PhD position (m/f/d) TV-L E13 (65%) für Ulm gesucht
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Job Kategorie: Sonstige Branchen Sonstige Tätigkeitsbereiche
Stellenangebot Basisdaten
- Arbeitsort:
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DE 89081 Ulm
- Umkreis:
-
keine Angabe.
- Art der Arbeitsstelle:
-
- Letze Aktualisierung:
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24.12.20242024-12-24
Stellenausschreibung: PhD position (m/f/d) TV-L E13 (65%)
- Arbeitgeber bzw.
Arbeitsvermittler
-
Universitätsklinikum Ulm in Schwetzingen
- Branche
-
Sonstige Branchen
- Kategorie
-
Sonstige Tätigkeitsbereiche
- Stellenbeschreibung
- The Institute of Physiological Chemistry of Ulm University, Germany
offers a
PhD position (m/f/d) TV-L E13 (65%)
Job Summary: The project is supported by a grant from the Wilhelm
Sander Foundation. Topic: "Proteolytic targeting of menin/MEN1 for the
treatment of acute B-cell lymphoblastic leukemia, B-cell lymphoma and
multiple myeloma". MEN1 is a protein that regulates many cellular
processes by interacting with various proteins. Inhibition of the
interaction of MEN1 with the oncogenic products of MLL/KMT2A
rearrangements (MLLr) by MEN1-binding inhibitors leads to clinical
remissions in acute myeloid and B-cell acute lymphoblastic leukemia
(AML and B-ALL) with MLLr. Unfortunately, this effect has only been
observed in a subset of MLLr leukemia patients and is followed by
relapse due to mutations in the KMT2A binding domain of MEN1. Since
the functions of MEN1 are not limited to its interaction with KMT2A,
we hypothesized that pharmacological degradation of the MEN1 protein
may outperform the effect of inhibitors. This can be achieved through
the use of proteolysis targeting chimeras (PROTACs), which promote
targeted protein degradation. The availability of clinically tested
inhibitors will enable rapid and targeted development of PROTACs. The
project is based on our recent publication (Wolffhardt T. et al. Int J
Mol Sci. 2023 24(22):16472) and will be carried out in collaboration
with the Chemical Epigenetics research group, Institute of
Pharmacological Sciences, Albert-Ludwigs University, Freiburg.
Objectives:
- - Investigate the mechanisms of MEN1 dependency in B-ALLs driven by
MLLr and other oncogenic mutations and identify targetable
co-dependencies.
- - To evaluate and optimize the protein degrading activity and
cytotoxic effect of MEN1-targeted PROTACs.
- - Investigate the activity of the most effective PROTACs against
MLLr clones that have acquired resistance to MEN1 binders.
Qualifications:
- Master's degree in biochemistry/biotechnology, biomedical sciences,
cell biology, bioengineering or related disciplines.
Contract: limited
Level of employment: part-time
application deadline: 01.02.2025
Application procedure:
- Please send CV by 1 February 2025. The successful candidate is
expected to start no later than 1 March 2025. The position is limited
to 24 months but can be extended.
Contact information:
- Dr. Alexey Ushmorov, Ulm University, Institute of Physiological
Chemistry, Albert-Einstein-Allee 11, 89081 Ulm Germany. Phone: +49 731
50 33847. E-mail: alexey.ushmorov@uni-ulm.de.
Employment takes place through the administration department of the
University Medical Center Ulm, which acts in the name and on behalf of
the federal state of Baden-Württemberg. Handicapped people with equal
qualifications will be employed preferentially. The Ulm-University
strives for an increased proportion of woman in research and teaching
and therefore strongly encourages qualified female scientists to apply
for the position.
The Institute of Physiological Chemistry of Ulm University, Germany
offers a
PhD position (m/f/d) TV-L E13 (65%)
Job Summary: The project is supported by a grant from the Wilhelm
Sander Foundation. Topic: "Proteolytic targeting of menin/MEN1 for the
treatment of acute B-cell lymphoblastic leukemia, B-cell lymphoma and
multiple myeloma". MEN1 is a protein that regulates many cellular
processes by interacting with various proteins. Inhibition of the
interaction of MEN1 with the oncogenic products of MLL/KMT2A
rearrangements (MLLr) by MEN1-binding inhibitors leads to clinical
remissions in acute myeloid and B-cell acute lymphoblastic leukemia
(AML and B-ALL) with MLLr. Unfortunately, this effect has only been
observed in a subset of MLLr leukemia patients and is followed by
relapse due to mutations in the KMT2A binding domain of MEN1. Since
the functions of MEN1 are not limited to its interaction with KMT2A,
we hypothesized that pharmacological degradation of the...
- Qualifikation
- Arbeitskräfte
- Verdienst:
- n.a.
- Bewerbung an
- Universitätsklinikum Ulm
Carl-Benz-Straße 5
De 68723 Schwetzingen
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