Implications of differential peroxyl radical-induced inactivation of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase for the pentose phosphate pathway
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
2045-2322
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Anmerkungen
-
online resource.
- Erschienen in
-
Implications of differential peroxyl radical-induced inactivation of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase for the pentose phosphate pathway ; volume:12 ; number:1 ; day:7 ; month:12 ; year:2022 ; pages:1-19 ; date:12.2022
Scientific reports ; 12, Heft 1 (7.12.2022), 1-19, 12.2022
- Urheber
-
Reyes, Juan Sebastián
Fuentes-Lemus, Eduardo
Figueroa, Juan David
Rojas, Javier
Fierro, Angélica
Arenas, Felipe
Hägglund, Per M.
Davies, Michael J.
López-Alarcón, Camilo
- Beteiligte Personen und Organisationen
-
SpringerLink (Online service)
- DOI
-
10.1038/s41598-022-25474-x
- URN
-
urn:nbn:de:101:1-2023021721113123206282
- Rechteinformation
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
14.08.2025, 10:51 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
- Reyes, Juan Sebastián
- Fuentes-Lemus, Eduardo
- Figueroa, Juan David
- Rojas, Javier
- Fierro, Angélica
- Arenas, Felipe
- Hägglund, Per M.
- Davies, Michael J.
- López-Alarcón, Camilo
- SpringerLink (Online service)
Ähnliche Objekte (12)
A new inhibitor of glucose-6-phosphate dehydrogenase blocks pentose phosphate pathway and suppresses malignant proliferation and metastasis in vivo
Glyceraldehyde-3-phosphate dehydrogenase, GAP DH 2
Glyceraldehyde-3-phosphate dehydrogenase, GAP DH 1
Enhanced Eryptosis in Glucose-6-Phosphate Dehydrogenase Deficiency
![In vitro and in vivo regulation of glyceraldehyde-3-phosphate dehydrogenase isozymes [glyceraldehyde-phosphate-dehydrogenase-isozymes] from chenopodium rubrum L.](/assets/placeholder/searchResultMediaNoDigitisedMedia.png)
In vitro and in vivo regulation of glyceraldehyde-3-phosphate dehydrogenase isozymes [glyceraldehyde-phosphate-dehydrogenase-isozymes] from chenopodium rubrum L.
Testis-specific glyceraldehyde-3-phosphate dehydrogenase: origin and evolution
Mitochondrial glycerol 3‐phosphate dehydrogenase promotes skeletal muscle regeneration
Genetic determinants of glucose-6-phosphate dehydrogenase activity in Kenya
Glucose-6-phosphate dehydrogenase deficiency accelerates arterial aging in diabetes
Glyceraldehyde-3-phosphate dehydrogenase is overexpressed in colorectal cancer onset
Regulation of the pentose phosphate pathway in cancer
Co-production of hydrogen and ethanol from glucose in Escherichia coli by activation of pentose-phosphate pathway through deletion of phosphoglucose isomerase (pgi) and overexpression of glucose-6-phosphate dehydrogenase (zwf) and 6-phosphogluconate dehydrogenase (gnd)
A new inhibitor of glucose-6-phosphate dehydrogenase blocks pentose phosphate pathway and suppresses malignant proliferation and metastasis in vivo
Glyceraldehyde-3-phosphate dehydrogenase, GAP DH 2
Glyceraldehyde-3-phosphate dehydrogenase, GAP DH 1
Enhanced Eryptosis in Glucose-6-Phosphate Dehydrogenase Deficiency
In vitro and in vivo regulation of glyceraldehyde-3-phosphate dehydrogenase isozymes [glyceraldehyde-phosphate-dehydrogenase-isozymes] from chenopodium rubrum L.
Testis-specific glyceraldehyde-3-phosphate dehydrogenase: origin and evolution
Mitochondrial glycerol 3‐phosphate dehydrogenase promotes skeletal muscle regeneration
Genetic determinants of glucose-6-phosphate dehydrogenase activity in Kenya
Glucose-6-phosphate dehydrogenase deficiency accelerates arterial aging in diabetes
Glyceraldehyde-3-phosphate dehydrogenase is overexpressed in colorectal cancer onset
Regulation of the pentose phosphate pathway in cancer
Co-production of hydrogen and ethanol from glucose in Escherichia coli by activation of pentose-phosphate pathway through deletion of phosphoglucose isomerase (pgi) and overexpression of glucose-6-phosphate dehydrogenase (zwf) and 6-phosphogluconate dehydrogenase (gnd)
A new inhibitor of glucose-6-phosphate dehydrogenase blocks pentose phosphate pathway and suppresses malignant proliferation and metastasis in vivo
Glyceraldehyde-3-phosphate dehydrogenase, GAP DH 2
Glyceraldehyde-3-phosphate dehydrogenase, GAP DH 1
Enhanced Eryptosis in Glucose-6-Phosphate Dehydrogenase Deficiency
In vitro and in vivo regulation of glyceraldehyde-3-phosphate dehydrogenase isozymes [glyceraldehyde-phosphate-dehydrogenase-isozymes] from chenopodium rubrum L.
Testis-specific glyceraldehyde-3-phosphate dehydrogenase: origin and evolution
Mitochondrial glycerol 3‐phosphate dehydrogenase promotes skeletal muscle regeneration
Genetic determinants of glucose-6-phosphate dehydrogenase activity in Kenya
Glucose-6-phosphate dehydrogenase deficiency accelerates arterial aging in diabetes
Glyceraldehyde-3-phosphate dehydrogenase is overexpressed in colorectal cancer onset
Regulation of the pentose phosphate pathway in cancer