<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Staudt DE</submitter><funding>Zebra Investments</funding><funding>NHMRC Targeted Research Grant</funding><funding>NHMRC Ideas Grant</funding><funding>Cancer Institute ECF</funding><funding>Cancer Institute NSW</funding><funding>National Health and Medical Research Council</funding><pagination>48</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9762002</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>19(1)</volume><pubmed_abstract>Global high-throughput phosphoproteomic profiling is increasingly being applied to cancer specimens to identify the oncogenic signaling cascades responsible for promoting disease initiation and disease progression; pathways that are often invisible to genomics analysis. Hence, phosphoproteomic profiling has enormous potential to inform and improve individualized anti-cancer treatment strategies. However, to achieve the adequate phosphoproteomic depth and coverage necessary to identify the activated, and hence, targetable kinases responsible for driving oncogenic signaling pathways, affinity phosphopeptide enrichment techniques are required and often coupled with offline high-pressure liquid chromatographic (HPLC) separation prior to nanoflow liquid chromatography-tandem mass spectrometry (</pubmed_abstract><journal>Clinical proteomics</journal><pubmed_title>Phospho-heavy-labeled-spiketide FAIMS stepped-CV DDA (pHASED) provides real-time phosphoproteomics data to aid in cancer drug selection.</pubmed_title><pmcid>PMC9762002</pmcid><funding_grant_id>GNT1173892</funding_grant_id><funding_grant_id>MDD00487</funding_grant_id><funding_grant_id>001</funding_grant_id><funding_grant_id>APP1188400</funding_grant_id><funding_grant_id>GA65801</funding_grant_id><pubmed_authors>Skerrett-Byrne DA</pubmed_authors><pubmed_authors>Mannan A</pubmed_authors><pubmed_authors>Findlay IJ</pubmed_authors><pubmed_authors>Murray HC</pubmed_authors><pubmed_authors>McLachlan T</pubmed_authors><pubmed_authors>Verrills NM</pubmed_authors><pubmed_authors>Staudt DE</pubmed_authors><pubmed_authors>Kearney PS</pubmed_authors><pubmed_authors>Kahl RGS</pubmed_authors><pubmed_authors>Dun MD</pubmed_authors><pubmed_authors>Duchatel RJ</pubmed_authors><pubmed_authors>Germon ZP</pubmed_authors><pubmed_authors>Jackson ER</pubmed_authors><pubmed_authors>Smith ND</pubmed_authors><pubmed_authors>Douglas AM</pubmed_authors><pubmed_authors>Jamaluddin MFB</pubmed_authors><pubmed_authors>Nixon B</pubmed_authors><pubmed_authors>McEwen HP</pubmed_authors></additional><is_claimable>false</is_claimable><name>Phospho-heavy-labeled-spiketide FAIMS stepped-CV DDA (pHASED) provides real-time phosphoproteomics data to aid in cancer drug selection.</name><description>Global high-throughput phosphoproteomic profiling is increasingly being applied to cancer specimens to identify the oncogenic signaling cascades responsible for promoting disease initiation and disease progression; pathways that are often invisible to genomics analysis. Hence, phosphoproteomic profiling has enormous potential to inform and improve individualized anti-cancer treatment strategies. However, to achieve the adequate phosphoproteomic depth and coverage necessary to identify the activated, and hence, targetable kinases responsible for driving oncogenic signaling pathways, affinity phosphopeptide enrichment techniques are required and often coupled with offline high-pressure liquid chromatographic (HPLC) separation prior to nanoflow liquid chromatography-tandem mass spectrometry (</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Dec</publication><modification>2025-04-04T08:45:04.01Z</modification><creation>2024-11-13T04:09:04.597Z</creation></dates><accession>S-EPMC9762002</accession><cross_references><pubmed>36536316</pubmed><doi>10.1186/s12014-022-09385-7</doi></cross_references></HashMap>