- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
2041-1723
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
online resource.
- Bibliographic citation
-
Identification of human D lactate dehydrogenase deficiency ; volume:10 ; number:1 ; day:1 ; month:4 ; year:2019 ; pages:1-8 ; date:12.2019
Nature Communications ; 10, Heft 1 (1.4.2019), 1-8, 12.2019
- Classification
-
Naturwissenschaften
- Creator
-
Monroe, Glen R.
van Eerde, Albertien M.
Tessadori, Federico
Duran, Karen J.
Savelberg, Sanne M. C.
van Alfen, Johanna C.
Terhal, Paulien A.
van der Crabben, Saskia N.
Lichtenbelt, Klaske D.
Fuchs, Sabine A.
Gerrits, Johan
van Roosmalen, Markus J.
van Gassen, Koen L.
van Aalderen, Mirjam
Koot, Bart G.
Oostendorp, Marlies
Duran, Marinus
Visser, Gepke
de Koning, Tom J.
Calì, Francesco
Bosco, Paolo
Geleijns, Karin
de Sain-van der Velden, Monique G. M.
Knoers, Nine V.
Bakkers, Jeroen
Verhoeven-Duif, Nanda M.
van Haaften, Gijs
Jans, Judith J.
- Contributor
-
SpringerLink (Online service)
- DOI
-
10.1038/s41467-019-09458-6
- URN
-
urn:nbn:de:101:1-2019041722581532733216
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2025, 10:53 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
- Monroe, Glen R.
- van Eerde, Albertien M.
- Tessadori, Federico
- Duran, Karen J.
- Savelberg, Sanne M. C.
- van Alfen, Johanna C.
- Terhal, Paulien A.
- van der Crabben, Saskia N.
- Lichtenbelt, Klaske D.
- Fuchs, Sabine A.
- Gerrits, Johan
- van Roosmalen, Markus J.
- van Gassen, Koen L.
- van Aalderen, Mirjam
- Koot, Bart G.
- Oostendorp, Marlies
- Duran, Marinus
- Visser, Gepke
- de Koning, Tom J.
- Calì, Francesco
- Bosco, Paolo
- Geleijns, Karin
- de Sain-van der Velden, Monique G. M.
- Knoers, Nine V.
- Bakkers, Jeroen
- Verhoeven-Duif, Nanda M.
- van Haaften, Gijs
- Jans, Judith J.
- SpringerLink (Online service)
Other Objects (12)
True Arrhenius Relationships of Human Lactate Dehydrogenase
Identification of isobutyryl-CoA dehydrogenase and its deficiency in humans
Serumenzymbestimmungen zur Diagnostik von Herzerkrankungen bei Hund und Pferd : Transaminasen, Lactat-Dehydrogenase, Lactat-Dehydrogenase-1-Isoenzym, Sorbit-Dehydrogenase und Creatinphosphokinase.
A Further Study of Seminal Plasma: Lactate Dehydrogenase and Lactate Dehydrogenase-X Activities and Diluted Semen Absorbance
Lactat-Dehydrogenase, Glycerophosphat-Dehydrogenase, Glyceraldehydphosphat-Dehydrogenase, Fructose-Aldolase und Malat-Dehydrogenase in gesundem, regenerierendem und neoplastischem Gewebe
Kinetic characterization of lactate dehydrogenase in normal and malignant human breast tissues
The Isoenzymes of Lactate Dehydrogenase in the Nephton of the Healthy Human Kidney
Carbon nanodots interference with lactate dehydrogenase assay in human monocyte THP-1 cells
Overexpression of lactate dehydrogenase-A in human intrahepatic cholangiocarcinoma: its implication for treatment
Lactate dehydrogenase A (LDHA)-mediated lactate generation promotes pulmonary vascular remodeling in pulmonary hypertension
Protein cysteine S-nitrosylation provides reducing power by enhancing lactate dehydrogenase activity in Trichomonas vaginalis under iron deficiency
Lactat-Dehydrogenase und unspezifische Esterase in Lymphozyten der Maus
True Arrhenius Relationships of Human Lactate Dehydrogenase
Identification of isobutyryl-CoA dehydrogenase and its deficiency in humans
Serumenzymbestimmungen zur Diagnostik von Herzerkrankungen bei Hund und Pferd : Transaminasen, Lactat-Dehydrogenase, Lactat-Dehydrogenase-1-Isoenzym, Sorbit-Dehydrogenase und Creatinphosphokinase.
A Further Study of Seminal Plasma: Lactate Dehydrogenase and Lactate Dehydrogenase-X Activities and Diluted Semen Absorbance
Lactat-Dehydrogenase, Glycerophosphat-Dehydrogenase, Glyceraldehydphosphat-Dehydrogenase, Fructose-Aldolase und Malat-Dehydrogenase in gesundem, regenerierendem und neoplastischem Gewebe
Kinetic characterization of lactate dehydrogenase in normal and malignant human breast tissues
The Isoenzymes of Lactate Dehydrogenase in the Nephton of the Healthy Human Kidney
Carbon nanodots interference with lactate dehydrogenase assay in human monocyte THP-1 cells
Overexpression of lactate dehydrogenase-A in human intrahepatic cholangiocarcinoma: its implication for treatment
Lactate dehydrogenase A (LDHA)-mediated lactate generation promotes pulmonary vascular remodeling in pulmonary hypertension
Protein cysteine S-nitrosylation provides reducing power by enhancing lactate dehydrogenase activity in Trichomonas vaginalis under iron deficiency
Lactat-Dehydrogenase und unspezifische Esterase in Lymphozyten der Maus
True Arrhenius Relationships of Human Lactate Dehydrogenase
Identification of isobutyryl-CoA dehydrogenase and its deficiency in humans
Serumenzymbestimmungen zur Diagnostik von Herzerkrankungen bei Hund und Pferd : Transaminasen, Lactat-Dehydrogenase, Lactat-Dehydrogenase-1-Isoenzym, Sorbit-Dehydrogenase und Creatinphosphokinase.
A Further Study of Seminal Plasma: Lactate Dehydrogenase and Lactate Dehydrogenase-X Activities and Diluted Semen Absorbance
Lactat-Dehydrogenase, Glycerophosphat-Dehydrogenase, Glyceraldehydphosphat-Dehydrogenase, Fructose-Aldolase und Malat-Dehydrogenase in gesundem, regenerierendem und neoplastischem Gewebe
Kinetic characterization of lactate dehydrogenase in normal and malignant human breast tissues
The Isoenzymes of Lactate Dehydrogenase in the Nephton of the Healthy Human Kidney
Carbon nanodots interference with lactate dehydrogenase assay in human monocyte THP-1 cells
Overexpression of lactate dehydrogenase-A in human intrahepatic cholangiocarcinoma: its implication for treatment
Lactate dehydrogenase A (LDHA)-mediated lactate generation promotes pulmonary vascular remodeling in pulmonary hypertension
Protein cysteine S-nitrosylation provides reducing power by enhancing lactate dehydrogenase activity in Trichomonas vaginalis under iron deficiency