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 Uptake of the antifungal cationic peptide Histatin 5 by Candida albicans Ssa2p requires binding to non-conventional sites within the ATPase domain

Class:IdLiteratureReference:8861713
_displayNameUptake of the antifungal cationic peptide Histatin 5 by Candida albicans Ssa2p requires binding to non-conventional sites within the ATPase domain
_timestamp2016-02-20 01:02:35
author[Person:8861725] Sun, Jianing N
[Person:8861677] Li, Wansheng
[Person:8861736] Jang, Woong Sik
[Person:8861635] Nayyar, Namrata
[Person:8861698] Sutton, Mark D
[Person:8861697] Edgerton, Mira
created[InstanceEdit:8861701] Shamovsky, Veronica, 2016-02-20
journalMol. Microbiol.
pages1246-60
pubMedIdentifier19006817
titleUptake of the antifungal cationic peptide Histatin 5 by Candida albicans Ssa2p requires binding to non-conventional sites within the ATPase domain
volume70
year2008
(literatureReference)[Summation:8861674] Histatins (HTNs) is a family of small, histidine-rich (18-28...
[Change default viewing format]
No pathways have been reviewed or authored by Uptake of the antifungal cationic peptide Histatin 5 by Candida albicans Ssa2p requires binding to non-conventional sites within the ATPase domain (8861713)