Essential role ofBordetellaNadC in a quinolinate salvage pathway for NAD biosynthesis
Author:
Affiliation:
1. Department of Microbiology and ImmunologyUniversity of Minnesota Medical School, 3‐117 Microbiology Research Facility689 23rd Ave. S.EMinneapolis MN55455‐1507 USA
Funder
University of Minnesota Faculty Incentive Research Account
Publisher
Wiley
Subject
Molecular Biology,Microbiology
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1111/mmi.13566
Reference72 articles.
1. NAD+Released during Inflammation Participates in T Cell Homeostasis by Inducing ART2-Mediated Death of Naive T Cells In Vivo
2. Overrepresentation of a Gene Family Encoding Extracytoplasmic Solute Receptors in Bordetella
3. Roles for Cationic Residues at the Quinolinic Acid Binding Site of Quinolinate Phosphoribosyltransferase
4. Interactions at the 2 and 5 Positions of 5-Phosphoribosyl Pyrophosphate Are Essential in Salmonella typhimurium Quinolinate Phosphoribosyltransferase
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1. Periplasmic binding proteins Bug69 and Bug27 from Bordetella pertussis are in vitro high‐affinity quinolinate binders with a potential role in NAD biosynthesis;FEBS Open Bio;2024-08-08
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3. Bacterial NadQ (COG4111) is a Nudix-like, ATP-responsive regulator of NAD biosynthesis;Journal of Structural Biology;2022-12
4. Cyclic di-GMP Regulates the Type III Secretion System and Virulence in Bordetella bronchiseptica;Infection and Immunity;2022-06-16
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