(Q24307486)

GOA release 2020-03-11

pore complex assembly

1 reference

Biochimica et Biophysica Acta

GOA release 2020-03-11

1 reference

6

Kristian Schweimer

Kristian

Schweimer

1 reference

9 December 2023

4

Jochen Kuper

Jochen

Kuper

1 reference

9 December 2023

5

Roland Benz

Roland

Benz

1 reference

9 December 2023

1

Lisa Polzien

Lisa

Polzien

1 reference

9 December 2023

2

Angela Baljuls

Angela

Baljuls

1 reference

9 December 2023

Heide-Marie Roth

3

Heide-Marie

Roth

1 reference

9 December 2023

Mirko Hekman

series ordinal

7

author given names

Mirko

author last names

Hekman

1 reference

9 December 2023

Ulf R Rapp

series ordinal

8

author given names

Ulf R

author last names

Rapp

1 reference

9 December 2023

language of work or name

English

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publication date

February 2011

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published in

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volume

1810

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issue

2

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page(s)

162-9

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cites work

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Inhibitors of permeability transition interfere with the disruption of the mitochondrial transmembrane potential during apoptosis.

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Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death

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Permeation of hydrophilic solutes through mitochondrial outer membranes: review on mitochondrial porins

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The mitochondrial permeability transition.

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BAD association with membranes is regulated by Raf kinases and association with 14-3-3 proteins

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Structural biology of the Bcl-2 family of proteins

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Rafts: a simple way to control apoptosis by subcellular redistribution

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How do Bax and Bak lead to permeabilization of the outer mitochondrial membrane?

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Molecular modeling of human BAD and its interaction with PKAc or PP1c

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Bad targets the permeability transition pore independent of Bax or Bak to switch between Ca2+-dependent cell survival and death

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The structure of the C-terminal domain of the pro-apoptotic protein Bak and its interaction with model membranes.

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Insights into programmed cell death through structural biology

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Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)

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Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane

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Cell death: critical control points

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Apoptosis: mitochondrial membrane permeabilization--the (w)hole story?

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14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation

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Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies

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Study of the secondary structure of the C-terminal domain of the antiapoptotic protein bcl-2 and its interaction with model membranes

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Conformation of the C-terminal domain of the pro-apoptotic protein Bax and mutants and its interaction with membranes

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Lipid rafts and signal transduction

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

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Bcl-2 proteins: regulators of apoptosis or of mitochondrial homeostasis?

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The BCL-2 protein family: opposing activities that mediate cell death

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BAD: undertaker by night, candyman by day.

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Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets

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Bcl-x(L) sequesters its C-terminal membrane anchor in soluble, cytosolic homodimers

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7 January 2021

Specificity of 14-3-3 isoform dimer interactions and phosphorylation

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Mitochondrial respiratory control is lost during growth factor deprivation

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Channel formation by antiapoptotic protein Bcl-2.

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

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Bax, but not Bcl-xL, decreases the lifetime of planar phospholipid bilayer membranes at subnanomolar concentrations

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7 January 2021

Ion channel activity of the BH3 only Bcl-2 family member, BID.

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7 January 2021

Identification of novel in vivo phosphorylation sites of the human proapoptotic protein BAD: pore-forming activity of BAD is regulated by phosphorylation

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7 January 2021

Associations of B- and C-Raf with cholesterol, phosphatidylserine, and lipid second messengers: preferential binding of Raf to artificial lipid rafts.

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https://api.crossref.org/works/10.1016%2FJ.BBAGEN.2010.11.002

7 January 2021

Reversible membrane interaction of BAD requires two C-terminal lipid binding domains in conjunction with 14-3-3 protein binding

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7 January 2021

Mitochondrial control of nuclear apoptosis.

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7 January 2021

BCL-2 family members and the mitochondria in apoptosis

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7 January 2021

Solution Structure of the Integral Human Membrane Protein VDAC-1 in Detergent Micelles

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7 January 2021

Inhibition of Bax channel-forming activity by Bcl-2

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7 January 2021

The Bcl-2 protein family: arbiters of cell survival

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7 January 2021

The domains of apoptosis: a genomics perspective

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7 January 2021

The role of mitochondria in apoptosis*.

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7 January 2021

Studies on human porin. VII. The channel properties of the human B-lymphocyte membrane-derived "Porin 31HL" are similar to those of mitochondrial porins

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7 January 2021

Modulation of synaptic transmission by the BCL-2 family protein BCL-xL.

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https://api.crossref.org/works/10.1016%2FJ.BBAGEN.2010.11.002

7 January 2021

Segregation of Bad from lipid rafts is implicated in the induction of apoptosis.

1 reference

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7 January 2021