Structure of detergent-activated BAK dimers derived from the inert monomer

Homogeneous Oligomers of Pro-apoptotic BAX Reveal Structural Determinants of Mitochondrial Membrane Permeabilization

(2020) Zachary J. Hauseman et al.   MOLECULAR CELL

BAK core dimers bind lipids and can be bridged by them

(2020) Angus D. Cowan et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Avoiding adsorption of Bcl-2 proteins to plasticware is important for accurate quantitation

(2019) Colin Hockings et al.   CELL DEATH AND DIFFERENTIATION

Structures of BCL-2 in complex with venetoclax reveal the molecular basis of resistance mutations

(2019) Richard W. Birkinshaw et al.   Nature Communications

MX2: a high-flux undulator microfocus beamline serving both the chemical and macromolecular crystallography communities at the Australian Synchrotron

(2018) David Aragão et al.   JOURNAL OF SYNCHROTRON RADIATION

Conversion of Bim-BH3 from Activator to Inhibitor of Bak through Structure-Based Design

(2017) Jason M. Brouwer et al.   MOLECULAR CELL

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

(2017) Rachel T. Uren et al.   PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES

BAK α6 permits activation by BH3-only proteins and homooligomerization via the canonical hydrophobic groove

(2017) Mark Xiang Li et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Disordered clusters of Bak dimers rupture mitochondria during apoptosis

(2017) Rachel T Uren et al.   eLife

Targeting BCL2 with Venetoclax in Relapsed Chronic Lymphocytic Leukemia

(2016) Andrew W. Roberts et al.   NEW ENGLAND JOURNAL OF MEDICINE

Assembly of Bak homodimers into higher order homooligomers in the mitochondrial apoptotic pore

(2016) Tirtha Mandal et al.   Scientific Reports

Bak apoptotic pores involve a flexible C-terminal region and juxtaposition of the C-terminal transmembrane domains

(2015) S Iyer et al.   CELL DEATH AND DIFFERENTIATION

BH3-in-groove dimerization initiates and helix 9 dimerization expands Bax pore assembly in membranes

(2015) Z. Zhang et al.   EMBO JOURNAL

Crystal structure of Bax bound to the BH3 peptide of Bim identifies important contacts for interaction

(2015) A Y Robin et al.   Cell Death & Disease

Bid chimeras indicate that most BH3-only proteins can directly activate Bak and Bax and show no preference for Bak versus Bax

(2015) C Hockings et al.   Cell Death & Disease

Dissociation of Bak α1 helix from the core and latch domains is required for apoptosis

(2015) Amber E. Alsop et al.   Nature Communications

Bax monomers form dimer units in the membrane that further self-assemble into multiple oligomeric species

(2015) Yamunadevi Subburaj et al.   Nature Communications

Bak Core and Latch Domains Separate during Activation, and Freed Core Domains Form Symmetric Homodimers

(2014) Jason M. Brouwer et al.   MOLECULAR CELL

Structural Model of Active Bax at the Membrane

(2014) Stephanie Bleicken et al.   MOLECULAR CELL

Apoptotic pore formation is associated with in-plane insertion of Bak or Bax central helices into the mitochondrial outer membrane

(2014) Dana Westphal et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Bax Crystal Structures Reveal How BH3 Domains Activate Bax and Nucleate Its Oligomerization to Induce Apoptosis

(2013) Peter E. Czabotar et al.   CELL

Assembly of the Bak Apoptotic Pore

(2013) Stephen Ma et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Organization of the Mitochondrial Apoptotic BAK Pore

(2013) Sreevidya Aluvila et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

ABT-199, a potent and selective BCL-2 inhibitor, achieves antitumor activity while sparing platelets

(2013) Andrew J Souers et al.   NATURE MEDICINE

Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy

(2013) Peter E. Czabotar et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

BID-induced structural changes in BAK promote apoptosis

(2013) Tudor Moldoveanu et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Towards automated crystallographic structure refinement withphenix.refine

(2012) Pavel V. Afonine et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Exploiting structure similarity in refinement: automated NCS and target-structure restraints inBUSTER

(2012) Oliver S. Smart et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Translocation of a Bak C-Terminus Mutant from Cytosol to Mitochondria to Mediate Cytochrome c Release: Implications for Bak and Bax Apoptotic Function

(2012) Pedro Eitz Ferrer et al.   PLoS One

Bax dimerizes via a symmetric BH3:groove interface during apoptosis

(2011) G Dewson et al.   CELL DEATH AND DIFFERENTIATION

Integration, scaling, space-group assignment and post-refinement

(2010) Wolfgang Kabsch   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Features and development ofCoot

(2010) P. Emsley et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Bax Forms an Oligomer via Separate, Yet Interdependent, Surfaces

(2010) Zhi Zhang et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Molecular Details of Bax Activation, Oligomerization, and Membrane Insertion

(2009) Stephanie Bleicken et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Bak Activation for Apoptosis Involves Oligomerization of Dimers via Their α6 Helices

(2009) Grant Dewson et al.   MOLECULAR CELL

To Trigger Apoptosis, Bak Exposes Its BH3 Domain and Homodimerizes via BH3:Groove Interactions

(2008) Grant Dewson et al.   MOLECULAR CELL