Reactome: A Curated Pathway Database

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.

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Pathways authored by Lill, R (199224)

DB_ID Name
2395516 Electron transport from NADPH to Ferredoxin
1362409 Mitochondrial iron-sulfur cluster biogenesis
2564818 Cytosolic iron-sulfur cluster assembly (yeast)
2564830 Cytosolic iron-sulfur cluster assembly

Details on Person Lill, R

Class:IdPerson:199224
_displayNameLill, R
_timestamp2017-08-22 20:38:47
created[InstanceEdit:199189] D'Eustachio, P, 2007-07-09 22:03:12
firstnameRoland
initialR
surnameLill
(author)[InstanceEdit:2473458] Lill, R, 2012-09-24
[InstanceEdit:2564829] Lill, Roland, 2012-11-07
[LiteratureReference:199196] The yeast mitochondrial carrier Leu5p and its human homologue Graves' disease protein are required for accumulation of coenzyme A in the matrix
[LiteratureReference:382534] Identification of a human mitochondrial ABC transporter, the functional orthologue of yeast Atm1p
[LiteratureReference:1252328] Apocytochrome c requires the TOM complex for translocation across the mitochondrial outer membrane
[LiteratureReference:2395466] Humans possess two mitochondrial ferredoxins, Fdx1 and Fdx2, with distinct roles in steroidogenesis, heme, and Fe/S cluster biosynthesis
[LiteratureReference:2399650] The role of mitochondria in cellular iron-sulfur protein biogenesis and iron metabolism
[LiteratureReference:2466288] Function and biogenesis of iron-sulphur proteins
[LiteratureReference:2466293] Iron-sulfur proteins in health and disease
[LiteratureReference:2466306] Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p
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