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 A ubiquitin-like system mediates protein lipidation
| Class:Id | LiteratureReference:5681995 |
| _displayName | A ubiquitin-like system mediates protein lipidation |
| _timestamp | 2015-03-04 13:28:40 |
| author | [Person:5671845] Ichimura, Y [Person:5671833] Kirisako, T [Person:2514897] Takao, T [Person:5682002] Satomi, Y [Person:2514873] Shimonishi, Y [Person:5682004] Ishihara, N [Person:5671837] Mizushima, N [Person:5682009] Tanida, I [Person:5681984] Kominami, E [Person:5671828] Ohsumi, M [Person:5671580] Noda, T [Person:5671568] Ohsumi, Y |
| created | [InstanceEdit:5681983] Jupe, Steve, 2015-03-04 |
| journal | Nature |
| modified | [InstanceEdit:5682015] Jupe, Steve, 2015-03-04 |
| pages | 488-92 |
| pubMedIdentifier | 11100732 |
| title | A ubiquitin-like system mediates protein lipidation |
| volume | 408 |
| year | 2000 |
| (literatureReference) | [Summation:5678489] The ATG16L1 complex (consisting of ATG12, ATG5 and ATG16L1) ... [Summation:5681979] The activated LC3 protein is transferred to Cys-263 of ATG3 ... [Summation:5682006] The exposed LC3 protein C-terminal glycine forms a thioester... [Summation:5682901] The ATG7 dimer with bound LC3 binds ATG3. Deletion mutagenes... |
|
[Change default viewing format]
|
No pathways have been reviewed or authored by A ubiquitin-like system mediates protein lipidation (5681995)