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PROPERTIES OF HURWITZ POLYNOMIAL AND HURWITZ SERIES RINGS
Elliott, Jesse,Kim, Hwankoo Korean Mathematical Society 2018 대한수학회보 Vol.55 No.3
In this paper, we study the closedness such as seminomality and t-closedness, and Noetherian-like properties such as piecewise Noetherianness and Noetherian spectrum, of Hurwitz polynomial rings and Hurwitz series rings. To do so, we construct an isomorphism between a Hurwitz polynomial ring (resp., a Hurwitz series ring) and a factor ring of a polynomial ring (resp., a power series ring) in a countably infinite number of indeterminates.
Elliott, Paul ,R.,Irvine, Andrew ,F.,Jung, Hyun ,Suk,Tozawa, Kaeko,Pastok, Martyna ,W.,Picone, Remigio,Badyal, Sandip ,K.,Basran, Jaswir,Rudland, Philip ,S.,Barraclough, Roger Cell Press 2012 Structure Vol.20 No.4
<P><B>Summary</B></P><P>Filament assembly of nonmuscle myosin IIA (NMIIA) is selectively regulated by the small Ca<SUP>2+</SUP>-binding protein, S100A4, which causes enhanced cell migration and metastasis in certain cancers. Our NMR structure shows that an S100A4 dimer binds to a single myosin heavy chain in an asymmetrical configuration. NMIIA in the complex forms a continuous helix that stretches across the surface of S100A4 and engages the Ca<SUP>2+</SUP>-dependent binding sites of each subunit in the dimer. Synergy between these sites leads to a very tight association (K<SUB>D</SUB> ∼1 nM) that is unique in the S100 family. Single-residue mutations that remove this synergy weaken binding and ameliorate the effects of S100A4 on NMIIA filament assembly and cell spreading in A431 human epithelial carcinoma cells. We propose a model for NMIIA filament disassembly by S100A4 in which initial binding to the unstructured NMIIA tail initiates unzipping of the coiled coil and disruption of filament packing.</P>