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Andrew J. Fisher

Researcher at University of California, Davis

Publications -  89
Citations -  4421

Andrew J. Fisher is an academic researcher from University of California, Davis. The author has contributed to research in topics: Active site & RNA. The author has an hindex of 29, co-authored 89 publications receiving 3999 citations. Previous affiliations of Andrew J. Fisher include Purdue University & University College West.

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Small-bandgap endohedral metallofullerenes in high yield and purity

TL;DR: In this article, a new family of stable endohedral fullerenes encapsulating trimetallic nitride clusters, ErxSc3-xN@C80 (x = 0-3), was synthesized.
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X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-.

TL;DR: The three-dimensional structures of the truncated myosin head from Dictyostelium discoideumMyosin II complexed with beryllium and aluminum fluoride and magnesium ADP are reported at 2.0 and 2.6 A resolution, respectively.
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Ordered duplex RNA controls capsid architecture in an icosahedral animal virus.

TL;DR: The X-ray structure of Flock House virus is reported, which reveals an ordered RNA duplex of 20 nucleotides and a protein segment that control the subunit interactions in this animal virus, indicating that RNA associated with the cleaved polypeptide may be important in the infection process.
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Structures of human ADAR2 bound to dsRNA reveal base-flipping mechanism and basis for site selectivity.

TL;DR: These structures, together with structure-guided mutagenesis and RNA-modification experiments, explain the basis of the ADAR deaminase domain's dsRNA specificity, its base-flipping mechanism, and its nearest-neighbor preferences, and provide a structural framework for understanding the effects of ADAR mutations associated with human disease.
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Functional implications of quasi-equivalence in a T=3 icosahedral animal virus established by cryo-electron microscopy and X-ray crystallography

TL;DR: A model for nodavirus infection is proposed that is conceptually similar to that proposed for poliovirus but differs from it in detail, including the constraints of a single protein type in the capsid.