A new Reliable Numerical Algorithm Based on the First Kind of Bessel Functions to Solve Prandtl–Blasius Laminar Viscous Flow over a Semi-Infinite Flat Plate

2012 ◽  
Vol 67 (12) ◽  
pp. 665-673 ◽  
Author(s):  
Kourosh Parand ◽  
Mehran Nikarya ◽  
Jamal Amani Rad ◽  
Fatemeh Baharifard
Keyword(s):  
Viscous Flow ◽  
Flat Plate ◽  
Numerical Algorithm ◽  
Bessel Functions ◽  
Nonlinear Ordinary Differential Equation ◽  
Finite Domain ◽  
Algebraic Equations ◽  
Infinite Domain ◽  
Third Order ◽  
Domain Truncation

In this paper, a new numerical algorithm is introduced to solve the Blasius equation, which is a third-order nonlinear ordinary differential equation arising in the problem of two-dimensional steady state laminar viscous flow over a semi-infinite flat plate. The proposed approach is based on the first kind of Bessel functions collocation method. The first kind of Bessel function is an infinite series, defined on ℝ and is convergent for any x ∊ℝ. In this work, we solve the problem on semi-infinite domain without any domain truncation, variable transformation basis functions or transformation of the domain of the problem to a finite domain. This method reduces the solution of a nonlinear problem to the solution of a system of nonlinear algebraic equations. To illustrate the reliability of this method, we compare the numerical results of the present method with some well-known results in order to show the applicability and efficiency of our method.

Unique CD18 mutations involving a deletion in the extracellular stalk region and a major truncation of the cytoplasmic domain in a patient with leukocyte adhesion deficiency type 1

Blood ◽  
2004 ◽  
Vol 103 (3) ◽  
pp. 1105-1113 ◽  
Author(s):  
Patricia Hixson ◽  
C. Wayne Smith ◽  
Susan B. Shurin ◽  
Michael F. Tosi
Keyword(s):  
Leukocyte Adhesion ◽  
Cytoplasmic Domain ◽  
Lymphocyte Function ◽  
Wild Type ◽  
Leukocyte Adhesion Deficiency ◽  
Binding Function ◽  
Domain Truncation ◽  
Low Levels ◽  
Deficiency Type

AbstractTwo novel CD18 mutations were identified in a patient who was a compound heterozygote with type 1 leukocyte adhesion deficiency and whose phenotype was typical except that he exhibited hypertrophic scarring. A deletion of 36 nucleotides in exon 12 (1622del36) predicted the net loss of 12 amino acid (aa) residues in the third cysteine-rich repeat of the extracellular stalk region (mut-1). A nonsense mutation in exon 15 (2200G>T), predicted a 36-aa truncation of the cytoplasmic domain (mut-2). Lymphocyte function-associated antigen 1 (LFA-1) and macrophage antigen-1 (Mac-1) containing the mut-1 β2 subunit were expressed at very low levels compared with wild-type (wt) β2. Mac-1 and LFA-1 expression with the mut-2 β2 subunit were equivalent to results with wt β2. Binding function of Mac-1 with mut-2 β2 was equivalent to that with wt β2. However, binding function of LFA-1 with the mut-2 β2 subunit was reduced by 50% versus wt β2. It was concluded that (1) the portion of the CD18 stalk region deleted in mut-1 is critical for β2 integrin heterodimer expression but the portion of the cytoplasmic domain truncated in mut-2 is not; and (2) the mut-2 cytoplasmic domain truncation impairs binding function of LFA-1 but not of Mac-1. Studies with the patient's neutrophils (PMNs) were consistent with functional impairment of LFA-1 but not of Mac-1. (Blood. 2004;103:1105-1113)

scholarly journals The Carboxy-Terminal Tail of Human Cytomegalovirus (HCMV) US28 Regulates both Chemokine-Independent and Chemokine-Dependent Signaling in HCMV-Infected Cells

