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2. Novel mutation of the PRNP gene of a clinical CJD case

Author

Collinge John, Kazis Dimitrios, Plaitakis Andreas, Latsoudis Helen, Bostantjopoulou Sevasti, Paspaltsis Ioannis, Kotta Konstantia, and Sklaviadis Theodoros

Subjects
Infectious and parasitic diseases, RC109-216
Abstract

Abstract Background Transmissible spongiform encephalopathies (TSEs), a group of neurodegenerative diseases, are thought to be caused by an abnormal isoform of a naturally occurring protein known as cellular prion protein, PrPC. The abnormal form of prion protein, PrPSc accumulates in the brain of affected individuals. Both isoforms are encoded by the same prion protein gene (PRNP), and the structural changes occur post-translationally. Certain mutations in the PRNP gene result in genetic TSEs or increased susceptibility to TSEs. Case presentation A 70 year old woman was admitted to the hospital with severe confusion and inability to walk. Relatives recognized memory loss, gait and behavioral disturbances over a six month period prior to hospitalization. Neurological examination revealed Creutzfeldt-Jakob disease (CJD) related symptoms such as incontinence, Babinski sign and myoclonus. EEG showed periodic sharp waves typical of sporadic CJD and cerebrospinal fluid analysis (CSF) was positive for the presence of the 14-3-3-protein. As the disease progressed the patient developed akinetic mutism and died in the tenth month after onset of the disease symptoms. Unfortunately, no autopsy material was available. PRNP sequencing showed the occurrence of a point mutation on one allele at codon 193, which is altered from ACC, coding for a threonine, to ATC, encoding an isoleucine (T193I). Conclusion Here we report a novel mutation of the PRNP gene found in an elderly female patient resulting in heterozygosity for isoleucine and threonine at codon 193, in which normally homozygosity for threonine is expected (T193). The patient presented typical clinical symptoms of CJD. EEG findings and the presence of the 14-3-3 protein in the CSF, contributed to CJD diagnosis, allowing the classification of this case as a probable CJD according to the World Health Organization (WHO) accepted criteria.

Published
2006
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3. A short purification process for quantitative isolation of PrPSc from naturally occurring and experimental transmissible spongiform encephalopathies

Author

Stack Mick J, Chaplin Melanie J, Groschup Martin, Verghese-Nikolakaki Susan, Polymenidou Magdalini, Plaitakis Andreas, and Sklaviadis Theodoros

Subjects
Infectious and parasitic diseases, RC109-216
Abstract

Abstract Background Transmissible spongiform encephalopathies (TSEs) are neurodegenerative diseases affecting both humans and animals. They are associated with post-translational conversion of the normal cellular prion protein (PrPC) into a heat- and protease-resistant abnormal isoform (PrPSc). Detection of PrPSc in individuals is widely utilized for the diagnosis of prion diseases. Methods TSE brain tissue samples have been processed in order to quantitatively isolate PrPSc. The protocol includes an initial homogenization, digestion with proteinase K and salt precipitation. Results Here we show that over 97 percent of the PrPSc present can be precipitated from infected brain material using this simple salting-out procedure for proteins. No chemically harsh conditions are used during the process in order to conserve the native quality of the isolated protein. Conclusion The resulting PrPSc-enriched preparation should provide a suitable substrate for analyzing the structure of the prion agent and for scavenging for other molecules with which it may associate. In comparison with most methods that exist today, the one described in this study is rapid, cost-effective and does not demand expensive laboratory equipment.

