(Q77136049)

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Induction of the mitochondrial permeability transition as a mechanism of liver injury during cholestasis: a potential role for mitochondrial proteases

scientific article published on 01 August 1998

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3 December 2019

Induction of the mitochondrial permeability transition as a mechanism of liver injury during cholestasis: a potential role for mitochondrial proteases (English)

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3 December 2019

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G J Gores

1

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3 December 2019

H Miyoshi

2

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3 December 2019

R Botla

3

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H I Aguilar

4

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3 December 2019

S F Bronk

5

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1 August 1998

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3 December 2019

Biochimica et Biophysica Acta

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3 December 2019

1366

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3 December 2019

1-2

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167-175

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3 December 2019

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Glycochenodeoxycholate-induced lethal hepatocellular injury in rat hepatocytes. Role of ATP depletion and cytosolic free calcium

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The permeability transition pore. Control points of a cyclosporin A-sensitive mitochondrial channel involved in cell death

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Recent progress on regulation of the mitochondrial permeability transition pore; a cyclosporin-sensitive pore in the inner mitochondrial membrane

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A rapid and simple procedure to deplete rat-liver mitochondria of lysosomal activity

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Taurine-conjugated bile acids act as calcium ionophores

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Acidosis protects against lethal oxidative injury of liver sinusoidal endothelial cells

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Calpain: new perspectives in molecular diversity and physiological-pathological involvement.

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Calcium-activated proteolytic activity in rat liver mitochondria

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7 January 2021

Ceramide induces hepatocyte cell death through disruption of mitochondrial function in the rat.

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Enzymatic properties of the inner and outer membranes of rat liver mitochondria

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tBHP induced in vitro swelling of rat liver mitochondria.

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An epithelial serine protease activates the amiloride-sensitive sodium channel

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The central executioner of apoptosis: multiple connections between protease activation and mitochondria in Fas/APO-1/CD95- and ceramide-induced apoptosis

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Mitochondria are excitable organelles capable of generating and conveying electrical and calcium signals.

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Spectroscopic study of the activation and oligomerization of the channel-forming toxin aerolysin: identification of the site of proteolytic activation.

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The peptide mastoparan is a potent facilitator of the mitochondrial permeability transition

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7 January 2021

Identifiers

10.1016/S0005-2728(98)00111-X

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Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9714791%20AND%20SRC:MED&resulttype=core&format=json

3 December 2019

1 reference

Europe PubMed Central

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3 December 2019

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