Tracking and elucidating alphavirus host protein interactions
(1997) The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SH3 binding consensus sequence. Pineda-Lucena A, Ho CS, Mao DY, Sheng Y, Laister RC, et al.
(2005) A structure-based model of the c-Myc/Bin1 protein interaction shows alternative splicing of Bin1 and c-Myc phosphorylation are key binding determinants. Lastarza MW, Grakoui A, Rice CM (1994) Deletion and duplication mutations in the C-terminal nonconserved region of Sindbis virus ns P3: effects on phosphorylation and on virus replication in vertebrate and invertebrate cells. Masumi A, Aizaki H, Suzuki T, Du Hadaway JB, Prendergast GC, et al.
Although green fluorescent protein (GFP) has been widely applied for visualization of proteins, it has been relatively little used as a tool for the isolation of protein complexes.
Among the four non-structural proteins of alphaviruses the function of ns P3 is the least well understood.
Ns P3 is a component of the viral replication complex, and composed of a conserved aminoterminal macro domain implicated in viral RNA synthesis, and a poorly conserved carboxyterminal region.
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(2007) Role of the amphipathic peptide of Semliki forest virus replicase protein ns P1 in membrane association and virus replication. (2005) Reduction of hepatitis C virus NS5A phosphorylation through its interaction with amphiphysin II. Zech B, Kurtenbach A, Krieger N, Strand D, Blencke S, et al.(2003) Identification and characterization of amphiphysin II as a novel cellular interaction partner of the hepatitis C virus NS5A protein. Moradpour D, Gosert R, Egger D, Penin F, Blum HE, et al.Protein complexes mediate the majority of cellular processes.Knowledge of the localization and composition of such complexes provides key insights into their functions.Accepted for publication 29 September 2015 Published 1 December 2015 Volume 2015:7 Pages 57—66 DOI https://doi.org/10.2147/VAAT.Tags: Adult Dating, affair dating, sex dating