{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T21:16:54Z","timestamp":1788902214975,"version":"build-2803163510"},"reference-count":42,"publisher":"SAGE Publications","issue":"2","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["JHD"],"published-print":{"date-parts":[[2016,7,1]]},"DOI":"10.3233\/jhd-150180","type":"journal-article","created":{"date-parts":[[2016,7,1]],"date-time":"2016-07-01T10:52:36Z","timestamp":1467370356000},"page":"133-147","source":"Crossref","is-referenced-by-count":34,"title":["AUTEN-67 (Autophagy Enhancer-67) Hampers the Progression of Neurodegenerative Symptoms in a Drosophila model of Huntington\u2019s Disease"],"prefix":"10.1177","volume":"5","author":[{"given":"Viktor","family":"Billes","sequence":"first","affiliation":[{"name":"Velgene Biotechnology Research Ltd., Szeged, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tibor","family":"Kov\u00e1cs","sequence":"additional","affiliation":[{"name":"Velgene Biotechnology Research Ltd., Szeged, Hungary"},{"name":"Department of Genetics, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bernadette","family":"Hotzi","sequence":"additional","affiliation":[{"name":"Velgene Biotechnology Research Ltd., Szeged, Hungary"},{"name":"Department of Genetics, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anna","family":"Manz\u00e9ger","sequence":"additional","affiliation":[{"name":"Department of Genetics, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kinga","family":"Tagscherer","sequence":"additional","affiliation":[{"name":"Department of Genetics, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marcell","family":"Koml\u00f3s","sequence":"additional","affiliation":[{"name":"Velgene Biotechnology Research Ltd., Szeged, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anna","family":"Tarn\u00f3ci","sequence":"additional","affiliation":[{"name":"Velgene Biotechnology Research Ltd., Szeged, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zsolt","family":"P\u00e1d\u00e1r","sequence":"additional","affiliation":[{"name":"Velgene Biotechnology Research Ltd., Szeged, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Attila","family":"Erd\u0151s","sequence":"additional","affiliation":[{"name":"Velgene Biotechnology Research Ltd., Szeged, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Annamaria","family":"Bjelik","sequence":"additional","affiliation":[{"name":"Department of Cell Biology and Molecular Medicine, University of Szeged, Szeged, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Adam","family":"Legradi","sequence":"additional","affiliation":[{"name":"Department of Cell Biology and Molecular Medicine, University of Szeged, Szeged, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"K\u00e1roly","family":"Gulya","sequence":"additional","affiliation":[{"name":"Department of Cell Biology and Molecular Medicine, University of Szeged, Szeged, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bal\u00e1zs","family":"Guly\u00e1s","sequence":"additional","affiliation":[{"name":"Karolinska Institute, Department of Clinical Neuroscience, Stockholm, Sweden"},{"name":"Lee Kong Chian School of Medicine, Nanyang Technological University, Singapore"},{"name":"Imperial College London, Department of Medicine, Division of Brain Sciences, London, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tibor","family":"Vellai","sequence":"additional","affiliation":[{"name":"Velgene Biotechnology Research Ltd., Szeged, Hungary"},{"name":"Department of Genetics, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"179","reference":[{"issue":"Pt 1","key":"10.3233\/JHD-150180_ref1","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1242\/jcs.01620","article-title":"The molecular machinery of autophagy: Unanswered questions","volume":"118","author":"Klionsky","year":"2005","journal-title":"J Cell Sci"},{"issue":"7182","key":"10.3233\/JHD-150180_ref2","doi-asserted-by":"crossref","first-page":"1069","DOI":"10.1038\/nature06639","article-title":"Autophagy fights disease through cellular self-digestion","volume":"451","author":"Mizushima","year":"2008","journal-title":"Nature"},{"issue":"10","key":"10.3233\/JHD-150180_ref3","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1016\/j.tcb.2009.07.007","article-title":"The