{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Vallejo-Schmidt T"],"funding":["NIGMS NIH HHS"],"pagination":["563-576"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11374754"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8(8)"],"pubmed_abstract":["TLRs initiate innate immune signaling pathways via Toll/IL-1R (TIR) domains on their cytoplasmic tails. Various bacterial species also express TIR domain-containing proteins that contribute to bacterial evasion of the innate immune system. Bacterial TIR domains, along with the mammalian sterile α and TIR motif-containing protein 1 and TIRs from plants, also have been found to exhibit NADase activity. Initial X-ray crystallographic studies of the bacterial TIR from Acinetobacter baumannii provided insight into bacterial TIR structure but were unsuccessful in cocrystallization with the NAD+ ligand, leading to further questions about the TIR NAD binding site. In this study, we designed a Course-Based Undergraduate Research Experience (CURE) involving 16-20 students per year to identify amino "],"journal":["ImmunoHorizons"],"pubmed_title":["Characterization of the Structural Requirements for the NADase Activity of Bacterial Toll/IL-1R domains in a Course-based Undergraduate Research Experience."],"pmcid":["PMC11374754"],"funding_grant_id":["T32 GM146694","R25 GM119970","R25 GM058264"],"pubmed_authors":["Riedlbauer D","Williams AN","Vallejo-Schmidt T","Eromosele IR","Stefano A","Obiorah T","Hamilton S","Duff R","Jones JK","Sultana S","Schmidt K","Snyder GA","Chaudhry SS","Scudder AH","Poteat AM","Shoemaker P","Rolle LTA","Weldon JE","Guzman-Cruz E","Price SE","Mercanti MA","Snyder MLD","Riddick T","Fallah D","Keshmiri N","David J","Sterling MK","Riaz T","Bader C","Dada TA","Conteh M","Toneygay L","Pascoe ER","Ingram LP","Akingbehin V","Nallar S","Koudjra AR","Erickson BC","De Leon R","Calkins PH","Ojo MA","Palm C","Anderson JT","Collins H","Alexander Z","Onwezi-Nwugwo J"],"additional_accession":[]},"is_claimable":false,"name":"Characterization of the Structural Requirements for the NADase Activity of Bacterial Toll/IL-1R domains in a Course-based Undergraduate Research Experience.","description":"TLRs initiate innate immune signaling pathways via Toll/IL-1R (TIR) domains on their cytoplasmic tails. Various bacterial species also express TIR domain-containing proteins that contribute to bacterial evasion of the innate immune system. Bacterial TIR domains, along with the mammalian sterile α and TIR motif-containing protein 1 and TIRs from plants, also have been found to exhibit NADase activity. Initial X-ray crystallographic studies of the bacterial TIR from Acinetobacter baumannii provided insight into bacterial TIR structure but were unsuccessful in cocrystallization with the NAD+ ligand, leading to further questions about the TIR NAD binding site. In this study, we designed a Course-Based Undergraduate Research Experience (CURE) involving 16-20 students per year to identify amino ","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Aug","modification":"2026-06-01T12:13:24.828Z","creation":"2024-11-15T21:29:20.616Z"},"accession":"S-EPMC11374754","cross_references":{"pubmed":["39172026"],"doi":["10.4049/immunohorizons.2300062"]}}