Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Emmanouela Kallergi"'
Autor:
Niki Ktena, Stefanos Ioannis Kaplanis, Irina Kolotuev, Alexandros Georgilis, Emmanouela Kallergi, Vasiliki Stavroulaki, Vassiliki Nikoletopoulou, Maria Savvaki, Domna Karagogeos
Publikováno v:
Cell Stress, Vol 6, Iss 12, Pp 93-107 (2022)
(Macro)autophagy is a major lysosome-dependent degradation mechanism which engulfs, removes and recycles unwanted cytoplasmic material, including damaged organelles and toxic protein aggregates. Although a few studies implicate autophagy in CNS demye
Externí odkaz:
https://doaj.org/article/35de64cb355d47f599fc61372a4dfb4a
Autor:
Emmanouela Kallergi, Akrivi-Dimitra Daskalaki, Angeliki Kolaxi, Come Camus, Evangelia Ioannou, Valentina Mercaldo, Per Haberkant, Frank Stein, Kyriaki Sidiropoulou, Yannis Dalezios, Mikhail M. Savitski, Claudia Bagni, Daniel Choquet, Eric Hosy, Vassiliki Nikoletopoulou
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-23 (2022)
Pruning dendritic spines requires autophagy. Here, the authors show that autophagy is required for long-term depression (LTD), a major form of synaptic plasticity. LTD induces the biogenesis of autophagic vesicles locally in dendrites to facilitate t
Externí odkaz:
https://doaj.org/article/4c1ae7d8ce5140a2bdf18204c150e182
Publikováno v:
Cell Stress, Vol 5, Iss 10, Pp 146-166 (2021)
Aging represents a cumulative form of cellular stress, which is thought to challenge many aspects of proteostasis. The non-dividing, long-lived neurons are particularly vulnerable to stress, and, not sur-prisingly, even normal aging is highly associa
Externí odkaz:
https://doaj.org/article/ac786b7499c7439b9550f3b89b58136f
Autor:
Benjamin Compans, Come Camus, Emmanouela Kallergi, Silvia Sposini, Magalie Martineau, Corey Butler, Adel Kechkar, Remco V. Klaassen, Natacha Retailleau, Terrence J. Sejnowski, August B. Smit, Jean-Baptiste Sibarita, Thomas M. Bartol, David Perrais, Vassiliki Nikoletopoulou, Daniel Choquet, Eric Hosy
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-18 (2021)
Long-term depression (LTD) of synaptic strength contributes to circuit remodeling, memory encoding and erasure. Here, the authors show that P2XR- and NMDAR-dependent LTD are associated with distinct and precise molecular modifications that lead to sp
Externí odkaz:
https://doaj.org/article/42d7f0f08a7745138e490a7bf976a87f
Publikováno v:
Cell Stress
Cell Stress, Vol 5, Iss 10, Pp 146-166 (2021)
Cell stress
Cell Stress, Vol 5, Iss 10, Pp 146-166 (2021)
Cell stress
Aging represents a cumulative form of cellular stress, which is thought to challenge many aspects of proteostasis. The non-dividing, long-lived neurons are particularly vulnerable to stress, and, not sur-prisingly, even normal aging is highly associa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6470ce81941d8831a2d24df292b8163b
http://europepmc.org/articles/PMC8490955
http://europepmc.org/articles/PMC8490955
Autor:
Niki Ktena, Stefanos Ioannis Kaplanis, Irina Kolotuev, Alexandros Georgilis, Vasiliki Stavroulaki, Emmanouela Kallergi, Vassiliki Nikoletopoulou, Domna Karagogeos, Maria Savvaki
(Macro)autophagy comprises a major lysosome-dependent degradation mechanism which engulfs, removes and recycles unwanted cytoplasmic material, including damaged organelles and toxic protein aggregates. Although a few studies implicate autophagy in CN
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5ccc2c747f1bc56a0a33853d521314a0
https://doi.org/10.1101/2022.06.20.496817
https://doi.org/10.1101/2022.06.20.496817
Autor:
Konstantinos Tokatlidis, Phanee Manganas, Lacko E, Emmanouela Kallergi, Mauricio Cardenas-Rodriguez, Afroditi Chatzi, Robert Edwards
Mitochondria biogenesis crucially depends on the oxidative folding system in the mitochondrial intermembrane space. The oxidative capacity needs however to be balanced by a reductive pathway for optimal mitochondrial fitness. Here we report that the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ccd4d21365eb35054ad4855eed46bf40
https://doi.org/10.1101/2021.06.22.449413
https://doi.org/10.1101/2021.06.22.449413
Autor:
Emmanouela Kallergi, Lucia Banci, Chiara Cefaro, Isabella C. Felli, Nitsa Katrakili, Anna Pavelkova, Kostas Tokatlidis, Maria Andreadaki, Ivano Bertini, Karolina Gajda, Charalambos Pozidis, Angelo Gallo, Simone Ciofi-Baffoni
Publikováno v:
Journal of Molecular Biology. 425:594-608
The functional role of unstructured protein domains is an emerging field in the frame of intrinsically disordered proteins. The involvement of intrinsically disordered domains (IDDs) in protein targeting and biogenesis processes in mitochondria is so
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ebb8407fefbd2fd7f2fe6b966370fe7
https://doi.org/10.1016/j.jmb.2012.11.032
https://doi.org/10.1016/j.jmb.2012.11.032
Autor:
Lucia Banci, Charalambos Pozidis, Riccardo Peruzzini, Kostas Tokatlidis, Maria Andreadaki, Simone Ciofi-Baffoni, Karolina Gajda, Emmanouela Kallergi, Chiara Cefaro, Nitsa Katrakili, Paraskevi Kritsiligkou, Ivano Bertini
Publikováno v:
ACS Chemical Biology. 7:707-714
The interaction of Mia40 with Erv1/ALR is central to the oxidative protein folding in the intermembrane space of mitochondria (IMS) as Erv1/ALR oxidizes reduced Mia40 to restore its functional state. Here we address the role of Mia40 in the import an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4709cddf2e409f6c79dd68c773123d54
https://doi.org/10.1021/cb200485b
https://doi.org/10.1021/cb200485b
Publikováno v:
Neurochemical research. 39(3)
Mitochondria biogenesis is a fundamental process for the organization and normal function of all cells. Since the majority of mitochondrial proteins are synthesized in the cytosol, protein import is the major mechanism for mitochondria biogenesis. We
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5a1e7a00b607065474d60c1dd40ba88
https://pubmed.ncbi.nlm.nih.gov/24005821
https://pubmed.ncbi.nlm.nih.gov/24005821