal-title":"Int Rev Neurobiol"},{"issue":"5334","key":"853_CR9","doi-asserted-by":"publisher","first-page":"1990","DOI":"10.1126\/science.277.5334.1990","volume":"277","author":"M DiFiglia","year":"1997","unstructured":"DiFiglia M, Sapp E, Chase KO, Davies SW, Bates GP, Vonsattel JP, Aronin N (1997) Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277(5334):1990\u20131993. \nhttps:\/\/doi.org\/10.1126\/science.277.5334.1990","journal-title":"Science"},{"issue":"1","key":"853_CR10","doi-asserted-by":"publisher","first-page":"575","DOI":"10.1146\/annurev.neuro.29.051605.113042","volume":"30","author":"HT Orr","year":"2007","unstructured":"Orr HT, Zoghbi HY (2007) Trinucleotide repeat disorders. Annu Rev Neurosci 30(1):575\u2013621. \nhttps:\/\/doi.org\/10.1146\/annurev.neuro.29.051605.113042","journal-title":"Annu Rev Neurosci"},{"issue":"10","key":"853_CR11","doi-asserted-by":"publisher","first-page":"743","DOI":"10.1038\/nrg1691","volume":"6","author":"JR Gatchel","year":"2005","unstructured":"Gatchel JR, Zoghbi HY (2005) Diseases of unstable repeat expansion: mechanisms and common principles. Nat Rev Genet 6(10):743\u2013755. \nhttps:\/\/doi.org\/10.1038\/nrg1691","journal-title":"Nat Rev Genet"},{"key":"853_CR12","doi-asserted-by":"crossref","first-page":"218","DOI":"10.3389\/fncel.2014.00218","volume":"8","author":"J Margulis","year":"2014","unstructured":"Margulis J, Finkbeiner S (2014) Proteostasis in striatal cells and selective neurodegeneration in Huntington\u2019s disease. Front Cell Neurosci 8:218","journal-title":"Front Cell Neurosci"},{"issue":"20","key":"853_CR13","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1017\/S1462399403006549","volume":"5","author":"DC Rubinsztein","year":"2003","unstructured":"Rubinsztein DC, Carmichael J (2003) Huntington\u2019s disease: molecular basis of neurodegeneration. Expert Rev Mol Med 5(20):1\u201321. \nhttps:\/\/doi.org\/10.1017\/S1462399403006549","journal-title":"Expert Rev Mol Med"},{"issue":"2","key":"853_CR14","doi-asserted-by":"publisher","first-page":"95","DOI":"10.1016\/S0891-0618(03)00029-2","volume":"26","author":"NR Jana","year":"2003","unstructured":"Jana NR, Nukina N (2003) Recent advances in understanding the pathogenesis of polyglutamine diseases: involvement of molecular chaperones and ubiquitin-proteasome pathway. J Chem Neuroanat 26(2):95\u2013101. \nhttps:\/\/doi.org\/10.1016\/S0891-0618(03)00029-2","journal-title":"J Chem Neuroanat"},{"issue":"17","key":"853_CR15","doi-asserted-by":"publisher","first-page":"4263","DOI":"10.1111\/j.1742-4658.2008.06562.x","volume":"275","author":"S Sarkar","year":"2008","unstructured":"Sarkar S, Rubinsztein DC (2008) Huntington\u2019s disease: degradation of mutant huntingtin by autophagy. FEBS J 275(17):4263\u20134270. \nhttps:\/\/doi.org\/10.1111\/j.1742-4658.2008.06562.x","journal-title":"FEBS J"},{"issue":"6","key":"853_CR16","doi-asserted-by":"publisher","first-page":"1177","DOI":"10.1083\/jcb.200709080","volume":"180","author":"J Wang","year":"2008","unstructured":"Wang J, Wang CE, Orr A, Tydlacka S, Li SH, Li XJ (2008) Impaired ubiquitin-proteasome system activity in the synapses of Huntington\u2019s disease mice. J Cell Biol 180(6):1177\u20131189. \nhttps:\/\/doi.org\/10.1083\/jcb.200709080","journal-title":"J Cell