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 Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization

Class:IdLiteratureReference:1471334
_displayNameCrystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization
_timestamp2011-08-03 09:36:34
author[Person:190131] Hill, CP
[Person:1471340] Yee, J
[Person:1461968] Selsted, ME
[Person:977123] Eisenberg, D
created[InstanceEdit:1471368] Jupe, S, 2011-08-03
journalScience
pages1481-5
pubMedIdentifier2006422
titleCrystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization
volume251
year1991
(literatureReference)[Reaction:1462014] Alpha-defensins form biologically active dimers [Homo sapiens]
[Summation:1471353] The crystal structure of human alpha-defensin HNP-3 revealed...
[Change default viewing format]
No pathways have been reviewed or authored by Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization (1471334)