TY  - JOUR
A1  - Zaho, Huaying
A1  - Ghirlando, Rodolfo
A1  - Alfonso, Carlos
A1  - Arisaka, Fumio
A1  - Attali, Ilan
A1  - Bain, David L.
A1  - Bakhtina, Marina M.
A1  - Becker, Donald F.
A1  - Bedwell, Gregory J.
A1  - Bekdemir, Ahmet
A1  - Besong, Tabot M. D.
A1  - Birck, Catherine
A1  - Brautigam, Chad A.
A1  - Brennerman, William
A1  - Byron, Olwyn
A1  - Bzowska, Agnieszka
A1  - Chaires, Jonathan B.
A1  - Chaton, Catherine T.
A1  - Coelfen, Helmbut
A1  - Connaghan, Keith D.
A1  - Crowley, Kimberly A.
A1  - Curth, Ute
A1  - Daviter, Tina
A1  - Dean, William L.
A1  - Diez, Ana I.
A1  - Ebel, Christine
A1  - Eckert, Debra M.
A1  - Eisele, Leslie E.
A1  - Eisenstein, Edward
A1  - England, Patrick
A1  - Escalante, Carlos
A1  - Fagan, Jeffrey A.
A1  - Fairman, Robert
A1  - Finn, Ron M.
A1  - Fischle, Wolfgang
A1  - Garcia de la Torre, Jose
A1  - Gor, Jayesh
A1  - Gustafsson, Henning
A1  - Hall, Damien
A1  - Harding, Stephen E.
A1  - Hernandez Cifre, Jose G.
A1  - Herr, Andrew B.
A1  - Howell, Elizabeth E.
A1  - Isaac, Richard S.
A1  - Jao, Shu-Chuan
A1  - Jose, Davis
A1  - Kim, Soon-Jong
A1  - Kokona, Bashkim
A1  - Kornblatt, Jack A.
A1  - Kosek, Dalibor
A1  - Krayukhina, Elena
A1  - Krzizike, Daniel
A1  - Kusznir, Eric A.
A1  - Kwon, Hyewon
A1  - Larson, Adam
A1  - Laue, Thomas M.
A1  - Le Roy, Aline
A1  - Leech, Andrew P.
A1  - Lilie, Hauke
A1  - Luger, Karolin
A1  - Luque-Ortega, Juan R.
A1  - Ma, Jia
A1  - May, Carrie A.
A1  - Maynard, Ernest L.
A1  - Modrak-Wojcik, Anna
A1  - Mok, Yee-Foong
A1  - Mücke, Norbert
A1  - Nagel-Steger, Luitgard
A1  - Narlikar, Geeta J.
A1  - Noda, Masanori
A1  - Nourse, Amanda
A1  - Obsil, Thomas
A1  - Park, Chad K
A1  - Park, Jin-Ku
A1  - Pawelek, Peter D.
A1  - Perdue, Erby E.
A1  - Perkins, Stephen J.
A1  - Perugini, Matthew A.
A1  - Peterson, Craig L.
A1  - Peverelli, Martin G.
A1  - Piszczek, Grzegorz
A1  - Prag, Gali
A1  - Prevelige, Peter E.
A1  - Raynal, Bertrand D. E.
A1  - Rezabkova, Lenka
A1  - Richter, Klaus
A1  - Ringel, Alison E.
A1  - Rosenberg, Rose
A1  - Rowe, Arthur J.
A1  - Rufer, Arne C.
A1  - Scott, David J.
A1  - Seravalli, Javier G.
A1  - Solovyova, Alexandra S.
A1  - Song, Renjie
A1  - Staunton, David
A1  - Stoddard, Caitlin
A1  - Stott, Katherine
A1  - Strauss, Holder M.
A1  - Streicher, Werner W.
A1  - Sumida, John P.
A1  - Swygert, Sarah G.
A1  - Szczepanowski, Roman H.
A1  - Tessmer, Ingrid
A1  - Toth, Ronald T.
A1  - Tripathy, Ashutosh
A1  - Uchiyama, Susumu
A1  - Uebel, Stephan F. W.
A1  - Unzai, Satoru
A1  - Gruber, Anna Vitlin
A1  - von Hippel, Peter H.
A1  - Wandrey, Christine
A1  - Wang, Szu-Huan
A1  - Weitzel, Steven E
A1  - Wielgus-Kutrowska, Beata
A1  - Wolberger, Cynthia
A1  - Wolff, Martin
A1  - Wright, Edward
A1  - Wu, Yu-Sung
A1  - Wubben, Jacinta M.