Biol"},{"issue":"10","key":"853_CR17","doi-asserted-by":"publisher","first-page":"1049","DOI":"10.1093\/hmg\/10.10.1049","volume":"10","author":"NR Jana","year":"2001","unstructured":"Jana NR, Zemskov EA, Wang G, Nukina N (2001) Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release. Hum Mol Genet 10(10):1049\u20131059. \nhttps:\/\/doi.org\/10.1093\/hmg\/10.10.1049","journal-title":"Hum Mol Genet"},{"issue":"7154","key":"853_CR18","doi-asserted-by":"publisher","first-page":"704","DOI":"10.1038\/nature06022","volume":"448","author":"EJ Bennett","year":"2007","unstructured":"Bennett EJ, Shaler TA, Woodman B, Ryu KY, Zaitseva TS, Becker CH, Bates GP, Schulman H et al (2007) Global changes to the ubiquitin system in Huntington\u2019s disease. Nature 448(7154):704\u2013708. \nhttps:\/\/doi.org\/10.1038\/nature06022","journal-title":"Nature"},{"issue":"7","key":"853_CR19","doi-asserted-by":"publisher","first-page":"963","DOI":"10.1016\/j.drudis.2014.02.014","volume":"19","author":"CJ Cortes","year":"2014","unstructured":"Cortes CJ, La Spada AR (2014) The many faces of autophagy dysfunction in Huntington\u2019s disease: from mechanism to therapy. Drug Discov Today 19(7):963\u2013971. \nhttps:\/\/doi.org\/10.1016\/j.drudis.2014.02.014","journal-title":"Drug Discov Today"},{"issue":"6","key":"853_CR20","doi-asserted-by":"publisher","first-page":"583","DOI":"10.1177\/1073858405280639","volume":"11","author":"AG Valera","year":"2005","unstructured":"Valera AG, Diaz-Hernandez M, Hernandez F, Ortega Z, Lucas JJ (2005) The ubiquitin-proteasome system in Huntington\u2019s disease. Neuroscientist 11(6):583\u2013594. \nhttps:\/\/doi.org\/10.1177\/1073858405280639","journal-title":"Neuroscientist"},{"issue":"7342","key":"853_CR21","doi-asserted-by":"publisher","first-page":"226","DOI":"10.1038\/nature09873","volume":"472","author":"S Alavez","year":"2011","unstructured":"Alavez S, Vantipalli MC, Zucker DJ, Klang IM, Lithgow GJ (2011) Amyloid-binding compounds maintain protein homeostasis during ageing and extend lifespan. Nature 472(7342):226\u2013229. \nhttps:\/\/doi.org\/10.1038\/nature09873","journal-title":"Nature"},{"issue":"20","key":"853_CR22","doi-asserted-by":"publisher","first-page":"6383","DOI":"10.1113\/JP274334","volume":"595","author":"WA Sands","year":"2017","unstructured":"Sands WA, Page MM, Selman C (2017) Proteostasis and ageing: insights from long-lived mutant mice. J Physiol 595(20):6383\u20136390. \nhttps:\/\/doi.org\/10.1113\/JP274334","journal-title":"J Physiol"},{"issue":"15","key":"853_CR23","doi-asserted-by":"publisher","first-page":"2983","DOI":"10.1038\/emboj.2011.237","volume":"30","author":"K Rajalingam","year":"2011","unstructured":"Rajalingam K, Dikic I (2011) Healthy ageing through regulated proteostasis. EMBO J 30(15):2983\u20132985. \nhttps:\/\/doi.org\/10.1038\/emboj.2011.237","journal-title":"EMBO J"},{"issue":"7113","key":"853_CR24","doi-asserted-by":"publisher","first-page":"780","DOI":"10.1038\/nature05291","volume":"443","author":"DC Rubinsztein","year":"2006","unstructured":"Rubinsztein DC (2006) The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 443(7113):780\u2013786. \nhttps:\/\/doi.org\/10.1038\/nature05291","journal-title":"Nature"},{"issue":"10","key":"853_CR25","doi-asserted-by":"publisher","first-page":"2737","DOI":"10.1093\/hmg\/ddt667","volume":"23","author":"M Maheshwari","year":"2014","unstructured":"Maheshwari