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Pore formation by dimeric Bak and Bax: an unusual pore?

Pore formation by dimeric Bak and Bax: an unusual pore?

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Membrane pores: from structure and assembly, to medicine and technology The Bcl-2 Family in Host-Virus Interactions.The BCL-2 arbiters of apoptosis and their growing role as cancer targets.

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Pore formation by dimeric Bak and Bax: an unusual pore?

http://www.wikidata.org/entity/Q39384356

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年學術文章

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2017年學術文章

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2017年學術文章

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name

Pore formation by dimeric Bak and Bax: an unusual pore?

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Pore formation by dimeric Bak and Bax: an unusual pore?

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type

label

Pore formation by dimeric Bak and Bax: an unusual pore?

@en

Pore formation by dimeric Bak and Bax: an unusual pore?

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prefLabel

Pore formation by dimeric Bak and Bax: an unusual pore?

@en

Pore formation by dimeric Bak and Bax: an unusual pore?

@nl

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Philosophical Transactions of the Royal Society B

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Pore formation by dimeric Bak and Bax: an unusual pore?

@en

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tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c

Bax crystal structures reveal how BH3 domains activate Bax and nucleate its oligomerization to induce apoptosis

Inhibition of Bax channel-forming activity by Bcl-2

Vaccinia virus anti-apoptotic F1L is a novel Bcl-2-like domain-swapped dimer that binds a highly selective subset of BH3-containing death ligands

Spatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosis

BAX unleashed: the biochemical transformation of an inactive cytosolic monomer into a toxic mitochondrial pore

BID-induced structural changes in BAK promote apoptosis

Phosphoinositide-mediated oligomerization of a defensin induces cell lysis

Bak core and latch domains separate during activation, and freed core domains form symmetric homodimers

X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death

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scholarly article

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10.1098/RSTB.2016.0218

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1726

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372

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2017-08-01T00:00:00Z

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5483520

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