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In many designs, a low supply voltage is selected for efficient use of power. However, this often leads to low reverse-isolation which is critical to the RF front-end circuits and particularly to the low-noise amplifier (LNA). In this letter, a fully integrated differential low-voltage CMOS LNA with high reverse-isolation is presented. This LNA makes use of the single-stage noncascode structure and the capacitive cross-coupling (CCC) technique. The CCC technique has been utilized in many LNA designs. However, in all of the reported works using CCC, the CCC technique was mainly used to improve the noise figure (NF), not the reverse-isolation. The poor reverse-isolation problem in single-stage noncascode structure has never been analyzed in the capacitive cross-coupling cascaded low noise amplifier (CCCLNA). This work shows a novel analysis on the feedback self-cancellation mechanism to improve the reverse-isolation. Other analyses on input matching, gain and NF were also performed to show the feasibility of using CCC technique for the low-voltage LNA as well as the advantages of the CCCLNA over the conventional common-source and common-gate (CG) LNA. The LNA consumes only 0.5 mW from 0.6 V supply voltage. It achieves a gain of 14 dB and a NF of 3.55 dB. © 2011 Wiley Periodicals, Inc. Microwave Opt Technol Lett, 54:374-379, 2012; View this article online at wileyonlinelibrary.com. DOI 10.1002/mop.26542 [ABSTRACT FROM AUTHOR]

The original version of this article unfortunately contained a mistake. The legends of Tables 2 and 3, Fig. 1 are incorrect. The corrected legends are given below, [ABSTRACT FROM AUTHOR]

Since interleukin-8 (IL-8/CXCL8) and its receptor, CXCR1 and CXCR2, were known in the early 1990s, biological pathways related to these proteins were proven to have high clinical value in cancer and inflammatory/autoimmune conditions treatment. Recently, IL-8 has been identified as biomarker for severe COVID-19 patients and COVID-19 prognosis. Boyles et al. (mAbs 12 (2020), pp. 1831880) have published a high-resolution X-ray crystal structure of the LY3041658 Fab in a complex human CXCL8. They described the ability to bind to IL-8 and the blocking of IL-8/its receptors interaction by the LY3041658 monoclonal antibody. Therefore, the study has been designed to identify potential small molecules inhibiting interleukin-8 by targeting LY3041658/IL-8 complex structure using an in silico approach. A structure‑based pharmacophore and molecular docking models of the protein active site cavity were generated to identify possible candidates, followed by virtual screening with the ZINC database. ADME analysis of hit compounds was also conducted. Molecular dynamics simulations were then performed to survey the behaviour and stability of the ligand-protein complexes. Furthermore, the MM/PBSA technique has been utilized to evaluate the free binding energy. The final data confirmed that one newly obtained compound, ZINC21882765, may serve as the best potential inhibitor for IL-8.