(Q42468203)

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Glial expression of the 90-kDa heat shock protein (HSP90) and the 94-kDa glucose-regulated protein (GRP94) following an excitotoxic lesion in the mouse hippocampus

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Europe PubMed Central

PubMed publication ID

1 November 2017

Glial expression of the 90-kDa heat shock protein (HSP90) and the 94-kDa glucose-regulated protein (GRP94) following an excitotoxic lesion in the mouse hippocampus (English)

1 reference

Europe PubMed Central

PubMed publication ID

1 November 2017

1 reference

based on heuristic

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author name string

Gye Sun Jeon

1

1 reference

Europe PubMed Central

PubMed publication ID

1 November 2017

Sang Wook Park

2

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Europe PubMed Central

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1 November 2017

Dong Woon Kim

3

1 reference

Europe PubMed Central

PubMed publication ID

1 November 2017

Je Hoon Seo

4

1 reference

Europe PubMed Central

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1 November 2017

Jaeyoung Cho

5

1 reference

Europe PubMed Central

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1 November 2017

So Young Lim

6

1 reference

Europe PubMed Central

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1 November 2017

Seong Deok Kim

7

1 reference

Europe PubMed Central

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1 November 2017

Sa Sun Cho

8

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Europe PubMed Central

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1 November 2017

publication date

1 November 2004

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Europe PubMed Central

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1 November 2017

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Europe PubMed Central

PubMed publication ID

1 November 2017

48

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Europe PubMed Central

PubMed publication ID

1 November 2017

3

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Europe PubMed Central

PubMed publication ID

1 November 2017

250-258

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Europe PubMed Central

PubMed publication ID

1 November 2017

Induction of heat shock proteins and their possible roles in macrophages during activation by macrophage colony-stimulating factor

1 reference

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Glial expression of small heat shock proteins following an excitotoxic lesion in the immature rat brain

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GRP94 (94 kDa glucose-regulated protein) suppresses ischemic neuronal cell death against ischemia/reperfusion injury

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Heme oxygenase-1 (HSP-32) and heme oxygenase-2 induction in neurons and glial cells of cerebral regions and its relation to iron accumulation after focal cortical photothrombosis.

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Heat shock protein 90 mediates macrophage activation by Taxol and bacterial lipopolysaccharide

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Erythrophagocytosis induces heat shock protein synthesis by human monocytes-macrophages

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The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review

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Protein kinase C isozymes and the regulation of diverse cell responses

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Correlation between seizure intensity and stress protein expression after limbic epilepsy in the rat brain

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Exposure of astrocytes to hypoxia/reoxygenation enhances expression of glucose-regulated protein 78 facilitating astrocyte release of the neuroprotective cytokine interleukin 6

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Microglia-specific localisation of a novel calcium binding protein, Iba1

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Induction of transcription factor c-myb expression in reactive astrocytes following intracerebroventricular kainic acid injection in mouse hippocampus

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Induction of HSP90 alpha heat shock mRNA after transient global ischemia in gerbil hippocampus

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Expression of the Endoplasmic Reticulum Chaperone GRP94 Gene in Ischemic Gerbil Brain

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Mammalian stress response: induction of the glucose-regulated protein family

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Intracerebroventricular injections in mice. Some methodological refinements

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The heat-shock proteins

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Induction of glucose-regulated protein (glucose-regulated protein 78/BiP and glucose-regulated protein 94) and heat shock protein 70 transcripts in the immature rat brain following status epilepticus.

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Vitamin E, ascorbate, glutathione, glutathione disulfide, and enzymes of glutathione metabolism in cultures of chick astrocytes and neurons: evidence that astrocytes play an important role in antioxidative processes in the brain

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Mouse Lymphoma Cells Destined to Undergo Apoptosis in Response to Thapsigargin Treatment Fail to Generate a Calcium-mediatedgrp78/grp94Stress Response

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Induction of heat-shock proteins and phagocytic function of chicken macrophage following in vitro heat exposure

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Microglial and astrocytic cell responses in the rat hippocampus after an intracerebroventricular kainic acid injection

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7 January 2021

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Cells in stress: transcriptional activation of heat shock genes

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Stress protein co-localization to autofluorescent astrocytic inclusions in situ and in cysteamine-treated glial cultures

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Degeneration of hippocampal CA3 pyramidal cells induced by intraventricular kainic acid

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Heat shock protein 90.

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Roles of molecular chaperones in the nervous system

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Interrelationships between astrocyte function, oxidative stress and antioxidant status within the central nervous system.

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7 January 2021

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Heat shock proteins: regulators of stress response and apoptosis

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Expression of 27 kDa heat shock protein (Hsp27) in immature rat brain after a cortical aspiration lesion.

1 reference

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Heat-shock protein protection.

1 reference

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Heat shock protein-90-induced microglial clearance of exogenous amyloid-beta1-42 in rat hippocampus in vivo

1 reference

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ORP150 protects against hypoxia/ischemia-induced neuronal death

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Hsp47: a molecular chaperone that interacts with and stabilizes correctly-folded procollagen

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[Stress response of cultured astrocytes to hypoxia/reoxygenation]

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Heme oxygenase-1 is induced in glia throughout brain by subarachnoid hemoglobin

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Geldanamycin inhibits the production of inflammatory cytokines in activated macrophages by reducing the stability and translation of cytokine transcripts

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Binding specificity of avian heat shock protein 108

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PKC epsilon is a unique regulator for hsp90 beta gene in heat shock response

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Colocalization of Ca2+-ATPase and GRP94 with p58 and the effects of thapsigargin on protein recycling suggest the participation of the pre-Golgi intermediate compartment in intracellular Ca2+ storage

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Heat shock protein 90 as an endogenous protein enhancer of inducible nitric-oxide synthase

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Increase in vulnerability of middle-aged rat brain to lead by cerebral energy depletion

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Induction of P-glycoprotein expression in astrocytes following intracerebroventricular kainate injections

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Identifiers

10.1002/GLIA.20075

1 reference

Europe PubMed Central

PubMed publication ID

1 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 November 2017

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