Identification and functional characterization of carbohydrate-recognition structures in proteins using combinations of proteolysis and affinity- mass spectrometry
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Anmerkungen
-
Konstanz, Universität Konstanz, Dissertation, 2018
- Schlagwort
-
Identification
Mass spectrometry
Proteins
Proteolysis
Combinations
- Ereignis
-
Veröffentlichung
- (wo)
-
Konstanz
- (wer)
-
KOPS Universität Konstanz
- (wann)
-
2018
- Urheber
-
Eggers, Frederike
- URN
-
urn:nbn:de:bsz:352-2-11uvq243dk9np2
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
14.08.2025, 11:00 MESZ
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
- Eggers, Frederike
- KOPS Universität Konstanz
Entstanden
- 2018
Ähnliche Objekte (12)
Development and application of affinity-mass spectrometry to identify protein-carbohydrate interactions
Identification and quantification of carbohydrate interacting structures in proteins using affinity-mass spectrometry
Focus on affinity mass spectrometry
Design of a high-affinity carbohydrate binding protein
Affinity maturation generates greatly improved xyloglucan-specific carbohydrate binding modules
Chemistry of proteolysis
Detection of protein complexes from affinity purification/mass spectrometry data
Predicting direct protein interactions from affinity purification mass spectrometry data
Identification of intracellular glycosaminoglycan-interacting proteins by affinity purification mass spectrometry
Chromatin affinity purification coupled with mass spectrometry indetifies novel histone ubiquitylation interactors
Compartment specific proteolysis in mitochondria
Proteomic analysis of cellular proteolysis
Development and application of affinity-mass spectrometry to identify protein-carbohydrate interactions
Identification and quantification of carbohydrate interacting structures in proteins using affinity-mass spectrometry
Focus on affinity mass spectrometry
Design of a high-affinity carbohydrate binding protein
Affinity maturation generates greatly improved xyloglucan-specific carbohydrate binding modules
Chemistry of proteolysis
Detection of protein complexes from affinity purification/mass spectrometry data
Predicting direct protein interactions from affinity purification mass spectrometry data
Identification of intracellular glycosaminoglycan-interacting proteins by affinity purification mass spectrometry
Chromatin affinity purification coupled with mass spectrometry indetifies novel histone ubiquitylation interactors
Compartment specific proteolysis in mitochondria
Proteomic analysis of cellular proteolysis
Development and application of affinity-mass spectrometry to identify protein-carbohydrate interactions
Identification and quantification of carbohydrate interacting structures in proteins using affinity-mass spectrometry
Focus on affinity mass spectrometry
Design of a high-affinity carbohydrate binding protein
Affinity maturation generates greatly improved xyloglucan-specific carbohydrate binding modules
Chemistry of proteolysis
Detection of protein complexes from affinity purification/mass spectrometry data
Predicting direct protein interactions from affinity purification mass spectrometry data
Identification of intracellular glycosaminoglycan-interacting proteins by affinity purification mass spectrometry
Chromatin affinity purification coupled with mass spectrometry indetifies novel histone ubiquitylation interactors
Compartment specific proteolysis in mitochondria