{"doi":"10.7287/peerj.preprints.564","title":"Association between intrinsic disorder and serine/threonine phosphorylation in\n                  <i>Mycobacterium tuberculosis</i>","abstract":"<jats:p>\n                  Serine/threonine phosphorylation is an important mechanism to regulate protein function. In eukaryotes phosphorylation occurs predominantly in intrinsically disordered regions of proteins. While serine/threonine phosphorylation and protein disorder are much less prevalent in prokaryotes,\n                  <jats:italic>M. tuberculosis</jats:italic>\n                  has both high serine/threonine phosphorylation and disorder. Here I show that, similar to eukaryotes, serine/threonine phosphorylation sites in\n                  <jats:italic>M. tuberculosis</jats:italic>\n                  are highly enriched in intrinsically disordered regions\n                  <jats:italic>,</jats:italic>\n                  indicating similarity in substrate recognition mechanism of eukaryotic and\n                  <jats:italic>M. tuberculosis</jats:italic>\n                  kinases. Serine/threonine phosphorylation has been linked to the pathogenicity and survival of\n                  <jats:italic>M. tuberculosis</jats:italic>\n                  , thus better understanding of how its kinases recognize their substrates could have important implications in understanding and controlling the biology of this deadly pathogen.\n                </jats:p>","journal":null,"year":null,"id":597094,"datarank":0.0,"base_score":0.0,"endowment":0.0,"self_citation_contribution":0.0,"citation_network_contribution":0.0,"self_endowment_contribution":0.0,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":0,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Association between intrinsic disorder and serine/threonine phosphorylation in\n                  <i>Mycobacterium tuberculosis</i>","abstract":"<jats:p>\n                  Serine/threonine phosphorylation is an important mechanism to regulate protein function. In eukaryotes phosphorylation occurs predominantly in intrinsically disordered regions of proteins. While serine/threonine phosphorylation and protein disorder are much less prevalent in prokaryotes,\n                  <jats:italic>M. tuberculosis</jats:italic>\n                  has both high serine/threonine phosphorylation and disorder. Here I show that, similar to eukaryotes, serine/threonine phosphorylation sites in\n                  <jats:italic>M. tuberculosis</jats:italic>\n                  are highly enriched in intrinsically disordered regions\n                  <jats:italic>,</jats:italic>\n                  indicating similarity in substrate recognition mechanism of eukaryotic and\n                  <jats:italic>M. tuberculosis</jats:italic>\n                  kinases. Serine/threonine phosphorylation has been linked to the pathogenicity and survival of\n                  <jats:italic>M. tuberculosis</jats:italic>\n                  , thus better understanding of how its kinases recognize their substrates could have important implications in understanding and controlling the biology of this deadly pathogen.\n                </jats:p>","is_dataset_classified":null,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"23304386","pmcid":null,"openalex_id":"https://openalex.org/W4255835953","authors":[],"funders":[],"total_grants":0,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[],"oa_status":"gold","license":"cc-by","oa_locations":[{"url":"https://peerj.com/preprints/564v1.pdf","host_type":""},{"url":"https://peerj.com/preprints/564v1.pdf","host_type":""},{"url":"https://peerj.com/preprints/564v1.xml","host_type":"publisher"},{"url":"https://peerj.com/preprints/564v1.html","host_type":"publisher"},{"url":"https://doi.org/10.7287/peerj.preprints.564","host_type":""}],"fields_of_study":["Tuberculosis Research and Epidemiology","Biochemical and Molecular Research","Mycobacterium research and diagnosis"],"mesh_terms":[],"keywords":["Serine","Phosphorylation","Threonine","Protein phosphorylation","Protein-Serine-Threonine Kinases","Kinase","Mycobacterium tuberculosis","Biology","Phosphorylation cascade","Biochemistry","Cell biology","Protein kinase A","Tuberculosis","Medicine"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Good health and well-being"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-28T12:14:40.370942Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}