<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Ren W</submitter><funding>NCI NIH HHS</funding><pagination>410-3</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4689136</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>52(2)</volume><pubmed_abstract>We propose an ultrasensitive SERS-based peptide biosensor platform to monitor phosphorylation catalyzed by kinase in a dynamic format. The developed SERS strategy has a short response time with potential to monitor phosphorylation in live cells.</pubmed_abstract><journal>Chemical communications (Cambridge, England)</journal><pubmed_title>Kinase phosphorylation monitoring with i-motif DNA cross-linked SERS probes.</pubmed_title><pmcid>PMC4689136</pmcid><funding_grant_id>R21CA157395</funding_grant_id><funding_grant_id>R21 CA157395</funding_grant_id><pubmed_authors>Ren W</pubmed_authors><pubmed_authors>Damayanti NP</pubmed_authors><pubmed_authors>Wang X</pubmed_authors><pubmed_authors>Irudayaraj JM</pubmed_authors></additional><is_claimable>false</is_claimable><name>Kinase phosphorylation monitoring with i-motif DNA cross-linked SERS probes.</name><description>We propose an ultrasensitive SERS-based peptide biosensor platform to monitor phosphorylation catalyzed by kinase in a dynamic format. The developed SERS strategy has a short response time with potential to monitor phosphorylation in live cells.</description><dates><release>2016-01-01T00:00:00Z</release><publication>2016 Jan</publication><modification>2025-04-22T19:47:50.68Z</modification><creation>2019-03-27T02:05:41Z</creation></dates><accession>S-EPMC4689136</accession><cross_references><pubmed>26525744</pubmed><doi>10.1039/c5cc06566f</doi></cross_references></HashMap>