regulation of aging: Does autophagy underlie longevity?","volume":"19","author":"Vellai","year":"2009","journal-title":"Trends Cell Biol"},{"issue":"2","key":"10.3233\/JHD-150180_ref4","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1080\/15548627.2015.1082023","article-title":"AUTEN-67, an autophagy-enhancing drug candidate with potent antiaging and neuroprotective effects","volume":"12","author":"Papp","year":"2015","journal-title":"Autophagy"},{"issue":"9557","key":"10.3233\/JHD-150180_ref5","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1016\/S0140-6736(07)60111-1","article-title":"Huntington\u2019s disease","volume":"369","author":"Walker","year":"2007","journal-title":"Lancet"},{"issue":"17","key":"10.3233\/JHD-150180_ref6","doi-asserted-by":"crossref","first-page":"4263","DOI":"10.1111\/j.1742-4658.2008.06562.x","article-title":"Huntington\u2019s disease: Degradation of mutant huntingtin by autophagy","volume":"275","author":"Sarkar","year":"2008","journal-title":"FEBS J"},{"issue":"4","key":"10.3233\/JHD-150180_ref7","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1083\/jcb.200507002","article-title":"p62\/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death","volume":"171","author":"Bj\u00f8rk\u00f8y","year":"2005","journal-title":"J Cell Biol"},{"issue":"2","key":"10.3233\/JHD-150180_ref8","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/j.molcel.2010.04.007","article-title":"The selective macroautophagic degradation of aggregated proteins requires the PI3P-binding protein Alfy","volume":"38","author":"Filimonenko","year":"2010","journal-title":"Mol Cell"},{"issue":"3","key":"10.3233\/JHD-150180_ref9","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1016\/j.cell.2014.05.048","article-title":"Autophagic clearance of polyQ proteins mediated by ubiquitin-Atg8 adaptors of the conserved CUET protein family","volume":"158","author":"Lu","year":"2014","journal-title":"Cell"},{"issue":"5","key":"10.3233\/JHD-150180_ref10","doi-asserted-by":"crossref","first-page":"1478","DOI":"10.1091\/mbc.e08-07-0726","article-title":"Mutant huntingtin impairs post-Golgi trafficking to lysosomes by delocalizing optineurin\/Rab8 complex from the Golgi apparatus","volume":"20","author":"del Toro","year":"2009","journal-title":"Mol Biol Cell"},{"issue":"5","key":"10.3233\/JHD-150180_ref11","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1038\/nn.2528","article-title":"Cargo recognition failure is responsible for inefficient autophagy in Huntington\u2019s disease","volume":"13","author":"Martinez-Vicente","year":"2010","journal-title":"Nat Neurosci"},{"issue":"4","key":"10.3233\/JHD-150180_ref12","doi-asserted-by":"crossref","first-page":"1293","DOI":"10.1523\/JNEUROSCI.1870-13.2014","article-title":"The regulation of autophagosome dynamics by huntingtin and HAP1 is disrupted by expression of mutant huntingtin, leading to defective cargo degradation","volume":"34","author":"Wong","year":"2014","journal-title":"J Neurosci"},{"issue":"1","key":"10.3233\/JHD-150180_ref13","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.tins.2014.09.003","article-title":"Autophagy in Huntington disease and huntingtin in autophagy","volume":"38","author":"Martin","year":"2015","journal-title":"Trends Neurosci"},{"issue":"47","key":"10.3233\/JHD-150180_ref14","doi-asserted-by":"crossref","first-page":"16889","DOI":"10.1073\/pnas.1420103111","article-title":"Potential function for the Huntingtin protein as a scaffold for selective autophagy","volume":"111","author":"Ochaba","year":"2014","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"3","key":"10.3233\/JHD-150180_ref15","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1038\/ncb3101","article-title":"Huntingtin functions as a scaffold for selective macroautophagy","volume":"17","author":"Rui","year":"2015","journal-title":"Nat Cell Biol"},{"issue":"10","key":"10.3233\/JHD-150180_ref16","doi-asserted-by":"crossref","first-page":"1711","DOI":"10.1080\/15548627.2015.1043076","article-title":"Differential regulatory functions of three classes of phosphatidylinositol and phosphoinositide 3-kinases in