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 reviewed by Meloche, Sylvain (5627529)

DB_ID Name
5687128 MAPK6/MAPK4 signaling

Details on Person Meloche, Sylvain

_displayNameMeloche, Sylvain
_timestamp2017-08-22 20:40:40
created[InstanceEdit:5627524] May, Bruce, 2014-10-19
(author)[LiteratureReference:5627528] A novel proteomics approach to identify SUMOylated proteins and their modification sites in human cells
[LiteratureReference:5683019] Atypical mitogen-activated protein kinases: structure, regulation and functions
[LiteratureReference:5686757] Activation loop phosphorylation of ERK3/ERK4 by group I p21-activated kinases (PAKs) defines a novel PAK-ERK3/4-MAPK-activated protein kinase 5 signaling pathway
[LiteratureReference:5686762] Activation loop phosphorylation of the atypical MAP kinases ERK3 and ERK4 is required for binding, activation and cytoplasmic relocalization of MK5
[LiteratureReference:5686768] Activation of MK5/PRAK by the atypical MAP kinase ERK3 defines a novel signal transduction pathway
[LiteratureReference:5686833] N-Terminal ubiquitination of extracellular signal-regulated kinase 3 and p21 directs their degradation by the proteasome
[LiteratureReference:5686836] Rapid turnover of extracellular signal-regulated kinase 3 by the ubiquitin-proteasome pathway defines a novel paradigm of mitogen-activated protein kinase regulation during cellular differentiation
[LiteratureReference:5686841] Regulation of MAPK-activated protein kinase 5 activity and subcellular localization by the atypical MAPK ERK4/MAPK4
[LiteratureReference:5692616] C-terminal domain phosphorylation of ERK3 controlled by Cdk1 and Cdc14 regulates its stability in mitosis
[LiteratureReference:5692641] Nuclear export of ERK3 by a CRM1-dependent mechanism regulates its inhibitory action on cell cycle progression
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