LTQ-XL mass spectrometry proteome analysis expands the Pseudomonas aeruginosa AmpR regulon to include cyclic di-GMP phosphodiesterases and phosphoproteins, and identifies novel open reading frames Article

Kumari, Hansi, Murugapiran, Senthil K, Balasubramanian, Deepak et al. (2014). LTQ-XL mass spectrometry proteome analysis expands the Pseudomonas aeruginosa AmpR regulon to include cyclic di-GMP phosphodiesterases and phosphoproteins, and identifies novel open reading frames . JOURNAL OF PROTEOMICS, 96 328-342. 10.1016/j.jprot.2013.11.018

Open Access

cited authors

  • Kumari, Hansi; Murugapiran, Senthil K; Balasubramanian, Deepak; Schneper, Lisa; Merighi, Massimo; Sarracino, David; Lory, Stephen; Mathee, Kalai

sustainable development goals

authors

publication date

  • January 16, 2014

published in

keywords

  • ALGINATE PRODUCTION
  • ANAEROBIC GROWTH
  • AmpR
  • Antibiotic resistance
  • BETA-LACTAMASE
  • Biochemical Research Methods
  • Biochemistry & Molecular Biology
  • Core Proteome
  • Cyclic di-GMP
  • ESCHERICHIA-COLI
  • EXPRESSION
  • Life Sciences & Biomedicine
  • MOLECULAR-BIOLOGY
  • OUTER-MEMBRANE PERMEABILITY
  • PEPTIDE IDENTIFICATION
  • Phosphoproteome
  • RESISTANCE
  • Science & Technology
  • TRANSCRIPTIONAL REGULATOR
  • Transcriptional regulators

Digital Object Identifier (DOI)

publisher

  • ELSEVIER

start page

  • 328

end page

  • 342

volume

  • 96