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Mass affinity selection

Regnier, F. E. Riggs, L. Zhang, R. Xiong, L. Liu, P. Chakraborty A. Seeley E. Sioma, C. Thompson, R. A. Comparative proteomics based on stable isotope labeling and affinity selection. J. Mass. Spectrom. 2002,37,133-145. [Pg.225]

Rhode, B.M., Hartmuth, K., Urlaub, H., and Liihrmann, R. (2003) Analysis of site-specific protein-RNA cross-links in isolated RNP complexes, combining affinity selection and mass spectrometry. RNA 9, 1542. [Pg.1107]

ALIS An Affinity Selection-Mass Spectrometry System for the Discovery and Characterization of Protein-Ligand Interactions... [Pg.121]

Kaur, S., McGuire, L., Tang, D., Dollinger, G., Heubner, V. Affinity selection and mass spectrometry-based strategies to identify lead compounds in combinatorial libraries. J. Prot. Chem. 1997, 16, 505-511. [Pg.152]

E. A. An affinity selection-mass spectrometry method for the identification of small molecule ligands from self-encoded combinatorial libraries, discovery of a novel antagonist of E. coli dihydrofolate reductase. Int. J. Mass. Spectrom. 2004, 238, 77-83. [Pg.154]

Several affinity screening methodologies that include MS-based readout and work under protein-excess conditions have been developed in the past decade [1]. Some examples include affinity selection/mass spectrometry (ASMS Abbott Labs [10]), size exclusion chromatography with LC-ESI-MS (see Chapter 2 and 3 [11-19]), the use of coupled or non-coupled pulsed ultra-filtration/mass spectrometry (summarized in this chapter [11, 20-23]), restricted access phase chromatography (see Chapter 5 [24, 25]), capillary electrophoresis [26, 27], target shift mass spectrometry [28], and multitarget affinity/specificity screening (MASS, see Chapter 10 [29, 30]). [Pg.162]

We have developed a high throughput ultrafiltration affinity screening method coupled to MS (affinity selection/mass spectrometry ASMS), which works with any soluble target and small molecule library (including natural products). ASMS is amenable to parallelization, efficient and robust enough to allow study... [Pg.163]

Annis A, Chuang C-C, Nazef N An affinity selection-mass spectrometry system for the discovery and characterization of protein-ligand interactions, chapter 3. [Pg.182]

For those readers who are not yet familiar with mass spectrometry, the introduction provides an explanation of the basics of mass spectrometry and its instrumentation as well as practical aspects and applications in bioanalysis. Next, a block of three chapters shows different affinity selection procedures suitable to identify hits from combinatorial compound libraries. This subject, being metaphorically speaking a search for a needle in a haystack, is of outstanding relevance for big pharma . The techniques described here offer real high throughput capabilities and are implemented already in the routine industrial screening... [Pg.460]

Annis, D. A., Nickbarg, E., Yang, X., Ziebell, M. R., Whitehurst, . E. (2007) Affinity selection-mass spectrometry screening techniques for small molecule drug discovery. Curr Opin Chem Biol 11, 518-526. [Pg.251]

Annis D.A., Athanasopoulos J., Curran P.J., Felsch J.S., Kalghatgi K., Lee W.H., Nash H.M., Orminati J.P.A., Rosner K.E., Shipps GW., Thaddupathy G.R.A., Tyler A.N., Vilenchik L., Wagner C.R., Wintner E.A., An affinity selection-mass spectrometry method for the identification of small molecule ligands from self-encoded combinatorial libraries. Discovery of a novel antagonist of E. coli dihydrofolate reductase Int. J. Mass Spectrom. 2004, 238, 77-83. [Pg.242]


See other pages where Mass affinity selection is mentioned: [Pg.298]    [Pg.1106]    [Pg.116]    [Pg.123]    [Pg.152]    [Pg.155]    [Pg.163]    [Pg.166]    [Pg.171]    [Pg.179]    [Pg.254]    [Pg.212]    [Pg.543]    [Pg.178]    [Pg.88]   
See also in sourсe #XX -- [ Pg.280 ]




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