Heteroatom(isotope)-tagged genomics and proteomics

Sanz-Medel, Alfredo
January 2008
Analytical & Bioanalytical Chemistry;Jan2008, Vol. 390 Issue 1, p1
Academic Journal
The article discusses various reports published within the issue including one on the state-of-the-art of the use of ICP-MS for quantitative proteomics and another on the emerging concept of labelling with elements or isotopes.


Related Articles

  • Multiplexed absolute quantification in proteomics using artificial QCAT proteins of concatenated signature peptides. Beynon, Robert J.; Doherty, Mary K.; Pratt, Julie M.; Gaskell, Simon J. // Nature Methods;Aug2005, Vol. 2 Issue 8, p587 

    Absolute quantification in proteomics usually involves simultaneous determination of representative proteolytic peptides and stable isotope–labeled analogs. The principal limitation to widespread implementation of this approach is the availability of standard signature peptides in...

  • Stable isotopic labeling of proteins for quantitative proteomic applications. Becker, Gerald W. // Briefings in Functional Genomics & Proteomics;Sep2008, Vol. 7 Issue 5, p371 

    Straightforward methods for the introduction of stable isotopes into proteins with subsequent isolation and purification of the proteins will greatly aid the field of quantitative proteomics. Proteins containing amino acids with one or more of the stable isotopes of deuterium, 13C, 15N or 18O...

  • Mass spectrometry-based quantitative proteomic profiling. Wei Yan; Chen, Sharon S. // Briefings in Functional Genomics & Proteomics;May2005, Vol. 4 Issue 1, p27 

    Quantitative proteomics involves the identification and quantitation of protein components in various biological systems. Stable isotope labelling technology, by both metabolic and chemical methods, has been the most commonly used approach for global proteome-wide profiling. Recently, its...

  • Quantitative mass spectrometry in proteomics: a critical review. Bantscheff, Marcus; Schirle, Markus; Sweetman, Gavain; Rick, Jens; Kuster, Bernhard // Analytical & Bioanalytical Chemistry;Oct2007, Vol. 389 Issue 4, p1017 

    The quantification of differences between two or more physiological states of a biological system is among the most important but also most challenging technical tasks in proteomics. In addition to the classical methods of differential protein gel or blot staining by dyes and fluorophores,...

  • Double deficiency of cathepsins B and L results in massive secretome alterations and suggests a degradative cathepsin-MMP axis. Tholen, Stefan; Biniossek, Martin; Gansz, Martina; Ahrens, Theresa; Schlimpert, Manuel; Kizhakkedathu, Jayachandran; Reinheckel, Thomas; Schilling, Oliver // Cellular & Molecular Life Sciences;Mar2014, Vol. 71 Issue 5, p899 

    Endolysosomal cysteine cathepsins functionally cooperate. Cathepsin B (Ctsb) and L (Ctsl) double-knockout mice die 4 weeks after birth accompanied by (autophago-) lysosomal accumulations within neurons. Such accumulations are also observed in mouse embryonic fibroblasts (MEFs) deficient for Ctsb...

  • A quantitative analysis software tool for mass spectrometry—based proteomics. Sung Kyu Park; Venable, John D.; Tao Xu; Yates, III, John R. // Nature Methods;Apr2008, Vol. 5 Issue 4, p319 

    We describe Census, a quantitative software tool compatible with many labeling strategies as well as with label-free analyses, single-stage mass spectrometry (MS1) and tandem mass spectrometry (MS/MS) scans, and high- and low-resolution mass spectrometry data. Census uses robust algorithms to...

  • Comparison of data analysis parameters and MS/MS fragmentation techniques for quantitative proteome analysis using isobaric peptide termini labeling (IPTL). Koehler, Christian; Arntzen, Magnus; Treumann, Achim; Thiede, Bernd // Analytical & Bioanalytical Chemistry;2012, Vol. 404 Issue 4, p1103 

    Isobaric peptide termini labeling (IPTL) is a quantification method which permits relative quantification using quantification points distributed throughout the whole tandem mass spectrometry (MS/MS) spectrum. It is based on the complementary derivatization of peptide termini with different...

  • Targeted protein quantification using sparse reference labeling. Chang, Ching-Yun; Sabidó, Eduard; Aebersold, Ruedi; Vitek, Olga // Nature Methods;Mar2014, Vol. 11 Issue 3, p301 

    Targeted proteomics is a method of choice for accurate and high-throughput quantification of predefined sets of proteins. Many workflows use isotope-labeled reference peptides for every target protein, which is time consuming and costly. We report a statistical approach for quantifying full...

  • Mass Spectrometry-Based Label-Free Quantitative Proteomics. Wenhong Zhu; Smith, Jeffrey W.; Chun-Ming Huang // Journal of Biomedicine & Biotechnology;2010, p1 

    In order to study the differential protein expression in complex biological samples, strategies for rapid, highly reproducible and accurate quantification are necessary. Isotope labeling and fluorescent labeling techniques have been widely used in quantitative proteomics research. However,...


Read the Article


Sorry, but this item is not currently available from your library.

Try another library?
Sign out of this library

Other Topics