Published
2002
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4. Study of Alzheimer's disease- and frontotemporal dementia-associated genes in the Cretan Aging Cohort

Author

Mathioudakis, Lambros, Dimovasili, Christina, Bourbouli, Mara, Latsoudis, Helen, Kokosali, Evgenia, Gouna, Garyfallia, Vogiatzi, Emmanouella, Basta, Maria, Kapetanaki, Stefania, Panagiotakis, Simeon, Kanterakis, Alexandros, Boumpas, Dimitrios, Lionis, Christos, Plaitakis, Andreas, Simos, Panagiotis, Vgontzas, Alexandros, Kafetzopoulos, Dimitrios, and Zaganas, Ioannis

Published
2023
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6. High Hereditary Transthyretin-Related Amyloidosis Prevalence in Crete: Genetic Heterogeneity and Distinct Phenotypes

Author

Tzagournissakis, Minas, Foukarakis, Emmanouil, Samonakis, Dimitrios, Tsilimbaris, Miltiadis, Michaelidou, Kleita, Mathioudakis, Lambros, Marinis, Anastasios, Giannakoudakis, Emmanouil, Spanaki, Cleanthe, Skoula, Irene, Erimaki, Sofia, Amoiridis, Georgios, Koutsis, Georgios, Koukouraki, Sofia, Stylianou, Kostas, Plaitakis, Andreas, Mitsias, Panayiotis D., and Zaganas, Ioannis

Published
2022
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9. Natalizumab treatment shows low cumulative probabilities of confirmed disability worsening to EDSS milestones in the long-term setting

