Search results for "Dimerization"
showing 3 items of 143 documents
Solvatochromic behaviour of new donor–acceptor oligothiophenes
2021
Oligothiophene derivatives play a central role in the formulation of materials used in devices in the field of organic electronics. In this work, we report the results of the study of UV-vis absorption and fluorescence spectra, in several solvents, of a series of oligothiophenes recently synthesized in our laboratory. The studied oligothiophenes present different structures due to several factors: the donor– acceptor (D–A) or acceptor–donor–acceptor (A–D–A) architecture, the number of thiophene rings in the backbone (ranging from three to eight), the number and position of solubilizing octyl chains in the backbone, and the type of acceptor moieties (from Knoevenagel condensation either with…
Rac1 and PAK1 are upstream of IKK-ε and TBK-1 in the viral activation of interferon regulatory factor-3
2004
The anti-viral type I interferon (IFN) response is initiated by the immediate induction of IFN beta, which is mainly controlled by the IFN-regulatory factor-3 (IRF-3). The signaling pathways mediating viral IRF-3 activation are only poorly defined. We show that the Rho GTPase Rac1 is activated upon virus infection and controls IRF-3 phosphorylation and activity. Inhibition of Rac1 leads to reduced IFN beta promoter activity and to enhanced virus production. As a downstream mediator of Rac signaling towards IRF-3, we have identified the kinase p21-activated kinase (PAK1). Furthermore, both Rac1 and PAK1 regulate the recently described IRF-3 activators, I kappa B kinase- and TANK-binding kina…
Lipid Binding Controls Dimerization of the Coat Protein p24 Transmembrane Helix
2019
Abstract Coat protein (COP) I and COP II complexes are involved in the transport of proteins between the endoplasmic reticulum and the Golgi apparatus in eukaryotic cells. The formation of COP I/II complexes at membrane surfaces is an early step in vesicle formation and is mastered by p24, a type I transmembrane protein. Oligomerization of p24 monomers was suggested to be mediated and/or stabilized via interactions within the transmembrane domain, and the p24 transmembrane helix appears to selectively bind a single sphingomyelin C18:0 molecule. Furthermore, a potential cholesterol-binding sequence has also been predicted in the p24 transmembrane domain. Thus, sphingomyelin and/or cholestero…