Exploring Pathogenic Mutations at Phosphorylation Sites through a Peptide-Based Proteomics Screen
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Anmerkungen
-
Berlin, Humboldt-Universität zu Berlin, Dissertation, 2024
- Schlagwort
-
Proteomanalyse
Proteine
Phosphorylierung
Protein-Protein-Wechselwirkung
Wechselwirkung
- Ereignis
-
Veröffentlichung
- (wo)
-
Berlin
- (wer)
-
Humboldt-Universität zu Berlin
- (wann)
-
2024
- Urheber
- Beteiligte Personen und Organisationen
-
Selbach, Matthias
Blüthgen, Nils
Ivarsson, Ylva
- DOI
-
10.18452/28699
- URN
-
urn:nbn:de:kobv:11-110-18452/30100-0
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
25.03.2025, 13:54 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
- Rrustemi, Trëndelina
- Selbach, Matthias
- Blüthgen, Nils
- Ivarsson, Ylva
- Humboldt-Universität zu Berlin
Entstanden
- 2024
Ähnliche Objekte (12)
Phenotypic characterization of pathogenic mutations in GPIBDs
Development of Proteomics Methods to Investigate Protein Phosphorylation and Pyrophosphorylation
A peptide-based interaction screen on disease-related mutations
Gene therapeutic approaches and characterization of pathogenic mutations in liver-associated genes
Pathogenic mutations in catalytic subunit isoforms of the cAMP-dependent protein kinase
CaV1.3 gating modulation by S1475 phosphorylation and disease-associated CACNA1D missense mutations
Characterization of genetically modified mice carrying pathogenic mutations in the Notch2 or Wnt1 gene
Pathogenic bi-allelic mutations in NDUFAF8 cause Leigh syndrome with an isolated complex I deficiency
Pathogenic yeasts
Establishment of quantitative proteomics in cyanobacteria reveals O-phosphorylation as fundamental process for stress-acclimation to nitrogen deficiency
Computational proteomics
Microbial proteomics
Phenotypic characterization of pathogenic mutations in GPIBDs
Development of Proteomics Methods to Investigate Protein Phosphorylation and Pyrophosphorylation
A peptide-based interaction screen on disease-related mutations
Gene therapeutic approaches and characterization of pathogenic mutations in liver-associated genes
Pathogenic mutations in catalytic subunit isoforms of the cAMP-dependent protein kinase
CaV1.3 gating modulation by S1475 phosphorylation and disease-associated CACNA1D missense mutations
Characterization of genetically modified mice carrying pathogenic mutations in the Notch2 or Wnt1 gene
Pathogenic bi-allelic mutations in NDUFAF8 cause Leigh syndrome with an isolated complex I deficiency
Pathogenic yeasts
Establishment of quantitative proteomics in cyanobacteria reveals O-phosphorylation as fundamental process for stress-acclimation to nitrogen deficiency
Computational proteomics
Microbial proteomics
Phenotypic characterization of pathogenic mutations in GPIBDs
Development of Proteomics Methods to Investigate Protein Phosphorylation and Pyrophosphorylation
A peptide-based interaction screen on disease-related mutations
Gene therapeutic approaches and characterization of pathogenic mutations in liver-associated genes
Pathogenic mutations in catalytic subunit isoforms of the cAMP-dependent protein kinase
CaV1.3 gating modulation by S1475 phosphorylation and disease-associated CACNA1D missense mutations
Characterization of genetically modified mice carrying pathogenic mutations in the Notch2 or Wnt1 gene
Pathogenic bi-allelic mutations in NDUFAF8 cause Leigh syndrome with an isolated complex I deficiency
Pathogenic yeasts
Establishment of quantitative proteomics in cyanobacteria reveals O-phosphorylation as fundamental process for stress-acclimation to nitrogen deficiency
Computational proteomics