scholarly journals Anormal Thermal History Effect on the Structural Dynamics of Probucol Infiltrated into Porous Alumina

2021 ◽  
Vol 125 (7) ◽  
pp. 3901-3912
Author(s):  
Agnieszka Talik ◽  
Magdalena Tarnacka ◽  
Aldona Minecka ◽  
Barbara Hachuła ◽  
Joanna Grelska ◽  
...  
2016 ◽  
Vol 119 (24) ◽  
pp. 245113 ◽  
Author(s):  
S. Wang ◽  
Y. F. Ye ◽  
S. Q. Shi ◽  
Y. Yang

Author(s):  
Takumi SHIRAKAWABE ◽  
Hailong WANG ◽  
Shigeru GOTO ◽  
Shuichi YAMAMOTO ◽  
Hideo KOMINE

Author(s):  
J. R. Michael ◽  
A. D. Romig ◽  
D. R. Frear

Al with additions of Cu is commonly used as the conductor metallizations for integrated circuits, the Cu being added since it improves resistance to electromigration failure. As linewidths decrease to submicrometer dimensions, the current density carried by the interconnect increases dramatically and the probability of electromigration failure increases. To increase the robustness of the interconnect lines to this failure mode, an understanding of the mechanism by which Cu improves resistance to electromigration is needed. A number of theories have been proposed to account for role of Cu on electromigration behavior and many of the theories are dependent of the elemental Cu distribution in the interconnect line. However, there is an incomplete understanding of the distribution of Cu within the Al interconnect as a function of thermal history. In order to understand the role of Cu in reducing electromigration failures better, it is important to characterize the Cu distribution within the microstructure of the Al-Cu metallization.


2019 ◽  
Vol 47 (5) ◽  
pp. 1247-1257 ◽  
Author(s):  
Mateusz Dyla ◽  
Sara Basse Hansen ◽  
Poul Nissen ◽  
Magnus Kjaergaard

Abstract P-type ATPases transport ions across biological membranes against concentration gradients and are essential for all cells. They use the energy from ATP hydrolysis to propel large intramolecular movements, which drive vectorial transport of ions. Tight coordination of the motions of the pump is required to couple the two spatially distant processes of ion binding and ATP hydrolysis. Here, we review our current understanding of the structural dynamics of P-type ATPases, focusing primarily on Ca2+ pumps. We integrate different types of information that report on structural dynamics, primarily time-resolved fluorescence experiments including single-molecule Förster resonance energy transfer and molecular dynamics simulations, and interpret them in the framework provided by the numerous crystal structures of sarco/endoplasmic reticulum Ca2+-ATPase. We discuss the challenges in characterizing the dynamics of membrane pumps, and the likely impact of new technologies on the field.


2018 ◽  
Vol 190 (02) ◽  
pp. 113-136
Author(s):  
Sergei A. Aseyev ◽  
A.S. Akhmanov ◽  
G.V. Girichev ◽  
Anatoly A. Ischenko ◽  
Igor V. Kochikov ◽  
...  

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