Authors : PERCY W. HAWKES, DVM, Regulatory Consultant, Retired Foreign Service Diplomat for USDA (APHIS) Read the article in PDF

Authors: Percy William Hawkes Read the publication in PDF

The structure of BPSL1549, a protein of unknown function from Burkholderia pseudomallei reveals a similarity to E. coli cytotoxic necrotizing factor 1. We found that BPSL1549 acted as a potent cytotoxin against eukaryotic cells and was lethal when administered to mice. Expression levels of bpsl1549 correlate with conditions expected to promote or suppress pathogenicity. BPSL1549 promotes deamidation of Gln of the translation initiation factor eIF4A, abolishing its helicase activity and inhibiting translation. We propose to name BPSL1549 Burkholderia Lethal Factor 1 (BLF1). More informations.   Authors : Abimael Cruz, Guillaume M. Hautbergue, Peter J. Artymiuk, Patrick J. Baker, Monika Bokori-Brown, Chung-Te Chang, Mark J. Dickman, Angela Essex-Lopresti, Sarah V. Harding, Nor Muhammad Mahadi, Laura E. Marshall, Rahmah Mohamed,…

Authors:Stefanie V. Schütz, Andres J. Schrader, Friedemann Zengerling, Felicitas Genze, Marcus V. Cronauer, Mark Schrader   In order to generate genomic signals, the androgen receptor (AR) has to be transported into the nucleus upon androgenic stimuli. However, there is evidence from in vitro experiments that in castration-resistant prostate cancer (CRPC) cells the AR is able to translocate into the nucleus in a ligand-independent manner. The recent finding that inhibition of the glycogen-synthase-kinase 3β (GSK-3β) induces a rapid nuclear export of the AR in androgen-stimulated prostate cancer cells prompted us to analyze the effects of a GSK-3β inhibition in the castration-resistant LNCaP sublines C4-2 and LNCaP-SSR. Both cell lines exhibit high levels of…

Authors:Bohuslav Rezek, Marie Krátká, Egor Ukraintsev, Oleg Babchenko, Alexander Kromka, Antonín Brož and Marie Kalbacova   Read the publication in PDF

Authors Kenta Saito, Noriyuki Hatsugai, Kazuki Horikawa, Kentaro Kobayashi, Toru Matsu-ura, Katsuhiko Mikoshiba, Takeharu Nagai   BackgroundEfficient bioluminescence resonance energy transfer (BRET) from a bioluminescent protein to a fluorescent protein with high fluorescent quantum yield has been utilized to enhance luminescence intensity, allowing single-cell imaging in near real time without external light illumination.   Methodology/Principal FindingsWe applied BRET to develop an autoluminescent Ca2+ indicator, BRAC, which is composed of Ca2+-binding protein, calmodulin, and its target peptide, M13, sandwiched between a yellow fluorescent protein variant, Venus, and an enhanced Renilla luciferase, RLuc8. Adjusting the relative dipole orientation of the luminescent protein’s chromophores improved the dynamic range of BRET signal change in…