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The ORF4a protein of human coronavirus 229E functions as a viroporin that regulates viral production
Autor:
Kai Wang, Ronghua Zhang, Ke Xu, Wei Lv, Wolfgang Schwarz, Sidong Xiong, Wenjing Yu, Bing Sun, Shiqi Xie
Publikováno v:
Biochimica et Biophysica Acta. Biomembranes
In addition to a set of canonical genes, coronaviruses encode additional accessory proteins. A locus located between the spike and envelope genes is conserved in all coronaviruses and contains a complete or truncated open reading frame (ORF). Previou
Autor:
Helen M. Becker, Elangovan Gopal, Vadivel Ganapathy, Sudha Ananth, Carsten A. Wagner, Nagavedi S. Umapathy, Jaya P. Gnana-Prakasam, Puttur D. Prasad, Pamela M. Martin
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. (11):2690-2697
Recently, we cloned two Na+-coupled lactate transporters from mouse kidney, a high-affinity transporter (SMCT1 or slc5a8) and a low-affinity transporter (SMCT2 or slc5a12). Here we report on the cloning and functional characterization of human SMCT2
Autor:
Henry M. Colecraft, Tingting Yang
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. (7):1644-1654
RGK proteins belong to the Ras superfamily of monomeric G-proteins, and currently include four members - Rad, Rem, Rem2, and Gem/Kir. RGK proteins are broadly expressed, and are the most potent known intracellular inhibitors of high-voltage-activated
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. (4):1091-1099
Genetically encoded FRET glucose nanosensors have proven to be useful for imaging glucose flux in HepG2 cells. However, the dynamic range of the original sensor was limited and thus it did not appear optimal for high throughput screening of siRNA pop
Autor:
Jonathan Bandong, Rosemarie Vithayathil, Gabriel O. Moreno, Katherine M. Chrunyk, Melanie J. Cocco, Ali Alhoshani, Gregory A. Weiss
Publikováno v:
Alhoshani, A; Vithayathil, R; Bandong, J; Chrunyk, KM; Moreno, GO; Weiss, GA; et al.(2014). Glutamate provides a key structural contact between reticulon-4 (Nogo-66) and phosphocholine. Biochimica et Biophysica Acta-Biomembranes, 1838(9), 2350-2356. doi: 10.1016/j.bbamem.2014.05.021. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/4td8v2r3
Human reticulon 4 (RTN-4) has been identified as the neurite outgrowth inhibitor (Nogo). This protein contains a span of 66 amino acids (Nogo-66) flanked by two membrane helices at the C-terminus. We previously determined the NMR structure of Nogo-66
Autor:
Alexander I. Greenwood, Stephanie Tristram-Nagle, Richard M. Epand, John F. Nagle, Thalia T. Mills, Jianjun Pan
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. (4):1120-1130
This study uses low-angle (LAXS) and wide-angle (WAXS) X-ray synchrotron scattering, volume measurements and thin layer chromatography to determine the structure and interactions of SOPC, SOPC/cholesterol mixtures, SOPC/peptide and SOPC/cholesterol/p
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. (9):1804-1812
Helix–helix interactions in the putative three-helix bundle formation of the gp41 transmembrane (TM) domain may contribute to the process of virus–cell membrane fusion in HIV-1 infection. In this study, molecular dynamics is used to analyze and c
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. (2):538-546
Recent controversies associated with the structure of the M2 protein from influenza A virus and the binding site of drug molecules amantadine and rimantadine motivated the comparison here of the drug binding to three viral porins including the M2 pro
Autor:
Steven S. Scherer, Charles K. Abrams
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. (8):2030-2047
CNS glia and neurons express connexins, the proteins that form gap junctions in vertebrates. We review the connexins expressed by oligodendrocytes and astrocytes, and discuss their proposed physiologic roles. Of the 21 members of the human connexin f
Publikováno v:
Biochimica et Biophysica Acta. Biomembranes
In order to complete the fusion process of SARS-CoV virus, several regions of the S2 virus envelope glycoprotein are necessary. Recent studies have identified three membrane-active regions in the S2 domain of SARS-CoV glycoprotein, one situated downs