Dr. Alkmini Papadopoulou
| Telefon: | +49 (0) 821 598-71106 |
| E-Mail: | Alkmini.Papadopoulou@med.uni-augsburgmed.uni-augsburg.de () |
| Raum: | 1.03.09 (Business Campus München) |
| Adresse: | Parkring 11-13, 85748 Garching |
Forschungsschwerpunkte
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Investigating the physiological regulation of SPPL3 protein expression under starvation conditions and how that is connected to different nutrient sensing pathways. We are using multiple cell culture models and a variety of biochemistry techniques to figure out this complicated regulation mechanism.
Lebenslauf
Seit Januar 2020
Post Doctoral Researcher, 威尼斯赌博游戏_威尼斯赌博app-【官网】 of Augsburg, Augsburg, Germany
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Oktober 2019 – Dezember 2019
Post Doctoral Researcher, Ludwig-Maximilians 威尼斯赌博游戏_威尼斯赌博app-【官网】, Munich, Germany
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Juli 2014 – September 2019
PhD Candidate, International Max Planck Research School of Life Sciences and Ludwig-Maximilians 威尼斯赌博游戏_威尼斯赌博app-【官网】, Munich, Germany
Final Grade “Summa cum Laude”
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Oktober 2013 – Juni 2014
Postgraduate Research Student, Graduate School of 威尼斯赌博游戏_威尼斯赌博app-【官网】icine, Nagoya 威尼斯赌博游戏_威尼斯赌博app-【官网】, Japan
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September 2007 – Juli 2013
Diploma in Pharmacy, School of Pharmacy, Aristotle 威尼斯赌博游戏_威尼斯赌博app-【官网】 of Thessaloniki, Greece
Final Grade 7.53/10 (rating: very good, top 10% of faculty graduates)
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September 2001 – Juni 2007
Anatolia College of Thessaloniki, “Greek-American High School”
Final Grade 19.3/20 (rating: excellent)
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Mitgliedschaften
- Mitglied der Gesellschaft für Biochemie und Molekularbiologie e.V. (GBM)
Publikationen
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2023 |
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Smit P., Buehring-Uhle C., Nather C., Negraschus A., Goldmann U., Papadopoulou Alkmini A., Riviere J., Morath V., Henkel E., Bromberger T., Goetze K., Heinz L., Fluhrer Regina, Moser M., Superti-Furga G., Bassermann F., Eichner R..
Inhibiting MGAT1-mediated N-glycosylation reduces proliferation and adhesion of AML cells and increases affinities of anti-SLC3A2 directed immunotherapies [Abstract].
https://doi.org/10.1159/000533576
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2022 |
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Heard Amanda, Landmann Jack H., Hansen Ava R., Papadopolou Alkmini, Hsu Yu-Sung, Selli Mehmet Emrah, Warrington John M., Lattin John, Chang Jufang, Ha Helen, Haug-Kr?per Martina, Doray Balraj, Gill Saar, Ruella Marco, Hayer Katharina E., Weitzman Matthew D., Green Abby M., Fluhrer Regina, Singh Nathan.
Antigen glycosylation regulates efficacy of CAR T cells targeting CD19.
https://doi.org/10.1038/s41467-022-31035-7
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Papadopoulou Alkmini A., Stelzer Walter, Silber Mara, Schlosser Christine, Spitz Charlotte, Haug-Kr?per Martina, Straub Tobias, Müller Stephan A., Lichtenthaler Stefan F., Muhle-Goll Claudia, Langosch Dieter, Fluhrer Regina.
Helical stability of the GnTV transmembrane domain impacts on SPPL3 dependent cleavage.
https://doi.org/10.1038/s41598-022-24772-8
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Bühring-Uhle C., Smit P., Negraschus A., Morath V., Goldmann U., Papadopoulou Alkmini A., Heider M., Riviere J., G?tze K., Heinz L., Fluhrer Regina, Moser M., Superti-Furga G., Bassermann F., Eichner R..
SPPL3 and its substrate glycosyltransferases regulate the N-glycosylation of SLC3A2 and alter the affinities of anti-SLC3A2 immunotherapies in AML [Abstract].
https://doi.org/10.1159/000526456
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2020 |
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Papadopoulou Alkmini A., Fluhrer Regina.
Signalling functions of intramembrane aspartyl-proteases.
https://doi.org/10.3389/fcvm.2020.591787
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2019 |
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Papadopoulou Alkmini A., Müller Stephan A, Mentrup Torben, Shmueli Merav D, Niemeyer Johannes, Haug‐Kr?per Martina, von Blume Julia, Mayerhofer Artur, Feederle Regina, Schr?der Bernd, Lichtenthaler Stefan F., Fluhrer Regina.
Signal peptide peptidase‐like 2c (SPPL2c) impairs vesicular transport and cleavage of SNARE proteins.
https://doi.org/10.15252/embr.201846451
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Niemeyer Johannes, Mentrup Torben, Heidasch Ronny, Müller Stephan A, Biswas Uddipta, Meyer Rieke, Papadopoulou Alkmini A., Dederer Verena, Haug‐Kr?per Martina, Adamski Vivian, Lüllmann-Rauch Renate, Bergmann Martin, Mayerhofer Artur, Saftig Paul, Wennemuth Gunther, Jessberger Rolf, Fluhrer Regina, Lichtenthaler Stefan F., Lemberg Marius K, Schr?der Bernd.
The intramembrane protease SPPL2c promotes male germ cell development by cleaving?phospholamban.
https://doi.org/10.15252/embr.201846449
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2017 |
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Scilabra Simone D., Yamamoto Kazuhiro, Pigoni Martina, Sakamoto Kazuma, Müller Stephan A., Papadopoulou Alkmini A., Lichtenthaler Stefan F., Troeberg Linda, Nagase Hideaki, Kadomatsu Kenji.
Dissecting the interaction between tissue inhibitor of metalloproteinases-3 (TIMP-3) and low density lipoprotein receptor-related protein-1 (LRP-1): Development of a “TRAP” to increase levels of TIMP-3 in the tissue.
https://doi.org/10.1016/j.matbio.2016.07.004
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