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Ultrafast force-clamp spectroscopy characterizes load dependence of the interaction between a single bead-attached myosin molecule (structure at center) and an actin filament (long polymer). Optical traps (red cones) apply constant forces on the actin ends. Artistic rendering by Marco Capitanio. Article p1013
Parallel reaction monitoring (PRM)-based targeted mass spectrometry is comparable in performance to selected reaction monitoring (SRM) but requires much less investment in assay development for targeted proteomics applications.
A new high-throughput method for monitoring G protein–coupled receptor activation is highly suited to assaying Gα12/13-coupled receptors and is used to deorphanize a group of receptors activated by lysophosphatidylserine.
A high-resolution 4C-seq protocol involving two restriction digests and a revised analysis pipeline allows robust detection of physical interactions between regulatory DNA elements.
An integrated system composed of a microfluidic device, computer-vision tools and statistical methods for automatically handling, imaging, classifying and sorting C. elegans organisms is presented. The system performs automated screens of subcellular phenotypes and is used here to identify genes involved in synaptogenesis.
Removing phosphopantetheine-tagged labels from acyl carrier proteins (ACPs) and ACP fusion proteins contributes to a versatile labeling method in which tags can be iteratively swapped.
This paper reports genetic manipulation of the malaria parasite Plasmodium falciparum with zinc-finger nucleases. It demonstrates gene disruption as well as replacement and site-specific editing of both an integrated reporter and an endogenous gene.
Development of the bright green and red fluorescent proteins, Clover and mRuby2, creates a fluorescence resonance energy transfer (FRET) pair with the highest Förster radius among existing ratiometric FRET pairs. Substitution of this pair for current FRET pairs in several existing sensors reliably and substantially improves sensor performance.
A dual-trap force-clamp configuration is used to apply a constant load between a binding protein and a single intermittently interacting biological polymer. This allows high-resolution measurements of short-lived molecular complexes and reveals previously undetected complex regulation of the myosin working stroke.
A G protein–coupled receptor (GPCR) signaling assay based on ectodomain shedding of a membrane-bound proform of alkaline phosphatase-tagged TGFα provides a platform for studying poorly characterized Gα12/13-coupled GPCRs. The assay allowed identification of three orphan GPCRs as Gα12/13-coupled lysophosphatidylserine receptors.