The lipopolysaccharide structure affects the detoxifying ability of intestinal alkaline phosphatases
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
1 Online-Ressource.
- Sprache
-
Englisch
- Erschienen in
-
The lipopolysaccharide structure affects the detoxifying ability of intestinal alkaline phosphatases ; volume:20 ; number:1 ; day:10 ; month:8 ; year:2024 ; pages:1-8 ; date:12.2024
BMC veterinary research ; 20, Heft 1 (10.8.2024), 1-8, 12.2024
- Urheber
-
Vermeire, Bjarne
Walsh, Maria
Cox, Eric
Devriendt, Bert
- Beteiligte Personen und Organisationen
-
SpringerLink (Online service)
- DOI
-
10.1186/s12917-024-04208-3
- URN
-
urn:nbn:de:101:1-2410292102500.466260208756
- Rechteinformation
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
15.08.2025, 07:20 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
- Vermeire, Bjarne
- Walsh, Maria
- Cox, Eric
- Devriendt, Bert
- SpringerLink (Online service)
Ähnliche Objekte (12)
Mammalian alkaline phosphatases : from biology to applications in medicine and biotechnology
Do metabolic HAD phosphatases moonlight as protein phosphatases?
Seasonal activity of non-specific acid and alkaline phosphatases in beech (Fagus sylvatica) leaves
Alkaline Phosphatases : Structure, substrate specificity and functional relatedness to other members of a large superfamily of enzymes
Voltage sensitive phosphatases: emerging kinship to protein tyrosine phosphatases from structure-function research
Aminoguanidine affects systemic and lung inflammation induced by lipopolysaccharide in rats
Protein phosphatases : with 15 tables
Protein phosphatases in TLR signaling
Protein phosphatases in TLR signaling
Protein tyrosine phosphatases in multiple myeloma
PP2C phosphatases—terminators of suicidal thoughts
Dual-Specificity Phosphatases and Kidney Diseases
Mammalian alkaline phosphatases : from biology to applications in medicine and biotechnology
Do metabolic HAD phosphatases moonlight as protein phosphatases?
Seasonal activity of non-specific acid and alkaline phosphatases in beech (Fagus sylvatica) leaves
Alkaline Phosphatases : Structure, substrate specificity and functional relatedness to other members of a large superfamily of enzymes
Voltage sensitive phosphatases: emerging kinship to protein tyrosine phosphatases from structure-function research
Aminoguanidine affects systemic and lung inflammation induced by lipopolysaccharide in rats
Protein phosphatases : with 15 tables
Protein phosphatases in TLR signaling
Protein phosphatases in TLR signaling
Protein tyrosine phosphatases in multiple myeloma
PP2C phosphatases—terminators of suicidal thoughts
Dual-Specificity Phosphatases and Kidney Diseases
Mammalian alkaline phosphatases : from biology to applications in medicine and biotechnology
Do metabolic HAD phosphatases moonlight as protein phosphatases?
Seasonal activity of non-specific acid and alkaline phosphatases in beech (Fagus sylvatica) leaves
Alkaline Phosphatases : Structure, substrate specificity and functional relatedness to other members of a large superfamily of enzymes
Voltage sensitive phosphatases: emerging kinship to protein tyrosine phosphatases from structure-function research
Aminoguanidine affects systemic and lung inflammation induced by lipopolysaccharide in rats
Protein phosphatases : with 15 tables
Protein phosphatases in TLR signaling
Protein phosphatases in TLR signaling
Protein tyrosine phosphatases in multiple myeloma
PP2C phosphatases—terminators of suicidal thoughts