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  • About
  • The Global ETD Search service is a free service for researchers to find electronic theses and dissertations. This service is provided by the Networked Digital Library of Theses and Dissertations.
    Our metadata is collected from universities around the world. If you manage a university/consortium/country archive and want to be added, details can be found on the NDLTD website.
51

Stability and aggregation propensities of ALS-associated human superoxide dismutase mutants

Tong, Ming Sze January 2010 (has links)
Amyotrophic lateral sclerosis (ALS) is the most common motor neuron disease and is characterized by progressive paralysis leading to death, typically, within 3-5 years of the onset of symptoms. The majority of ALS cases are sporadic with no known causative agent; however, 5-10% of ALS cases are genetically inherited and termed familial ALS (fALS). Approximately, 15-20% of these fALS cases have been linked to mutations in the gene encoding human Cu/Zn superoxide dismutase (hSOD). To date, over 140 hSOD mutations have been discovered. The mechanisms by which mutant hSOD confers toxicity in fALS patients are still unknown. However, there is growing evidence that ALS is a type of protein conformational disease whereby cell damage or death is caused by the accumulation of protein aggregates in the cell. It is hypothesized that mutations destabilise hSOD and increase its propensity to aggregate. There is some controversy as to which hSOD species contributes to aggregation. Many believe that only apo or mismetallated forms of hSOD are able to aggregate. Due to the abundance of fully metallated or holo hSOD in the cell, we hypothesize that holo hSOD can also lead to aggregation. Holo dimer interface mutants A4S, A4T and I113T as well as G41D were found to be destabilized compared to holo pseudo wildtype (pWT) while zinc binding mutant H80R was shown to form fragments via an unknown mechanism. Holo dimer interface mutants A4S and A4T were also shown to have an increased propensity to aggregate compared to pWT, which correlates to their decreased stability as well a short disease durations.
52

Stability and aggregation propensities of ALS-associated human superoxide dismutase mutants

Tong, Ming Sze January 2010 (has links)
Amyotrophic lateral sclerosis (ALS) is the most common motor neuron disease and is characterized by progressive paralysis leading to death, typically, within 3-5 years of the onset of symptoms. The majority of ALS cases are sporadic with no known causative agent; however, 5-10% of ALS cases are genetically inherited and termed familial ALS (fALS). Approximately, 15-20% of these fALS cases have been linked to mutations in the gene encoding human Cu/Zn superoxide dismutase (hSOD). To date, over 140 hSOD mutations have been discovered. The mechanisms by which mutant hSOD confers toxicity in fALS patients are still unknown. However, there is growing evidence that ALS is a type of protein conformational disease whereby cell damage or death is caused by the accumulation of protein aggregates in the cell. It is hypothesized that mutations destabilise hSOD and increase its propensity to aggregate. There is some controversy as to which hSOD species contributes to aggregation. Many believe that only apo or mismetallated forms of hSOD are able to aggregate. Due to the abundance of fully metallated or holo hSOD in the cell, we hypothesize that holo hSOD can also lead to aggregation. Holo dimer interface mutants A4S, A4T and I113T as well as G41D were found to be destabilized compared to holo pseudo wildtype (pWT) while zinc binding mutant H80R was shown to form fragments via an unknown mechanism. Holo dimer interface mutants A4S and A4T were also shown to have an increased propensity to aggregate compared to pWT, which correlates to their decreased stability as well a short disease durations.
53

Use of dietary chitin and chitosan in enhancing resistance of Penaeus monodon against WSSV and Vibrio infections

Yang, Jia-Horng 12 September 2002 (has links)
Three experiments were conducted to evaluate the effects of dietary chitin and chitosan on growth, immune responses and resistance of grass prawn Penaeus monodon against white spot syndrome virus (WSSV) and Vibrio infections. In the first experiment, two levels (0.5¡B1 g/100g diet) of chitin and three levels (0.5¡B1¡B5 g/100g diet) of chitosan were evaluated. The results show that weight gain of the shrimp fed on diet containing no chitosan or the lowest level of chitosan (0.5 %) was higher than other groups. In the second experiment, four levels of chitosan (0¡B0.5¡B1¡B5 g/100g diet) were tested. Weight gains of the control (0 %) and 0.5 % chitosan groups were significantly (P<0.05) higher than the 0.1 and 1 % chitosan groups. Shrimp survival rate was not influenced by chitosan inclusion. The test shrimp of the first experiment were evaluated for their immune responses after dietary exposures. The results show that phenoloxidase activity and superoxide dismutase were not significantly different (P>0.05) among treatments. The production of superoxide anion in the 0.5 % chitin group was significantly (P<0.05) lower than the other groups at day 3 and 12. The last experiment evaluated the effectiveness of dietary chitosan against infection of WSSV and Vibrio damsela. Shrimp were fed for 20 days on test diets containing four levels of chitosan (0¡B0.5¡B1¡B5 g/100g diet) and then challenged by injection of WSSV or Vibrio solution. In the WSSV challenge, except at day 7, shrimp survivals were not different among treatments. At day 7, however, the survival rates of the shrimp fed the diet containing 0.1 or 1 % chitosan were significantly (P<0.05) higher than those of the other groups. When challenged with Vibrio damsela, there was no difference in shrimp survival among dietary treatments. The present study shows that dietary chitin and chitosan do not significantly enhance immune responses and disease resistance of juvenile P. monodon. Dietary incorporation of chitin or chitosan negatively affects shrimp growth.
54

