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.
Pathways reviewed by Rouault, Tracey A (2395478)
Details on Person Rouault, Tracey A
| Class:Id | Person:2395478 |
|---|
| _displayName | Rouault, Tracey A |
|---|
| _timestamp | 2012-07-02 00:39:41 |
|---|
| created | [InstanceEdit:2395456] May, B, 2012-07-02 |
|---|
| firstname | Tracey A |
|---|
| initial | TA |
|---|
| surname | Rouault |
|---|
| (author) | [InstanceEdit:2520930] Rouault, Tracey A, 2012-10-11
[LiteratureReference:1362323] Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells
[LiteratureReference:1362362] Human ISD11 is essential for both iron-sulfur cluster assembly and maintenance of normal cellular iron homeostasis
[LiteratureReference:1481603] Human iron-sulfur cluster assembly, cellular iron homeostasis, and disease
[LiteratureReference:2395461] Both human ferredoxins 1 and 2 and ferredoxin reductase are important for iron-sulfur cluster biogenesis
[LiteratureReference:2520943] Subcellular compartmentalization of human Nfu, an iron-sulfur cluster scaffold protein, and its ability to assemble a [4Fe-4S] cluster
[LiteratureReference:2520956] Biogenesis of iron-sulfur clusters in mammalian cells: new insights and relevance to human disease
[LiteratureReference:2520962] Mutations in iron-sulfur cluster scaffold genes NFU1 and BOLA3 cause a fatal deficiency of multiple respiratory chain and 2-oxoacid dehydrogenase enzymes
[LiteratureReference:5690879] The bifunctional iron-responsive element binding protein/cytosolic aconitase: the role of active-site residues in ligand binding and regulation
[LiteratureReference:5690888] Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2. Structure, function, and post-translational regulation |
|---|
|
[Change default viewing format]
|
