R
Reza Vafabakhsh
Researcher at University of Illinois at Urbana–Champaign
Publications - 27
Citations - 3202
Reza Vafabakhsh is an academic researcher from University of Illinois at Urbana–Champaign. The author has contributed to research in topics: Medicine & G protein-coupled receptor. The author has an hindex of 13, co-authored 18 publications receiving 2640 citations. Previous affiliations of Reza Vafabakhsh include University of California, Berkeley & Northwestern University.
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Journal ArticleDOI
Self-motile colloidal particles: from directed propulsion to random walk.
Jonathan R. Howse,Richard A. L. Jones,Anthony J. Ryan,Tim Gough,Reza Vafabakhsh,Ramin Golestanian +5 more
TL;DR: The motion of an artificial microscale swimmer that uses a chemical reaction catalyzed on its own surface to achieve autonomous propulsion is fully characterized experimentally and suggests strategies for designing artificial chemotactic systems.
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Extreme Bendability of DNA Less than 100 Base Pairs Long Revealed by Single-Molecule Cyclization
TL;DR: A fluorescence-based, protein-free assay for studying the cyclization of single DNA molecules in real time, and finds significant looping, with the looping rate having only weak length dependence between 67 and 105 bp, which is inconsistent with the wormlike chain model.
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Antiparallel EmrE exports drugs by exchanging between asymmetric structures
Emma A. Morrison,Gregory T. DeKoster,Supratik Dutta,Reza Vafabakhsh,Michael W. Clarkson,Arjun Bahl,Dorothee Kern,Taekjip Ha,Katherine A. Henzler-Wildman +8 more
TL;DR: It is shown that asymmetric antiparallel EmrE exchanges between inward- and outward-facing states that are identical except that they have opposite orientation in the membrane are recorded.
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One influenza virus particle packages eight unique viral RNAs as shown by FISH analysis
TL;DR: The results support that the packaging of influenza viral genome is a selective process, with a high percentage of virus particles package all eight different segments of viral RNAs.
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Conformational dynamics of a class C G protein-coupled receptor
TL;DR: A general mechanism for the activation of mGluRs is supported, in which agonist binding induces closure of the LBDs, followed by dimer interface reorientation, which should be widely applicable to study conformational dynamics in GPCRs and other membrane proteins.