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Eric D. Smidansky

Researcher at Pennsylvania State University

Publications -  31
Citations -  2047

Eric D. Smidansky is an academic researcher from Pennsylvania State University. The author has contributed to research in topics: Polymerase & RNA. The author has an hindex of 22, co-authored 31 publications receiving 1935 citations. Previous affiliations of Eric D. Smidansky include Montana State University.

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Enhanced ADP-glucose pyrophosphorylase activity in wheat endosperm increases seed yield

TL;DR: Results indicate increased availability and utilization of resources in response to enhanced seed sink strength, increasing seed yield, and total plant biomass.
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Seed yield and plant biomass increases in rice are conferred by deregulation of endosperm ADP-glucose pyrophosphorylase.

TL;DR: Results demonstrate that deregulation of endosperm AGP increases overall plant sink strength, leading to larger, more productive plants in a manner similar to that in wheat having similar genetic modification.
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Nucleic acid polymerases use a general acid for nucleotidyl transfer.

TL;DR: The use of general acid catalysis by polymerases extends the mechanism of nucleotidyl transfer beyond that of the well-established two-metal-ion mechanism and permits manipulation of viral polymerase replication speed and/or fidelity for virus attenuation and vaccine development.
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Two proton transfers in the transition state for nucleotidyl transfer catalyzed by RNA- and DNA-dependent RNA and DNA polymerases

TL;DR: It is shown that nucleotidyl transfer depends on two ionizable groups with pKa values of 7.0 or 8.2 and 10.5, depending upon the divalent cation used in the reaction, and Interpretation of these data suggests the existence of a general base for deprotonation of the 3′-OH nucleophile, although use of a water molecule cannot be ruled out conclusively.
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Expression of wild-type pinB sequence in transgenic wheat complements a hard phenotype.

TL;DR: It is shown that the pinB-D1b alteration, common in hard textured wheats, can be complemented by the expression of wild-type pinB -D1a in transformed plants, indicating that thePinB-C1a alteration is most likely the causative Ha mutation in the majority of hard wheats.