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Eeva-Liisa Eskelinen
Researcher at University of Turku
Publications - 136
Citations - 32990
Eeva-Liisa Eskelinen is an academic researcher from University of Turku. The author has contributed to research in topics: Autophagy & Endosome. The author has an hindex of 60, co-authored 124 publications receiving 28293 citations. Previous affiliations of Eeva-Liisa Eskelinen include Dalhousie University & University of Kiel.
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Journal ArticleDOI
Crosstalk between Hsp70 molecular chaperone, lysosomes and proteasomes in autophagy-mediated proteolysis in human retinal pigment epithelial cells
Tuomas Ryhänen,Juha M.T. Hyttinen,Juergen Kopitz,Kirsi Rilla,Erkki Kuusisto,Eliisa Mannermaa,Johanna Viiri,Carina I. Holmberg,Ilkka Immonen,Seppo Meri,Jussi Parkkinen,Eeva-Liisa Eskelinen,Hannu Uusitalo,Antero Salminen,Kai Kaarniranta +14 more
TL;DR: The molecular chaperone Hsp70, proteasomes and autophagy have an important regulatory role in the protein turnover of human RPE cells and may thus open new avenues for understanding degenerative processes in retinal cells.
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Palmitoyl protein thioesterase (PPT) localizes into synaptosomes and synaptic vesicles in neurons: implications for infantile neuronal ceroid lipofuscinosis (INCL)
TL;DR: The current data imply that PPT has a role outside the lysosomes in the brain and may be associated with synaptic functioning, which opens a new route to study the neuropathological events associated with INCL.
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Deletion of the SNARE vti1b in mice results in the loss of a single SNARE partner, syntaxin 8.
Vadim Atlashkin,Vera Kreykenbohm,Eeva-Liisa Eskelinen,Dirk Wenzel,A Fayyazi,Gabriele Fischer von Mollard +5 more
TL;DR: Data indicate that vti1b is specifically required for the stability of a single SNARE partner, and suggests that other SNAREs can compensate for the reduction in syntaxin 8 and for the loss of vti2b in most mice even though vti 1b shows only 30% amino acid identity with its closest relative.
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Ultrastructural relationship of the phagophore with surrounding organelles.
TL;DR: This work has used serial block face scanning electron microscopy and electron tomography to image phagophore biogenesis in 3 dimensions and to determine the relationship between the phagophile and surrounding organelles at high resolution, and identified MCSs between thephagophores and membranes from putative ER exit sites, late endosomes or lysosomes, the Golgi complex and mitochondria.
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Oxidation of SQSTM1/p62 mediates the link between redox state and protein homeostasis.
Bernadette Carroll,Elsje G. Otten,Diego Manni,Rhoda Stefanatos,Fiona M. Menzies,Graham Smith,Diana Jurk,Niall S. Kenneth,Simon Wilkinson,João F. Passos,Johannes Attems,Elizabeth A. Veal,Elisa Teyssou,Danielle Seilhean,Stéphanie Millecamps,Eeva-Liisa Eskelinen,Agnieszka K. Bronowska,David C. Rubinsztein,Alberto Sanz,Viktor I. Korolchuk +19 more
TL;DR: It is proposed that the redox-sensitivity of p62 may have evolved in vertebrates as a mechanism that allows activation of autophagy in response to oxidative stress to maintain cellular homoeostasis and increase cell survival.