- Alternative title
-
Der Einfluss von Tyrosin-Phosphorylierung auf den Dscam1-Signalweg
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Deutsch
- Notes
-
Kiel, Christian-Albrechts-Universität, Dissertation, 2016
- Classification
-
Biowissenschaften, Biologie
- Event
-
Veröffentlichung
- (where)
-
Kiel
- (who)
-
Universitätsbibliothek Kiel
- (when)
-
2016
- Creator
-
Erfurth, Maria-Luise
- URN
-
urn:nbn:de:gbv:8-diss-201295
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
- 14.08.2025, 10:48 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Object type
- Hochschulschrift
Associated
- Erfurth, Maria-Luise
- Universitätsbibliothek Kiel
Time of origin
- 2016
Other Objects (12)
The role of tyrosine phosphorylation in the regulation of TRPV6
The role of tyrosine phosphorylation during Dscam1-signaling : = Der Einfluss von Tyrosin-Phosphorylierung auf den Dscam 1-Signalweg = De Rol van Tyrosine-Fosforylering tijdens Dscam 1 Signalisatie
Tyrosine phosphorylation of Grb14 by Tie2
Dissecting the role of tyrosine phosphorylation of WAVE in macrophage migration
Tyrosine phosphorylation of NO-sensitive guanylyl cyclase
Tyrosine phosphorylation of NO-sensitive guanylyl cyclase
Photosensitive tyrosine analogues unravel site-dependent phosphorylation in TrkA initiated MAPK/ERK signaling
Large‐scale phosphorylation mapping reveals the extent of tyrosine phosphorylation in Arabidopsis
Tyrosine phosphorylation profiling via in situproximity ligation assay
The role of VE-cadherin tyrosine phosphorylation for the control of endothelial cell contacts
Tyrosine phosphorylation of myosin heavy chain during skeletal muscle differentiation: an integrated bioinformatics approach
Tyrosine phosphorylation and regulation of Wnt co-receptor LRP6
The role of tyrosine phosphorylation in the regulation of TRPV6
The role of tyrosine phosphorylation during Dscam1-signaling : = Der Einfluss von Tyrosin-Phosphorylierung auf den Dscam 1-Signalweg = De Rol van Tyrosine-Fosforylering tijdens Dscam 1 Signalisatie
Tyrosine phosphorylation of Grb14 by Tie2
Dissecting the role of tyrosine phosphorylation of WAVE in macrophage migration
Tyrosine phosphorylation of NO-sensitive guanylyl cyclase
Tyrosine phosphorylation of NO-sensitive guanylyl cyclase
Photosensitive tyrosine analogues unravel site-dependent phosphorylation in TrkA initiated MAPK/ERK signaling
Large‐scale phosphorylation mapping reveals the extent of tyrosine phosphorylation in Arabidopsis
Tyrosine phosphorylation profiling via in situproximity ligation assay
The role of VE-cadherin tyrosine phosphorylation for the control of endothelial cell contacts
Tyrosine phosphorylation of myosin heavy chain during skeletal muscle differentiation: an integrated bioinformatics approach
Tyrosine phosphorylation and regulation of Wnt co-receptor LRP6
The role of tyrosine phosphorylation in the regulation of TRPV6
The role of tyrosine phosphorylation during Dscam1-signaling : = Der Einfluss von Tyrosin-Phosphorylierung auf den Dscam 1-Signalweg = De Rol van Tyrosine-Fosforylering tijdens Dscam 1 Signalisatie
Tyrosine phosphorylation of Grb14 by Tie2
Dissecting the role of tyrosine phosphorylation of WAVE in macrophage migration
Tyrosine phosphorylation of NO-sensitive guanylyl cyclase
Tyrosine phosphorylation of NO-sensitive guanylyl cyclase
Photosensitive tyrosine analogues unravel site-dependent phosphorylation in TrkA initiated MAPK/ERK signaling
Large‐scale phosphorylation mapping reveals the extent of tyrosine phosphorylation in Arabidopsis
Tyrosine phosphorylation profiling via in situproximity ligation assay
The role of VE-cadherin tyrosine phosphorylation for the control of endothelial cell contacts
Tyrosine phosphorylation of myosin heavy chain during skeletal muscle differentiation: an integrated bioinformatics approach