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Richard C. Stevens

Researcher at Merck & Co.

Publications -  19
Citations -  1774

Richard C. Stevens is an academic researcher from Merck & Co.. The author has contributed to research in topics: Biosensor & Analyte. The author has an hindex of 15, co-authored 19 publications receiving 1617 citations. Previous affiliations of Richard C. Stevens include University of Washington.

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A quantitative atlas of polyadenylation in five mammals

TL;DR: PolyA-seq is shown to be as accurate as existing RNA sequencing approaches for digital gene expression (DGE), enabling simultaneous mapping of polyA sites and quantitative measurement of their usage, and usage is more similar within the same tissues across different species than within a species.
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Surface plasmon resonance detection using antibody-linked magnetic nanoparticles for analyte capture, purification, concentration, and signal amplification.

TL;DR: A method for rapid purification, concentration, and detection of target analytes from complex matrixes using antibody-coated superparamagnetic nanobeads (immunomagnetic beads, or IMBs), which dramatically increased the surface plasmon resonance (SPR) detection signal from staphylococcal enterotoxin B (SEB).
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Detection of cortisol in saliva with a flow-filtered, portable surface plasmon resonance biosensor system.

TL;DR: The development of a portable surface plasmon resonance (SPR) biosensor system for detection of cortisol in saliva that is sufficiently sensitive for clinical use and useful for a wide range of applications where small molecular weight analytes are found in complex matrixes.
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Mlc1p is a light chain for the unconventional myosin Myo2p in Saccharomyces cerevisiae.

TL;DR: Surprisingly, precise deletion of the six IQ sites in the neck region results in a myosin that can support the growth of a yeast strain at 90% the rate of a wild-type isogenic strain and suggests that MLC1p is responsible for stabilizing this myo2p by binding to the necks region.
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The unconventional myosin, Myo2p, is a calmodulin target at sites of cell growth in Saccharomyces cerevisiae

TL;DR: A genetic analysis indicates that mutations in CMD1 show allele- specific synthetic lethality with the myo2-66 conditional mutation, and four lines of evidence suggest that Myo2p is a target of calmodulin at sites of cell growth, and the interaction between Myo-2p and cal modulin is Ca2+ independent.