A Model System of Error Commission, Detection and Correction for High Precision Error Coupling in the Error Monitoring and Processing System: Role of Glycemic Allostasis Regulation

2015 ◽  
Author(s):  
Menizibeya Osain ◽  
Mastorakis Nikos ◽  
Elena Vyacheslavovna Pereverzeva ◽  
Pereverzev Vladimir Alexeevich
Keyword(s):  
High Precision ◽  
Processing System ◽  
Model System ◽  
Error Monitoring ◽  
Precision Error

scholarly journals Serine and Threonine Phosphorylation of the Paxillin LIM Domains Regulates Paxillin Focal Adhesion Localization and Cell Adhesion to Fibronectin

1998 ◽  
Vol 9 (7) ◽  
pp. 1803-1816 ◽  
Author(s):  
Michael C. Brown ◽  
Joseph A. Perrotta ◽  
Christopher E. Turner
Keyword(s):  
Cell Adhesion ◽  
Focal Adhesion ◽  
Binding Sites ◽  
Protein Localization ◽  
Model System ◽  
Lim Domain ◽  
Amino Terminal ◽  
Lim Domains ◽  
Inside Out

We have previously shown that the LIM domains of paxillin operate as the focal adhesion (FA)-targeting motif of this protein. In the current study, we have identified the capacity of paxillin LIM2 and LIM3 to serve as binding sites for, and substrates of serine/threonine kinases. The activities of the LIM2- and LIM3-associated kinases were stimulated after adhesion of CHO.K1 cells to fibronectin; consequently, a role for LIM domain phosphorylation in regulating the subcellular localization of paxillin after adhesion to fibronectin was investigated. An avian paxillin-CHO.K1 model system was used to explore the role of paxillin phosphorylation in paxillin localization to FAs. We found that mutations of paxillin that mimicked LIM domain phosphorylation accelerated fibronectin-induced localization of paxillin to focal contacts. Further, blocking phosphorylation of the LIM domains reduced cell adhesion to fibronectin, whereas constitutive LIM domain phosphorylation significantly increased the capacity of cells to adhere to fibronectin. The potentiation of FA targeting and cell adhesion to fibronectin was specific to LIM domain phosphorylation as mutation of the amino-terminal tyrosine and serine residues of paxillin that are phosphorylated in response to fibronectin adhesion had no effect on the rate of FA localization or cell adhesion. This represents the first demonstration of the regulation of protein localization through LIM domain phosphorylation and suggests a novel mechanism of regulating LIM domain function. Additionally, these results provide the first evidence that paxillin contributes to “inside-out” integrin-mediated signal transduction.

Preserving Integrity in the Face of Performance Threat

2012 ◽  
Vol 23 (12) ◽  
pp. 1455-1460 ◽  
Author(s):  
Lisa Legault ◽  
Timour Al-Khindi ◽  
Michael Inzlicht
Keyword(s):  
Error Detection ◽  
Error Monitoring ◽  
Error Related Negativity ◽  
Threatening Information ◽  
Electrophysiological Responses ◽  
The Face ◽  
And Performance ◽  
The Impact ◽  
The Brain

Self-affirmation produces large effects: Even a simple reminder of one’s core values reduces defensiveness against threatening information. But how, exactly, does self-affirmation work? We explored this question by examining the impact of self-affirmation on neurophysiological responses to threatening events. We hypothesized that because self-affirmation increases openness to threat and enhances approachability of unfavorable feedback, it should augment attention and emotional receptivity to performance errors. We further hypothesized that this augmentation could be assessed directly, at the level of the brain. We measured self-affirmed and nonaffirmed participants’ electrophysiological responses to making errors on a task. As we anticipated, self-affirmation elicited greater error responsiveness than did nonaffirmation, as indexed by the error-related negativity, a neural signal of error monitoring. Self-affirmed participants also performed better on the task than did nonaffirmed participants. We offer novel brain evidence that self-affirmation increases openness to threat and discuss the role of error detection in the link between self-affirmation and performance.

The Arabidopsis leaf as a model system for investigating the role of cell cycle regulation in organ growth

2005 ◽  
Vol 119 (1) ◽  
pp. 43-50 ◽  
Author(s):  
Gerrit T. S. Beemster ◽  
Steven Vercruysse ◽  
Lieven De Veylder ◽  
Martin Kuiper ◽  
Dirk Inzé
Keyword(s):  
Cell Cycle ◽  
Cell Cycle Regulation ◽  
Model System ◽  
Organ Growth ◽  
Cycle Regulation

Research on Key Technology of Data Mining for Volleyball Game Based on Service System

2014 ◽  
Vol 543-547 ◽  
pp. 4698-4701
Author(s):  
Juan Wang
Keyword(s):  
Data Mining ◽  
High Precision ◽  
Service System ◽  
Processing System ◽  
Machining Process ◽  
Precision Machining ◽  
Intelligent Processing ◽  
Mining Model ◽  
Processing Cycle ◽  
Key Parameter

During the processing of aircraft and other high precision machinery workpieces, if using the traditional machining methods, it will consume a amount of machining costs, and the mechanical processing cycle is long. In this context, this paper designs a kind of robot intelligent processing system with high precision machinery. And it has realized the intelligent online control on the machining process by using the high precision machining intelligent online monitoring technology and the numerical simulation prediction technology. Finally, this system is introduced into the process of data mining for volleyball game, and designs the partial differential variational data mining model, which has realized the key parameter data mining of volleyball games service system, and has provided reliable parameters and technical support for the training of volleyball players.

On the role of surface composition and curvature on biointerface formation and colloidal stability of nanoparticles in a protein-rich model system

2013 ◽  
Vol 108 ◽  
pp. 110-119 ◽  
Author(s):  
Guillermo Orts-Gil ◽  
Kishore Natte ◽  
Raphael Thiermann ◽  
Matthias Girod ◽  
Steffi Rades ◽  
...  
Keyword(s):  
Colloidal Stability ◽  
Surface Composition ◽  
Model System ◽  
Protein Rich

Tissue inhibitor of metalloproteinases (TIMP) regulates extracellular type I collagen degradation by chondrocytes and endothelial cells

1987 ◽  
Vol 87 (2) ◽  
pp. 357-362
Author(s):  
J. Gavrilovic ◽  
R.M. Hembry ◽  
J.J. Reynolds ◽  
G. Murphy
Keyword(s):  
Endothelial Cells ◽  
Type I Collagen ◽  
Model System ◽  
Collagen Degradation ◽  
Type I ◽  
Tissue Inhibitor Of Metalloproteinases ◽  
Regulatory Factor ◽  
Tissue Inhibitor ◽  
Cells Cultured

A specific antiserum to purified rabbit tissue inhibitor of metalloproteinases (TIMP) was raised in sheep, characterized and used to investigate the role of TIMP in a model system. Chondrocytes and endothelial cells cultured on 14C-labelled type I collagen films and stimulated to produce collagenase were unable to degrade the films unless the anti-TIMP antibody was added. The degradation induced was inhibited by a specific anti-rabbit collagenase antibody. It was concluded that TIMP is a major regulatory factor in cell-mediated collagen degradation.

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