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R. L. Carter, I. P. Fricks, M. O. Barrett, L. E. Burienek and Y Zhou, “Quantification of Gi-mediated Inhibition of Adenylyl Cyclase Activity Reveals That UDP Is a Potent Agonist of the Human P2Y14 Receptor,” Molecular Pharmacology, Vol. 76, No. 6, 2009, pp. 1341-1348. doi:10.1124/mol.109.058578

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.