Unlatched BAX pairs for death

Heather M. Lamb; J. Marie Hardwick

doi:10.1016/j.cell.2013.01.018

Unlatched BAX pairs for death

Heather M. Lamb, J. Marie Hardwick

Bloomberg School of Public Health

Research output: Contribution to journal › Short survey › peer-review

5 Scopus citations

Abstract

Self-interacting BAX proteins permeabilize outer mitochondrial membranes to trigger apoptotic cell death. Czabotar et al. present two revealing structures of BAX dimers: one dimer has an activator BH3 helix bound into its canonical cleft, and the other dimer exposes a planar hydrophobic face potentially critical for membrane interactions.

Original language	English (US)
Pages (from-to)	383-384
Number of pages	2
Journal	Cell
Volume	152
Issue number	3
DOIs	https://doi.org/10.1016/j.cell.2013.01.018
State	Published - Jan 31 2013

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

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10.1016/j.cell.2013.01.018

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title = "Unlatched BAX pairs for death",

abstract = "Self-interacting BAX proteins permeabilize outer mitochondrial membranes to trigger apoptotic cell death. Czabotar et al. present two revealing structures of BAX dimers: one dimer has an activator BH3 helix bound into its canonical cleft, and the other dimer exposes a planar hydrophobic face potentially critical for membrane interactions.",

author = "Lamb, {Heather M.} and Hardwick, {J. Marie}",

note = "Funding Information: The Hardwick laboratory is supported by funding from NIH grants RO1 NS037402 and F31 GM095253 and the CURE Epilepsy Foundation.",

year = "2013",

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doi = "10.1016/j.cell.2013.01.018",

language = "English (US)",

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T1 - Unlatched BAX pairs for death

AU - Lamb, Heather M.

AU - Hardwick, J. Marie

N1 - Funding Information: The Hardwick laboratory is supported by funding from NIH grants RO1 NS037402 and F31 GM095253 and the CURE Epilepsy Foundation.

PY - 2013/1/31

Y1 - 2013/1/31

N2 - Self-interacting BAX proteins permeabilize outer mitochondrial membranes to trigger apoptotic cell death. Czabotar et al. present two revealing structures of BAX dimers: one dimer has an activator BH3 helix bound into its canonical cleft, and the other dimer exposes a planar hydrophobic face potentially critical for membrane interactions.

AB - Self-interacting BAX proteins permeabilize outer mitochondrial membranes to trigger apoptotic cell death. Czabotar et al. present two revealing structures of BAX dimers: one dimer has an activator BH3 helix bound into its canonical cleft, and the other dimer exposes a planar hydrophobic face potentially critical for membrane interactions.

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DO - 10.1016/j.cell.2013.01.018

M3 - Short survey

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VL - 152

SP - 383

EP - 384

JO - Cell

JF - Cell

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ER -

Unlatched BAX pairs for death

Abstract

ASJC Scopus subject areas

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