Differential quantification of isobaric phosphopeptides using data-independent acquisition mass spectrometry.
Phosphorylation is a post-translational modification (PTM) fundamental for processes such as signal transduction and enzyme activity. We propose to apply data-independent acquisition (DIA) using mass spectrometry (MS) to determine unexplored phosphorylation events on isobarically modified peptides. Such peptides are commonly not quantitatively discriminated in phosphoproteomics due to their identical mass.
Epigenetics Program, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Room 9-124, 3400 Civic Center Blvd, Bldg 421, Philadelphia, PA 19104, USA. bgarci@mail.med.upenn.edu.
Simone
S
Sidoli
Epigenetics Program, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Room 9-124, 3400 Civic Center Blvd, Bldg 421, Philadelphia, PA 19104, USA. bgarci@mail.med.upenn.edu.
Rina
R
Fujiwara
Epigenetics Program, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Room 9-124, 3400 Civic Center Blvd, Bldg 421, Philadelphia, PA 19104, USA. bgarci@mail.med.upenn.edu and Division of Cancer Pathobiology, The Children's Hospital of Philadelphia, Philadelphia, PA 19104, USA.
Katarzyna
K
Kulej
Epigenetics Program, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Room 9-124, 3400 Civic Center Blvd, Bldg 421, Philadelphia, PA 19104, USA. bgarci@mail.med.upenn.edu.
Benjamin A
BA
Garcia
D013058:Mass Spectrometry / Q000379:methods*; D010748:Phosphopeptides / Q000737:chemistry*
D010748:Phosphopeptides