Author

Correale, Jorge, Caride, Alejandro, Deri, Norma H., Ballario, Carlos, Broadley, Simon, Kneebone, Chris, Barnett, Michael, Pollard, John, Hodgkinson, Suzanne, Kermode, Allan, Macdonell, Richard, King, John, Butzkueven, Helmut, Lechner-Scott, Jeannette, Saines, Noel, Slee, Mark, Plummer, Chris, Willekens, Barbara, Vanopdenbosch, Ludo, Belachew, Shibeshih, Phan-Ba, Rémy, Delvaux, Valérie, Bissay, Veronique, Debruyne, Jan, Decoo, Danny, Crols, Roeland, Symons, Anoek, Nagels, Guy, Van Pesch, Vincent, Sindic, Christian, Dubois, Benedicte, Medaer, Robert, D'Hooghe, Marie, Guillaume, Daniel, De Smet, Eric, Seeldrayers, Pierrette, Lysandropoulos, Andreas, Vokaer, Mathieu, Geens, Karine, Willems, Christina, Denayer, Pierre, Bureau, Michel, Retif, Cecile, Dupuis, Michel, Bouquiaux, Olivier, Vanderdonckt, Patrick, van Landegem, William, Caekebeke, Jo, Van Ingelghem, Erwin, Peeters, Katelijne, Gerard, Pascale, de Noordhout, Alain Maertens, Desfontaines, Philippe, Urbain, Etienne, Declercq, Inge, Van Wijmeersch, Bart, Vanroose, Erwin, Wibail, Alain, Barthomolé, Emmanuel, Ursell, Melanie, Sweet, Margaret Elizabeth, Howse, David, Jichici, Draga, Shawush, Melad, Namaka, Mike, Traboulsee, Anthony, Hashimoto, Stan, Lo, Raymond, Marchetti, Paul, Lapierre, Yves, Jacques, Francois, MacLean, Gregg, Bhan, Virender, Duquette, Pierre, Stewart, Bradley, Paulseth, John, Kremenchutzky, Marcelo, Vorobeychik, Galina, O'Connor, Paul, Grand'Maison, François, Havrdova, Eva, Meluzinová, Eva, Valis, Martin, Talab, Radomír, Stourac, Pavel, Zapletalová, Olga, Dufek, Michal, Sládková, Vladimíra, Novotna, Alena, Vancurová, Romana, Lhotaková, Libuse, Fiedler, Jiri, Vachova, Marta, Dolezil, David, Stetkarova, Ivana, Rehankova, Adela, Psenica, Petr, Ulehlova, Veronika, Feketova, Sona, Skoda, Ondrej, Färkkilä, Markus, Taneli, Sarasoja, Koivisto, Keijo, Seppä, Juha Matti, Airas, Laura, Elovaara, Irina, Hartikainen, Päivi, Pirttila, Tuula, Louchart, Pierre, Ille, Olivier, Thenint, Jean philippe, Godet, Etienne, Vioud, Marcel Maillet, Colamarino, Renato, Gugenheim, Michel, Grimaud, Jerome, Kopf, Audrey, Billy, Christophe, Huttin, Bernard, Borsotti, Jean paul, Devos, Philippe, Kendjuo, Jean bertin N, Verier, Albert, Chapuis, Stephane, Daluzeau, Nathalie, Angibaud, Gilles, Uriot, Marie-Sylvie Artaud, Ziegler, François, Sellal, François, Moulignier, Antoine, Lavenu, Isabelle, Ismail, Samir, Devy, Richard, Suceveanu, Manuel, Wagner, Marc, Marcel, Sebastien, Derouiche, Faycal, Mostoufizadehghalamfarsa, Sohrab, Delalande, Sophie, Ruggieri, Irene, Van Nieuwenhuyse, Catherine Bossu, Nifle, Chantal, Ondze, Basile, Vasilescu, Carmen Gurau, Vongsouthi, Cyrille, Coustans, Marc, Anne, Olivier, Amevigbe, Josephine, Servan, Jerome, Merienne, Marc, Eck, Philippe, Berroir, Stephane, Busson, Philippe, Barroso, Bruno, Larrieu, Jean-Marc, Giendaj, Catherine Louvet, Malkoun, Imad, Hautecoeur, Patrick, Kwiatkowski, Arnaud, Pouliquen, Andre, Garrigues, Guillaume, Delerue, Olivier, Giraud, Pierric, Gere, Julien, Vaunaize, Jean, Dereeper, Olivier, Seiller, Nicolas, Alsassa, Roger, Vlaicu, Mihaela, Neuville, Veronique, Faucheux, Jean Marc, Bernady, Patricia, Fanjaud, Guy, Viallet, François, Schroeter, Michael, Schlemilch-Paschen, Sylke, Lange, Thomas, Bohr, Kin-Arno, Jendroska, Klaus, Rehkopf, Elisabeth, Bergmann, Arnfin, Kleinschnitz, Christoph, Postert, Thomas, Scholz, Peter, Mauz, Uwe, Stratmann, Hubert, Siefjediers, Veneta, Prantl, Martin, Gehring, Klaus, Zellner, Ruth, Junge, Kathrin, Zellner, Anton, Bacay, Valerina, Schlegel, Eugen, Polzer, Udo, Strauss, Erik, Link, Andreas, Stenzel, Christoph, Freidel, Matthias, Drews, Joachim, Neudert, Christian, Schmitz, Frank, Jaeger, Joachim, Masri, Said, Heuberger, Wolfgang, Trausch, Beate, Ruhnke, Oliver, Scarel, Serena, Bach, Kathlen, Ernst, Michael, Landefeld, Harald, Richter, Nils, Schmidt, Stephan, Krause, Michaela, Dressel, Alezander, Ruth, Roland, Anvari, Kerstin, Gossling, Jens, Schenk, Christoph, Tiedge, Oliver, Bode, Lutz, Eder, Hans-Thomas, Pfeffer, Oliver, Krug, Reinhard, Lassek, Christoph, Fleischer, Eberhard, Meuth, Sven, Klotz, Luisa