Cargando…
DPP9 is a novel component of the N-end rule pathway targeting the tyrosine kinase Syk
The aminopeptidase DPP9 removes dipeptides from N-termini of substrates having a proline or alanine in second position. Although linked to several pathways including cell survival and metabolism, the molecular mechanisms underlying these outcomes are poorly understood. We identified a novel interact...
Autores principales: | Justa-Schuch, Daniela, Silva-Garcia, Maria, Pilla, Esther, Engelke, Michael, Kilisch, Markus, Lenz, Christof, Möller, Ulrike, Nakamura, Fumihiko, Urlaub, Henning, Geiss-Friedlander, Ruth |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5039030/ https://www.ncbi.nlm.nih.gov/pubmed/27614019 http://dx.doi.org/10.7554/eLife.16370 |
Ejemplares similares
-
A deep proteomics perspective on CRM1-mediated nuclear export and nucleocytoplasmic partitioning
por: Kırlı, Koray, et al.
Publicado: (2015) -
The target of the DEAH-box NTP triphosphatase Prp43 in Saccharomyces cerevisiae spliceosomes is the U2 snRNP-intron interaction
por: Fourmann, Jean-Baptiste, et al.
Publicado: (2016) -
Nanobodies: site-specific labeling for super-resolution imaging, rapid epitope-mapping and native protein complex isolation
por: Pleiner, Tino, et al.
Publicado: (2015) -
Correction: Nanobodies: site-specific labeling for super-resolution imaging, rapid epitope-mapping and native protein complex isolation
por: Pleiner, Tino, et al.
Publicado: (2016) -
Autoinhibition of Bruton's tyrosine kinase (Btk) and activation by soluble inositol hexakisphosphate
por: Wang, Qi, et al.
Publicado: (2015)