Clofilium, a potassium channel blocker, induces apoptosis of human promyelocytic leukemia (HL-60) cells via Bcl-2-insensitive activation of caspase-3. (Q42483203)

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scientific article published on December 1999

Language	Label	Description	Also known as
English	Clofilium, a potassium channel blocker, induces apoptosis of human promyelocytic leukemia (HL-60) cells via Bcl-2-insensitive activation of caspase-3.	scientific article published on December 1999

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

1 November 2017

Clofilium, a potassium channel blocker, induces apoptosis of human promyelocytic leukemia (HL-60) cells via Bcl-2-insensitive activation of caspase-3. (English)

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Europe PubMed Central

PubMed publication ID

1 November 2017

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author name string

B Y Choi

1

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1 November 2017

H Y Kim

2

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1 November 2017

K H Lee

3

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1 November 2017

Y H Cho

4

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1 November 2017

G Kong

5

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1 November 2017

language of work or name

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publication date

1 December 1999

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1 November 2017

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1 November 2017

147

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1 November 2017

1-2

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1 November 2017

85-93

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1 November 2017

Screening for novel drug effects with a microphysiometer: a potent effect of clofilium unrelated to potassium channel blockade

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Inhibition of calmodulin and protein kinase C by amiodarone and other class III antiarrhythmic agents

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The effect of clofilium, a K-channel blocker, on the electrogenic K secretion and the sensory discharge at the frog semicircular canal

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Caspases: the executioners of apoptosis

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Caspases: killer proteases

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Mitochondria and apoptosis

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The Bcl-2 protein family: arbiters of cell survival

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Life, death, and the pursuit of apoptosis.

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Bcl-2 and the ICE family of apoptotic regulators: making a connection.

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Human ICE/CED-3 protease nomenclature

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Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE

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Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase

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Molecular ordering of the cell death pathway. Bcl-2 and Bcl-xL function upstream of the CED-3-like apoptotic proteases

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Apoptosis induced by anticancer drugs

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Programmed cell death (apoptosis) and response to anti-cancer drugs.

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Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis

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The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation

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RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death

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Identifiers

10.1016/S0304-3835(99)00280-3

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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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