autophagy","volume":"11","author":"Yu","year":"2015","journal-title":"Autophagy"},{"issue":"8","key":"10.3233\/JHD-150180_ref17","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1016\/j.tcb.2006.06.001","article-title":"Myotubularin phosphatases: Policing 3-phosphoinositides","volume":"16","author":"Robinson","year":"2006","journal-title":"Trends Cell Biol"},{"issue":"15","key":"10.3233\/JHD-150180_ref18","doi-asserted-by":"crossref","first-page":"2244","DOI":"10.1038\/emboj.2009.159","article-title":"Control of autophagy initiation by phosphoinositide 3-phosphatase Jumpy","volume":"28","author":"Vergne","year":"2009","journal-title":"EMBO J"},{"issue":"11","key":"10.3233\/JHD-150180_ref19","doi-asserted-by":"crossref","first-page":"1126","DOI":"10.1002\/bies.20489","article-title":"Autophagy in neuronal cell loss: A road to death","volume":"28","author":"Tak\u00e1cs-Vellai","year":"2006","journal-title":"Bioessays"},{"issue":"23","key":"10.3233\/JHD-150180_ref20","doi-asserted-by":"crossref","first-page":"2592","DOI":"10.1101\/gad.1984410","article-title":"Alternative cell death mechanisms in development and beyond","volume":"24","author":"Yuan","year":"2010","journal-title":"Genes Dev"},{"issue":"1","key":"10.3233\/JHD-150180_ref21","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1038\/cdd.2008.126","article-title":"Autophagy genes and ageing","volume":"16","author":"Vellai","year":"2009","journal-title":"Cell Death Differ"},{"issue":"3","key":"10.3233\/JHD-150180_ref22","doi-asserted-by":"crossref","first-page":"330","DOI":"10.4161\/auto.5618","article-title":"Longevity pathways converge on autophagy genes to regulate life span in Caenorhabditis elegans","volume":"4","author":"T\u00f3th","year":"2008","journal-title":"Autophagy"},{"issue":"6","key":"10.3233\/JHD-150180_ref23","doi-asserted-by":"crossref","first-page":"1194","DOI":"10.1016\/j.cell.2013.05.039","article-title":"The hallmarks of aging","volume":"153","author":"L\u00f3pez-Ot\u00edn","year":"2013","journal-title":"Cell"},{"issue":"1","key":"10.3233\/JHD-150180_ref24","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.cell.2007.12.018","article-title":"Autophagy in the pathogenesis of disease","volume":"132","author":"Levine","year":"2008","journal-title":"Cell"},{"issue":"7113","key":"10.3233\/JHD-150180_ref25","doi-asserted-by":"crossref","first-page":"780","DOI":"10.1038\/nature05291","article-title":"The roles of intracellular protein-degradation pathways in neurodegeneration","volume":"443","author":"Rubinsztein","year":"2006","journal-title":"Nature"},{"issue":"6","key":"10.3233\/JHD-150180_ref26","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1038\/nchembio883","article-title":"Small molecules enhance autophagy and reduce toxicity in Huntington\u2019s disease models","volume":"3","author":"Sarkar","year":"2007","journal-title":"Nat Chem Biol"},{"issue":"1","key":"10.3233\/JHD-150180_ref27","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1038\/nchembio.500","article-title":"Chemical modulators of autophagy as biological probes and potential therapeutics","volume":"7","author":"Fleming","year":"2011","journal-title":"Nat Chem Biol"},{"issue":"7","key":"10.3233\/JHD-150180_ref28","doi-asserted-by":"crossref","first-page":"2004","DOI":"10.1091\/mbc.e08-12-1250","article-title":"An Atg1\/Atg13 complex with multiple roles in TOR-mediated autophagy regulation","volume":"20","author":"Chang","year":"2009","journal-title":"Mol Biol Cell"},{"key":"10.3233\/JHD-150180_ref29","doi-asserted-by":"crossref","first-page":"e44214","DOI":"10.1371\/journal.pone.0044214","article-title":"Advantages and limitations of different p62-based assays for estimating autophagic activity in Drosophila","volume":"7","author":"Pircs","year":"2012","journal-title":"PloS One"},{"key":"10.3233\/JHD-150180_ref30","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.brainresbull.2013.01.007","article-title":"Long-term effects of selective immunolesions of cholinergic neurons of the nucleus basalis magnocellularis on the ascending cholinergic pathways in the rat: A model for Alzheimer\u2019s disease","volume":"94","author":"Szigeti","year":"2013","journal-title":"Brain Res