<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>13</volume><submitter>Suri A</submitter><pubmed_abstract>Peptidyl-prolyl &lt;i>cis-trans&lt;/i> isomerases (PPIases) are ubiquitous proteins which are essential for &lt;i>cis-trans&lt;/i> isomerisation of peptide bonds preceding the proline residue. PPIases are categorized into four sub-families &lt;i>viz&lt;/i>., cyclophilins, FK506-binding proteins (FKBPs), parvulins and protein phosphatase 2A phosphatase activators (PTPAs). Apart from catalysing the &lt;i>cis-trans&lt;/i> isomerization, these proteins have also been implicated in diverse cellular functions. Though PPIases have been identified in several important crop plants, information on these proteins, except cyclophilins, is scanty in wheat. In order to understand the role of these genes in wheat, we carried out genome-wide identification using computational approaches. The present study resulted in identificat</pubmed_abstract><journal>Frontiers in plant science</journal><pagination>1053524</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9797600</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Genome-wide characterization of FK506-binding proteins, parvulins and phospho-tyrosyl phosphatase activators in wheat and their regulation by heat stress.</pubmed_title><pmcid>PMC9797600</pmcid><pubmed_authors>Singh H</pubmed_authors><pubmed_authors>Suri A</pubmed_authors><pubmed_authors>Kaur K</pubmed_authors><pubmed_authors>Kaachra A</pubmed_authors><pubmed_authors>Singh P</pubmed_authors></additional><is_claimable>false</is_claimable><name>Genome-wide characterization of FK506-binding proteins, parvulins and phospho-tyrosyl phosphatase activators in wheat and their regulation by heat stress.</name><description>Peptidyl-prolyl &lt;i>cis-trans&lt;/i> isomerases (PPIases) are ubiquitous proteins which are essential for &lt;i>cis-trans&lt;/i> isomerisation of peptide bonds preceding the proline residue. PPIases are categorized into four sub-families &lt;i>viz&lt;/i>., cyclophilins, FK506-binding proteins (FKBPs), parvulins and protein phosphatase 2A phosphatase activators (PTPAs). Apart from catalysing the &lt;i>cis-trans&lt;/i> isomerization, these proteins have also been implicated in diverse cellular functions. Though PPIases have been identified in several important crop plants, information on these proteins, except cyclophilins, is scanty in wheat. In order to understand the role of these genes in wheat, we carried out genome-wide identification using computational approaches. The present study resulted in identificat</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022</publication><modification>2025-04-18T22:25:27.807Z</modification><creation>2024-12-04T11:37:17.582Z</creation></dates><accession>S-EPMC9797600</accession><cross_references><pubmed>36589073</pubmed><doi>10.3389/fpls.2022.1053524</doi></cross_references></HashMap>