Query author contributions in Reactome

Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.

If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.

Details on Person Formation of reactive oxygen species by human and bacterial pyruvate and 2-oxoglutarate dehydrogenase multienzyme complexes reconstituted from recombinant components

Class:Id	LiteratureReference:9853977
_displayName	Formation of reactive oxygen species by human and bacterial pyruvate and 2-oxoglutarate dehydrogenase multienzyme complexes reconstituted from recombinant components
_timestamp	2023-11-22 09:17:58
author	[Person:9853681] Ambrus, Attila [Person:9853667] Nemeria, Natalia S [Person:9853971] Torocsik, Beata [Person:9853669] Tretter, Laszlo [Person:9853983] Nilsson, Mattias [Person:9853690] Jordan, Frank [Person:9853660] Adam-Vizi, Vera
created	[InstanceEdit:9853986] Stephan, Ralf, 2023-11-22
journal	Free Radic Biol Med
pages	642-50
pubMedIdentifier	26456061
title	Formation of reactive oxygen species by human and bacterial pyruvate and 2-oxoglutarate dehydrogenase multienzyme complexes reconstituted from recombinant components
volume	89
year	2015
(literatureReference)	[Reaction:9853499] DLD dimer dehydrogenates dihydrolipoyl [Homo sapiens] [Reaction:9858589] DLD dimer dehydrogenates dihydrolipoyl [Homo sapiens] [Reaction:9859172] DLD dimer dehydrogenates dihydrolipoyl [Homo sapiens] [Reaction:9861616] DLD dimer dehydrogenates dihydrolipoyl [Homo sapiens]
[Change default viewing format]

No pathways have been reviewed or authored by Formation of reactive oxygen species by human and bacterial pyruvate and 2-oxoglutarate dehydrogenase multienzyme complexes reconstituted from recombinant components (9853977)