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.

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

Pathways reviewed by Wu, C (203543)

DB_ID Name
446343 Localization of the PINCH-ILK-PARVIN complex to focal adhesions
446353 Cell-extracellular matrix interactions
446388 Regulation of cytoskeletal remodeling and cell spreading by IPP complex components

Details on Person Wu, C

Class:IdPerson:203543
_displayNameWu, C
_timestamp2017-08-22 20:38:55
created[InstanceEdit:203590] Hemish, J, 2007-11-15 17:00:52
initialC
surnameWu
(author)[InstanceEdit:446332] Wu, C, 2009-11-12
[LiteratureReference:203605] Interaction between caveolin-1 and the reductase domain of endothelial nitric-oxide synthase. Consequences for catalysis.
[LiteratureReference:208049] Differential phosphorylation of the signal-responsive domain of I kappa B alpha and I kappa B beta by I kappa B kinases
[LiteratureReference:215787] Identification of a new biological function for the integrin alpha v beta 3: initiation of fibronectin matrix assembly
[LiteratureReference:430277] Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation
[LiteratureReference:432844] Assembly of the PINCH-ILK-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites
[LiteratureReference:446321] Migfilin interacts with vasodilator-stimulated phosphoprotein (VASP) and regulates VASP localization to cell-matrix adhesions and migration
[LiteratureReference:446336] The structure of alpha-parvin CH2-paxillin LD1 complex reveals a novel modular recognition for focal adhesion assembly
[LiteratureReference:446338] The parvins
[LiteratureReference:446358] A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading
List all 16 refering instances
[Change default viewing format]