(Q24336699)

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Knockdown of glutamate-cysteine ligase by small hairpin RNA reveals that both catalytic and modulatory subunits are essential for the survival of primary neurons

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scholarly article

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Knockdown of glutamate-cysteine ligase by small hairpin RNA reveals that both catalytic and modulatory subunits are essential for the survival of primary neurons (English)

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Glutamate-cysteine ligase modifier subunit

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GOA release 2020-03-11

Glutamate-cysteine ligase catalytic subunit

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GOA release 2020-03-11

glutamate-cysteine ligase activity

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GOA release 2020-03-11

María Delgado Esteban

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ORCID Public Data File 2021

author name string

Juan I Diaz-Hernandez

1

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Angeles Almeida

2

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Maria Delgado-Esteban

3

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Emilio Fernandez

4

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Juan P Bolaños

5

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language of work or name

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publication date

25 November 2005

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Journal of Biological Chemistry

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280

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47

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38992-9001

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Metabolism and functions of glutathione in brain.

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Free radicals and aging.

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Amino acid sequence of rat kidney glutathione synthetase

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Knockout of the mouse glutamate cysteine ligase catalytic subunit (Gclc) gene: embryonic lethal when homozygous, and proposed model for moderate glutathione deficiency when heterozygous

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Glutathione synthesis is essential for mouse development but not for cell growth in culture

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Initial characterization of the glutamate-cysteine ligase modifier subunit Gclm(-/-) knockout mouse. Novel model system for a severely compromised oxidative stress response

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Glutathione depletion resulting in selective mitochondrial complex I inhibition in dopaminergic cells is via an NO-mediated pathway not involving peroxynitrite: implications for Parkinson's disease

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Determination of glutamate-cysteine ligase (gamma-glutamylcysteine synthetase) activity by high-performance liquid chromatography and electrochemical detection

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Peroxynitrite protects neurons against nitric oxide-mediated apoptosis. A key role for glucose-6-phosphate dehydrogenase activity in neuroprotection

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Multi-faceted regulation of gamma-glutamylcysteine synthetase

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Oligodendroglial cells in culture effectively dispose of exogenous hydrogen peroxide: comparison with cultured neurones, astroglial and microglial cells.

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Gamma-glutamylcysteine ethyl ester-induced up-regulation of glutathione protects neurons against Abeta(1-42)-mediated oxidative stress and neurotoxicity: implications for Alzheimer's disease

1 reference

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Glial cells protect neurons against oxidative stress via transcriptional up-regulation of the glutathione synthesis

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Differential effect of nitric oxide on glutathione metabolism and mitochondrial function in astrocytes and neurones: implications for neuroprotection/neurodegeneration?

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Co-culture of neurones with glutathione deficient astrocytes leads to increased neuronal susceptibility to nitric oxide and increased glutamate-cysteine ligase activity

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Depletion of brain glutathione is accompanied by impaired mitochondrial function and decreased N-acetyl aspartate concentration.

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Nitric oxide mediates glutamate neurotoxicity in primary cortical cultures

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Gene regulation and DNA damage in the ageing human brain

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Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues

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7 January 2021

based on heuristic

inferred from DOI database lookup

Nitric oxide-mediated mitochondrial damage: a potential neuroprotective role for glutathione

1 reference

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7 January 2021

based on heuristic

inferred from DOI database lookup

Isolation of highly purified γ-glutamylcysteine synthetase from rat kidney

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507065200

7 January 2021

based on heuristic

inferred from DOI database lookup

Astrocytes provide cysteine to neurons by releasing glutathione

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507065200

7 January 2021

based on heuristic

inferred from DOI database lookup

Two types of astrocytes in cultures of developing rat white matter: differences in morphology, surface gangliosides, and growth characteristics

1 reference

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7 January 2021

based on heuristic

inferred from DOI database lookup

Identifiers

10.1074/JBC.M507065200

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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