Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC (Q22009974)

GOA release 2020-03-11

mitochondrion

1 reference

Erratum: correction: BcL-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC

inferred from title

corrigendum / erratum

1 reference

12 July 2019

http://api.crossref.org/works?select=update-to&filter=doi:10.1038/35037638

M Narita

2

Masashi

Narita

1 reference

6 September 2022

S Shimizu

1

Shigeomi

Shimizu

1 reference

1031691936

6 September 2022

Y Tsujimoto

series ordinal

3

author given names

Yoshihide

author last names

Tsujimoto

1 reference

1031691936

6 September 2022

Yoshihide Tsujimoto

author given names

Yoshihide

author last names

Tsujimoto

series ordinal

4

1 reference

1031691936

6 September 2022

language of work or name

English

0 references

publication date

3 June 1999

0 references

published in

Nature

0 references

volume

399

0 references

issue

6735

0 references

page(s)

483-7

0 references

cites work

Caspases: enemies within

1 reference

7 January 2021

Mitochondria and apoptosis

1 reference

7 January 2021

Bcl-2 gene family in the nervous system

1 reference

7 January 2021

The Bcl-2 protein family: arbiters of cell survival

1 reference

7 January 2021

Role of Bcl-2 family proteins in apoptosis: apoptosomes or mitochondria?

1 reference

7 January 2021

Bax directly induces release of cytochrome c from isolated mitochondria

1 reference

7 January 2021

Bax-induced cytochrome C release from mitochondria is independent of the permeability transition pore but highly dependent on Mg2+ ions

1 reference

7 January 2021

Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria

1 reference

7 January 2021

Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis

1 reference

7 January 2021

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

1 reference

7 January 2021

The mitochondrial permeability transition.

1 reference

7 January 2021

Voltage gating in the mitochondrial channel, VDAC.

1 reference

7 January 2021

Inhibition of Bax channel-forming activity by Bcl-2

1 reference

7 January 2021

Bcl-x(L) forms an ion channel in synthetic lipid membranes.

1 reference

7 January 2021

Channel formation by antiapoptotic protein Bcl-2.

1 reference

7 January 2021

Comparison of the ion channel characteristics of proapoptotic BAX and antiapoptotic BCL-2.

1 reference

7 January 2021

Bax-independent inhibition of apoptosis by Bcl-XL.

1 reference

7 January 2021

Role of mitochondria and C-terminal membrane anchor of Bcl-2 in Bax induced growth arrest and mortality in Saccharomyces cerevisiae

1 reference

7 January 2021

The Mitochondrial F0F1-ATPase proton pump is required for function of the proapoptotic protein Bax in yeast and mammalian cells.

1 reference

7 January 2021

Selectivity Changes in Site-Directed Mutants of the VDAC Ion Channel: Structural Implications

1 reference

7 January 2021

The role of yeast VDAC genes on the permeability of the mitochondrial outer membrane

1 reference

7 January 2021

Conformational changes in the mitochondrial channel protein, VDAC, and their functional implications

1 reference

7 January 2021

Bcl-2 prevents apoptotic mitochondrial dysfunction by regulating proton flux

1 reference

7 January 2021

A simple and rapid method for the purification of the mitochondrial porin from mammalian tissues

1 reference

7 January 2021

Reconstituted adenine nucleotide translocase forms a channel for small molecules comparable to the mitochondrial permeability transition pore

1 reference

7 January 2021

Transport properties and inhibitor sensitivity of isolated and reconstituted porin differ from those of intact mitochondria

1 reference

7 January 2021