All Stories

  1. Multidrug-Resistant Lineage of Enterotoxigenic Escherichia coli ST182 With Serotype O169:H41 in Airline Waste
  2. Protein cleavage influences surface protein presentation in Mycoplasma pneumoniae
  3. Genomic analysis of trimethoprim-resistant extraintestinal pathogenic Escherichia coli and recurrent urinary tract infections
  4. Duplication and diversification of a unique chromosomal virulence island hosting the subtilase cytotoxin in Escherichia coli ST58
  5. Cell surface processing of the P1 adhesin of Mycoplasma pneumoniae identifies novel domains that bind host molecules
  6. Escherichia coli ST302: Genomic Analysis of Virulence Potential and Antimicrobial Resistance Mediated by Mobile Genetic Elements
  7. Genomic Surveillance for One Health Antimicrobial Resistance: Understanding Human, Animal, and Environmental Reservoirs and Transmission
  8. The Diverse Functional Roles of Elongation Factor Tu (EF-Tu) in Microbial Pathogenesis
  9. Mycoplasma hyopneumoniae surface-associated proteases cleave bradykinin, substance P, neurokinin A and neuropeptide Y
  10. Formylated N-terminal methionine is absent from the Mycoplasma hyopneumoniae proteome: Implications for translation initiation
  11. Elongation factor Tu is a multifunctional and processed moonlighting protein
  12. Mycoplasma hyopneumoniae surface proteins are all cut up
  13. Mycoplasmal surface-associated aminopeptidases are multifunctional moonlighting proteins
  14. Microbial proteases with additional functions
  15. Multifunctional protein on the surface of pig respiratory pathogen
  16. Proteolytic processing of the cilium adhesin MHJ_0194 (P123J) inMycoplasma hyopneumoniaegenerates a functionally diverse array of cleavage fragments that bind multiple host molecules
  17. Cilium Adhesin P216 (MHJ_0493) Is a Target of Ectodomain Shedding and Aminopeptidase Activity on the Surface of Mycoplasma hyopneumoniae
  18. P159 from Mycoplasma hyopneumoniae Binds Porcine Cilia and Heparin and Is Cleaved in a Manner Akin to Ectodomain Shedding