- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
In: Biochemical and Biophysical Research Communications ; 137 (1986), 3. - S. 1049-1054. - ISSN 0006-291X
- Classification
-
Biowissenschaften, Biologie
- Event
-
Veröffentlichung
- (where)
-
Konstanz
- (who)
-
Bibliothek der Universität Konstanz
- (when)
-
2008
- Creator
-
Inagaki, Taisuke
Tsukagoshi, Norihiro
Ichihara, Chikako
Ohishi, Nobuko
Udaka, Shigezo
Ghisla, Sandro
Yagi, Kunio
- URN
-
urn:nbn:de:bsz:352-opus-56650
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2025, 11:02 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.
Associated
- Inagaki, Taisuke
- Tsukagoshi, Norihiro
- Ichihara, Chikako
- Ohishi, Nobuko
- Udaka, Shigezo
- Ghisla, Sandro
- Yagi, Kunio
- Bibliothek der Universität Konstanz
Time of origin
- 2008
Other Objects (12)
![Medium-chain acyl CoA dehydrogenase : evidence for phosphorylation [[Elektronische Ressource]]](/assets/placeholder/searchResultMediaUnknown.png)
Medium-chain acyl CoA dehydrogenase : evidence for phosphorylation [[Elektronische Ressource]]
Inactivation of General Acyl-CoA Dehydrogenase from Pig Kidney by a Metabolite of Hypoglycin A*
Inactivation of medium-chain acyl-CoA dehydrogenase from pig kidney by methylenecyclopropyl-acetyl-CoA : identification of a new flavin-inhibitor adduct
Immunochemical and molecular analysis of medium-chain acyl CoA dehydrogenase deficiency
Mechanism of alpha, beta-dehydrogenation of Fatty Acid CoA Derivatives by Flavin Enzymes
On the Inactivation of General Acyl-CoA-Dehydrogenase from Pig Kidney by Methylenecyclopropyl-Acetyl-CoA, a Metabolite of Hypoglycin : Studies with flavin modified enzymes
Inactivation of general acyl-CoA dehydrogenase from pig kidney by the suicide substrate methylenecyclopropylacetyl-CoA : structure of one of the covalent flavin-inhibitor adducts
Studies with general acyl-CoA dehydrogenase from pig kidney : inactivation by a novel type of "suicide" inhibitor, 3,4-pentadienoyl-CoA
Medium-chain acyl coenzyme A dehydrogenase from pig kidney has intrinsic enoyl coenzyme A hydratase activity
Reaction of General Acyl-CoA Dehydrogenase with 3,4-Pentadienoyl-CoA
Molecular cloning of cDNA for rat liver general acyl CoA dehydrogenase and homology between the rat liver and pig kidney enzymes
Molecular evolution and substrate specificity of acyl-CoA dehydrogenases : chimaeric 'medium/long' chain-specific enzyme from medium-chain acyl-CoA dehydrogenase
Medium-chain acyl CoA dehydrogenase : evidence for phosphorylation [[Elektronische Ressource]]
Inactivation of General Acyl-CoA Dehydrogenase from Pig Kidney by a Metabolite of Hypoglycin A*
Inactivation of medium-chain acyl-CoA dehydrogenase from pig kidney by methylenecyclopropyl-acetyl-CoA : identification of a new flavin-inhibitor adduct
Immunochemical and molecular analysis of medium-chain acyl CoA dehydrogenase deficiency
Mechanism of alpha, beta-dehydrogenation of Fatty Acid CoA Derivatives by Flavin Enzymes
On the Inactivation of General Acyl-CoA-Dehydrogenase from Pig Kidney by Methylenecyclopropyl-Acetyl-CoA, a Metabolite of Hypoglycin : Studies with flavin modified enzymes
Inactivation of general acyl-CoA dehydrogenase from pig kidney by the suicide substrate methylenecyclopropylacetyl-CoA : structure of one of the covalent flavin-inhibitor adducts
Studies with general acyl-CoA dehydrogenase from pig kidney : inactivation by a novel type of "suicide" inhibitor, 3,4-pentadienoyl-CoA
Medium-chain acyl coenzyme A dehydrogenase from pig kidney has intrinsic enoyl coenzyme A hydratase activity
Reaction of General Acyl-CoA Dehydrogenase with 3,4-Pentadienoyl-CoA
Molecular cloning of cDNA for rat liver general acyl CoA dehydrogenase and homology between the rat liver and pig kidney enzymes
Molecular evolution and substrate specificity of acyl-CoA dehydrogenases : chimaeric 'medium/long' chain-specific enzyme from medium-chain acyl-CoA dehydrogenase
Medium-chain acyl CoA dehydrogenase : evidence for phosphorylation [[Elektronische Ressource]]
Inactivation of General Acyl-CoA Dehydrogenase from Pig Kidney by a Metabolite of Hypoglycin A*
Inactivation of medium-chain acyl-CoA dehydrogenase from pig kidney by methylenecyclopropyl-acetyl-CoA : identification of a new flavin-inhibitor adduct
Immunochemical and molecular analysis of medium-chain acyl CoA dehydrogenase deficiency
Mechanism of alpha, beta-dehydrogenation of Fatty Acid CoA Derivatives by Flavin Enzymes
On the Inactivation of General Acyl-CoA-Dehydrogenase from Pig Kidney by Methylenecyclopropyl-Acetyl-CoA, a Metabolite of Hypoglycin : Studies with flavin modified enzymes
Inactivation of general acyl-CoA dehydrogenase from pig kidney by the suicide substrate methylenecyclopropylacetyl-CoA : structure of one of the covalent flavin-inhibitor adducts
Studies with general acyl-CoA dehydrogenase from pig kidney : inactivation by a novel type of "suicide" inhibitor, 3,4-pentadienoyl-CoA
Medium-chain acyl coenzyme A dehydrogenase from pig kidney has intrinsic enoyl coenzyme A hydratase activity
Reaction of General Acyl-CoA Dehydrogenase with 3,4-Pentadienoyl-CoA
Molecular cloning of cDNA for rat liver general acyl CoA dehydrogenase and homology between the rat liver and pig kidney enzymes