Characterization of Nested Complexes in Protein Interaction Networks

2014 ◽  
Author(s):  
Nazar Zaki ◽  
Antonio Mora
Keyword(s):  
Protein Interaction ◽  
Protein Interaction Networks ◽  
Interaction Networks

scholarly journals Characterization of protein-interaction networks in tumors

2007 ◽  
Vol 8 (1) ◽  
pp. 224 ◽  
Author(s):  
Alexander Platzer ◽  
Paul Perco ◽  
Arno Lukas ◽  
Bernd Mayer
Keyword(s):  
Protein Interaction ◽  
Protein Interaction Networks ◽  
Interaction Networks

Characterization of RNA-Protein Interaction Networks in Acute Leukemias

2020 ◽  
Author(s):  
K Schuschel ◽  
M Helwig ◽  
E Regényi ◽  
ML Yaspo ◽  
D Heckl ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Protein Interaction Networks ◽  
Interaction Networks ◽  
Acute Leukemias

scholarly journals Prediction and characterization of protein-protein interaction networks in swine

2012 ◽  
Vol 10 (1) ◽  
pp. 2 ◽  
Author(s):  
Fen Wang ◽  
Min Liu ◽  
Baoxing Song ◽  
Dengyun Li ◽  
Huimin Pei ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Protein Interaction Networks ◽  
Interaction Networks ◽  
Protein Protein Interaction ◽  
Protein Protein Interaction Networks

scholarly journals High-throughput characterization of protein–protein interactions by reprogramming yeast mating

2017 ◽  
Vol 114 (46) ◽  
pp. 12166-12171 ◽  
Author(s):  
David Younger ◽  
Stephanie Berger ◽  
David Baker ◽  
Eric Klavins
Keyword(s):  
High Throughput ◽  
Protein Interaction ◽  
Protein Interactions ◽  
Binding Proteins ◽  
Protein Interaction Networks ◽  
Interaction Networks ◽  
Protein Protein Interactions ◽  
Mating Efficiency ◽  
Extracellular Environment

High-throughput methods for screening protein–protein interactions enable the rapid characterization of engineered binding proteins and interaction networks. While existing approaches are powerful, none allow quantitative library-on-library characterization of protein interactions in a modifiable extracellular environment. Here, we show that sexual agglutination ofSaccharomyces cerevisiaecan be reprogrammed to link interaction strength with mating efficiency using synthetic agglutination (SynAg). Validation of SynAg with 89 previously characterized interactions shows a log-linear relationship between mating efficiency and protein binding strength for interactions withKds ranging from below 500 pM to above 300 μM. Using induced chromosomal translocation to pair barcodes representing binding proteins, thousands of distinct interactions can be screened in a single pot. We demonstrate the ability to characterize protein interaction networks in a modifiable environment by introducing a soluble peptide that selectively disrupts a subset of interactions in a representative network by up to 800-fold. SynAg enables the high-throughput, quantitative characterization of protein–protein interaction networks in a fully defined extracellular environment at a library-on-library scale.

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