S
Sharad S. Singhal
Researcher at University of Texas at Arlington
Publications - 103
Citations - 5731
Sharad S. Singhal is an academic researcher from University of Texas at Arlington. The author has contributed to research in topics: Glutathione & Glutathione S-transferase. The author has an hindex of 43, co-authored 92 publications receiving 5566 citations. Previous affiliations of Sharad S. Singhal include University of Texas Medical Branch & University of Arkansas for Medical Sciences.
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Journal ArticleDOI
Naturally occurring human glutathione S-transferase GSTP1-1 isoforms with isoleucine and valine in position 104 differ in enzymic properties
Piotr Zimniak,Bindu Nanduri,Slawomir Pikula,Joanna Bandorowicz-Pikula,Sharad S. Singhal,Sanjay K. Srivastava,Sanjay Awasthi,Yogesh C. Awasthi +7 more
TL;DR: Data indicate that the residue in position 104 helps to define the geometry of the hydrophobic substrate-binding site, and may also influence activity by interacting with residues directly involved in substrate binding.
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Role of glutathione S-transferases in protection against lipid peroxidation. Overexpression of hGSTA2-2 in K562 cells protects against hydrogen peroxide-induced apoptosis and inhibits JNK and caspase 3 activation.
Yusong Yang,Ji-Zhong Cheng,Sharad S. Singhal,Manjit K. Saini,Utpal Pandya,Sanjay Awasthi,Yogesh C. Awasthi +6 more
TL;DR: The physiological significance of the selenium-independent glutathione peroxidase (GPx) activity of the major Alpha class isoenzymes, associated with the major GSTs hGSTA1-1 and hGstA2-2, is not known as mentioned in this paper.
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Mechanisms of anticarcinogenic properties of curcumin: the effect of curcumin on glutathione linked detoxification enzymes in rat liver
John T. Piper,Sharad S. Singhal,Mohammad S Salameh,Robert T. Torman,Yogesh C. Awasthi,Sanjay Awasthi +5 more
TL;DR: The results suggest that induction of enzymes involved in the detoxification of the electrophilic products of lipid peroxidation may contribute to the anti-inflammatory and anti-cancer activities of curcumin.
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Human glutathione S-transferases
TL;DR: GST isoenzymes present in human tissues are dimers of subunits belonging to three distinct gene families namely alpha, mu and pi as discussed by the authors, and only the subunits within each class hybridize to give active dimers.
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Accelerated metabolism and exclusion of 4-hydroxynonenal through induction of RLIP76 and hGST5.8 is an early adaptive response of cells to heat and oxidative stress.
Ji-Zhong Cheng,Rajendra Sharma,Yusong Yang,Sharad S. Singhal,Abha Sharma,Manjit K. Saini,Shivendra V. Singh,Piotr Zimniak,Sanjay Awasthi,Yogesh C. Awasthi +9 more
TL;DR: Stress-pre-conditioned cells with induced hGST5.8 and RLIP76 acquired resistance to 4-HNE and H2O2-mediated apoptosis by suppressing a sustained activation of c-Jun N-terminal kinase and caspase 3, suggesting a role of LPO products, particularly 4- HNE, in the initial phase of stress mediated signaling.