To write without styles, LaTeX is great solution but MS Office is still (almost) gold standard for writing. I have never heard an instititue that accepts dissertation report in TeX format. LibreOffice has compatibility problems. As result, MS Office for ~9$ is slightly expensive than free :)

With "Microsoft Home Use Program" you can have genuine Office 2013 for just ~9$
www.microsofthup.com/hupus/chooser.aspx?culture=en-US

Some universities sell softwares by their IT ; but If yours don't or more expensive than this offer, Home Use Program sounds cool especially for people that want keep budget.

Unfortunately, my university is not one of affiliated so I can't buy for cheap. If someone who has chance to but doesn't think to buy share his/her "Program Code" via PM, I will be grateful.

Here is the article :
www.sendspace.com/file/ambrgn

...and to remove after use :
www.sendspace.com/delete/ambrgn/84ca69ea41f3f8dfc4098ede8ef88098

Title : Oxidative shielding or oxidative stress?
Authors : Naviaux RK
Journal : The journal of pharmacology and experimental therapeutics
Publication Date : 2012
Direct Link : "jpet.aspetjournals.org/content/342/3/608.long"
Abstract :
In this review I report evidence that the mainstream field of oxidative damage biology has been running fast in the wrong direction for more than 50 years. Reactive oxygen species (ROS) and chronic oxidative changes in membrane lipids and proteins found in many chronic diseases are not the result of accidental damage. Instead, these changes are the result of a highly evolved, stereotyped, and protein-catalyzed "oxidative shielding" response that all eukaryotes adopt when placed in a chemically or microbially hostile environment. The machinery of oxidative shielding evolved from pathways of innate immunity designed to protect the cell from attack and limit the spread of infection. Both oxidative and reductive stress trigger oxidative shielding. In the cases in which it has been studied explicitly, functional and metabolic defects occur in the cell before the increase in ROS and oxidative changes. ROS are the response to disease, not the cause. Therefore, it is not the oxidative changes that should be targeted for therapy, but rather the metabolic conditions that create them. This fresh perspective is relevant to diseases that range from autism, type 1 diabetes, type 2 diabetes, cancer, heart disease, schizophrenia, Parkinson's disease, and Alzheimer disease. Research efforts need to be redirected. Oxidative shielding is protective and is a misguided target for therapy. Identification of the causal chemistry and environmental factors that trigger innate immunity and metabolic memory that initiate and sustain oxidative shielding is paramount for human health.

Third one is "free to access" (www.tandfonline.com/doi/pdf/10.1080/2154896X.2012.679553).
Sorry for others...

*bump!*

It looks like your article is NOT available online, unfortunately (to check : "corrosionjournal.org/toc/corr/46/1").
It would be great if someone from a rooted institute searches the article at library archive

My deepest thanks to you, Memo...

My deepest thanks to you...

You may upload to "sendspace.com" or send to e-mail add. that I PM'd...

Title : Formation and reduction of glutathione-protein mixed disulfides during oxidative stress: A study with isolated hepatocytes and menadione (2-methyl-1,4-naphthoquinone)
Authors : G. Bellomo, F. Mirabelli, D. DiMonte, P. Richelmi, H. Thor, C. Orrenius, S. Orrenius
Journal : Biochemical Pharmacology
Publication Date : 1987
Direct Link : "www.sciencedirect.com/science/article/pii/0006295287900876"
Abstract :
Incubation of isolated rat hepatocytes with menadione (2-methyl-1,4-naphthoquinone) resulted in a dose-dependent depletion of intracellular reduced glutathione (GSH), most of which was oxidized to glutathione disulfide (GSSG). Menadione metabolism was also associated with a dose- and time-dependent inhibition of glutathione reductase, impairing the regeneration of GSH from GSSG produced during menadione-induced oxidative stress. Inhibition of glutathione reductase by pretreatment of hepatocytes with 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU) greatly potentiated both GSH depletion and GSSG formation during the metabolism of low concentrations of menadione.
Concomitant with GSH oxidation, mixed disulfides between glutathione and protein thiols were formed. The amount of mixed disulfides produced and the kinetics of their formation were dependent on both the intracellular GSH/GSSG ratio and the activity of glutathione reductase. The mixed disulfides were mainly recovered in the cytosolic fraction and, to a lesser extent, in the microsomal and mitochodrial fractions.
The removal of glutathione from protein mixed disulfides formed in hepatocytes exposed to oxidative stress was dependent on GSH and/or cysteine and appeared to occur predominantly via a thioldisulfide exchange mechanism. However, incubation of the microsomal fraction from menadione-treated hepatocytes with purified glutathione reductase in the presence of NADPH also resulted in the reduction of a significant portion of the glutathione-protein mixed disulfides present in this fraction.
Our results suggest that the formation of glutathione-protein mixed disulfides occurs as a result of increased GSSG formation and inhibition of glutathione reductase activity during menadione metabolism in hepatocytes.

