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High-throughput proteomics

Shen, Y., Tolic, N., Zhao, R., Pasa-Tolic, L., Li, L., Berger, S.J., Harkewicz, R., Anderson, G.A., Belov, M.E., Smith, R.D. (2001). High-throughput proteomics using high efficiency multiple-capillary liquid chromatography with on-line high performance ESI FTICR mass spectrometry. Anal. Chem. 73, 3011-3021. [Pg.34]

Sawasaki, T., Ogasawara, T., Morishita, R. and Endo, Y. (2002) A cell-free protein synthesis system for high-throughput proteomics. Proceedings of the National Academy of Sciences of the United States of America, 99 (23), 14652-14657. [Pg.59]

Many diseases are characterized by the expression of specific proteins1 in some cases, malignant cells yield unique protein profiles when total cellular protein extracts are analyzed by proteomic methods such as two-dimensional gel electrophoresis or matrix-assisted laser desorption ionization-mass spectrometry (MALDI-MS).2 High-throughput proteomic studies may be useful to differentiate normal cells from cancer cells, to identify and define the use of biomarkers for specific cancers, and to characterize the clinical course of disease. Proteomics can also be used to isolate and characterize potential drug targets and to evaluate the efficacy of treatments. [Pg.235]

Groseclose MR, Massion PP, Chaurand P, et al. High-throughput proteomic analysis of formalin-fixed paraffin-embedded tissue microarrays using MALDI imaging mass spectrometry. Proteomics 2008 8 3715-3724. [Pg.331]

High-throughput proteomic methods hold great promise for the discovery of novel protein biomarkers that can be translated into practical interventions for the diagnosis, treatment, and prevention of disease. These approaches may also facilitate the development of therapeutic agents that are targeted to specific molecular alterations in diseases such as cancer. In many cases, malignant cells yield unique protein profiles when total protein extracts from such cells are analyzed by 2-D gel electrophoresis or mass spectrometry (MS) methods. Such proteomic studies have the potential to provide an important complement to the analysis of DNA and mRNA extracts from these tissues.1... [Pg.335]

Lesley, S. 2001. High-throughput proteomics protein expression and purification in the post-genomic world. Protein Expression and Purification 22(2), 159-164. [Pg.104]

Belov ME, Anderson GA, Wingerd MA, et al. An automated high performance capillary liquid chromatography-Fourier transform ion cyclotron resonance mass spectrometer for high-throughput proteomics. J Am Soc Mass Spectrom 2004 15(2) 212-232. [Pg.182]

Doyle, S. A., Murphy, M. B., Massi, J. M., and Richardson, P. M. (2002) High-throughput proteomics a flexible and efficient pipeline for protein production. [Pg.121]

Figure 6 The SELDI technology. This type of proteomic analytical tool is a class of mass spectroscopy instrument that is useful in high-throughput proteomic fingerprinting of serum. Using a robotic sample dispenser, 1 p,L of serum is applied to the surface of a protein-binding chip. A subset of the proteins in the sample binds to the surface of the chip. The bound proteins are treated with a matrix-assisted laser desorption and ionization matrix and are washed and dried. The chip, which contains multiple patient samples, is inserted into a vacuum chamber where it is irradiated with a laser. The laser desorbs the adherent proteins and causes them to be launched as ions. The TOF of the ion before detection by an electrode is a measure of the mass-to-charge (m/z) value of the ion. The ion spectra can be analyzed by computer-assisted tools that classify a subset of the spectra by characteristic patterns of relative intensity (adapted from www.evmsdoctors.com). Figure 6 The SELDI technology. This type of proteomic analytical tool is a class of mass spectroscopy instrument that is useful in high-throughput proteomic fingerprinting of serum. Using a robotic sample dispenser, 1 p,L of serum is applied to the surface of a protein-binding chip. A subset of the proteins in the sample binds to the surface of the chip. The bound proteins are treated with a matrix-assisted laser desorption and ionization matrix and are washed and dried. The chip, which contains multiple patient samples, is inserted into a vacuum chamber where it is irradiated with a laser. The laser desorbs the adherent proteins and causes them to be launched as ions. The TOF of the ion before detection by an electrode is a measure of the mass-to-charge (m/z) value of the ion. The ion spectra can be analyzed by computer-assisted tools that classify a subset of the spectra by characteristic patterns of relative intensity (adapted from www.evmsdoctors.com).
Borrebaeck, C.A.K. and Wingren, C. 2007. High-throughput proteomics using antibody microarrays An update. Expert Rev Mol Diagn 7 673-686. [Pg.108]

High throughput proteome-wide predsion measurements of protein expression using mass spectrometry. [Pg.85]

Lee, H., Griffin, T.J., Gygi, S.P., Rist, B. and Aebersold, R. (2002) Development of a multiplexed microcapillary liquid chromatography system for high-throughput proteome analysis. Anal. Chem. 74, 4353-4360. [Pg.377]

Liao L, Pilotte J, Xu T, Wong CC, Edelman GM, et al. BDNF induces widespread changes in synaptic protein content and up-regulates components of the translation machinery an analysis using high-throughput proteomics. J. Proteome Res. 2007 6 1059-1071. [Pg.1236]

R.D. Smith, G.A. Anderson, M.S. Lipton, L. Pasa-Tolic, Y. Shen, T.P. Conrads, T.D. Veenstra, H.R. Udseth, An AMT strategy for quantitative and high-throughput proteome measurements, Proteomics, 2 (2002) 513. [Pg.515]

Wingren, C. Borrebaeck, C. A., High-throughput proteomics using antibody microarrays, Expert Rev. Proteomics 2004, 1, 355-364... [Pg.244]


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