{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kennedy EN"],"funding":["NIGMS NIH HHS"],"pagination":["fow068"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5815161"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(6)"],"pubmed_abstract":["Rapid response to external stimuli is crucial for survival and proliferation of microorganisms. Pathogenic fungi employ histidine-to-aspartate multistep phosphorelay systems to respond to environmental stress, progress through developmental stages and to produce virulence factors. Because these His-to-Asp phosphorelay systems are not found in humans, they are potential targets for the development of new antifungal therapies. Here we report the characterization of the histidine phosphotransfer (HPt) protein Ypd1 from the human fungal pathogen Cryptococcus neoformans Results from this study demonstrate that CnYpd1 indeed functions as a phosphorelay protein in vitro, and that H138 is confirmed as the site of phosphorylation. We found that CnYpd1 exhibits unique characteristics in comparison t"],"journal":["FEMS yeast research"],"pubmed_title":["Extended N-terminal region of the essential phosphorelay signaling protein Ypd1 from Cryptococcus neoformans contributes to structural stability, phosphostability and binding of calcium ions."],"pmcid":["PMC5815161"],"funding_grant_id":["P20 GM103640"],"pubmed_authors":["Menon SK","West AH","Kennedy EN"],"additional_accession":[]},"is_claimable":false,"name":"Extended N-terminal region of the essential phosphorelay signaling protein Ypd1 from Cryptococcus neoformans contributes to structural stability, phosphostability and binding of calcium ions.","description":"Rapid response to external stimuli is crucial for survival and proliferation of microorganisms. Pathogenic fungi employ histidine-to-aspartate multistep phosphorelay systems to respond to environmental stress, progress through developmental stages and to produce virulence factors. Because these His-to-Asp phosphorelay systems are not found in humans, they are potential targets for the development of new antifungal therapies. Here we report the characterization of the histidine phosphotransfer (HPt) protein Ypd1 from the human fungal pathogen Cryptococcus neoformans Results from this study demonstrate that CnYpd1 indeed functions as a phosphorelay protein in vitro, and that H138 is confirmed as the site of phosphorylation. We found that CnYpd1 exhibits unique characteristics in comparison t","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Sep","modification":"2026-04-07T19:58:23.067Z","creation":"2019-03-26T23:03:45Z"},"accession":"S-EPMC5815161","cross_references":{"pubmed":["27549628"],"doi":["10.1093/femsyr/fow068"]}}