Direct experimental evidence for diffusion of dopants via pairs with intrinsic point defects

1992 ◽  
Vol 60 (8) ◽  
pp. 953-955 ◽  
Author(s):  
P. Pichler ◽  
R. Schork ◽  
T. Klauser ◽  
H. Ryssel
Keyword(s):  
Experimental Evidence ◽  
Point Defects ◽  
Intrinsic Point Defects ◽  
Direct Experimental Evidence

Experimental Study of Self-Diffusion in Silicon Using Isotopically Enriched Structures

1999 ◽  
Vol 568 ◽  
Author(s):  
Ant Ural ◽  
Peter B. Griffin ◽  
James D. Plummer
Keyword(s):  
Experimental Study ◽  
Experimental Evidence ◽  
Thermal Oxidation ◽  
Point Defects ◽  
Weak Dependence ◽  
Phosphorus Diffusion ◽  
Temperature Range ◽  
Intrinsic Point Defects ◽  
Self Diffusion ◽  
Fractional Contribution

ABSTRACTSelf-diffusion in silicon has been studied using epitaxially grown isotopically enriched structures under nonequilibrium concentrations of intrinsic point defects created by thermal oxidation and nitridation. Comparison of identical anneals for self, antimony, and phosphorus diffusion in silicon enables us to determine bounds on the fractional contributions of microscopic mechanisms for Si self-diffusion in the temperature range 800–1100°C. We obtain direct experimental evidence for a dual vacancy-interstitial mechanism of self-diffusion in silicon and show that the fractional contribution of each mechanism has a weak dependence on temperature.

Intrinsic point defects and charge carrier trapping in monolayer BiOX (X = I, Br, and Cl)

2021 ◽  
Author(s):  
Haixi Pan ◽  
Liping Feng ◽  
Xiaodong Zhang ◽  
Yang Chen ◽  
Gangquan Li ◽  
...  
Keyword(s):  
Charge Carrier ◽  
Point Defects ◽  
Carrier Trapping ◽  
Intrinsic Point Defects ◽  
Charge Carrier Trapping

Effect of intrinsic point defects on copper precipitation in large-diameter Czochralski silicon

2003 ◽  
Vol 83 (15) ◽  
pp. 3048-3050 ◽  
Author(s):  
Zhenqiang Xi ◽  
Deren Yang ◽  
Jin Xu ◽  
Yujie Ji ◽  
Duanlin Que ◽  
...  
Keyword(s):  
Point Defects ◽  
Large Diameter ◽  
Czochralski Silicon ◽  
Intrinsic Point Defects ◽  
Copper Precipitation

Overexpression of cysteine dioxygenase reduces intracellular cysteine and glutathione pools in HepG2/C3A cells

2007 ◽  
Vol 293 (1) ◽  
pp. E62-E69 ◽  
Author(s):  
John E. Dominy ◽  
Jesse Hwang ◽  
Martha H. Stipanuk
Keyword(s):  
Steady State ◽  
Experimental Evidence ◽  
Cysteine Dioxygenase ◽  
Wild Type ◽  
Hepatic Expression ◽  
Direct Experimental Evidence ◽  
Homeostatic Response ◽  
Catabolic Enzyme ◽  
In Cells

Cysteine levels are carefully regulated in mammals to balance metabolic needs against the potential for cytotoxicity. It has been postulated that one of the major regulators of intracellular cysteine levels in mammals is cysteine dioxygenase (CDO). Hepatic expression of this catabolic enzyme increases dramatically in response to increased cysteine availability and may therefore be part of a homeostatic response to shunt excess toxic cysteine to more benign metabolites such as sulfate or taurine. Direct experimental evidence, however, is lacking to support the hypothesis that CDO is capable of altering steady-state intracellular cysteine levels. In this study, we expressed either the wild-type (WT) or a catalytically inactivated mutant (H86A) isoform of CDO in HepG2/C3A cells (which do not express endogenous CDO protein) and cultured them in different concentrations of extracellular cysteine. WT CDO, but not H86A CDO, was capable of reducing intracellular cysteine levels in cells incubated in physiologically relevant concentrations of cysteine. WT CDO also decreased the glutathione pool and potentiated the toxicity of CdCl2. These results demonstrate that CDO is capable of altering intracellular cysteine levels as well as glutathione levels.

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