Bull"},{"key":"10.3233\/JHD-150180_ref31","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1016\/j.neuroscience.2013.03.033","article-title":"Development of the microglial phenotype in culture","volume":"241","author":"Szabo","year":"2013","journal-title":"Neuroscience"},{"issue":"7","key":"10.3233\/JHD-150180_ref32","first-page":"36","article-title":"Image processing with ImageJ","volume":"11","author":"Abr\u00e0moff","year":"2004","journal-title":"Biophotonics Int"},{"issue":"1","key":"10.3233\/JHD-150180_ref33","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.neuron.2007.11.025","article-title":"Suppression of neurodegeneration and increased neurotransmission caused by expanded full-length huntingtin accumulating in the cytoplasm","volume":"57","author":"Romero","year":"2008","journal-title":"Neuron"},{"key":"10.3233\/JHD-150180_ref34","first-page":"2","article-title":"Drosophila models of Huntington\u2019s disease exhibit sleep abnormalities","author":"Gonzales","year":"2010","journal-title":"PLoS Curr"},{"issue":"1","key":"10.3233\/JHD-150180_ref35","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.ymeth.2014.03.014","article-title":"Assays to monitor autophagy in Drosophila","volume":"68","author":"Mauvezin","year":"2014","journal-title":"Methods"},{"issue":"24","key":"10.3233\/JHD-150180_ref36","doi-asserted-by":"crossref","first-page":"8787","DOI":"10.1128\/MCB.22.24.8787-8795.2002","article-title":"The Drosophila atypical protein kinase C-Ref(2)P complex constitutes a conserved module for signaling in the toll pathway","volume":"22","author":"Avila","year":"2002","journal-title":"Mol Cell Biol"},{"issue":"6","key":"10.3233\/JHD-150180_ref37","doi-asserted-by":"crossref","first-page":"1065","DOI":"10.1083\/jcb.200711108","article-title":"Ref(2)P, the Drosophila melanogaster homologue of mammalian p62, is required for the formation of protein aggregates in adult brain","volume":"180","author":"Nezis","year":"2008","journal-title":"J Cell Biol"},{"issue":"1","key":"10.3233\/JHD-150180_ref38","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1111\/j.1471-4159.2004.02692.x","article-title":"Increased expression of p62 in expanded polyglutamine-expressing cells and its association with polyglutamine inclusions","volume":"91","author":"Nagaoka","year":"2004","journal-title":"J Neurochem"},{"issue":"6968","key":"10.3233\/JHD-150180_ref39","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1038\/nature02263","article-title":"Protein degradation and protection against misfolded or damaged proteins","volume":"426","author":"Goldberg","year":"2003","journal-title":"Nature"},{"issue":"1","key":"10.3233\/JHD-150180_ref40","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1006\/exnr.1998.7005","article-title":"Huntington\u2019s disease intranuclear inclusions contain truncated, ubiquitinated huntingtin protein","volume":"156","author":"Sieradzan","year":"1999","journal-title":"Exp Neurol"},{"issue":"6","key":"10.3233\/JHD-150180_ref41","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1038\/ng1362","article-title":"Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease","volume":"36","author":"Ravikumar","year":"2004","journal-title":"Nat Genet"},{"issue":"6","key":"10.3233\/JHD-150180_ref42","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/j.molmed.2012.04.004","article-title":"Myotubularin phosphoinositide phosphatases: Cellular functions and disease pathophysiology","volume":"18","author":"Hnia","year":"2012","journal-title":"Trends Mol Med"}],"container-title":["Journal of Huntington's Disease"],"original-title":[],"link":[{"URL":"https:\/\/content.iospress.com\/download?id=10.3233\/JHD-150180","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,4,29]],"date-time":"2026-04-29T08:57:09Z","timestamp":1777453029000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.sagepub.com\/doi\/full\/10.3233\/JHD-150180"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,7,1]]},"references-count":42,"journal-issue":{"issue":"2"},"URL":"https:\/\/doi.org\/10.3233\/jhd-150180","relation":{},"ISSN":["1879-6397","1879-6400"],"issn-type":[{"value":"1879-6397","type":"print"},{"value":"1879-6400","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016,7,1]]}}}