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Cellular and Molecular Life Sciences : CMLS|February 25, 2014
The amino terminus extension in the long dipeptidyl peptidase 9 isoform contains a nuclear localization signal targeting the active peptidase to the nucleusDaniela Justa-Schuch, Ulrike Möller, Ruth Geiss-Friedlander
Methods in Molecular Biology (Clifton, N.J.)|December 25, 2008
Performing in vitro sumoylation reactions using recombinant enzymesAndreas Werner, Marie-Christine Moutty, Ulrike Möller, et al.
The Journal of Biological Chemistry|November 16, 2012
A novel SUMO1-specific interacting motif in dipeptidyl peptidase 9 (DPP9) that is important for enzymatic regulationEsther Pilla, Ulrike Möller, Guido Sauer, et al.
The Journal of Biological Chemistry|August 12, 2009
The cytoplasmic peptidase DPP9 is rate-limiting for degradation of proline-containing peptidesRuth Geiss-Friedlander, Nicolas Parmentier, Ulrike Möller, et al.
EMBO Reports|April 11, 2024
Phosphorylation of ELYS promotes its interaction with VAPB at decondensing chromosomes during mitosisChristina James, Ulrike Möller, Christiane Spillner, et al.
Proceedings of the National Academy of Sciences of the United States of America|March 11, 2004
A Fenton reaction at the endoplasmic reticulum is involved in the redox control of hypoxia-inducible gene expressionQing Liu, Utta Berchner-Pfannschmidt, Ulrike Möller, et al.
Elife|September 11, 2016
DPP9 is a novel component of the N-end rule pathway targeting the tyrosine kinase SykDaniela Justa-Schuch, Maria Silva-Garcia, Esther Pilla, et al.
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