@inbook{a2326a72888f43b5963d5806fb04916b,
title = "Exploring extracellular matrix degradomes by TMT-TAILS N-terminomics",
abstract = "Global characterization of protein N termini provides valuable information on proteome dynamics and diversity in health and disease. Driven by the progress in mass spectrometry-based proteomics, novel approaches for the dedicated investigation of protein N termini and protease substrates have been recently developed. Terminal amine isotopic labeling of substrates (TAILS) is a quantitative proteomics approach suitable for high-throughput and system-wide profiling of protein N termini in complex biological matrices. TAILS employs isotopic labeling of primary amines of intact proteins in combination with an amine-reactive high molecular weight polymer (HPG-ALD) for depletion of internal tryptic peptides and high enrichment of protein N termini by negative selection. Thereby, TAILS allows simultaneous identification of the natural N termini, protease-generated neo-N termini, and endogenously modified (e.g., acetylated) N termini. In this chapter, we provide a protocol for tandem mass tag (TMT)-TAILS analysis and further discuss specific considerations regarding N-terminome data interpretation using Proteome Discoverer{\texttrademark} software.",
keywords = "N-terminome, Proteolysis, Proteome Discoverer{\texttrademark}, TAILS, TMT",
author = "Elizabeta Madzharova and Fabio Sabino and {auf dem Keller}, Ulrich",
year = "2019",
doi = "10.1007/978-1-4939-9095-5_8",
language = "English",
isbn = "978-1-4939-9094-8",
series = "Methods in Molecular Biology",
publisher = "Humana Press",
pages = "115--126",
editor = "Irit Sagi and Afratis, {Nikolaos A.}",
booktitle = "Collagen",
address = "United States",
}