scholarly journals Label-Free Quantitative Mass Spectrometry Reveals Novel Pathways Involved in LL-37 Expression

2013 ◽  
Vol 6 (3) ◽  
pp. 365-376 ◽  
Author(s):  
Andreas Cederlund ◽  
Frank Nylén ◽  
Erica Miraglia ◽  
Peter Bergman ◽  
Gudmundur H. Gudmundsson ◽  
...  
PROTEOMICS ◽  
2011 ◽  
Vol 11 (4) ◽  
pp. 535-553 ◽  
Author(s):  
Karlie A. Neilson ◽  
Naveid A. Ali ◽  
Sridevi Muralidharan ◽  
Mehdi Mirzaei ◽  
Michael Mariani ◽  
...  

PROTEOMICS ◽  
2016 ◽  
Vol 16 (6) ◽  
pp. 920-924 ◽  
Author(s):  
David C. Gemperline ◽  
Mark Scalf ◽  
Lloyd M. Smith ◽  
Richard D. Vierstra

2012 ◽  
Vol 41 (1) ◽  
pp. e28-e28 ◽  
Author(s):  
Arne H. Smits ◽  
Pascal W. T. C. Jansen ◽  
Ina Poser ◽  
Anthony A. Hyman ◽  
Michiel Vermeulen

2013 ◽  
Vol 2013 ◽  
pp. 1-13 ◽  
Author(s):  
Xianyin Lai ◽  
Lianshui Wang ◽  
Frank A. Witzmann

To address the challenges associated with differential expression proteomics, label-free mass spectrometric protein quantification methods have been developed as alternatives to array-based, gel-based, and stable isotope tag or label-based approaches. In this paper, we focus on the issues associated with label-free methods that rely on quantitation based on peptide ion peak area measurement. These issues include chromatographic alignment, peptide qualification for quantitation, and normalization. In addressing these issues, we present various approaches, assembled in a recently developed label-free quantitative mass spectrometry platform, that overcome these difficulties and enable comprehensive, accurate, and reproducible protein quantitation in highly complex protein mixtures from experiments with many sample groups. As examples of the utility of this approach, we present a variety of cases where the platform was applied successfully to assess differential protein expression or abundance in body fluids, in vitro nanotoxicology models, tissue proteomics in genetic knock-in mice, and cell membrane proteomics.


Biomolecules ◽  
2017 ◽  
Vol 7 (4) ◽  
pp. 58 ◽  
Author(s):  
Heidi N. Danielsen ◽  
Susan H. Hansen ◽  
Florian-Alexander Herbst ◽  
Henrik Kjeldal ◽  
Allan Stensballe ◽  
...  

2017 ◽  
Vol 398 (5-6) ◽  
pp. 687-699 ◽  
Author(s):  
Claudia Lindemann ◽  
Nikolas Thomanek ◽  
Franziska Hundt ◽  
Thilo Lerari ◽  
Helmut E. Meyer ◽  
...  

Abstract Quantitative mass spectrometry approaches are used for absolute and relative quantification in global proteome studies. To date, relative and absolute quantification techniques are available that differ in quantification accuracy, proteome coverage, complexity and robustness. This review focuses on most common relative or absolute quantification strategies exemplified by three experimental studies. A label-free relative quantification approach was performed for the investigation of the membrane proteome of sensory cilia to the depth of olfactory receptors in Mus musculus. A SILAC-based relative quantification approach was successfully applied for the identification of core components and transient interactors of the peroxisomal importomer in Saccharomyces cerevisiae. Furthermore, AQUA using stable isotopes was exemplified to unraveling the prenylome influenced by novel prenyltransferase inhibitors. Characteristic enrichment and fragmentation strategies for a robust quantification of the prenylome are also summarized.


2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Maaike Rijkers ◽  
Bart L. van den Eshof ◽  
Pieter F. van der Meer ◽  
Floris P. J. van Alphen ◽  
Dirk de Korte ◽  
...  

Amino Acids ◽  
2012 ◽  
Vol 43 (3) ◽  
pp. 1119-1129 ◽  
Author(s):  
Nicole Sessler ◽  
Karsten Krug ◽  
Alfred Nordheim ◽  
Benjamin Mordmüller ◽  
Boris Macek

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