Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC)
Methods and Protocols
(Sprache: Englisch)
Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC): Methods and Protocols provides a synopsis of a large array of different SILAC methods by presenting a set of protocols that have been established by renowned scientists and their working...
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Klappentext zu „Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC) “
Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC): Methods and Protocols provides a synopsis of a large array of different SILAC methods by presenting a set of protocols that have been established by renowned scientists and their working groups. These include methods and protocols for the labeling of various model organisms as well as advanced strategies relying on SILAC, e.g. for the analysis of protein interactions, the mapping of posttranslational modifications or the characterization of subcellular proteomes. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by step, readily reproducible laboratory protocols, and key tips on troubleshooting and avoiding known pitfalls.Authoritative and practical, Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC): Methods and Protocols will serve students and experienced scientists alike as a valuable reference of how to make use of the SILAC technology for their own research.
Inhaltsverzeichnis zu „Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC) “
1. Twelve Years of Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC)Matthias Mann
2. Stable Isotope Labeling by Amino Acids Applied to Bacterial Cell Culture
Boumediene Soufi and Boris Macek
3. SILAC Labeling of Yeast for the Study of Membrane Protein Complexes
Silke Oeljeklaus, Andreas Schummer, Ida Suppanz, and Bettina Warscheid
4. Whole Proteome Analysis of the Protozoan Parasite Trypanosoma brucei using Stable Isotope Labeling by Amino Acids in Cell Culture and Mass Spectrometry
Olivera Cirovic and Torsten Ochsenreiter
5. Stable Isotope Labeling by Amino Acids in Cultured Primary Neurons
Guoan Zhang, Katrin Deinhardt, and Thomas A. Neubert
6. SILAC and Alternatives in Studying Cellular Proteomes of Plants
Annemarie Matthes, Karin Köhl, and Waltraud Schulze
7. In Vivo Stable Isotope Labeling by Amino Acids in Drosophila melanogaster
Matthias D. Sury, Jia-Xuan Chen, and Matthias Selbach
8. Stable Isotope Labeling for Proteomic Analysis of Tissues in Mouse
Aaron Ruhs, Soraya Hölper, and Marcus Krüger
9. Identification of Novel Protein Functions and Signaling Mechanisms by Genetics and Quantitative Phosphoproteomics in Caenorhabditis elegans
Julius Fredens, Kasper Engholm-Keller, Jakob Møller-Jensen, Martin Røssel Larsen, and Nils J. Færgeman
10. SILAC-based Temporal Phosphoproteomics
Chiara Francavilla, Omid Hekmat, Blagoy Blagoev, and Jesper V. Olsen
11. Global Ubiquitination Analysis by SILAC in Mammalian Cells
Zhiping Wu, Chan Hyun Na, Haiyan Tan, and Junmin Peng
12. Quantifying In Vivo, Site-specific Changes in Protein Methylation with SILAC
Ho-Tak Lau, Karen A. Lewis, and Shao-En Ong
13. Applying SILAC for the Differential Analysis of Protein Complexes
Karsten Boldt, Christian J. Gloeckner, Yves Texier, Felix von Zweydorf, and Marius Ueffing
14. Defining Dynamic Protein Interactions Using SILAC-based Quantitative Mass spectrometry
Xiaorong Wang and Lan Huang
15. Identifying Nuclear
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Protein-Protein Interactions using GFP Affinity Purification and SILAC-based Quantitative Mass Spectrometry
H. Irem Baymaz, Cornelia G. Spruijt, and Michiel Vermeulen
16. Analyzing the Protein Assembly and Dynamics of the Human Spliceosome with SILAC
Carla Schmidt, Monika Raabe, Reinhard Lührmann, and Henning Urlaub
17. Identification and Validation of Protein-Protein Interactions by Combining Co-immunoprecipitation, Antigen Competition, and Stable Isotope Labeling
Frederik Sommer, Timo Mühlhaus, Dorothea Hemme, Daniel Veyel, and Michael Schroda
18. Protein Correlation Profiling-SILAC to Study Protein-Protein Interactions
Anders R. Kristensen and Leonard J. Foster
19. Autophagosomal Proteome Analysis by Protein Correlation Profiling-SILAC
Andrea C. Becker and Jörn Dengjel
20. Design and Application of Super-SILAC for Proteome Quantification
Yair Pozniak and Tamar Geiger
21. Proteomics Meets Genetics: SILAC Labeling of Drosophila melanogaster Larvae and Cells for In Vivo Functional Studies
Alessandro Cuomo, Roberta Sanfilippo, Thomas Vaccari, and Tiziana Bonaldi
22. Analysis of Secreted Proteins using SILAC
Jeanette Henningsen, Blagoy Blagoev, and Irina Kratchmarova
23. Identification of MicroRNA Targets by Pulsed SILAC
Markus Kaller, Silke Oeljeklaus, Bettina Warscheid, and Heiko Hermeking
24. MaxQuant for In-Depth Analysis of Large SILAC Datasets
Stefka Tyanova, Matthias Mann, and Juergen Cox
H. Irem Baymaz, Cornelia G. Spruijt, and Michiel Vermeulen
16. Analyzing the Protein Assembly and Dynamics of the Human Spliceosome with SILAC
Carla Schmidt, Monika Raabe, Reinhard Lührmann, and Henning Urlaub
17. Identification and Validation of Protein-Protein Interactions by Combining Co-immunoprecipitation, Antigen Competition, and Stable Isotope Labeling
Frederik Sommer, Timo Mühlhaus, Dorothea Hemme, Daniel Veyel, and Michael Schroda
18. Protein Correlation Profiling-SILAC to Study Protein-Protein Interactions
Anders R. Kristensen and Leonard J. Foster
19. Autophagosomal Proteome Analysis by Protein Correlation Profiling-SILAC
Andrea C. Becker and Jörn Dengjel
20. Design and Application of Super-SILAC for Proteome Quantification
Yair Pozniak and Tamar Geiger
21. Proteomics Meets Genetics: SILAC Labeling of Drosophila melanogaster Larvae and Cells for In Vivo Functional Studies
Alessandro Cuomo, Roberta Sanfilippo, Thomas Vaccari, and Tiziana Bonaldi
22. Analysis of Secreted Proteins using SILAC
Jeanette Henningsen, Blagoy Blagoev, and Irina Kratchmarova
23. Identification of MicroRNA Targets by Pulsed SILAC
Markus Kaller, Silke Oeljeklaus, Bettina Warscheid, and Heiko Hermeking
24. MaxQuant for In-Depth Analysis of Large SILAC Datasets
Stefka Tyanova, Matthias Mann, and Juergen Cox
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Bibliographische Angaben
- 2014, 2014, XIV, 372 Seiten, 27 farbige Abbildungen, Maße: 18,3 x 26,3 cm, Gebunden, Englisch
- Herausgegeben: Bettina Warscheid
- Verlag: Springer, Berlin
- ISBN-10: 1493911414
- ISBN-13: 9781493911417
Sprache:
Englisch
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