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Deconvolution of Targeted Protein–Protein Interaction Maps

Journal of Proteome Research, 2012
Current proteomic techniques allow researchers to analyze chosen biological pathways or an ensemble of related protein complexes at a global level via the measure of physical protein-protein interactions by affinity purification mass spectrometry (AP-MS). Such experiments yield information-rich but complex interaction maps whose unbiased interpretation
Alexey, Stukalov   +2 more
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Mapping Protein–Protein Interactions by Quantitative Proteomics

2010
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.
Dengjel, Jörn   +2 more
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Protein interaction maps on the fly

Nature Biotechnology, 2004
A protein interaction map for the fruit fly Drosophila melanogaster promises to facilitate functional analysis of many eukaryotic proteins.
Uetz, P., Pankratz, M. J.
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Mapping of RNA–protein interactions

Analytica Chimica Acta, 2009
RNA-protein interactions are important biological events that perform multiple functions in all living organisms. The wide range of RNA interactions demands diverse conformations to provide contacts for the selective recognition of proteins. Various analytical procedures are presently available for quantitative analyses of RNA-protein complexes, but ...
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Protein interaction maps for model organisms

Nature Reviews Molecular Cell Biology, 2001
Until recently, classical genetics and biochemistry were the main techniques used to investigate how organisms develop, reproduce, behave and age. But with the availability of complete genome sequences new approaches are emerging. Complete sets of proteins — 'proteomes' — can be predicted from genome sequences and used to characterize protein functions
A J, Walhout, M, Vidal
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Mapping protein–protein interactions with combinatorial biology methods

Current Opinion in Biotechnology, 2001
Extremely diverse, DNA-encoded libraries of peptides and proteins have been constructed that include a linkage between each polypeptide and the encoding DNA. Library members can be selected by virtue of a particular binding specificity, and their protein sequence can be deduced from the sequence of the cognate DNA.
J, Pelletier, S, Sidhu
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Novel approaches to map protein interactions

Current Opinion in Biotechnology, 2003
Although we now have the sequence of the human genome at hand, we face the challenge of assigning function to the identified genes. Genes usually ascribe their function through proteins, and the role of proteins is to interact with other molecules. Therefore, if we could map the interactions of proteins we would be able to understand protein function ...
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The protein–protein interaction map of Helicobacter pylori

Nature, 2001
With the availability of complete DNA sequences for many prokaryotic and eukaryotic genomes, and soon for the human genome itself, it is important to develop reliable proteome-wide approaches for a better understanding of protein function. As elementary constituents of cellular protein complexes and pathways, protein-protein interactions are key ...
J C, Rain   +12 more
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Transcriptome-Wide Mapping of Protein–RNA Interactions

2020
RNA and RNA-binding proteins (RBPs) control multiple biological processes. The spatial and temporal arrangement of RNAs and RBPs underlies the delicate regulation of these processes. The strategy called CLIP-seq (cross-linking and immunoprecipitation) has been developed to capture endogenous protein-RNA interactions with UV cross-linking followed by ...
Xianju, Bi, Xiaohua, Shen
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Proteolytic DNA for Mapping Protein−DNA Interactions

Biochemistry, 2002
We describe a technique to determine sites on proteins involved in protein-DNA interactions. DNA was synthesized via polymerase chain reaction (PCR) to produce four polynucleotide products with phosphorothioate nucleotides at the A, T, G, or C residues.
Brian D, Schmidt, Claude F, Meares
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