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Mass spectrometry–based targeted proteomics, our choice for Method of the Year 2012, is allowing biologists to follow sets of proteins with high sensitivity, reliability and quantitative accuracy. Cover design by Erin Dewalt. Special feature starts on p19.
By delivering precise, reproducible quantification of proteins of interest in biological samples, targeted proteomics approaches are allowing researchers to apply the scientific method using mass spectrometry.
A fully automated pipeline that systematically models three-dimensional (3D) structural details of protein interactions will allow researchers to interpret perturbation effects within protein pathways and networks.
Interactome3D is an interactive resource allowing biologists to use available structural information to model protein-protein interactions and structurally annotate protein interaction networks.
Improved mass spectrometry–based detection of low-abundance proteins in complex proteomes is made possible with a method to selectively digest and deplete high-abundance proteins.
A systematic evaluation of parameters that affect short amplicons sequenced on Illumina platforms provides guidelines for how to eliminate erroneous reads and improve data interpretation.
Open-source software that allows biologists to create a variety of behavior classifiers for automatically annotating video of behaving animals is presented. The program, called JAABA, uses state-of-the-art machine-learning methods and is applicable to tracking data from different organisms, including mice and adult and larval Drosophila.
A method is reported for optical trap calibration on lipid droplets in cell extract. It should permit quantitative studies of motor proteins in a more natural context than on beads.
The eXpress software uses an online algorithm to accurately assign ambiguously mapping sequence reads for real-time read abundance estimation, thereby dramatically enhancing the efficiency of any analysis that uses large-scale sequencing.
Human fibroblasts undergo conversion to angioblast-like progenitors and then to endothelial cells by brief exposure to pluripotency factors, which is then followed by differentiation.
Nature Methods' choice for Method of the Year 2012 is targeted proteomics. A collection of articles showcases how mass spectrometry technology is being developed and applied for targeted protein analysis in both basic and translational research.