scholarly journals Corrigendum: The Dihydrofolate Reductase Protein-Fragment Complementation Assay: A Survival-Selection Assay for Large-Scale Analysis of Protein–Protein Interactions

2022 ◽  
Vol 2022 (1) ◽  
pp. pdb.corr107812
Author(s):  
Stephen W. Michnick ◽  
Emmanuel D. Levy ◽  
Christian R. Landry ◽  
Jacqueline Kowarzyk ◽  
Vincent Messier
Keyword(s):  
Dihydrofolate Reductase ◽  
Protein Interactions ◽  
Large Scale ◽  
Scale Analysis ◽  
Protein Protein Interactions ◽  
Protein Fragment ◽  
Large Scale Analysis ◽  
Survival Selection ◽  
Protein Fragment Complementation ◽  
Protein Fragment Complementation Assay

scholarly journals Protein-fragment complementation assays for large-scale analysis of protein–protein interactions

2021 ◽  
Author(s):  
Ewa Blaszczak ◽  
Natalia Lazarewicz ◽  
Aswani Sudevan ◽  
Robert Wysocki ◽  
Gwenaël Rabut
Keyword(s):  
Protein Interactions ◽  
Drug Targets ◽  
Large Scale ◽  
Protein Protein Interactions ◽  
Protein Fragment ◽  
Ppi Networks ◽  
Large Scale Analysis ◽  
Cellular Environment ◽  
Protein Fragment Complementation ◽  
Fragment Complementation

Protein–protein interactions (PPIs) orchestrate nearly all biological processes. They are also considered attractive drug targets for treating many human diseases, including cancers and neurodegenerative disorders. Protein-fragment complementation assays (PCAs) provide a direct and straightforward way to study PPIs in living cells or multicellular organisms. Importantly, PCAs can be used to detect the interaction of proteins expressed at endogenous levels in their native cellular environment. In this review, we present the principle of PCAs and discuss some of their advantages and limitations. We describe their application in large-scale experiments to investigate PPI networks and to screen or profile PPI targeting compounds.

scholarly journals Reliable identification of protein-protein interactions by crosslinking mass spectrometry

2020 ◽  
Author(s):  
Swantje Lenz ◽  
Ludwig R. Sinn ◽  
Francis J. O’Reilly ◽  
Lutz Fischer ◽  
Fritz Wegner ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Protein Interactions ◽  
Large Scale ◽  
Protein Complexes ◽  
Estimation Procedure ◽  
Scale Analysis ◽  
Protein Protein Interactions ◽  
False Discovery ◽  
Large Scale Analysis ◽  
False Discovery Rate Estimation

Crosslinking mass spectrometry is widening its scope from structural analyzes of purified multi-protein complexes towards systems-wide analyzes of protein-protein interactions. Assessing the error in these large datasets is currently a challenge. Using a controlled large-scale analysis of Escherichia coli cell lysate, we demonstrate a reliable false-discovery rate estimation procedure for protein-protein interactions identified by crosslinking mass spectrometry.

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