Analysis of transient phosphorylation-dependent protein-protein interactions in living mammalian cells using split-TEV
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
1472-6750
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
online resource.
- Bibliographic citation
-
Analysis of transient phosphorylation-dependent protein-protein interactions in living mammalian cells using split-TEV ; volume:8 ; number:1 ; day:13 ; month:7 ; year:2008 ; pages:1-15 ; date:12.2008
BMC biotechnology ; 8, Heft 1 (13.7.2008), 1-15, 12.2008
- Creator
- Contributor
-
Reinecke, Lisa
Botvinnik, Anna
Rossner, Moritz J.
SpringerLink (Online service)
- DOI
-
10.1186/1472-6750-8-55
- URN
-
urn:nbn:de:1111-2016072533891
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2025, 11:03 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.
Associated
- Wehr, Michael C.
- Reinecke, Lisa
- Botvinnik, Anna
- Rossner, Moritz J.
- SpringerLink (Online service)
Other Objects (12)
Pathogenic mutations of human phosphorylation sites affect protein–protein interactions
Protein-protein interactions
Protein-protein interaction
The regulation of bZIP63 through posttranslational phosphorylation and protein-protein interaction
SPServer: split-statistical potentials for the analysis of protein structures and protein–protein interactions
High-throughput mammalian two-hybrid screening for protein-protein interactions using transfected cell arrays
Human protein-protein interaction prediction
Kartierung diskontinuierlicher Protein-Protein Wechselwirkungen
Protein-protein interactions in drug discovery
Streamlined Protein‐Protein Interface Loop Mimicry
Streamlined Protein‐Protein Interface Loop Mimicry
Intercellular protein–protein interactions at synapses
Pathogenic mutations of human phosphorylation sites affect protein–protein interactions
Protein-protein interactions
Protein-protein interaction
The regulation of bZIP63 through posttranslational phosphorylation and protein-protein interaction
SPServer: split-statistical potentials for the analysis of protein structures and protein–protein interactions
High-throughput mammalian two-hybrid screening for protein-protein interactions using transfected cell arrays
Human protein-protein interaction prediction
Kartierung diskontinuierlicher Protein-Protein Wechselwirkungen
Protein-protein interactions in drug discovery
Streamlined Protein‐Protein Interface Loop Mimicry
Streamlined Protein‐Protein Interface Loop Mimicry
Intercellular protein–protein interactions at synapses
Pathogenic mutations of human phosphorylation sites affect protein–protein interactions
Protein-protein interactions
Protein-protein interaction
The regulation of bZIP63 through posttranslational phosphorylation and protein-protein interaction
SPServer: split-statistical potentials for the analysis of protein structures and protein–protein interactions
High-throughput mammalian two-hybrid screening for protein-protein interactions using transfected cell arrays
Human protein-protein interaction prediction
Kartierung diskontinuierlicher Protein-Protein Wechselwirkungen
Protein-protein interactions in drug discovery
Streamlined Protein‐Protein Interface Loop Mimicry
Streamlined Protein‐Protein Interface Loop Mimicry