Structure of Bax: coregulation of dimer formation and intracellular localization (Q27628839)

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2 November 2019

title

Structure of Bax: coregulation of dimer formation and intracellular localization (English)

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1

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2 November 2019

author name string

R J Youle

series ordinal

2

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2 November 2019

N Tjandra

series ordinal

3

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2 November 2019

publication date

1 November 2000

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2 November 2019

language of work or name

0 references

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2 November 2019

volume

103

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2 November 2019

issue

4

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2 November 2019

page(s)

645-654

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The Bcl-2 protein family: arbiters of cell survival

2 November 2019

cites work

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Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria

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Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible.

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Solution structure of BID, an intracellular amplifier of apoptotic signaling

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A robust method for determining the magnitude of the fully asymmetric alignment tensor of oriented macromolecules in the absence of structural information

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Validation of Protein Structure from Anisotropic Carbonyl Chemical Shifts in a Dilute Liquid Crystalline Phase

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Protein backbone angle restraints from searching a database for chemical shift and sequence homology

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Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis

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Regulated targeting of BAX to mitochondria.

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Mitochondria and apoptosis

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Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis

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BCL-2 family members and the mitochondria in apoptosis

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Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins.

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Refined solution structure and backbone dynamics of HIV-1 Nef.

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Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions

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Nonionic detergents induce dimerization among members of the Bcl-2 family

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7 January 2021

Bax in Murine Thymus Is a Soluble Monomeric Protein That Displays Differential Detergent-induced Conformations

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Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis

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Withdrawal of IL-7 induces Bax translocation from cytosol to mitochondria through a rise in intracellular pH.

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Evidence for multiple mechanisms for membrane binding and integration via carboxyl-terminal insertion sequences

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MOLMOL: a program for display and analysis of macromolecular structures

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Sampling and efficiency of metric matrix distance geometry: a novel partial metrization algorithm

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Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis

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Bid, a Bcl2 Interacting Protein, Mediates Cytochrome c Release from Mitochondria in Response to Activation of Cell Surface Death Receptors

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Changes in intramitochondrial and cytosolic pH: early events that modulate caspase activation during apoptosis

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Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists

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Bcl-xL regulates apoptosis by heterodimerization-dependent and -independent mechanisms

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

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Conformation of the Bax C-terminus regulates subcellular location and cell death

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Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death

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7 January 2021

Bicelle-based liquid crystals for NMR-measurement of dipolar couplings at acidic and basic pH values

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Measurement of Dipolar Couplings for Methylene and Methyl Sites in Weakly Oriented Macromolecules and Their Use in Structure Determination

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Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

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7 January 2021

Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis

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Direct Measurement of Distances and Angles in Biomolecules by NMR in a Dilute Liquid Crystalline Medium

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7 January 2021

BID: a novel BH3 domain-only death agonist

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Mutagenesis of the BH3 Domain of BAX Identifies Residues Critical for Dimerization and Killing

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Movement of Bax from the Cytosol to Mitochondria during Apoptosis

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Identifiers

DOI

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Consolidated OpenCitations Corpus – April 2017

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11106734%20AND%20SRC:MED&resulttype=core&format=json

2 November 2019

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Consolidated OpenCitations Corpus – April 2017

2 references

Consolidated OpenCitations Corpus – April 2017