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Kunju Sridhar

Researcher at Stanford University

Publications -  25
Citations -  1101

Kunju Sridhar is an academic researcher from Stanford University. The author has contributed to research in topics: Heme oxygenase & Myelodysplastic syndromes. The author has an hindex of 10, co-authored 23 publications receiving 957 citations. Previous affiliations of Kunju Sridhar include United States Department of Veterans Affairs & VA Palo Alto Healthcare System.

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Hematopoietic stem cell and progenitor cell mechanisms in myelodysplastic syndromes

TL;DR: A recurrent loss of granulocyte-macrophage progenitors (GMPs) in the bone marrow of low risk MDS patients that can distinguish lowrisk MDS from clinical mimics, thus providing a simple diagnostic tool.
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Interaction of rat hormone-sensitive lipase with adipocyte lipid-binding protein

TL;DR: Results suggest that HSL-derived fatty acids are bound by ALBP to facilitate intracellular trafficking of hydrophobic lipids.
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Heme oxygenase-mediated resistance to oxygen toxicity in hamster fibroblasts

TL;DR: HO mediates cytoprotection to oxygen toxicity within a narrow range of expression and it is speculated that this protective effect may be mediated in part through increased metabolism of the pro-oxidant heme but that higher levels of HO activity obviate protection by increased redox active iron release.
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Protective effects of transient HO-1 overexpression on susceptibility to oxygen toxicity in lung cells

TL;DR: Rat fetal lung cells were transiently transfected with a full-length rat heme oxygenase (HO)-1 cDNA construct and exposed to hyperoxia to conclude that moderate overexpression of HO-1 is protective against oxidative injury, but it is speculated that there is a beneficial threshold ofHO-1 expression.
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Characterization of the functional interaction of adipocyte lipid-binding protein with hormone-sensitive lipase.

TL;DR: HSL and ALBP constitute a functionally important lipolytic complex that increases the hydrolytic activity of HSL through its ability to bind and sequester fatty acids and via specific protein-protein interaction.