scholarly journals Origin of Small Barriers in Jahn–Teller Systems: Quantifying the Role of 3d–4s Hybridization in the Model System NaCl:Ni+

2013 ◽  
Vol 52 (16) ◽  
pp. 9338-9348 ◽  
Author(s):  
M. T. Barriuso ◽  
B. Ortiz-Sevilla ◽  
J. A. Aramburu ◽  
P. García-Fernández ◽  
J. M. García-Lastra ◽  
...  
Keyword(s):  
Model System ◽  
Jahn Teller

Unveiling the role of Mn-interstitial defect and particle size on the Jahn-Teller distortion of the LiMn2O4 cathode material

2021 ◽  
Vol 490 ◽  
pp. 229519
Author(s):  
Renier Arabolla Rodríguez ◽  
Nelcy Della Santina Mohallem ◽  
Manuel Avila Santos ◽  
Demetrio A. Sena Costa ◽  
Luciano Andrey Montoro ◽  
...  
Keyword(s):  
Particle Size ◽  
Cathode Material ◽  
Teller Distortion ◽  
Interstitial Defect ◽  
Jahn Teller ◽  
Limn2o4 Cathode ◽  
Jahn Teller Distortion

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.

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

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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