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Syam Nair

Researcher at University of Gothenburg

Publications -  25
Citations -  781

Syam Nair is an academic researcher from University of Gothenburg. The author has contributed to research in topics: Neuroprotection & Inflammation. The author has an hindex of 12, co-authored 21 publications receiving 512 citations. Previous affiliations of Syam Nair include National Institute of Technology Calicut.

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Lipopolysaccharide-induced alteration of mitochondrial morphology induces a metabolic shift in microglia modulating the inflammatory response in vitro and in vivo

TL;DR: The data show that the activation of microglia to a classically pro‐inflammatory state is associated with a switch to glycolysis that is mediated by mitochondrial fission, a process which may be a pharmacological target for immunomodulation.
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Cell Death in the Developing Brain after Hypoxia-Ischemia

TL;DR: The aim of this review is update on what cell death mechanisms that are operating particularly in the setting of the developing CNS, and the provision of alternative routes through which the cell undergoes death has to be taken into account in the hunt for novel brain protective strategies.
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Temporal Characterization of Microglia/Macrophage Phenotypes in a Mouse Model of Neonatal Hypoxic-Ischemic Brain Injury.

TL;DR: HI was characterized by an early mixed gene response, but with a large expansion of mainly the CD86 positive population during the first day, suggesting a novel role in cell infiltration and immunomodulation for this cell population after neonatal injury.
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Mitochondrial dynamics, mitophagy and biogenesis in neonatal hypoxic-ischaemic brain injury.

TL;DR: Mitoprotective therapies may offer a new avenue of intervention for babies who suffer lifelong disabilities due to birth asphyxia, and act as a focal point in injury development in the immature brain.
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Computational identification of novel histone deacetylase inhibitors by docking based QSAR

TL;DR: Six compounds with good absorption, distribution, metabolism, and excretion (ADME) properties were selected as potential HDAC inhibitors and the molecular interactions of these inhibitors with the HDAC active site residues were discussed in detail.