Institution
University of Madras
Education•Chennai, Tamil Nadu, India•
About: University of Madras is a education organization based out in Chennai, Tamil Nadu, India. It is known for research contribution in the topics: Ring (chemistry) & Lipid peroxidation. The organization has 8496 authors who have published 11369 publications receiving 211152 citations. The organization is also known as: Madras University & University of Chennai.
Papers published on a yearly basis
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TL;DR: Increased‐concentration AgNPs show increased recovery action in comparison to the positive drug treated group, and Groups IV and V showed much better healing properties than did the positiveDrug treated group VI.
60 citations
TL;DR: The assessment of oxygen consumption, filtration and ATPases system can be used as a valid biomarker in aquatic ecotoxicology studies and indicates that chromium was more toxic to mussels when compared to silver.
60 citations
TL;DR: The increase in lipid peroxidation and superoxide dismutase (SOD) activity, associated with a decrease in catalase activity and glutathione level, are the salient features observed in tissues of hyperoxaluric rats.
60 citations
TL;DR: The results indicate that the ion pairs may contribute to the stability of solvent‐exposed alpha helices, and since the stabilization of protein secondary structure, may throw light on the mechanism of protein folding.
Abstract: A survey of 47 globular proteins was made to determine the probability of occurrence of ion pairs separated by 1,2,3,... and 8 residues in the alpha helices. As a control, the probability of occurrence of like charged pairs was also determined. The survey showed that ion pairs of the type i,i +/- 3 and i, i +/- 4 are the most predominant. Such a preference was not observed for like charged pairs. The observed frequency of ion pairs is significantly greater than their expected frequency. The normalized frequencies of occurrence of the ion pairs were also found to increase generally with the helix length. These results indicate that the ion pairs may contribute to the stability of solvent-exposed alpha helices. Since the stabilization of protein secondary structure enhances the stability of protein tertiary structure, these results may throw light on the mechanism of protein folding.
60 citations
TL;DR: The bimediator modified electrode was found to exhibit good stability and reproducibility and electrocatalytic activity towards oxidation of gallic acid with NiHCF and reduction of hydrogen peroxide with TH was evaluated.
60 citations
Authors
Showing all 8535 results
| Name | H-index | Papers | Citations |
|---|---|---|---|
| David A. Kass | 127 | 580 | 58747 |
| Viswanathan Mohan | 110 | 964 | 64896 |
| Sridevi Devaraj | 85 | 365 | 21831 |
| Raghavan Srinivasan | 80 | 959 | 37821 |
| Muthupandian Ashokkumar | 76 | 511 | 20771 |
| K.V. Rajagopalan | 71 | 223 | 15129 |
| Rajasekhar Balasubramanian | 65 | 276 | 13854 |
| Savarimuthu Ignacimuthu | 64 | 498 | 17752 |
| Pappannan Thiyagarajan | 59 | 245 | 10650 |
| Ravi Subrahmanyan | 59 | 353 | 14244 |
| Fritz Scholz | 55 | 385 | 11420 |
| M. Lakshmanan | 54 | 533 | 13357 |
| Nagarajan Selvamurugan | 52 | 153 | 9477 |
| Kumarasamy Thangaraj | 47 | 361 | 11869 |
| Suniti Solomon | 46 | 191 | 6400 |