<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Ying YL</submitter><funding>National Ten Thousand Talent Program for Young Top-Notch Talent</funding><pagination>1050735</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6944226</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>2019</volume><pubmed_abstract>The phosphorylation of oligonucleotides and peptides plays a critical role in regulating virtually all cellular processes. To fully understand these complex and fundamental regulatory pathways, the cellular phosphorylate changes of both oligonucleotides and peptides should be simultaneously identified and characterized. Here, we demonstrated a single-molecule, high-throughput, label-free, general, and one-step aerolysin nanopore method to comprehensively evaluate the phosphorylation of both oligonucleotide and peptide substrates. By virtue of electrochemically confined effects in aerolysin, our results show that the phosphorylation accelerates the traversing speed of a negatively charged substrate for about hundreds of time while significantly enhances the translocation frequency of a posi</pubmed_abstract><journal>Research (Washington, D.C.)</journal><pubmed_title>A Nanopore Phosphorylation Sensor for Single Oligonucleotides and Peptides.</pubmed_title><pmcid>PMC6944226</pmcid><funding_grant_id>ZYJH004</funding_grant_id><funding_grant_id>21834001</funding_grant_id><funding_grant_id>21922405</funding_grant_id><funding_grant_id>61871183</funding_grant_id><pubmed_authors>Li MY</pubmed_authors><pubmed_authors>Meng FN</pubmed_authors><pubmed_authors>Yang J</pubmed_authors><pubmed_authors>Li S</pubmed_authors><pubmed_authors>Ying YL</pubmed_authors><pubmed_authors>Long YT</pubmed_authors></additional><is_claimable>false</is_claimable><name>A Nanopore Phosphorylation Sensor for Single Oligonucleotides and Peptides.</name><description>The phosphorylation of oligonucleotides and peptides plays a critical role in regulating virtually all cellular processes. To fully understand these complex and fundamental regulatory pathways, the cellular phosphorylate changes of both oligonucleotides and peptides should be simultaneously identified and characterized. Here, we demonstrated a single-molecule, high-throughput, label-free, general, and one-step aerolysin nanopore method to comprehensively evaluate the phosphorylation of both oligonucleotide and peptide substrates. By virtue of electrochemically confined effects in aerolysin, our results show that the phosphorylation accelerates the traversing speed of a negatively charged substrate for about hundreds of time while significantly enhances the translocation frequency of a posi</description><dates><release>2019-01-01T00:00:00Z</release><publication>2019</publication><modification>2025-05-29T21:40:34.865Z</modification><creation>2025-05-29T21:40:34.865Z</creation></dates><accession>S-EPMC6944226</accession><cross_references><pubmed>31912023</pubmed><doi>10.34133/2019/1050735</doi></cross_references></HashMap>