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Andrew D. Ellington
Researcher at University of Texas at Austin
Publications - 599
Citations - 48723
Andrew D. Ellington is an academic researcher from University of Texas at Austin. The author has contributed to research in topics: Aptamer & RNA. The author has an hindex of 96, co-authored 569 publications receiving 43262 citations. Previous affiliations of Andrew D. Ellington include Harvard University & UPRRP College of Natural Sciences.
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Journal ArticleDOI
Real-time sequence-validated loop-mediated isothermal amplification assays for detection of Middle East respiratory syndrome coronavirus (MERS-CoV).
Sanchita Bhadra,Yu Sherry Jiang,Mia R. Kumar,Reed F. Johnson,Lisa E. Hensley,Andrew D. Ellington +5 more
TL;DR: The asymmetric five-primer reverse transcription loop-mediated isothermal amplification (RT-LAMP) assays for detection of MERS-CoV will facilitate the development of portable point-of-care diagnostics that are crucial for management of emerging infections.
Book ChapterDOI
In vitro selection of nucleic acid aptamers that bind proteins.
TL;DR: Surprisingly, in vitro selection can also be used to isolate aptamers that can specifically interact, with proteins that are not normally thought to bind nucleic acids.
Journal ArticleDOI
Robust strand exchange reactions for the sequence-specific, real-time detection of nucleic acid amplicons.
TL;DR: Loop-mediated isothermal amplification of DNA is a powerful isothermal nucleic acid amplification method that can generate upward of 10(9) copies from less than 100 copies of template DNA within an hour, but real-time detection of different genes in multiplex LAMP reactions remains analytically challenging.
Journal ArticleDOI
Pattern transformation with DNA circuits
TL;DR: This work design and implement non-enzymatic DNA circuits capable of performing pattern transformation algorithms such as edge detection that will provide programmable platforms for prototyping CRNs, for discovering bottom-up construction principles, and for generating patterns in materials.
Journal ArticleDOI
Arginine-rich motifs present multiple interfaces for specific binding by RNA.
TL;DR: A model in which individual arginine residues govern binding to an RNA ligand is supported, and the inherent flexibility of the peptide backbone may make it possible for "semi-specific" recognition of a discreteSet of RNAs by a discrete set of ARM peptides and proteins.