M, Bhutani S, Das A, Mukherjee R, Sharma A, Kino Y, Nukina N, Jana NR (2014) Dexamethasone induces heat shock response and slows down disease progression in mouse and fly models of Huntington\u2019s disease. Hum Mol Genet 23(10):2737\u20132751. \nhttps:\/\/doi.org\/10.1093\/hmg\/ddt667","journal-title":"Hum Mol Genet"},{"issue":"41","key":"853_CR26","doi-asserted-by":"publisher","first-page":"34908","DOI":"10.1074\/jbc.M506288200","volume":"280","author":"M Fujimoto","year":"2005","unstructured":"Fujimoto M, Takaki E, Hayashi T, Kitaura Y, Tanaka Y, Inouye S, Nakai A (2005) Active HSF1 significantly suppresses polyglutamine aggregate formation in cellular and mouse models. J Biol Chem 280(41):34908\u201334916. \nhttps:\/\/doi.org\/10.1074\/jbc.M506288200","journal-title":"J Biol Chem"},{"issue":"5","key":"853_CR27","doi-asserted-by":"publisher","first-page":"e37929","DOI":"10.1371\/journal.pone.0037929","volume":"7","author":"SM Chafekar","year":"2012","unstructured":"Chafekar SM, Duennwald ML (2012) Impaired heat shock response in cells expressing full-length polyglutamine-expanded huntingtin. PLoS One 7(5):e37929. \nhttps:\/\/doi.org\/10.1371\/journal.pone.0037929","journal-title":"PLoS One"},{"key":"853_CR28","doi-asserted-by":"publisher","first-page":"14405","DOI":"10.1038\/ncomms14405","volume":"8","author":"R Gomez-Pastor","year":"2017","unstructured":"Gomez-Pastor R, Burchfiel ET, Neef DW, Jaeger AM, Cabiscol E, McKinstry SU, Doss A, Aballay A et al (2017) Abnormal degradation of the neuronal stress-protective transcription factor HSF1 in Huntington\u2019s disease. Nat Commun 8:14405. \nhttps:\/\/doi.org\/10.1038\/ncomms14405","journal-title":"Nat Commun"},{"issue":"12","key":"853_CR29","doi-asserted-by":"publisher","first-page":"930","DOI":"10.1038\/nrd3453","volume":"10","author":"DW Neef","year":"2011","unstructured":"Neef DW, Jaeger AM, Thiele DJ (2011) Heat shock transcription factor 1 as a therapeutic target in neurodegenerative diseases. Nat Rev Drug Discov 10(12):930\u2013944. \nhttps:\/\/doi.org\/10.1038\/nrd3453","journal-title":"Nat Rev Drug Discov"},{"issue":"1","key":"853_CR30","doi-asserted-by":"publisher","first-page":"46","DOI":"10.1038\/cdd.2008.110","volume":"16","author":"S Sarkar","year":"2009","unstructured":"Sarkar S, Ravikumar B, Floto RA, Rubinsztein DC (2009) Rapamycin and mTOR-independent autophagy inducers ameliorate toxicity of polyglutamine-expanded huntingtin and related proteinopathies. Cell Death Differ 16(1):46\u201356. \nhttps:\/\/doi.org\/10.1038\/cdd.2008.110","journal-title":"Cell Death Differ"},{"issue":"6","key":"853_CR31","doi-asserted-by":"publisher","first-page":"585","DOI":"10.1038\/ng1362","volume":"36","author":"B Ravikumar","year":"2004","unstructured":"Ravikumar B, Vacher C, Berger Z, Davies JE, Luo S, Oroz LG, Scaravilli F, Easton DF et al (2004) Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease. Nat Genet 36(6):585\u2013595. \nhttps:\/\/doi.org\/10.1038\/ng1362","journal-title":"Nat Genet"},{"issue":"24","key":"853_CR32","doi-asserted-by":"publisher","first-page":"22044","DOI":"10.1074\/jbc.M212235200","volume":"278","author":"YC Tsai","year":"2003","unstructured":"Tsai YC, Fishman PS, Thakor NV, Oyler GA (2003) Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function. J Biol Chem 