Nifedipine kinetics and dynamics during rectal infusion to steady state with an osmotic system

1984 ◽  
Vol 36 (3) ◽  
pp. 396-401 ◽  
Author(s):  
C H Kleinbloesem ◽  
J Van Harten ◽  
L G J de Leede ◽  
P van Brummelen ◽  
D D Breimer
1982 ◽  
Vol 32 (6) ◽  
pp. 749-757 ◽  
Author(s):  
Ingrid W Reimann ◽  
Ulrich Klotz ◽  
Jürgen C Frölich

Langmuir ◽  
2005 ◽  
Vol 21 (21) ◽  
pp. 9529-9536 ◽  
Author(s):  
Yunsheng Ma ◽  
Song Han ◽  
Tatsuo Matsushima

1999 ◽  
Vol 18 (3) ◽  
pp. 164-173 ◽  
Author(s):  
Lona L Christrup ◽  
Per Sjøgren ◽  
Niels-Henrik Jensen ◽  
Anne-Marie Banning ◽  
Karsten Elbæk ◽  
...  

2010 ◽  
Vol 16 (37) ◽  
pp. 11300-11310 ◽  
Author(s):  
Clelia Cogliati ◽  
Laura Ragona ◽  
Mariapina D'Onofrio ◽  
Ulrich Günther ◽  
Sara Whittaker ◽  
...  

2020 ◽  
pp. mcp.R120.002190
Author(s):  
Alison B. Ross ◽  
Julian David Langer ◽  
Marko Jovanovic

In all cells, proteins are continuously synthesized and degraded in order to maintain protein homeostasis and modify gene expression levels in response to stimuli. Collectively, the processes of protein synthesis and degradation are referred to as protein turnover. At steady state, protein turnover is constant to maintain protein homeostasis, but in dynamic responses, proteins change their rates of synthesis and degradation in order to adjust their proteomes to internal or external stimuli. Thus, probing the kinetics and dynamics of protein turnover lends insight into how cells regulate essential processes such as growth, differentiation, and stress response. Here we outline historical and current approaches to measuring the kinetics of protein turnover on a proteome-wide scale in both steady-state and dynamic systems, with an emphasis on metabolic tracing using stable-isotope-labeled amino acids. We highlight important considerations for designing proteome turnover experiments, key biological findings regarding the conserved principles of proteome turnover regulation, and future perspectives for both technological and biological investigation.


Author(s):  
R. C. Moretz ◽  
G. G. Hausner ◽  
D. F. Parsons

Use of the electron microscope to examine wet objects is possible due to the small mass thickness of the equilibrium pressure of water vapor at room temperature. Previous attempts to examine hydrated biological objects and water itself used a chamber consisting of two small apertures sealed by two thin films. Extensive work in our laboratory showed that such films have an 80% failure rate when wet. Using the principle of differential pumping of the microscope column, we can use open apertures in place of thin film windows.Fig. 1 shows the modified Siemens la specimen chamber with the connections to the water supply and the auxiliary pumping station. A mechanical pump is connected to the vapor supply via a 100μ aperture to maintain steady-state conditions.


2021 ◽  
Author(s):  
Wu Lan ◽  
Yuan Peng Du ◽  
Songlan Sun ◽  
Jean Behaghel de Bueren ◽  
Florent Héroguel ◽  
...  

We performed a steady state high-yielding depolymerization of soluble acetal-stabilized lignin in flow, which offered a window into challenges and opportunities that will be faced when continuously processing this feedstock.


2008 ◽  
Vol 45 ◽  
pp. 161-176 ◽  
Author(s):  
Eduardo D. Sontag

This paper discusses a theoretical method for the “reverse engineering” of networks based solely on steady-state (and quasi-steady-state) data.


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