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Biol."],"published-print":{"date-parts":[[2020,3,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    The aggregation of intrinsically disordered proteins is a hallmark of neurodegenerative diseases, such as Alzheimer\u2019s, Parkinson\u2019s and Huntington\u2019s disease. Although we currently have a good molecular level understanding on how protein aggregation occurs\n                    <jats:italic>in vitro<\/jats:italic>\n                    , the details of its self-assembly in live cells are still mainly unknown. During the last ten years, we have witnessed the rapid development of advanced imaging techniques, especially super-resolution and fluorescence lifetime-based microscopy, in different areas of cell biology. These methods have been revolutionising our understanding of how proteins aggregate, providing unprecedented high spatial-temporal resolution which permits us to capture the kinetics of aggregate seeding and expansion, the motion and distribution of individual aggregates within the cells, and its structural change. In this article, we will review the study of\n                    <jats:italic>in situ<\/jats:italic>\n                    protein aggregation using advanced imaging techniques, with the focus on protein aggregate structure and its assembly dynamics.\n                  <\/jats:p>","DOI":"10.1088\/1478-3975\/ab694e","type":"journal-article","created":{"date-parts":[[2020,1,8]],"date-time":"2020-01-08T17:51:51Z","timestamp":1578505911000},"page":"021001","update-policy":"https:\/\/doi.org\/10.1088\/crossmark-policy","source":"Crossref","is-referenced-by-count":28,"title":["Advanced fluorescence imaging of in situ protein aggregation"],"prefix":"10.1088","volume":"17","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9311-2666","authenticated-orcid":false,"given":"Meng","family":"Lu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Clemens F","family":"Kaminski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gabriele S Kaminski","family":"Schierle","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"266","published-online":{"date-parts":[[2020,2,11]]},"reference":[{"key":"pbab694ebib001","doi-asserted-by":"publisher","first-page":"6968","DOI":"10.1038\/nature02261","article-title":"Protein folding and misfolding","volume":"426","author":"Dobson","year":"2003","journal-title":"Nature"},{"key":"pbab694ebib002","doi-asserted-by":"publisher","first-page":"267","DOI":"10.1146\/annurev.neuro.26.010302.081142","article-title":"Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders","volume":"26","author":"Caughey","year":"2003","journal-title":"Annu. 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