Hildegard, Peglau, Ines, Kukowski, Borries, Herting, Birgit, Guthke, Kersten, Schierenbeck, Jurgen, Brockmeier, Bernd, Albrecht, Holger, Wuttke, Matthias, Augspach-Hofmann, Regine, Gunther, Stefan, Redbrake, Martin, Franke, Christian, Buchner, Klaus, Gratz, Thomas, Horn, Rolf, Doemges, Frank, Schreiber, Martin, Brosch, Thomas, Horn, Markus, Kittlitz, Matthias, Vulturius, Gabriele, Hinse, Paul, Malessa, Rolf, Wiehler, Stephan, Katsarava, Zaza, Kastrup, Oliver, Kausch, Ulrich, Gullekes, Martin, Fickinger, Markus, Wenzel, Wilhelm, Botefur, Ingolf C., Reifschneider, Gerd, Rauer, Sebastian, Lang, Michael, Harms, Lutz, Eckhardt, Ulrich, Cursiefen, Simone, Linker, Ralf, Angstwurm, Klemens, Haas, Judith, Schuetze, Ivo, Rohm, Eva, Stienker-Fisse, H., Sailer, Michael, Bohringer, Johannes, Maurer, Mathias, Bause, Eberhard, Wersching, Ronald, Dachsel, Reinhardt, Domke, Sylke, Hoffman, Frank, Tackenberg, Bjorn, Roch, Kerstin, Ziebold, Uwe, Kallmann, Boris, Buehler, Bernhard, Faiss, Judith, Faiss, Juergen, Schimrigk, Sebastian, Menges, Christian, Knop, Karl Christian, Koehler, Wolfgang, Siever, Arno, Bufler, Johannes, Gramsl, Georg, Kuhnler, Benedicta, Maschke, Matthias, Stogbauer, Florian, Staude, Lisa, Bethke, Florian, Bitsch, Andreas, Harmjanz, Arndt D., Windsheimer, Jorg, Kieseier, Bernd C., Berkenfeld, Ralf, Tumani, Hayrettin, Kirsch, Michael, Wildemann, Brigitte, Daniels, Regina, Gottwald, Klaus, Elias, Wolfgang-Gerhard, Hoffmann, Olaf, Schwab, Matthias, Pilz, Christopher, Klostermann, Fabian, Hellwig, Kerstin, Berthele, Achim, Bayas, Antonios, Molitor, Daniel, Grothe, Christoph, Wagner, Bert, Karageorgiou, Klimentini, Mitsikostas, Dimosthenis, Kodounis, Antonios, Plaitakis, Andreas, Papadimitriou, Alexandros, Grigoriadis, Nikolaos, Vlaikidis, Nikolaos, Koutlas, Evaggelos, Kyritsis, Athanassios, Papathanassopoulos, Panagiotis, Makris, Nikolaos, Tavernarakis, Antonios, Scarpini, Elio, Montanari, Enrico, Marrosu, Maria Giovanna, Trojano, Maria, Amato, Maria Pia, Rottoli, Mariarosa, Lugaresi, Alessandra, Florio, Ciro, Gasperini, Claudio, Grimaldi, Luigi, Millefiorini, Enrico, Koudriavtseva, Tatiana, Perla, Franco, Mantegazza, Renato, Bertolotto, Antonio, Ghezzi, Angelo, Aguilar, Sandra Quinones, Eisenberg, Eli Skromne, Lopez, Leondardo Llamas, Estudillo, Rocio Marquez, Schrijver, H.M., Wittebol, M.C., Baart, J.C., van Golde, A.E.L., Hengstman, G.J.D., Pop, P.H.M., Bos (Geldrop), M., Medaer, R., Schyns-Soeterboek, Angelique, van der Zwart, A., van Diepen, A.J.H., Verheul, G.A.M., Verhagen, W.I.M., Bos (Helmond), M., Witjes, R.J.G.M., Sinnige, L.G.F., van Munster, E.Th.L., Sanders, E.A.C.M., van Dijl, Ron, Hupperts, R.M.M., Frequin, S.T.F.M., Visser, L.H., Henselmans, J.M.L., Moll, J.W.B., Midgard, Rune, Myhr, Kjell Morten, Edland, Astrid, Telstad, Wenche, Hognestad, Tone, Lund, Christian, Hovdal, Harald, Kamaljit, Kaur, Schepel, Jan, Hogenesch, Roelfien Ida, Schüler, Stephan, Odeh, Francis, Alstadhaug, Karl B., Korsgaard, Olav, Farbu, Elisabeth, Ingvaldsen, Teis Barclay, Soares (SCO), Diana, Rente, José, Guerra, José Manuel Costa, Morganho, Armando, Leitão, António, de Sá, João, Sá, Maria José, Marques, Pinto, Veloso, Mário, Baptista, Miguel Viana, Szilasiová, Jarmila, Copikova-Cudrakova, Daniela, Prochazkova, Lubica, Klimová, Eleonóra, Donath, Vladimir, Brozman, Miroslav, Ramo, Cristina, Ruiz, Domingo Pérez, Hernández, Carmen Calles, Sola, María Eugenia Marzo, Moro, Roberto Suarez, Vidal, Jose Antonio, Rodríguez, Ana Belén Caminero, Ozaeta, Gisela Martin, Nadal, Jordi Batlle, Esquide, Amaya Alvarez de Arcaya, Urtaza, Javier Olascoaga, Martínez-Yélamos, Sergio, Arbizu, Txomin, Torrenta, Lluis Ramio i, Boggild, Mike, Wilson, Martin, Al-Araji, Adnan, Nicholas, Richard, Harrower, Timothy, Redmond, Ian, Wolf, Tilo, Osei-Bonsu, Michael, Mazibrada, Gordon, Rog, David, Cottrell, David, Constantinescu, Cris, Gray, Orla, Belhag, Mohamed, Shehu, Abdullah, Rashid, Waqar, Duddy, Martin, Kappos, Ludwig, Wiendl, Heinz, Spelman, Tim, Pellegrini, Fabio, Chen, Yi, Dong, Qunming, and Koendgen, Harold