2009 ◽  
Vol 83 (19) ◽  
pp. 10016-10027 ◽  
Author(s):  
Melissa P. Stropes ◽  
Olivia D. Schneider ◽  
William A. Zagorski ◽  
Jeanette L. C. Miller ◽  
William E. Miller
Keyword(s):  
Human Cytomegalovirus ◽  
Calcium Release ◽  
Hcmv Infection ◽  
Calcium Signal ◽  
Terminal Domain ◽  
Carboxy Terminal Domain ◽  
Domain Truncation ◽  
Infected Cells ◽  
Heterologous Expression Systems ◽  
Carboxy Terminal

ABSTRACT The human cytomegalovirus (HCMV)-encoded G-protein-coupled receptor (GPCR) US28 is a potent activator of a number of signaling pathways in HCMV-infected cells. The intracellular carboxy-terminal domain of US28 contains residues critical for the regulation of US28 signaling in heterologous expression systems; however, the role that this domain plays during HCMV infection remains unknown. For this study, we constructed an HCMV recombinant virus encoding a carboxy-terminal domain truncation mutant of US28, FLAG-US28/1-314, to investigate the role that this domain plays in US28 signaling. We demonstrate that US28/1-314 exhibits a more potent phospholipase C-β (PLC-β) signal than does wild-type US28, indicating that the carboxy-terminal domain plays an important role in regulating agonist-independent signaling in infected cells. Moreover, HMCV-infected cells expressing the US28/1-314 mutant exhibit a prolonged calcium signal in response to CCL5, indicating that the US28 carboxy-terminal domain also regulates agonist-dependent signaling. Finally, while the chemokine CX3CL1 behaves as an inverse agonist or inhibitor of constitutive US28 signaling to PLC-β, we demonstrate that CX3CL1 functions as an agonist with regard to US28-stimulated calcium release. This study is the first to demonstrate that the carboxy terminus of US28 controls US28 signaling in the context of HCMV infection and indicates that chemokines such as CX3CL1 can decrease constitutive US28 signals and yet simultaneously promote nonconstitutive US28 signals.

scholarly journals Numerical Simulation on the Whole Sinking Process of Open Caisson with an Improved SPH Method

2021 ◽  
Vol 2021 ◽  
pp. 1-9
Author(s):  
Jiahe Zhang
Keyword(s):  
Pore Water Pressure ◽  
Water Pressure ◽  
Dynamic Change ◽  
Soil Pressure ◽  
Shield Tunneling ◽  
Material Interfaces ◽  
Engineering Problems ◽  
Domain Truncation ◽  
Particle Hydrodynamics ◽  
Sph Simulation

The phenomena of dynamic change in the material interfaces and mechanical properties are often involved in the caisson construction. Using conventional methods to simulate these phenomena is quite difficult due to the extremely large deformation. In this study, we proposed an improved soil-water-caisson interaction algorithm with the method of smoothed-particle hydrodynamics (SPH). This algorithm dealt with the support domain truncation of the particles near the blade and applied δ − SPH to avoid the pressure fluctuation. Meanwhile, the application of dynamic particles birth and death method could simulate the whole sinking process of an open caisson with underwater soil excavation. According to the comparison between SPH simulation and centrifuge test, the distribution of sidewall effective soil pressure was consistent, which indicated promising applicability of the algorithm. It should be noted that the considerable excess pore water pressure appeared in the surrounding soil under the blade. With the dissipation of the pressure over time, the effective soil stress increased correspondingly, and it would lead to the increasing difficulty of the sinking process. Therefore, the caisson should be avoided to stop for a long time during the sinking process or it would cause the stagnation of sinking. This algorithm could simulate engineering problems involving underwater construction effectively and provide theoretical and technical support for underwater excavation, shield tunneling, and other engineering problems.

scholarly journals Functional characterization of the non-catalytic ectodomains of the nucleotide pyrophosphatase/phosphodiesterase NPP1

2003 ◽  
Vol 371 (2) ◽  
pp. 321-330 ◽  
Author(s):  
Rik GIJSBERS ◽  
Hugo CEULEMANS ◽  
Mathieu BOLLEN
Keyword(s):  
Catalytic Activity ◽  
Catalytic Domain ◽  
Transmembrane Domain ◽  
Functional Characterization ◽  
Structure Stability ◽  
Subunit Structure ◽  
Terminal Domain ◽  
Nucleotide Pyrophosphatase ◽  
Domain Truncation ◽  
And Function

