<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Jensen SM</submitter><funding>NIH HHS</funding><funding>NIGMS NIH HHS</funding><pagination>2216-2219</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5170875</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>17(23)</volume><pubmed_abstract>Chemical crosslinking is a versatile tool for the examination of biochemical interactions, in particular host-pathogen interactions. We report the critical first step toward the goal of probing these interactions by the synthesis and use of a new heterobifunctional crosslinker containing a triazabutadiene scaffold. The triazabutadiene is stable to protein conjugation and liberates a reactive aryl diazonium species upon irradiation with 350 nm light. We highlight the use of this technology by modifying the surface of several proteins, including the dengue virus envelope protein.</pubmed_abstract><journal>Chembiochem : a European journal of chemical biology</journal><pubmed_title>Light-Activated Triazabutadienes for the Modification of a Viral Surface.</pubmed_title><pmcid>PMC5170875</pmcid><funding_grant_id>T32 GM008804</funding_grant_id><funding_grant_id>S10 OD013237</funding_grant_id><pubmed_authors>Jewett JC</pubmed_authors><pubmed_authors>Kimani FW</pubmed_authors><pubmed_authors>Jensen SM</pubmed_authors></additional><is_claimable>false</is_claimable><name>Light-Activated Triazabutadienes for the Modification of a Viral Surface.</name><description>Chemical crosslinking is a versatile tool for the examination of biochemical interactions, in particular host-pathogen interactions. We report the critical first step toward the goal of probing these interactions by the synthesis and use of a new heterobifunctional crosslinker containing a triazabutadiene scaffold. The triazabutadiene is stable to protein conjugation and liberates a reactive aryl diazonium species upon irradiation with 350 nm light. We highlight the use of this technology by modifying the surface of several proteins, including the dengue virus envelope protein.</description><dates><release>2016-01-01T00:00:00Z</release><publication>2016 Dec</publication><modification>2026-04-16T17:20:09.292Z</modification><creation>2019-03-27T02:31:58Z</creation></dates><accession>S-EPMC5170875</accession><cross_references><pubmed>27647786</pubmed><doi>10.1002/cbic.201600508</doi></cross_references></HashMap>