Published
2018
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11. Mutations in a Human ROBO Gene Disrupt Hindbrain Axon Pathway Crossing and Morphogenesis

Author

Jen, Joanna C., Chan, Wai-Man, Bosley, Thomas M., Wan, Jijun, Carr, Janai R., Rüb, Udo, Shattuck, David, Salamon, Georges, Kudo, Lili C., Ou, Jing, Kansu, Tülay, al Dhalaan, Hesham, al Zayed, Zayed, MacDonald, David B., Stigsby, Bent, Plaitakis, Andreas, Dretakis, Emmanuel K., Gottlob, Irene, Pieh, Christina, Traboulsi, Elias I., Wang, Qing, Wang, Lejin, Andrews, Caroline, Yamada, Koki, Demer, Joseph L., Karim, Shaheen, Alger, Jeffry R., Geschwind, Daniel H., Deller, Thomas, Sicotte, Nancy L., Nelson, Stanley F., Baloh, Robert W., and Engle, Elizabeth C.

Published
2004

12. Structural Evolution of Primate Glutamate Dehydrogenase 2 as Revealed by In Silico Predictions and Experimentally Determined Structures.

Author

Litso, Ionela, Plaitakis, Andreas, Fadouloglou, Vasiliki E., Providaki, Mary, Kokkinidis, Michael, and Zaganas, Ioannis

Subjects
*GLUTAMATE dehydrogenase, *PRIMATES, *PROTEIN structure prediction, *NEURODEGENERATION, *APES
Abstract

Glutamate dehydrogenase (GDH) interconverts glutamate to a-ketoglutarate and ammonia, interconnecting amino acid and carbohydrate metabolism. In humans, two functional GDH genes, GLUD1 and GLUD2, encode for hGDH1 and hGDH2, respectively. GLUD2 evolved from retrotransposition of the GLUD1 gene in the common ancestor of modern apes. These two isoenzymes are involved in the pathophysiology of human metabolic, neoplastic, and neurodegenerative disorders. The 3D structures of hGDH1 and hGDH2 have been experimentally determined; however, no information is available about the path of GDH2 structure changes during primate evolution. Here, we compare the structures predicted by the AlphaFold Colab method for the GDH2 enzyme of modern apes and their extinct primate ancestors. Also, we analyze the individual effect of amino acid substitutions emerging during primate evolution. Our most important finding is that the predicted structure of GDH2 in the common ancestor of apes was the steppingstone for the structural evolution of primate GDH2s. Two changes with a strong functional impact occurring at the first evolutionary step, Arg443Ser and Gly456Ala, had a destabilizing and stabilizing effect, respectively, making this step the most important one. Subsequently, GDH2 underwent additional modifications that fine-tuned its enzymatic properties to adapt to the functional needs of modern-day primate tissues. [ABSTRACT FROM AUTHOR]