278(24):22044\u201322055. \nhttps:\/\/doi.org\/10.1074\/jbc.M212235200","journal-title":"J Biol Chem"},{"issue":"40","key":"853_CR33","doi-asserted-by":"publisher","first-page":"9152","DOI":"10.1523\/JNEUROSCI.3001-05.2005","volume":"25","author":"VM Miller","year":"2005","unstructured":"Miller VM, Nelson RF, Gouvion CM, Williams A, Rodriguez-Lebron E, Harper SQ, Davidson BL, Rebagliati MR et al (2005) CHIP suppresses polyglutamine aggregation and toxicity in vitro and in vivo. J Neurosci 25(40):9152\u20139161. \nhttps:\/\/doi.org\/10.1523\/JNEUROSCI.3001-05.2005","journal-title":"J Neurosci"},{"issue":"12","key":"853_CR34","doi-asserted-by":"publisher","first-page":"11635","DOI":"10.1074\/jbc.M412042200","volume":"280","author":"NR Jana","year":"2005","unstructured":"Jana NR, Dikshit P, Goswami A, Kotliarova S, Murata S, Tanaka K, Nukina N (2005) Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes. J Biol Chem 280(12):11635\u201311640. \nhttps:\/\/doi.org\/10.1074\/jbc.M412042200","journal-title":"J Biol Chem"},{"issue":"15","key":"853_CR35","doi-asserted-by":"publisher","first-page":"5706","DOI":"10.1073\/pnas.1402215111","volume":"111","author":"KP Bhat","year":"2014","unstructured":"Bhat KP, Yan S, Wang CE, Li S, Li XJ (2014) Differential ubiquitination and degradation of huntingtin fragments modulated by ubiquitin-protein ligase E3A. Proc Natl Acad Sci U S A 111(15):5706\u20135711. \nhttps:\/\/doi.org\/10.1073\/pnas.1402215111","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"12","key":"853_CR36","doi-asserted-by":"publisher","first-page":"7648","DOI":"10.1074\/jbc.M706620200","volume":"283","author":"A Mishra","year":"2008","unstructured":"Mishra A, Dikshit P, Purkayastha S, Sharma J, Nukina N, Jana NR (2008) E6-AP promotes misfolded polyglutamine proteins for proteasomal degradation and suppresses polyglutamine protein aggregation and toxicity. J Biol Chem 283(12):7648\u20137656. \nhttps:\/\/doi.org\/10.1074\/jbc.M706620200","journal-title":"J Biol Chem"},{"issue":"3","key":"853_CR37","doi-asserted-by":"publisher","first-page":"538","DOI":"10.1016\/j.yexcr.2006.10.031","volume":"313","author":"H Yang","year":"2007","unstructured":"Yang H, Zhong X, Ballar P, Luo S, Shen Y, Rubinsztein DC, Monteiro MJ, Fang S (2007) Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity of polyglutamine-expanded huntingtin. Exp Cell Res 313(3):538\u2013550. \nhttps:\/\/doi.org\/10.1016\/j.yexcr.2006.10.031","journal-title":"Exp Cell Res"},{"issue":"1","key":"853_CR38","doi-asserted-by":"publisher","first-page":"139","DOI":"10.1016\/j.mito.2010.09.001","volume":"11","author":"A Sugiura","year":"2011","unstructured":"Sugiura A, Yonashiro R, Fukuda T, Matsushita N, Nagashima S, Inatome R, Yanagi S (2011) A mitochondrial ubiquitin ligase MITOL controls cell toxicity of polyglutamine-expanded protein. Mitochondrion 11(1):139\u2013146. \nhttps:\/\/doi.org\/10.1016\/j.mito.2010.09.001","journal-title":"Mitochondrion"},{"issue":"48","key":"853_CR39","doi-asserted-by":"publisher","first-page":"78281","DOI":"10.18632\/oncotarget.12930","volume":"7","author":"VK Nelson","year":"2016","unstructured":"Nelson VK, Ali A, Dutta N, Ghosh S, Jana M, Ganguli A, Komarov A, Paul S et al (2016) Azadiradione ameliorates polyglutamine expansion disease in Drosophila by potentiating DNA binding activity of heat shock factor 