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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Name Email address

Pathways reviewed by Hannun, Yusuf A (194329)

DB_ID Name
428157 Sphingolipid metabolism

Details on Person Hannun, Yusuf A

_displayNameHannun, Yusuf A
_timestamp2017-08-22 20:38:37
affiliation[Affiliation:1237446] Medical University of South Carolina, Department of Biochemistry and Molecular Biology
created[InstanceEdit:194346] Jassal, B, 2007-03-13 16:41:41
crossReference[DatabaseIdentifier:5625815] ORCID:0000-0003-3349-3369
firstnameYusuf A
modified[InstanceEdit:428122] D'Eustachio, P, 2009-07-02
[InstanceEdit:1237444] D'Eustachio, P, 2011-03-30
[InstanceEdit:5625812] Matthews, Lisa, 2014-10-07
[InstanceEdit:8932050] D'Eustachio, Peter, 2016-07-20
(author)[InstanceEdit:446905] Hannun, YA, Luberto, C, 2009-11-18
[LiteratureReference:194334] Neurotrophins induce sphingomyelin hydrolysis. Modulation by co-expression of p75NTR with Trk receptors.
[LiteratureReference:194361] Activation of the sphingomyelin cycle through the low-affinity neurotrophin receptor
[LiteratureReference:428160] Principles of bioactive lipid signalling: lessons from sphingolipids
[LiteratureReference:1606270] Biochemical properties of mammalian neutral sphingomyelinase 2 and its role in sphingolipid metabolism
[LiteratureReference:1660665] An overview of sphingolipid metabolism: from synthesis to breakdown
[LiteratureReference:1861786] Identification of a novel amidase motif in neutral ceramidase
[LiteratureReference:5626979] The Polycomb group protein EED couples TNF receptor 1 to neutral sphingomyelinase
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