Published
2024
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39. Human GLUD1 and GLUD2 glutamate dehydrogenase localize to mitochondria and endoplasmic reticulum

Author

Mastorodemos, Vasileios, Kotzamani, Dimitra, Zaganas, Ioannis, Arianoglou, Giovanna, Latsoudis, Helen, and Plaitakis, Andreas

Subjects
Endoplasmic reticulum -- Physiological aspects -- Research, Genes -- Physiological aspects -- Research, Mitochondria -- Physiological aspects -- Research, Glutamate dehydrogenase -- Physiological aspects -- Research, Biological sciences, Physiological aspects, Research
Abstract

Mammalian glutamate dehydrogenase (GDH), an enzyme central to glutamate metabolism, is thought to localize to the mitochondrial matrix, although there are also suggestions for the extramitochondrial presence of this protein. Whereas GDH in mammals is encoded by the GLUD1 gene, humans and the great apes have, in addition, a GLUD2 gene showing a distinct expression pattern. The encoded hGDH1 and hGDH2 isoenzymes are highly homologous, but their leader sequences are more divergent. To explore their subcellular targeting, we constructed expression vectors in which hGDH1 or hGDH2 was fused with the enhanced green fluorescent protein (EGFP) and used these to transfect COS 7, HeLa, CHO, HEK293, or neuroblastoma SHSY-5Y cells. Confocal microscopy revealed GDH-EGFP fluorescence in the cytoplasm within coarse structures. Cotransfection experiments using organelle-specific markers revealed that hGDH1 or hGDH2 colocalized with the mitochondrial marker DsRed2-Mito and to a lesser extent with the endoplasmic reticulum marker DsRed2-ER. Western blots detected two GDH-EGFP specific bands: a ~90 kDa band and a ~95 kDa band associated with the mitochondria and the endoplasmic reticulum containing cytosol, respectively. Deletion of the signal sequence, while altering drastically the fluoresce distribution within the cell, prevented GDH from entering the mitochondria, with the ~90 kDa band being retained in the cytosol. In addition, the deletion eliminated the ~95 kDa band from cell lysates, thus confirming that it represents the full-length GDH. Hence, while most of the hGDHs translocate into the mitochondria (a process associated with cleavage of the signal sequence), part of the protein localizes to the endoplasmic reticulum, probably serving additional functions. Key words: glutamate dehydrogenase, leader peptide deletion, subcellular localization, EGFP. La glutamate deshydrogenase de mammifere (GDH), une enzyme centrale du metabolisme du glutamate, est presumee etre localisee dans la matrice mitochondriale meme si sa presence hors de la mitochondrie a aussi ete suggeree. La GDH chez les mammiferes est codee par le gene GLUD1, mais les humains et les grands singes possedent en plus le gene GLUD2 montrant un patron d'expression distinct. Les isoenzymes hGDH1 et hGDH2 sont hautement homologues mais leurs sequences de tete sont plus divergentes. Afin d'explorer leur ciblage subcellulaire, nous avons construit des vecteurs d'expression dans lesquels hGDH1 ou hGDH2 sont fusionnees a la proteine fluorescente EGFP, et nous les avons utilise s pour transfecter des cellules COS 7, HeLa, CHO, HEK293 ou les neuroblastomes SHSY-5Y. La microscopie confocale a revele la presence de la fluorescence de la GDH-EGFP dans le cytoplasme, a l'interieur de structures grossieres. Des experiences de co-transfection avec des marqueurs specifiques d'organelles ont montre que hGDH1 ou hGDH2 sont co-localisees avec le marqueur mitochondrial DsRed2-Mito et, a un degre moindre, avec le marqueur du reticulum endoplasmique DsRed2-ER. L'immunobuvardage a permis de detecter deux bandes specifiques de GDH-EGFP : une bande de ~90 kDa associee a la mitochondrie et une bande de ~95 kDa presente dans le cytosol comprenant le reticulum endoplasmique. La deletion de la sequence signal, en modifiant la distribution cellulaire de la fluorescence de facon importante, empechait la GDH d'entrer dans la mitochondrie, la bande de ~90 kDa etant retenue dans le cytosol. En plus, la deletion a elimine la bande de ~95 kDa des lysats cellulaires, confirmant ainsi qu'elle correspondait a la GDH de pleine longueur. Ainsi, alors que les hGDH sont majoritairement transloquees dans la mitochondrie (un processus associe au clivage de la sequence signal), une partie des proteines se localisent dans le reticulum endoplasmique, jouant probablement d'autres roles. Mots-cles : glutamate deshydrogenase, deletion du peptide de tete, localisation sub-cellulaire, EGFP. [Traduit par la Redaction], Introduction Glutamate dehydrogenase (GDH) (EC 1.4.1.3) catalyzes the reversible oxidative deamination of glutamate to α-ketoglutarate and ammonia using NAD+ and (or) NADP+ as cofactors (Smith 1979). In many organisms, the [...]