A1  - Schuck, Peter
T1  - A Multilaboratory Comparison of Calibration Accuracy and the Performance of External References in Analytical Ultracentrifugation
JF  - PLoS ONE
N2  - Analytical ultracentrifugation (AUC) is a first principles based method to determine absolute sedimentation coefficients and buoyant molar masses of macromolecules and their complexes, reporting on their size and shape in free solution. The purpose of this multi-laboratory study was to establish the precision and accuracy of basic data dimensions in AUC and validate previously proposed calibration techniques. Three kits of AUC cell assemblies containing radial and temperature calibration tools and a bovine serum albumin (BSA) reference sample were shared among 67 laboratories, generating 129 comprehensive data sets. These allowed for an assessment of many parameters of instrument performance, including accuracy of the reported scan time after the start of centrifugation, the accuracy of the temperature calibration, and the accuracy of the radial magnification. The range of sedimentation coefficients obtained for BSA monomer in different instruments and using different optical systems was from 3.655 S to 4.949 S, with a mean and standard deviation of (4.304\(\pm\)0.188) S (4.4%). After the combined application of correction factors derived from the external calibration references for elapsed time, scan velocity, temperature, and radial magnification, the range of s-values was reduced 7-fold with a mean of 4.325 S and a 6-fold reduced standard deviation of \(\pm\)0.030 S (0.7%). In addition, the large data set provided an opportunity to determine the instrument-to-instrument variation of the absolute radial positions reported in the scan files, the precision of photometric or refractometric signal magnitudes, and the precision of the calculated apparent molar mass of BSA monomer and the fraction of BSA dimers. These results highlight the necessity and effectiveness of independent calibration of basic AUC data dimensions for reliable quantitative studies.
KW  - fluorescence-detected sedimentation
KW  - size exclusion chromatography
KW  - field flow fractionation
KW  - spinco ultracentrifuge
KW  - aggregation
KW  - bead models
KW  - velocity
KW  - hydrodynamics
KW  - biopharmaceuticals
KW  - proteins
Y1  - 2015
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-151903
VL  - 10
IS  - 5
ER  - 
TY  - JOUR
A1  - Wu, Yu
A1  - Pons, Valérie
A1  - Goudet, Amélie
A1  - Panigai, Laetitia
A1  - Fischer, Annette
A1  - Herweg, Jo-Ana
A1  - Kali, Sabrina
A1  - Davey, Robert A.
A1  - Laporte, Jérôme
A1  - Bouclier, Céline
A1  - Yousfi, Rahima
A1  - Aubenque, Céline
A1  - Merer, Goulven
A1  - Gobbo, Emilie
A1  - Lopez, Roman
A1  - Gillet, Cynthia
A1  - Cojean, Sandrine
A1  - Popoff, Michel R.
A1  - Clayette, Pascal
A1  - Le Grand, Roger
A1  - Boulogne, Claire
A1  - Tordo, Noël
A1  - Lemichez, Emmanuel
A1  - Loiseau, Philippe M.
A1  - Rudel, Thomas
A1  - Sauvaire, Didier
A1  - Cintrat, Jean-Christophe
A1  - Gillet, Daniel
A1  - Barbier, Julien
T1  - ABMA, a small molecule that inhibits intracellular toxins and pathogens by interfering with late endosomal compartments
JF  - Scientific Reports
N2  - Intracellular pathogenic microorganisms and toxins exploit host cell mechanisms to enter, exert their deleterious effects as well as hijack host nutrition for their development. A potential approach to treat multiple pathogen infections and that should not induce drug resistance is the use of small molecules that target host components. We identifed the compound 1-adamantyl (5-bromo-2-methoxybenzyl) amine (ABMA) from a cell-based high throughput screening for its capacity to protect human cells and mice against ricin toxin without toxicity. This compound efciently protects cells against various toxins and pathogens including viruses, intracellular bacteria and parasite. ABMA provokes Rab7-positive late endosomal compartment accumulation in mammalian cells without affecting other organelles (early endosomes, lysosomes, the Golgi apparatus, the endoplasmic reticulum or the nucleus). As the mechanism of action of ABMA is restricted to host-endosomal compartments, it reduces cell infection by pathogens that depend on this pathway to invade cells. ABMA may represent a novel class of broad-spectrum compounds with therapeutic potential against diverse severe infectious diseases.
KW  - biology
KW  - antimicrobials
KW  - high-throughput screening
KW  - infectious diseases
Y1  - 2017
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-173170
VL  - 7
ER  -