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of 4
pro vyhledávání: '"Stefan R, Weisshaar"'
Autor:
Marion, Schnellhardt, Kristina, Uzunova, Veronika N, Bade, Anke, Krause, Stefan R, Weisshaar, Gerrit J K, Praefcke, R Jürgen, Dohmen
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 832
Posttranslational modification of proteins with the small ubiquitin-related modifier (SUMO) has been implicated in many important physiological functions, including the regulation of transcription and DNA repair. In most cases, only a small fraction
Autor:
Kristina Uzunova, Stefan R. Weisshaar, R. Jürgen Dohmen, Gerrit J. K. Praefcke, Marion Schnellhardt, Veronika N. Bade, Anke Krause
Publikováno v:
Methods in Molecular Biology ISBN: 9781617794735
Posttranslational modification of proteins with the small ubiquitin-related modifier (SUMO) has been implicated in many important physiological functions, including the regulation of transcription and DNA repair. In most cases, only a small fraction
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1a0783b8424c201b4961ce11a726e880
https://doi.org/10.1007/978-1-61779-474-2_4
https://doi.org/10.1007/978-1-61779-474-2_4
Autor:
Kerstin Göttsche, Kirstin Keusekotten, Stefan R. Weisshaar, Gerrit J. K. Praefcke, Anke Krause, Christiane Horst, R. Jürgen Dohmen, Helen M. Springer
Publikováno v:
FEBS letters. 582(21-22)
We have recently reported that poly-SUMO-2/3 conjugates are subject to a ubiquitin-dependent proteolytic control in human cells. Here we show that arsenic trioxide (ATO) increases SUMO-2/3 modification of promyelocytic leukemia (PML) leading to its s
Autor:
Michaela T. Niessen, Hartmut Scheel, Erica S. Johnson, Kay Hofmann, Gerrit J. K. Praefcke, R. Jürgen Dohmen, Kerstin Göttsche, Christoph Glanemann, Stefan R. Weisshaar, Marion Schnellhardt, Maria Miteva, Kristina Uzunova
Publikováno v:
The Journal of biological chemistry. 282(47)
Posttranslational protein modification with small ubiquitin-related modifier (SUMO) is an important regulatory mechanism implicated in many cellular processes, including several of biomedical relevance. We report that inhibition of the proteasome lea