Proteome-wide drug and metabolite interaction mapping by thermal-stability profiling

Nature Methods

Volumn 12, Issue 11, 2015, Pages 1055-1057

  Huber, Kilian V M ^a,c,d   Olek, Karin M ^a   Müller, André C ^a   Tan, Chris Soon Heng ^a,e,f   Bennett, Keiryn L ^a   Colinge, Jacques ^a,g   Superti Furga, Giulio ^a,b  

^a ERICH SCHMID INSTITUTE OF MATERIALS SCIENCE   (Austria)

^b MEDICAL UNIVERSITY OF VIENNA   (Austria)

^c UNIVERSITY OF OXFORD   (United Kingdom)

^d UNIVERSITY OF OXFORD   (United Kingdom)

^e INSTITUTE OF MOLECULAR AND CELL BIOLOGY   (Singapore)

^f INSTITUTE OF MEDICAL BIOLOGY   (Singapore)

^g UNIV MONTPELLIER   (France)

Author keywords

[No Author keywords available]

Indexed keywords

CRIZOTINIB; DIMETHYL SULFOXIDE; MEMBRANE PROTEIN; METHOTREXATE; PROTEIN STING; PROTEOME; UNCLASSIFIED DRUG; CARRIER PROTEIN; LIGAND; PROTEIN BINDING; PROTEIN KINASE INHIBITOR; PYRAZOLE DERIVATIVE; PYRIDINE DERIVATIVE;

ANIMAL CELL; CELLULAR DISTRIBUTION; CONTROLLED STUDY; LIGAND BINDING; MASS SPECTROMETRY; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN INTERACTION; PROTEIN STABILITY; REVIEW; SIGNAL TRANSDUCTION; THERMOSTABILITY; ANIMAL; BIOLOGY; CELL LINE; CHEMISTRY; DRUG DESIGN; HUMAN; IMMUNE SYSTEM; K-562 CELL LINE; METABOLISM; MOUSE; PROTEOMICS; SYSTEMS BIOLOGY; TEMPERATURE; TUMOR CELL LINE;

ANIMALS; CARRIER PROTEINS; CELL LINE; CELL LINE, TUMOR; COMPUTATIONAL BIOLOGY; DRUG DESIGN; HUMANS; IMMUNE SYSTEM; K562 CELLS; LIGANDS; MASS SPECTROMETRY; METHOTREXATE; MICE; PROTEIN BINDING; PROTEIN KINASE INHIBITORS; PROTEOME; PROTEOMICS; PYRAZOLES; PYRIDINES; SIGNAL TRANSDUCTION; SYSTEMS BIOLOGY; TEMPERATURE;

EID: 84946480594     PISSN: 15487091     EISSN: 15487105     Source Type: Journal    
DOI: 10.1038/nmeth.3590     Document Type: Review

References (23)

1. Lee, J. & Bogyo, M. Curr. Opin. Chem. Biol. 17, 118-126 (2013).
2. Kambe, T., Correia, B.E., Niphakis, M.J. & Cravatt, B.F. J. Am. Chem. Soc. 136, 10777-10782 (2014).
3. Huber, K.V.M et al. Nature 508, 222-227 (2014).
4. Feng, Y. et al. Nat. Biotechnol. 32, 1036-1044 (2014).
5. Lomenick, B. et al. Proc. Natl. Acad. Sci. USA 106, 21984-21989 (2009).
6. Niesen, F.H., Berglund, H. & Vedadi, M. Nat. Protoc. 2, 2212-2221 (2007).
7. Fedorov, O. et al. Proc. Natl. Acad. Sci. USA 104, 20523-20528 (2007).
8. Martinez Molina, D et al. Science 341, 84-87 (2013).
9. Savitski, M.M et al. Science 346, 1255784 (2014).
10. Gad, H et al. Nature 508, 215-221 (2014).
11. Dayon, L. et al. Anal. Chem. 80, 2921-2931 (2008).
12. Parlanti, E., Locatelli, G., Maga, G. & Dogliotti, E. Nucleic Acids Res. 35, 1569-1577 (2007).
13. Allegra, C.J. et al. J. Biol. Chem. 260, 9720-9726 (1985).
14. Ablasser, A. Et Al. Nature 498, 380-384 (2013).
15. Cai, X., Chiu, Y.-H. & Chen, Z.J. Mol. Cell 54, 289-296 (2014).
16. Lambert, J.-P. et al. Nat. Methods 10, 1239-1245 (2013).
17. Yoh, S.M Et Al. Cell 161, 1293-1305 (2015).
18. Gilar, M., Olivova, P., Daly, A.E. & Gebler, J.C. J. Sep. Sci. 28, 1694-1703 (2005).
19. Olsen, J.V. et al. Mol. Cell. Proteomics 4, 2010-2021 (2005).
20. Perkins, D.N., Pappin, D.J.C., Creasy, D.M & Cottrell, J.S. Electrophoresis 20, 3551-3567 (1999).
21. Colinge, J., Masselot, A., Giron, M., Dessingy, T. & Magnin, J. Proteomics 3, 1454-1463 (2003).
22. Burkard, T.R. et al. BMC Syst. Biol. 5, 17 (2011).
23. Breitwieser, F.P. et al. J. Prot. Res. 10, 2758-2766 (2011).