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- 저자 : Mohle, C. (검색결과 2 건)
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Local transport measurements in graphene on SiO<sub>2</sub> using Kelvin probe force microscopy
Willke, P.,Mohle, C.,Sinterhauf, A.,Kotzott, T.,Yu, H.K.,Wodtke, A.,Wenderoth, M. Pergamon Press ; Elsevier Science Ltd 2016 Carbon Vol.102 No.-
<P>By using Kelvin Probe Force Microscopy with an additional applied electric field we investigate the local voltage drop in graphene on SiO2 under ambient conditions. We are able to quantify the variation of the local sheet resistance and to resolve localized voltage drops at line defects. Our data demonstrates that the resistance of line defects has been overestimated so far. Moreover, we show that wrinkles have the largest resistance, rho(Wrinkle) < 80 Omega mu m. Temperature-dependent measurements show that the local monolayer sheet resistance reflects the macroscopic increase in resistance with temperature while the defect resistance for folded wrinkles is best described by a temperature-independent model which we attribute to interlayer tunneling. (C) 2016 Elsevier Ltd. All rights reserved.</P>
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Structural and Mechanistic Insights into the Tropism of Epstein-Barr Virus
Mohl, Britta S.,Chen, Jia,Sathiyamoorthy, Karthik,Jardetzky, Theodore S.,Longnecker, Richard Korean Society for Molecular and Cellular Biology 2016 Molecules and cells Vol.39 No.4
Epstein-Barr virus (EBV) is the prototypical ${\gamma}$-herpesvirus and an obligate human pathogen that infects mainly epithelial cells and B cells, which can result in malignancies. EBV infects these target cells by fusing with the viral and cellular lipid bilayer membranes using multiple viral factors and host receptor(s) thus exhibiting a unique complexity in its entry machinery. To enter epithelial cells, EBV requires minimally the conserved core fusion machinery comprised of the glycoproteins gH/gL acting as the receptor-binding complex and gB as the fusogen. EBV can enter B cells using gp42, which binds tightly to gH/gL and interacts with host HLA class II, activating fusion. Previously, we published the individual crystal structures of EBV entry factors, such as gH/gL and gp42, the EBV/host receptor complex, gp42/HLA-DR1, and the fusion protein EBV gB in a postfusion conformation, which allowed us to identify structural determinants and regions critical for receptor-binding and membrane fusion. Recently, we reported different low resolution models of the EBV B cell entry triggering complex (gHgL/gp42/HLA class II) in "open" and "closed" states based on negative-stain single particle electron microscopy, which provide further mechanistic insights. This review summarizes the current knowledge of these key players in EBV entry and how their structures impact receptor-binding and the triggering of gB-mediated fusion.
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