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Disordered clusters of Bak dimers rupture mitochondria during apoptosis.
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Europe PubMed Central
PMC publication ID
5302884
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28182867%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 April 2020
title
Disordered clusters of Bak dimers rupture mitochondria during apoptosis
(English)
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stated in
Europe PubMed Central
PMC publication ID
5302884
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28182867%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 April 2020
main subject
apoptotic process
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mitochondrion
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inferred from title
author
Ruth Kluck
series ordinal
9
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Europe PubMed Central
PMC publication ID
5302884
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28182867%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 April 2020
Rachel T Uren
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1
1 reference
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Europe PubMed Central
PMC publication ID
5302884
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28182867%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 April 2020
Martin O'Hely
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2
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PMC publication ID
5302884
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28182867%20AND%20SRC:MED&resulttype=core&format=json
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2 April 2020
Sweta Iyer
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3
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5302884
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28182867%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 April 2020
Melissa X Shi
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5
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PMC publication ID
5302884
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28182867%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 April 2020
Amber E Alsop
series ordinal
7
1 reference
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Europe PubMed Central
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5302884
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28182867%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 April 2020
Grant Dewson
series ordinal
8
1 reference
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Europe PubMed Central
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5302884
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28182867%20AND%20SRC:MED&resulttype=core&format=json
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2 April 2020
author name string
Ray Bartolo
series ordinal
4
1 reference
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PMC publication ID
5302884
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28182867%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 April 2020
Jason M Brouwer
series ordinal
6
1 reference
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Europe PubMed Central
PMC publication ID
5302884
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28182867%20AND%20SRC:MED&resulttype=core&format=json
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2 April 2020
language of work or name
English
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publication date
6 February 2017
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Europe PubMed Central
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5302884
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28182867%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 April 2020
published in
eLife
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Europe PubMed Central
PMC publication ID
5302884
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28182867%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 April 2020
volume
6
1 reference
stated in
Europe PubMed Central
PMC publication ID
5302884
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28182867%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 April 2020
describes a project that uses
ImageJ
1 reference
stated in
Europe PubMed Central
retrieved
11 June 2022
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/PMC5302884/fullTextXML
based on heuristic
inferred from PubMed Central ID database lookup
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Bid chimeras indicate that most BH3-only proteins can directly activate Bak and Bax, and show no preference for Bak versus Bax.
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Dissociation of Bak α1 helix from the core and latch domains is required for apoptosis
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Apoptotic pore formation is associated with in-plane insertion of Bak or Bax central helices into the mitochondrial outer membrane
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Bak core and latch domains separate during activation, and freed core domains form symmetric homodimers
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Bax targets mitochondria by distinct mechanisms before or during apoptotic cell death: a requirement for VDAC2 or Bak for efficient Bax apoptotic function
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Organization of the mitochondrial apoptotic BAK pore: oligomerization of the BAK homodimers
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Process of inducing pores in membranes by melittin
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Assembly of the Bak apoptotic pore: a critical role for the Bak protein α6 helix in the multimerization of homodimers during apoptosis
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Direct activation of full-length proapoptotic BAK
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Bax crystal structures reveal how BH3 domains activate Bax and nucleate its oligomerization to induce apoptosis
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Bak Conformational Changes Induced by Ligand Binding: Insight into BH3 Domain Binding and Bak Homo-Oligomerization
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9 September 2017
Bax dimerizes via a symmetric BH3:groove interface during apoptosis
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PubMed Central
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9 September 2017
BH3 domains other than Bim and Bid can directly activate Bax/Bak
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PubMed Central
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9 September 2017
Inhibition of Bak activation by VDAC2 is dependent on the Bak transmembrane anchor
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9 September 2017
Bax forms an oligomer via separate, yet interdependent, surfaces
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9 September 2017
The structure of a cytolytic alpha-helical toxin pore reveals its assembly mechanism
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9 September 2017
Apoptosis is triggered when prosurvival Bcl-2 proteins cannot restrain Bax.
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PubMed Central
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5302884
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9 September 2017
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9 September 2017
A three-helix homo-oligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of Bax.
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9 September 2017
The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site
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9 September 2017
Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function
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VDAC2 inhibits BAK activation and mitochondrial apoptosis
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9 September 2017
Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation
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9 September 2017
Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis
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PubMed Central
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5302884
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9 September 2017
Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death
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9 September 2017
The combined functions of proapoptotic Bcl-2 family members bak and bax are essential for normal development of multiple tissues
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9 September 2017
Structure of Bax: coregulation of dimer formation and intracellular localization
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9 September 2017
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9 September 2017
The pro-apoptotic proteins, Bid and Bax, cause a limited permeabilization of the mitochondrial outer membrane that is enhanced by cytosol
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9 September 2017
Bax, but not Bcl-xL, decreases the lifetime of planar phospholipid bilayer membranes at subnanomolar concentrations
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9 September 2017
Conformation of the Bax C-terminus regulates subcellular location and cell death
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9 September 2017
Cell damage-induced conformational changes of the pro-apoptotic protein Bak in vivo precede the onset of apoptosis
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9 September 2017
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9 September 2017
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9 September 2017
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9 September 2017
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17 June 2018
BIM-mediated membrane insertion of the BAK pore domain is an essential requirement for apoptosis
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17 June 2018
Transient binding of an activator BH3 domain to the Bak BH3-binding groove initiates Bak oligomerization
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PubMed Central
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17 June 2018
Bak apoptotic pores involve a flexible C-terminal region and juxtaposition of the C-terminal transmembrane domains
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21 August 2018
Interaction of the full-length Bax protein with biomimetic mitochondrial liposomes: a small-angle neutron scattering and fluorescence study.
1 reference
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PubMed Central
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5302884
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21 August 2018
BH3-triggered structural reorganization drives the activation of proapoptotic BAX.
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21 August 2018
Bak activation for apoptosis involves oligomerization of dimers via their alpha6 helices
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PubMed Central
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5302884
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21 August 2018
To trigger apoptosis, Bak exposes its BH3 domain and homodimerizes via BH3:groove interactions.
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5302884
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21 August 2018
Lipidic pore formation by the concerted action of proapoptotic BAX and tBID.
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21 August 2018
Aggregation and vesiculation of membrane proteins by curvature-mediated interactions
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21 January 2018
Dynamics and structure of the Bax-Bak complex responsible for releasing mitochondrial proteins during apoptosis
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PubMed
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https://pubmed.ncbi.nlm.nih.gov/28182867
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12 December 2020
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Identifiers
DOI
10.7554/ELIFE.19944
1 reference
stated in
Europe PubMed Central
PMC publication ID
5302884
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28182867%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 April 2020
PMC publication ID
5302884
1 reference
stated in
Europe PubMed Central
PMC publication ID
5302884
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28182867%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 April 2020
PubMed publication ID
28182867
1 reference
stated in
Europe PubMed Central
PMC publication ID
5302884
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28182867%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 April 2020
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