Title : Catalase in vitro
Authors : Hugo Aebi
Journal : Methods in Enzymology
Publication Date : 1984
Direct Link : "www.sciencedirect.com/science/article/pii/S0076687984050163"
Abstract :
Catalase exerts a dual function: (1) decomposition of H2O2 to give H2O and O2 (catalytic activity) and (2) oxidation of H donors, for example, methanol, ethanol, formic acid, phenols, with the consumption of 1 mol of peroxide (peroxide activity). The kinetics of catalase does not obey the normal pattern. Measurements of enzyme activity at substrate saturation or determination of the Ks is therefore impossible. In contrast to reactions proceeding at substrate saturation, the enzymic decomposition of H2O2 is a first-order reaction, the rate of which is always proportional to the peroxide concentration present. Consequently, to avoid a rapid decrease in the initial rate of the reaction, the assay must be carried out with relatively low concentrations of H2O2 (about 0.01 M). This chapter discusses the catalytic activity of catalase. The method of choice for biological material, however, is ultraviolet (UV) spectrophotometry. Titrimetric methods are suitable for comparative studies. For large series of measurements, there are either simple screening tests, which give a quick indication of the approximative catalase activity, or automated methods.

Title : Plasma levels and distribution of flavonoids in rat brain after single and repeated doses of standardized Ginkgo biloba extract EGb 761®
Authors : Rangel-Ordóñez L, Nöldner M, Schubert-Zsilavecz M, Wurglics M.
Journal : Planta medica
Publication Date : 2010
Direct Link : "www.thieme-connect.com/DOI/DOI?10.1055/s-0030-1249962"
Abstract :
It is undisputed that terpene lactones and flavonoid glycosides of Ginkgo biloba are responsible for most of the extracts (e.g., EGb 761®) pharmacological actions. This investigation focused on the pharmacokinetic and the ability of the flavonoid constituents to cross the blood-brain barrier in rats, after single (600 mg/kg) or repeated (8 days, 100, or 600 mg/kg) oral administration of EGb 761®, and their distribution in different areas of the brain. For this purpose, we developed an HPLC-fluorescence method for the determination of the Ginkgo flavonoid metabolites (quercetin, kaempferol, and isorhamnetin derivatives) in the brain and plasma. A single dose of 600 mg/kg EGb 761® resulted in maximum plasma concentrations of 176, 341, and 183 ng/mL for quercetin, kaempferol, and isorhamnetin/tamarixetin, respectively and in maximum brain concentrations of 291 ng/g protein for kaempferol and 161 ng/g protein for isorhamnetin/tamarixetin. In comparison, the repeated administration of the same dose for 8 days led to an approximate 4.5-fold increase in the plasma concentration for quercetin, 11.5-fold increase for kaempferol, and 10-fold increase for isorhamnetin/tamarixetin. In the brain, an approximate 2-fold increase was observed for kaempferol and isorhamnetin/tamarixetin. About 90 % of the determined flavonoids were distributed in the hippocampus, frontal cortex, striatum, and cerebellum, which together represent only 38 % of the whole brain.

You may want to take a look at "www.911pi.co.il/en/articles/ValidatedPolygraphTechniques.pdf".

My deepest thanks to you...