Mapping Protein-Protein Interactions by Quantitative Proteomics

Publikation: Bidrag til tidsskriftTidsskriftartikelForskning

Resumé

Proteins exert their function inside a cell generally in multiprotein complexes. These complexes are highly dynamic structures changing their composition over time and cell state. The same protein may thereby fulfill different functions depending on its binding partners. Quantitative mass spectrometry (MS)-based proteomics in combination with affinity purification protocols has become the method of choice to map and track the dynamic changes in protein-protein interactions, including the ones occurring during cellular signaling events. Different quantitative MS strategies have been used to characterize protein interaction networks. In this chapter we describe in detail the use of stable isotope labeling by amino acids in cell culture (SILAC) for the quantitative analysis of stimulus-dependent dynamic protein interactions.
OriginalsprogEngelsk
TidsskriftMethods in Molecular Biology
Vol/bind658
Sider (fra-til)267-278
Antal sider12
ISSN1064-3745
DOI
StatusUdgivet - 2010

Fingeraftryk

Proteins
Isotope Labeling
Protein Interaction Maps
Amino Acids

Citer dette

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title = "Mapping Protein-Protein Interactions by Quantitative Proteomics",
abstract = "Proteins exert their function inside a cell generally in multiprotein complexes. These complexes are highly dynamic structures changing their composition over time and cell state. The same protein may thereby fulfill different functions depending on its binding partners. Quantitative mass spectrometry (MS)-based proteomics in combination with affinity purification protocols has become the method of choice to map and track the dynamic changes in protein-protein interactions, including the ones occurring during cellular signaling events. Different quantitative MS strategies have been used to characterize protein interaction networks. In this chapter we describe in detail the use of stable isotope labeling by amino acids in cell culture (SILAC) for the quantitative analysis of stimulus-dependent dynamic protein interactions.",
author = "Joern Dengjel and Irina Kratchmarova and Blagoy Blagoev",
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Mapping Protein-Protein Interactions by Quantitative Proteomics. / Dengjel, Joern; Kratchmarova, Irina; Blagoev, Blagoy.

I: Methods in Molecular Biology, Bind 658, 2010, s. 267-278.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskning

TY - JOUR

T1 - Mapping Protein-Protein Interactions by Quantitative Proteomics

AU - Dengjel, Joern

AU - Kratchmarova, Irina

AU - Blagoev, Blagoy

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N2 - Proteins exert their function inside a cell generally in multiprotein complexes. These complexes are highly dynamic structures changing their composition over time and cell state. The same protein may thereby fulfill different functions depending on its binding partners. Quantitative mass spectrometry (MS)-based proteomics in combination with affinity purification protocols has become the method of choice to map and track the dynamic changes in protein-protein interactions, including the ones occurring during cellular signaling events. Different quantitative MS strategies have been used to characterize protein interaction networks. In this chapter we describe in detail the use of stable isotope labeling by amino acids in cell culture (SILAC) for the quantitative analysis of stimulus-dependent dynamic protein interactions.

AB - Proteins exert their function inside a cell generally in multiprotein complexes. These complexes are highly dynamic structures changing their composition over time and cell state. The same protein may thereby fulfill different functions depending on its binding partners. Quantitative mass spectrometry (MS)-based proteomics in combination with affinity purification protocols has become the method of choice to map and track the dynamic changes in protein-protein interactions, including the ones occurring during cellular signaling events. Different quantitative MS strategies have been used to characterize protein interaction networks. In this chapter we describe in detail the use of stable isotope labeling by amino acids in cell culture (SILAC) for the quantitative analysis of stimulus-dependent dynamic protein interactions.

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DO - 10.1007/978-1-60761-780-8_16

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EP - 278

JO - Methods in Molecular Biology

JF - Methods in Molecular Biology

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