A Single-Step Correction Scheme of Crank–Nicolson Convolution Quadrature for the Subdiffusion Equation

2021 ◽  
Vol 87 (1) ◽  
Author(s):  
Jilu Wang ◽  
Jungang Wang ◽  
Lihong Yin
2013 ◽  
Vol 74 (1) ◽  
pp. 34-58
Author(s):  
F. Boyer ◽  
F. Dardalhon ◽  
C. Lapuerta ◽  
J.-C. Latché

2016 ◽  
Vol 13 (10) ◽  
pp. 7719-7725
Author(s):  
Jianguang Lu ◽  
Yong Feng ◽  
Xiaolin Qin ◽  
Juan Tang

The group preserving methods proposed by Liu [Int. J. Non-Linear Mech., 2001 and CMES-Comp. Model. Eng., 2006] for ordinary differential equations or differential algebraic equations (DAEs) adopted the Cayley transform or exponential mapping to formulate the Lie group from its Lie algebra. In this paper, we combine the Euler scheme with the group preserving methods to obtain the high accuracy group preserving techniques. We propose a group preserving correction scheme (GPCS) via exponential mapping and a modified group preserving correction scheme (MGPCS) by considering constraint. The two schemes provide single-step explicit time integrators for systems of DAEs. Some numerical examples are examined, showing that the GPCS and MGPCS work very well and have good computational efficiency and high accuracy.


2005 ◽  
Vol 173 (4S) ◽  
pp. 240-240
Author(s):  
Premal J. Desai ◽  
David A. Hadley ◽  
Lincoln J. Maynes ◽  
D. Duane Baldwin

1996 ◽  
Vol 75 (03) ◽  
pp. 497-502 ◽  
Author(s):  
Hadewijch L M Pekelharing ◽  
Henne A Kleinveld ◽  
Pieter F C.C.M Duif ◽  
Bonno N Bouma ◽  
Herman J M van Rijn

SummaryLp(a) is an LDL-like lipoprotein plus an additional apolipoprotein apo(a). Based on the structural homology of apo(a) with plasminogen, it is hypothesized that Lp(a) interferes with fibrinolysis. Extracellular matrix (ECM) produced by human umbilical vein endothelial cells was used to study the effect of Lp(a) and LDL on plasminogen binding and activation. Both lipoproteins were isolated from the same plasma in a single step. Plasminogen bound to ECM via its lysine binding sites. Lp(a) as well as LDL were capable of competing with plasminogen binding. The degree of inhibition was dependent on the lipoprotein donor as well as the ECM donor. When Lp(a) and LDL obtained from one donor were compared, Lp(a) was always a much more potent competitor. The effect of both lipoproteins on plasminogen binding was reflected in their effect on plasminogen activation. It is speculated that Lp(a) interacts with ECM via its LDL-like lipoprotein moiety as well as via its apo(a) moiety.


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