A study of the activity and characteristics of superoxide dismutase in the male reproductive parts of petunia

Moon, Bok Hee January 2006 (has links)
In the stamen (male reproductive tissue) of petunia 'Hurrah' flowers, the occurrence of SOD (superoxide dismutase) provided an effective anti-oxidative mechanism against superoxide production. Superoxide production and SOD activities at five developmental stages showed a positive correlation. The highest superoxide production and SOD activity in different parts of the stamen (anther, filament and pollen) were at stages with high metabolic activity: (i) during growing buds (in anthers and filaments) (ii) when flowers with predehiscent anthers were fully open (in pollen). In all parts of the stamen, SOD activity was the lowest at stage five (fully open flowers with dehiscent anthers), superoxide production was also lower at this stage with the exception of the pollen. The highest SOD activity was localized in anthers with the pollen, suggesting that the filaments only have a structural support function. SOD was examined on a native PAGE with regard to the isozymes present within the stamen of five developmental stages. Three isozymes, which were identified as Mn SOD, Fe SOD and Cu/Zn SOD by reactions with inhibitors, were commonly found at five developmental stages in crude extracts of anthers, filaments and pollen. The developmental stages with stronger isozyme bands on the native PAGE were consistent with the stages with higher SOD activities, and the Mn SOD and Fe SOD isozyme bands were more intense than Cu/Zn SOD bands, suggesting the activities of Mn SOD and Fe SOD in the crude extracts were much higher than Cu/Zn SOD. SOD from 1,000 stamens of dehiscent mature flowers was partially purified using ammonium sulphate fractionation and DEAE cellulose column chromatography. The purified bound fraction contained only one SOD isozyme on a native PAGE, which was shown to be a Mn SOD, as it is sensitive to neither hydrogen peroxide nor cyanide. The specific activity of the purified SOD was 66.5 U/mg and the yield of total activity was 3.0%. The progress of enzyme purification was monitored using SDS-PAGE and the bound fraction contained two major polypeptide bands. The purified enzyme activity was optimal in the range of neutral pH, but it was the highest at pH 7.8. Through incubation at various pH levels for 24 hours, favourable stability of the purified fraction was confirmed around a pH range of 7 to 8.5. The purified enzyme retained 87% of its initial activity at -20 ? after one month of storage, but at 4 ? only 38% of the initial activity remained after the same period of storage.
55

Oxy radicals and control of inflammation /

Cleland, Leslie G. January 1984 (has links) (PDF)
Thesis (M.D.)--University of Adelaide, Dept. of Medicine and Pathology, 1985. / Includes bibliographical references (leaves 161-204).
56

Protein folding studies of human superoxide dismutase and ALS associated mutants /

Lindberg, Mikael, January 2004 (has links)
Diss. (sammanfattning) Umeå : Univ., 2004. / Härtill 4 uppsatser.
57

Copper, zinc superoxide dismutase and mitochondria : implications for familial amyotrophic lateral sclerosis /

Fujita, Hibiki Kawamata. January 2008 (has links)
Thesis (Ph. D.)--Cornell University, August, 2008. / Vita. Includes bibliographical references (leaves 131-153).
58

Oxidative stress induced mitochondrial dysfunction accelerates age related muscle atrophy a dissertation /

Jang, Youngmok C. January 2008 (has links)
Dissertation (Ph.D.).--University of Texas Graduate School of Biomedical Sciences at San Antonio, 2008. / Vita. Includes bibliographical references.
59

The central role of calcium dysregulation in a primary cell culture model of amyotrophic lateral sclerosis

Tradewell, Miranda, January 1900 (has links)
Thesis (Ph.D.). / Written for the Dept. of Neurological Sciences. Title from title page of PDF (viewed 2009/06/11). Includes bibliographical references.
60

Importance des dérivés réduits de l'oxygène dans l'intoxication alcoolique chez le rat : rôle de la desferrioxamine /

Sinaceur, Jamal Eddine. January 1987 (has links)
Th.--Pharm.--Paris-Sud, 1985. / Bibliogr. p. 189-215.

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