1. Oncotarget 7(48):78281\u201378296. \nhttps:\/\/doi.org\/10.18632\/oncotarget.12930","journal-title":"Oncotarget"},{"issue":"2","key":"853_CR40","doi-asserted-by":"publisher","first-page":"149","DOI":"10.2174\/1568011053174828","volume":"5","author":"R Subapriya","year":"2005","unstructured":"Subapriya R, Nagini S (2005) Medicinal properties of neem leaves: a review. Curr Med Chem Anticancer Agents 5(2):149\u2013146. \nhttps:\/\/doi.org\/10.2174\/1568011053174828","journal-title":"Curr Med Chem Anticancer Agents"},{"issue":"7","key":"853_CR41","doi-asserted-by":"publisher","first-page":"505","DOI":"10.1016\/S2221-1691(13)60105-7","volume":"3","author":"VS Kumar","year":"2013","unstructured":"Kumar VS, Navaratnam V (2013) Neem (Azadirachta indica): prehistory to contemporary medicinal uses to humankind. Asian Pac J Trop Biomed 3(7):505\u2013514. \nhttps:\/\/doi.org\/10.1016\/S2221-1691(13)60105-7","journal-title":"Asian Pac J Trop Biomed"},{"issue":"5","key":"853_CR42","doi-asserted-by":"publisher","first-page":"704","DOI":"10.1016\/j.cell.2010.01.026","volume":"140","author":"PL Greer","year":"2010","unstructured":"Greer PL, Hanayama R, Bloodgood BL, Mardinly AR, Lipton DM, Flavell SW, Kim TK, Griffith EC et al (2010) The Angelman syndrome protein Ube3A regulates synapse development by ubiquitinating arc. Cell 140(5):704\u2013716. \nhttps:\/\/doi.org\/10.1016\/j.cell.2010.01.026","journal-title":"Cell"},{"issue":"16","key":"853_CR43","doi-asserted-by":"publisher","first-page":"10537","DOI":"10.1074\/jbc.M806804200","volume":"284","author":"A Mishra","year":"2009","unstructured":"Mishra A, Godavarthi SK, Maheshwari M, Goswami A, Jana NR (2009) The ubiquitin ligase E6-AP is induced and recruited to aggresomes in response to proteasome inhibition and may be involved in the ubiquitination of Hsp70-bound misfolded proteins. J Biol Chem 284(16):10537\u201310545. \nhttps:\/\/doi.org\/10.1074\/jbc.M806804200","journal-title":"J Biol Chem"},{"issue":"3","key":"853_CR44","doi-asserted-by":"publisher","first-page":"493","DOI":"10.1016\/S0092-8674(00)81369-0","volume":"87","author":"L Mangiarini","year":"1996","unstructured":"Mangiarini L, Sathasivam K, Seller M, Cozens B, Harper A, Hetherington C, Lawton M, Trottier Y et al (1996) Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice. Cell 87(3):493\u2013506. \nhttps:\/\/doi.org\/10.1016\/S0092-8674(00)81369-0","journal-title":"Cell"},{"issue":"23","key":"853_CR45","doi-asserted-by":"publisher","first-page":"6235","DOI":"10.1093\/hmg\/ddu343","volume":"23","author":"M Maheshwari","year":"2014","unstructured":"Maheshwari M, Shekhar S, Singh BK, Jamal I, Vatsa N, Kumar V, Sharma A, Jana NR (2014) Deficiency of Ube3a in Huntington\u2019s disease mice brain increases aggregate load and accelerates disease pathology. Hum Mol Genet 23(23):6235\u20136245. \nhttps:\/\/doi.org\/10.1093\/hmg\/ddu343","journal-title":"Hum Mol Genet"},{"issue":"16","key":"853_CR46","doi-asserted-by":"publisher","first-page":"1463","DOI":"10.1080\/14786419.2012.717288","volume":"27","author":"K Ilango","year":"2013","unstructured":"Ilango K, Maharajan G, Narasimhan S (2013) Anti-nociceptive and anti-inflammatory activities of Azadirachta indica fruit skin extract and its isolated constituent azadiradione. Nat Prod Res 27(16):1463\u20131467. \nhttps:\/\/doi.org\/10.1080\/14786419.2012.717288","journal-title":"Nat