- Alternative title
-
SH3 vermittelte Proteininteraktionen von Mena und VASP
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
Würzburg, Universität Würzburg, Dissertation, 2017
- Keyword
-
Histologie
Cytologie
- Event
-
Veröffentlichung
- (where)
-
Würzburg
- (who)
-
Universität Würzburg
- (when)
-
2017
- Creator
- Contributor
-
Schuh, Kai
- URN
-
urn:nbn:de:bvb:20-opus-154481
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:21 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
- Offner, Kristin
- Schuh, Kai
- Universität Würzburg
Time of origin
- 2017
Other Objects (12)
SH3-mediated protein interactions of Mena and VASP
Investigating the effect of Ena/VASP-EVH1 domain-mediated interactions inhibition in immune cells
Molecular basis for SH3 domain regulation of F-BAR-mediated membrane deformation
The role of VASP in cGMP-mediated vascular smooth muscle relaxation
ITSN1 regulates SAM68 solubility through SH3 domain interactions with SAM68 proline-rich motifs
Cellular functions of VASP phosphorylations
Prediction of virus–host interactions and identification of hot spot residues of DENV-2 and SH3 domain interactions
Mena/VASP and αII-Spectrin complexes regulate cytoplasmic actin networks in cardiomyocytes and protect from conduction abnormalities and dilated cardiomyopathy
Mena/VASP and alphaII-Spectrin complexes regulate cytoplasmic actin networks in cardiomyocytes and protect from conduction abnormalities and dilated cardiomyopathy
MENA’s Fake Pharma Conundrum
MENA’s Fake Pharma Conundrum
Identification of SH3 domain interaction partners of FasL using a human SH3 domain phage display library
SH3-mediated protein interactions of Mena and VASP
Investigating the effect of Ena/VASP-EVH1 domain-mediated interactions inhibition in immune cells
Molecular basis for SH3 domain regulation of F-BAR-mediated membrane deformation
The role of VASP in cGMP-mediated vascular smooth muscle relaxation
ITSN1 regulates SAM68 solubility through SH3 domain interactions with SAM68 proline-rich motifs
Cellular functions of VASP phosphorylations
Prediction of virus–host interactions and identification of hot spot residues of DENV-2 and SH3 domain interactions
Mena/VASP and αII-Spectrin complexes regulate cytoplasmic actin networks in cardiomyocytes and protect from conduction abnormalities and dilated cardiomyopathy
Mena/VASP and alphaII-Spectrin complexes regulate cytoplasmic actin networks in cardiomyocytes and protect from conduction abnormalities and dilated cardiomyopathy
MENA’s Fake Pharma Conundrum
MENA’s Fake Pharma Conundrum
Identification of SH3 domain interaction partners of FasL using a human SH3 domain phage display library
SH3-mediated protein interactions of Mena and VASP
Investigating the effect of Ena/VASP-EVH1 domain-mediated interactions inhibition in immune cells
Molecular basis for SH3 domain regulation of F-BAR-mediated membrane deformation
The role of VASP in cGMP-mediated vascular smooth muscle relaxation
ITSN1 regulates SAM68 solubility through SH3 domain interactions with SAM68 proline-rich motifs
Cellular functions of VASP phosphorylations
Prediction of virus–host interactions and identification of hot spot residues of DENV-2 and SH3 domain interactions
Mena/VASP and αII-Spectrin complexes regulate cytoplasmic actin networks in cardiomyocytes and protect from conduction abnormalities and dilated cardiomyopathy
Mena/VASP and alphaII-Spectrin complexes regulate cytoplasmic actin networks in cardiomyocytes and protect from conduction abnormalities and dilated cardiomyopathy
MENA’s Fake Pharma Conundrum
MENA’s Fake Pharma Conundrum