Reactome: A Curated Pathway Database
THIS SITE IS USED FOR CURATION AND TESTING
IT IS NOT STABLE, IS LINKED TO AN INCOMPLETE DATA SET, AND IS NOT MONITORED FOR PERFORMANCE. WE STRONGLY RECOMMEND THE USE OF OUR PUBLIC SITE

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.

Name Email address

Details on Person Reciprocal allosteric regulation of p38γ and PTPN3 involves a PDZ domain-modulated complex formation

Class:IdLiteratureReference:8867646
_displayNameReciprocal allosteric regulation of p38γ and PTPN3 involves a PDZ domain-modulated complex formation
_timestamp2016-04-15 14:54:16
author[Person:8867641] Chen, Kai-En
[Person:8867648] Lin, Shu-Yu
[Person:8867639] Wu, Mei-Ju
[Person:8867644] Ho, Meng-Ru
[Person:8867642] Santhanam, Abirami
[Person:8867647] Chou, Chia-Cheng
[Person:8867643] Meng, Tzu-Ching
[Person:8867640] Wang, Andrew H J
created[InstanceEdit:8867645] Rothfels, Karen, 2016-04-15
journalSci Signal
pagesra98
pubMedIdentifier25314968
titleReciprocal allosteric regulation of p38γ and PTPN3 involves a PDZ domain-modulated complex formation
volume7
year2014
(literatureReference)[Reaction:8867654] PTPN3 binds p-T183,Y185 MAPK12 [Homo sapiens]
[Reaction:8867658] PTPN3 dephosphorylates MAPK12 [Homo sapiens]
[Reaction:8868118] MAPK12 phosphorylates PTPN3 [Homo sapiens]
[Change default viewing format]
No pathways have been reviewed or authored by Reciprocal allosteric regulation of p38γ and PTPN3 involves a PDZ domain-modulated complex formation (8867646)