Prod Res"},{"issue":"6","key":"853_CR47","doi-asserted-by":"publisher","first-page":"910","DOI":"10.1002\/ptr.5332","volume":"29","author":"R Singh","year":"2015","unstructured":"Singh R, Mishra V, Pandeti S, Palit G, Barthwal MK, Pandey HP, Narender T (2015) Cytoprotective and anti-secretory effects of Azadiradione isolated from the seeds of Azadirachta indica (neem) on gastric ulcers in rat models. Phytother Res 29(6):910\u2013916. \nhttps:\/\/doi.org\/10.1002\/ptr.5332","journal-title":"Phytother Res"},{"issue":"12","key":"853_CR48","doi-asserted-by":"publisher","first-page":"6809","DOI":"10.1073\/pnas.120166397","volume":"97","author":"JA Bibb","year":"2000","unstructured":"Bibb JA, Yan Z, Svenningsson P, Snyder GL, Pieribone VA, Horiuchi A, Nairn AC, Messer A et al (2000) Severe deficiencies in dopamine signaling in presymptomatic Huntington\u2019s disease mice. Proc Natl Acad Sci U S A 97(12):6809\u20136814. \nhttps:\/\/doi.org\/10.1073\/pnas.120166397","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"35","key":"853_CR49","doi-asserted-by":"publisher","first-page":"29949","DOI":"10.1074\/jbc.M112.371724","volume":"287","author":"M Maheshwari","year":"2012","unstructured":"Maheshwari M, Samanta A, Godavarthi SK, Mukherjee R, Jana NR (2012) Dysfunction of the ubiquitin ligase Ube3a may be associated with synaptic pathophysiology in a mouse model of Huntington disease. J Biol Chem 287(35):29949\u201329957. \nhttps:\/\/doi.org\/10.1074\/jbc.M112.371724","journal-title":"J Biol Chem"},{"issue":"12","key":"853_CR50","doi-asserted-by":"publisher","first-page":"1307","DOI":"10.1093\/hmg\/10.12.1307","volume":"10","author":"A Sittler","year":"2001","unstructured":"Sittler A, Lurz R, Lueder G, Priller J, Lehrach H, Hayer-Hartl MK, Hartl FU, Wanker EE (2001) Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington\u2019s disease. Hum Mol Genet 10(12):1307\u20131315. \nhttps:\/\/doi.org\/10.1093\/hmg\/10.12.1307","journal-title":"Hum Mol Genet"},{"issue":"38","key":"853_CR51","doi-asserted-by":"publisher","first-page":"26188","DOI":"10.1074\/jbc.M710521200","volume":"283","author":"N Fujikake","year":"2008","unstructured":"Fujikake N, Nagai Y, Popiel HA, Okamoto Y, Yamaguchi M, Toda T (2008) Heat shock transcription factor 1-activating compounds suppress polyglutamine-induced neurodegeneration through induction of multiple molecular chaperones. J Biol Chem 283(38):26188\u201326197. \nhttps:\/\/doi.org\/10.1074\/jbc.M710521200","journal-title":"J Biol Chem"},{"issue":"8","key":"853_CR52","doi-asserted-by":"publisher","first-page":"3306","DOI":"10.1172\/JCI57413","volume":"121","author":"J Labbadia","year":"2011","unstructured":"Labbadia J, Cunliffe H, Weiss A, Katsyuba E, Sathasivam K, Seredenina T, Woodman B, Moussaoui S et al (2011) Altered chromatin architecture underlies progressive impairment of the heat shock response in mouse models of Huntington disease. J Clin Invest 121(8):3306\u20133319. \nhttps:\/\/doi.org\/10.1172\/JCI57413","journal-title":"J Clin Invest"},{"issue":"53","key":"853_CR53","doi-asserted-by":"publisher","first-page":"56053","DOI":"10.1074\/jbc.M409267200","volume":"279","author":"SD Westerheide","year":"2004","unstructured":"Westerheide SD, Bosman JD, Mbadugha BN, Kawahara TL, Matsumoto G, Kim S, Gu W, Devlin JP et al (2004) Celastrols as inducers of the heat shock response and cytoprotection. J Biol Chem 279(53):56053\u201356060. \nhttps:\/\/doi.org\/10.1074\/jbc.M409267200","journal-title":"J Biol Chem"},{"issue":"3","key":"853_CR54","doi-asserted-by":"publisher","first-page":"688","DOI":"10.1016\/j.bbrc.2005.05.008","volume":"332","author":"SV Sundar","year":"2005","unstructured":"Sundar SV, Li YY, Rollwagen FM, Maheshwari RK (2005) Hemorrhagic shock induces differential gene expression and apoptosis in mouse liver. Biochem Biophys Res Commun 332(3):688\u2013696. \nhttps:\/\/doi.org\/10.1016\/j.bbrc.2005.05.008","journal-title":"Biochem Biophys Res Commun"},{"issue":"1","key":"853_CR55","doi-asserted-by":"publisher","first-page":"55","DOI":"10.1007\/s12192-009-0121-1","volume":"15","author":"LA Sonna","year":"2010","unstructured":"Sonna LA, Hawkins L, Lissauer ME, Maldeis P, Towns M, Johnson SB, Moore R, Singh IS et al (2010) Core temperature correlates with expression of selected stress and immunomodulatory genes in febrile patients with sepsis and noninfectious SIRS. Cell Stress Chaperones 15(1):55\u201366. \nhttps:\/\/doi.org\/10.1007\/s12192-009-0121-1","journal-title":"Cell Stress Chaperones"},{"issue":"48","key":"853_CR56","doi-asserted-by":"publisher","first-page":"40400","DOI":"10.1074\/jbc.M112.410712","volume":"287","author":"H Xue","year":"2012","unstructured":"Xue H, Slavov D, Wischmeyer PE (2012) Glutamine-mediated dual regulation of heat shock transcription factor-1 activation and expression. J Biol Chem 287(48):40400\u201340413. \nhttps:\/\/doi.org\/10.1074\/jbc.M112.410712","journal-title":"J Biol Chem"},{"issue":"17","key":"853_CR57","doi-asserted-by":"publisher","first-page":"1901","DOI":"10.1007\/s00018-005-5084-5","volume":"62","author":"R Smith","year":"2005","unstructured":"Smith R, Brundin P, Li JY (2005) Synaptic dysfunction in Huntington\u2019s disease: a new perspective. Cell Mol Life Sci 62(17):1901\u20131912. \nhttps:\/\/doi.org\/10.1007\/s00018-005-5084-5","journal-title":"Cell Mol Life Sci"},{"issue":"7","key":"853_CR58","doi-asserted-by":"publisher","first-page":"990","DOI":"10.1016\/j.drudis.2014.02.006","volume":"19","author":"MD Sepers","year":"2014","unstructured":"Sepers MD, Raymond LA (2014) Mechanisms of synaptic dysfunction and excitotoxicity in Huntington\u2019s disease. Drug Discov Today 19(7):990\u2013996. \nhttps:\/\/doi.org\/10.1016\/j.drudis.2014.02.006","journal-title":"Drug Discov Today"}],"container-title":["Molecular Neurobiology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/article\/10.1007\/s12035-017-0853-3\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s12035-017-0853-3.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s12035-017-0853-3.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2018,7,19]],"date-time":"2018-07-19T22:39:09Z","timestamp":1532039949000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/s12035-017-0853-3"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,1,2]]},"references-count":58,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2018,8]]}},"alternative-id":["853"],"URL":"https:\/\/doi.org\/10.1007\/s12035-017-0853-3","relation":{},"ISSN":["0893-7648","1559-1182"],"issn-type":[{"value":"0893-7648","type":"print"},{"value":"1559-1182","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,1,2]]}}}