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A. Das, H. Ko, L. E. Burienek, M. O. Barrett and T. K. Harden, “Human P2Y(14) Receptor Agonists: Truncation of the Hexose Moiety of Uridine-5’-Diphosphoglucose and Its Replacement with Alkyl and Aryl Groups,” Journal of Medicinal Chemistry, Vol. 53, No. 1, 2010, pp. 471-480. doi:10.1021/jm901432g

has been cited by the following article:

• TITLE: Bacterial UDP-Glucose Hydrolases and P2 Receptor-Mediated Responses to Infection: A Commentary

  AUTHORS: Ifor R. Beacham, John P. Headrick

  KEYWORDS: UDP-Glucose Hydrolase; P2Y14 Receptor; Virulence Factor; Salmonella enterica; E. coli

  JOURNAL NAME: Advances in Infectious Diseases, Vol.3 No.2, June 5, 2013

  ABSTRACT: UDP-glucose hydrolases are a group of relatively little known membrane-bound or periplasmic enzymes found in Salmonella enterica and E. coli. UDP-glucose is an agonist for a specific P2 receptor (P2Y14) found on epithelial cells and cells associated with innate immunity. It is also recognised as a ‘danger signal’. Cells respond to mechanical damage by releasing UDP-glucose which activates P2Y14 to trigger an innate immune response; it is postulated that a similar response to bacterial infection may be protective against infection. However, the UDP-glucose hydrolases may constitute virulence factors able to abrogate this response by degradation of the released UDP-glucose.