Published
2009

42. Crystal structure of glutamate dehydrogenase 2, a positively selected novel human enzyme involved in brain biology and cancer pathophysiology

Author

Dimovasili, Christina, primary, Fadouloglou, Vasiliki E., additional, Kefala, Aikaterini, additional, Providaki, Mary, additional, Kotsifaki, Dina, additional, Kanavouras, Konstantinos, additional, Sarrou, Iosifina, additional, Plaitakis, Andreas, additional, Zaganas, Ioannis, additional, and Kokkinidis, Michael, additional

Published
2021
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45. Assessment of Parkinson's disease risk loci in Greece

Author

Kara, Eleanna, Xiromerisiou, Georgia, Spanaki, Cleanthe, Bozi, Maria, Koutsis, Georgios, Panas, Marios, Dardiotis, Efthimios, Ralli, Styliani, Bras, Jose, Letson, Christopher, Edsall, Connor, Pliner, Hannah, Arepalli, Sampath, Kalinderi, Kallirhoe, Fidani, Liana, Bostantjopoulou, Sevasti, Keller, Margaux F., Wood, Nicholas W., Hardy, John, Houlden, Henry, Stefanis, Leonidas, Plaitakis, Andreas, Hernandez, Dena, Hadjigeorgiou, Georgios M., Nalls, Mike A., and Singleton, Andrew B.

Published
2014
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46. A Comparison of Acute Hemorrhagic Stroke Outcomes in 2 Populations: The Crete–Boston Study

Author

Zaganas, Ioannis, Halpin, Amy P., Oleinik, Alexandra, Alegakis, Athanasios, Kotzamani, Dimitra, Zafiris, Spiros, Chlapoutaki, Chryssanthi, Tsimoulis, Dimitris, Giannakoudakis, Emmanouil, Chochlidakis, Nikolaos, Ntailiani, Aikaterini, Valatsou, Christina, Papadaki, Efrosini, Vakis, Antonios, Furie, Karen L., Greenberg, Steven M., and Plaitakis, Andreas

Published
2011
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48. High Prevalence of Transthyretin-Related Amyloidosis in Crete, Greece is Due to Three TTR Pathogenic Variants with Markedly Differing Phenotypic Presentations (3974)

Author

Tzagournissakis, Minas, primary, Foukarakis, Emanouil, additional, Marinis, Anastasios, additional, Mathioudakis, Lambros, additional, Michaelidou, Kleita, additional, Spanaki, Cleanthe, additional, Tsilimbaris, Miltiadis, additional, Plaitakis, Andreas, additional, Mitsias, Panayiotis, additional, and Zaganas, Ioannis, additional

Published
2020
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