The ubiquitous nucleotide pyrophosphatases/phosphodiesterases NPP1–3 consist of a short intracellular N-terminal domain, a single transmembrane domain and a large extracellular part, comprising two somatomedin-B-like domains, a catalytic domain and a poorly defined C-terminal domain. We show here that the C-terminal domain of NPP1–3 is structurally related to a family of DNA/RNA non-specific endonucleases. However, none of the residues that are essential for catalysis by the endonucleases are conserved in NPP1–NPP3, suggesting that the nuclease-like domain of NPP1–3 does not represent a second catalytic domain. Truncation analysis revealed that the nuclease-like domain of NPP1 is required for protein stability, for the targeting of NPP1 to the plasma membrane and for the expression of catalytic activity. We also demonstrate that 16 conserved cysteines in the somatomedin-B-like domains of NPP1, in concert with two flanking cysteines, mediate the dimerization of NPP1. The K173Q polymorphism of NPP1, which maps to the second somatomedin-B-like domain and has been associated with the aetiology of insulin resistance, did not affect the dimerization or catalytic activity of NPP1, and did not endow NPP1 with an affinity for the insulin receptor. Our data suggest that the non-catalytic ectodomains contribute to the subunit structure, stability and function of NPP1–3.

scholarly journals Impairment of the liver insulin receptor autoactivation cascade at full-term pregnancy in the rat

1995 ◽  
Vol 311 (2) ◽  
pp. 523-529 ◽  
Author(s):  
C Martinez ◽  
J C Molero ◽  
P Ruiz ◽  
A Del Arco ◽  
A Andres ◽  
...  
Keyword(s):  
Insulin Receptor ◽  
Structural Changes ◽  
Insulin Receptors ◽  
Kinase Domain ◽  
Full Term ◽  
Beta Subunits ◽  
Pregnant Rats ◽  
Functional Changes ◽  
Domain Truncation ◽  
Alternative Sites

Partially purified liver insulin receptors from full-term pregnant rats show decreased autophosphorylation rates if compared with receptors from virgins. We studied the molecular mechanism of this phenomenon, looking at possible structural and functional changes of several domains. The ATP-binding domain seems to be unaltered in receptors from pregnant rats since Km for ATP was similar to that observed in virgins. In contrast, the Vmax. is decreased some 45%, suggesting changes in the kinase domain. Truncation of a fragment of 10 kDa from the C-terminal tail does not normalize the kinase activity in receptors from pregnant rats, suggesting that this domain is not involved in the inhibitory regulation. Treatment with alkaline phosphatase increases the [32P]Pi incorporation into receptors from pregnant rats; however, the autophosphorylation remains lower than that observed in virgin rats. Tryptic phosphopeptide maps of phosphorylated receptors show that the same phosphopeptides are present in receptors from virgin and pregnant rats. However, the progression through the autoactivation cascade in the kinase domain is impaired in receptors from pregnant rats. Differences in the cleavage by trypsin at the two alternative sites in the kinase domain were observed, indicating possible structural changes in receptors from pregnant rats that could be related to the impairment of the autoactivation cascade. Integrity of the alpha- and beta-subunits, as well as differential expression of the two receptor isotypes, were shown to be unaltered. We conclude that (1) the decreased autophosphorylation rate of the liver insulin receptor from pregnant rats is associated with the impairment of its autoactivation cascade, probably as a consequence of the basal Ser/Thr phosphorylation; and (2) the inhibition of the autoactivation cascade does not account for the overall inhibition of autophosphorylation observed in receptors from pregnant rats.

scholarly journals Spherical Perfectly Matched Absorber for Finite-Volume 3-D Domain Truncation

2007 ◽  
Vol 55 (12) ◽  
pp. 2773-2781 ◽  
Author(s):  
Christophe Fumeaux ◽  
Krishnaswamy Sankaran ◽  
RÜdiger Vahldieck
Keyword(s):  
Finite Volume ◽  
Domain Truncation
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