scholarly journals Measurement of the inclusive electron spectrum in charmless semileptonicBdecays near the kinematic end point and determination of|Vub|

2006 ◽  
Vol 73 (1) ◽  
Author(s):  
B. Aubert ◽  
R. Barate ◽  
D. Boutigny ◽  
F. Couderc ◽  
Y. Karyotakis ◽  
...  
2017 ◽  
Vol 95 (7) ◽  
Author(s):  
J. P. Lees ◽  
V. Poireau ◽  
V. Tisserand ◽  
E. Grauges ◽  
A. Palano ◽  
...  

Author(s):  
Diana Spiegelberg ◽  
Jonas Stenberg ◽  
Pascale Richalet ◽  
Marc Vanhove

AbstractDesign of next-generation therapeutics comes with new challenges and emulates technology and methods to meet them. Characterizing the binding of either natural ligands or therapeutic proteins to cell-surface receptors, for which relevant recombinant versions may not exist, represents one of these challenges. Here we report the characterization of the interaction of five different antibody therapeutics (Trastuzumab, Rituximab, Panitumumab, Pertuzumab, and Cetuximab) with their cognate target receptors using LigandTracer. The method offers the advantage of being performed on live cells, alleviating the need for a recombinant source of the receptor. Furthermore, time-resolved measurements, in addition to allowing the determination of the affinity of the studied drug to its target, give access to the binding kinetics thereby providing a full characterization of the system. In this study, we also compared time-resolved LigandTracer data with end-point KD determination from flow cytometry experiments and hypothesize that discrepancies between these two approaches, when they exist, generally come from flow cytometry titration curves being acquired prior to full equilibration of the system. Our data, however, show that knowledge of the kinetics of the interaction allows to reconcile the data obtained by flow cytometry and LigandTracer and demonstrate the complementarity of these two methods.


1954 ◽  
Vol 100 (1) ◽  
pp. 81-88 ◽  
Author(s):  
Donald Greiff ◽  
Henry Pinkerton

A vacuum sublimation apparatus is described which will permit, (a) the removal of water from virus suspensions at temperatures ranging down to –80°C., (b) continuous operation with a minimum of attention from the investigator, (c) sealing off of samples at operating pressures (10–5 mm. Hg), (d) simultaneous lyophilization of aliquot samples at different temperatures, (e) isolation of a portion of the apparatus without disturbing the remainder of the system, and (f) determination of the end-point of sublimation without disturbing the samples. The time required for drying 0.1 ml. of influenza virus suspension was shown to increase markedly with decrease of temperature, 8 days being required for dehydration at –80°C. in contrast to 2 days at –30°C. and 1 day at 0°C.


1970 ◽  
Vol 58 (1) ◽  
pp. 52-57 ◽  
Author(s):  
J. Slanina ◽  
P. C. M. Frintrop ◽  
J. F. Mansveld ◽  
B. Griepink

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