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Annapurna Chalasani

Researcher at University College London

Publications -  12
Citations -  718

Annapurna Chalasani is an academic researcher from University College London. The author has contributed to research in topics: Mitochondrial disease & Cerebellar ataxia. The author has an hindex of 8, co-authored 12 publications receiving 579 citations. Previous affiliations of Annapurna Chalasani include Moorfields Eye Hospital.

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Nrf2 impacts cellular bioenergetics by controlling substrate availability for mitochondrial respiration

TL;DR: A novel role is demonstrated for Nrf2 in directly regulating mitochondrial bioenergetics in murine neurons and embryonic fibroblasts through modulating the availability of substrates for mitochondrial respiration and the importance of efficient energy metabolism in NRF2-mediated cytoprotection.
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Signal transducer and activator of transcription 2 deficiency is a novel disorder of mitochondrial fission.

TL;DR: A novel mutation in STAT2, which encodes a component of the JAK-STAT cytokine signalling pathway, is identified in three patients with severe neurological deterioration following viral infection, suggesting a new avenue for treatment of mitochondrial diseases and possibly common neurodegenerative disorders.
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Human neuronal coenzyme Q10 deficiency results in global loss of mitochondrial respiratory chain activity, increased mitochondrial oxidative stress and reversal of ATP synthase activity: implications for pathogenesis and treatment.

TL;DR: A neuronal cell model of CoQ10 deficiency is established by treatment of neuronal SH-SY5Y cell line with para-aminobenzoic acid, providing insights into the effects of coenzyme Q10 deficiency on neuronal mitochondrial function and oxidative stress.
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Autosomal-recessive cerebellar ataxia caused by a novel ADCK3 mutation that elongates the protein: clinical, genetic and biochemical characterisation

TL;DR: A novel homozygous frameshift mutation in ADCK3, which results in the loss of the stop codon, is identified in both siblings and broadens the phenotypic spectrum associated with ADCk3 mutations and provides further understanding of their pathogenic mechanism.