- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Anmerkungen
-
Frankfurt am Main, Johann Wolfgang Goethe-Universität, Dissertation, 2023
- Klassifikation
-
Medizin, Gesundheit
- Schlagwort
-
Enzyminhibitor
Proteinkinasen
Arzneimitteldesign
Signaltransduktion
- Ereignis
-
Veröffentlichung
- (wo)
-
Frankfurt am Main
- (wer)
-
Universitätsbibliothek Johann Christian Senckenberg
- (wann)
-
2023
- Urheber
- Beteiligte Personen und Organisationen
- DOI
-
10.21248/gups.73746
- URN
-
urn:nbn:de:hebis:30:3-737465
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
25.03.2025, 13:50 MEZ
Datenpartner
Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Amrhein, Jennifer Alisa
- Knapp, Stefan
- Proschak, Ewgenij
- Universitätsbibliothek Johann Christian Senckenberg
Entstanden
- 2023
Ähnliche Objekte (12)
Synthesis and investigation of novel p38 MAPK and DDR kinase inhibitors
![Escherichia coli 536: ein Modell zum Studium der Pathogenitätsmechanismen von harnwegsinfizierenden E[scherichia]-coli-Stämmen](/assets/placeholder/searchResultMediaNoDigitisedMedia.png)
Escherichia coli 536: ein Modell zum Studium der Pathogenitätsmechanismen von harnwegsinfizierenden E[scherichia]-coli-Stämmen
Synthesis and optimization of pyrazolo[1,5-α]pyrimidine-based macrocyclic kinase inhibitors
Chemical Proteomics Reveals the Target Landscape of Clinical Kinase Inhibitors.
Development of dual BET/HDAC inhibitors
Rational inhibitor development for epigenetic reader domains
Design, synthesis and evaluation of WD40-repeat containing protein 5 (WDR5) degraders
Large-scale analysis of kinase inhibitors' target binding kinetics : implications for drug discovery?
DFG-1 residue controls inhibitor binding mode and affinity, providing a basis for rational design of kinase inhibitor selectivity
DFG-1 residue controls inhibitor binding mode and affinity providing a basis for rational design of kinase inhibitor selectivity
5. Chemische Open-Access-Sonden für epigenetische Zielstrukturen
Structure and inhibitor binding characterization of oncogenic MLLT1 mutants
Synthesis and investigation of novel p38 MAPK and DDR kinase inhibitors
Escherichia coli 536: ein Modell zum Studium der Pathogenitätsmechanismen von harnwegsinfizierenden E[scherichia]-coli-Stämmen
Synthesis and optimization of pyrazolo[1,5-α]pyrimidine-based macrocyclic kinase inhibitors
Chemical Proteomics Reveals the Target Landscape of Clinical Kinase Inhibitors.
Development of dual BET/HDAC inhibitors
Rational inhibitor development for epigenetic reader domains
Design, synthesis and evaluation of WD40-repeat containing protein 5 (WDR5) degraders
Large-scale analysis of kinase inhibitors' target binding kinetics : implications for drug discovery?
DFG-1 residue controls inhibitor binding mode and affinity, providing a basis for rational design of kinase inhibitor selectivity
DFG-1 residue controls inhibitor binding mode and affinity providing a basis for rational design of kinase inhibitor selectivity
5. Chemische Open-Access-Sonden für epigenetische Zielstrukturen
Structure and inhibitor binding characterization of oncogenic MLLT1 mutants
Synthesis and investigation of novel p38 MAPK and DDR kinase inhibitors
Escherichia coli 536: ein Modell zum Studium der Pathogenitätsmechanismen von harnwegsinfizierenden E[scherichia]-coli-Stämmen
Synthesis and optimization of pyrazolo[1,5-α]pyrimidine-based macrocyclic kinase inhibitors
Chemical Proteomics Reveals the Target Landscape of Clinical Kinase Inhibitors.
Development of dual BET/HDAC inhibitors
Rational inhibitor development for epigenetic reader domains
Design, synthesis and evaluation of WD40-repeat containing protein 5 (WDR5) degraders
Large-scale analysis of kinase inhibitors' target binding kinetics : implications for drug discovery?
DFG-1 residue controls inhibitor binding mode and affinity, providing a basis for rational design of kinase inhibitor selectivity
DFG-1 residue controls inhibitor binding mode and affinity providing a basis for rational design of kinase inhibitor selectivity
5. Chemische Open-Access-Sonden für epigenetische Zielstrukturen