<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Yu S</submitter><funding>National Natural Science Foundation of China</funding><pagination>6574-6583</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6497428</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>33(5)</volume><pubmed_abstract>Mutations may ultimately change the local conformation of proteins; however, little attention has been paid to alterations in protein function caused by the incidence of &lt;i>cis&lt;/i>-peptide bonds (ICPB) in mammalian cells. In this study, a statistical approach, coimmunoprecipitation, and immunofluorescence staining have been used to confirm that S246→Y and S246→W missense mutations, which help increase the ICPB in Xaa246-P247 (Xaa is any amino acid) in human β-catenin, can reduce the interactions between β-catenin and adenomatous polyposis coli (APC) and between β-catenin and Ca2&lt;sup>+&lt;/sup>-dependent cell adhesion molecule family in epithelial tissue (E-cadherin), eventually leading to increased nuclear migration of β-catenin in the HepG2 cell line (an immortalized cell line consisting of </pubmed_abstract><journal>FASEB journal : official publication of the Federation of American Societies for Experimental Biology</journal><pubmed_title>Subcellular localization of mutated β-catenins with different incidences of &lt;i>cis&lt;/i>-peptide bonds at the Xaa246-P247 site in HepG2 cells.</pubmed_title><pmcid>PMC6497428</pmcid><funding_grant_id>31501100</funding_grant_id><pubmed_authors>Yang H</pubmed_authors><pubmed_authors>Yang Y</pubmed_authors><pubmed_authors>Yu S</pubmed_authors><pubmed_authors>Zhang Z</pubmed_authors><pubmed_authors>Zhang Y</pubmed_authors><pubmed_authors>Chen Y</pubmed_authors><pubmed_authors>Wu Y</pubmed_authors></additional><is_claimable>false</is_claimable><name>Subcellular localization of mutated β-catenins with different incidences of &lt;i>cis&lt;/i>-peptide bonds at the Xaa246-P247 site in HepG2 cells.</name><description>Mutations may ultimately change the local conformation of proteins; however, little attention has been paid to alterations in protein function caused by the incidence of &lt;i>cis&lt;/i>-peptide bonds (ICPB) in mammalian cells. In this study, a statistical approach, coimmunoprecipitation, and immunofluorescence staining have been used to confirm that S246→Y and S246→W missense mutations, which help increase the ICPB in Xaa246-P247 (Xaa is any amino acid) in human β-catenin, can reduce the interactions between β-catenin and adenomatous polyposis coli (APC) and between β-catenin and Ca2&lt;sup>+&lt;/sup>-dependent cell adhesion molecule family in epithelial tissue (E-cadherin), eventually leading to increased nuclear migration of β-catenin in the HepG2 cell line (an immortalized cell line consisting of </description><dates><release>2019-01-01T00:00:00Z</release><publication>2019 May</publication><modification>2026-04-14T13:39:00.59Z</modification><creation>2019-06-06T23:10:35Z</creation></dates><accession>S-EPMC6497428</accession><cross_references><pubmed>30807699</pubmed><doi>10.1096/fj.201801937RR</doi></cross_references></HashMap>