{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Burkholder NT"],"funding":["NIGMS NIH HHS"],"pagination":["269-297"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6701646"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["607"],"pubmed_abstract":["Proline isomerization is ubiquitous in proteins and is important for regulating important processes such as folding, recognition, and enzymatic activity. In humans, peptidyl-prolyl isomerase cis-trans isomerase NIMA interacting 1 (Pin1) is responsible for mediating fast conversion between cis- and trans-conformations of serine/threonine-proline (S/T-P) motifs in a large number of cellular pathways, many of which are involved in normal development as well as progression of several cancers and diseases. One of the major processes that Pin1 regulates is phosphatase activity against the RNA polymerase II C-terminal domain (RNAPII CTD). However, molecular tools capable of distinguishing the effects of proline conformation on phosphatase function have been lacking. A key tool that allows us to u"],"journal":["Methods in enzymology"],"pubmed_title":["Chemical Tools for Studying the Impact of cis/trans Prolyl Isomerization on Signaling: A Case Study on RNA Polymerase II Phosphatase Activity and Specificity."],"pmcid":["PMC6701646"],"funding_grant_id":["R01 GM104896","R01 GM125882"],"pubmed_authors":["Medellin B","Zhang YJ","Burkholder NT","Showalter SA","Matthews W","Irani S"],"additional_accession":[]},"is_claimable":false,"name":"Chemical Tools for Studying the Impact of cis/trans Prolyl Isomerization on Signaling: A Case Study on RNA Polymerase II Phosphatase Activity and Specificity.","description":"Proline isomerization is ubiquitous in proteins and is important for regulating important processes such as folding, recognition, and enzymatic activity. In humans, peptidyl-prolyl isomerase cis-trans isomerase NIMA interacting 1 (Pin1) is responsible for mediating fast conversion between cis- and trans-conformations of serine/threonine-proline (S/T-P) motifs in a large number of cellular pathways, many of which are involved in normal development as well as progression of several cancers and diseases. One of the major processes that Pin1 regulates is phosphatase activity against the RNA polymerase II C-terminal domain (RNAPII CTD). However, molecular tools capable of distinguishing the effects of proline conformation on phosphatase function have been lacking. A key tool that allows us to u","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018","modification":"2025-04-04T13:43:19.495Z","creation":"2019-08-24T07:03:46Z"},"accession":"S-EPMC6701646","cross_references":{"pubmed":["30149861"],"doi":["10.1016/bs.mie.2018.04.020"]}}