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Solution structure of the antiapoptotic protein bcl-2

https://doi.org/10.1073/pnas.041619798
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Alternative promoters and exons, somatic mutation and deregulation of the Bcl‐2‐Ig fusion gene in lymphoma.
inferredcites →https://doi.org/10.1002/prot.340110407openalex-snapshot
Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
inferredcites →https://doi.org/10.1006/prep.1998.0996openalex-snapshot
Refolding, Purification, and Characterization of a Loop Deletion Mutant of Human Bcl-2 from Bacterial Inclusion Bodies
inferredcites →https://doi.org/10.1016/0022-2364(88)90144-8openalex-snapshot
Heteronuclear three-dimensional nmr spectroscopy. A strategy for the simplification of homonuclear two-dimensional NMR spectra
inferredcites →https://doi.org/10.1016/0076-6879(81)74003-5openalex-snapshot
[1] Equilibrium and kinetic inhibition assays based upon fluorescence polarization
inferredcites →https://doi.org/10.1016/0092-8674(86)90362-4openalex-snapshot
Cloning and structural analysis of cDNAs for bcl-2 and a hybrid bcl-2/immunoglobulin transcript resulting from the t(14;18) translocation
inferredcites →https://doi.org/10.1016/0092-8674(93)80065-mopenalex-snapshot
Bcl-2-deficient mice demonstrate fulminant lymphoid apoptosis, polycystic kidneys, and hypopigmented hair
inferredcites →https://doi.org/10.1016/0092-8674(93)90508-nopenalex-snapshot
bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell death
inferredcites →https://doi.org/10.1016/0092-8674(95)90411-5openalex-snapshot
Bad, a heterodimeric partner for Bcl-xL and Bcl-2, displaces bax and promotes cell death
inferredcites →https://doi.org/10.1016/0263-7855(87)80010-3openalex-snapshot
Ribbon models of macromolecules
inferredcites →https://doi.org/10.1016/s0076-6879(94)39013-4openalex-snapshot
[11] Multidimensional heteronuclear nuclear magnetic resonance of proteins
inferredcites →https://doi.org/10.1016/s0092-8674(00)00167-7openalex-snapshot
Structure of Bax
inferredcites →https://doi.org/10.1016/s0092-8674(85)80070-2openalex-snapshot
Cloning the chromosomal breakpoint of t(14;18) human lymphomas: clustering around Jh on chromosome 14 and near a transcriptional unit on 18
inferredcites →https://doi.org/10.1016/s0304-419x(97)00019-xopenalex-snapshot
The role of the bcl-2/ced-9 gene family in cancer and general implications of defects in cell death control for tumourigenesis and resistance to chemotherapy
inferredcites →https://doi.org/10.1016/s0962-8924(98)01321-xopenalex-snapshot
Bcl-2-family proteins: the role of the BH3 domain in apoptosis
inferredcites →https://doi.org/10.1016/s0969-2126(99)80167-1openalex-snapshot
Establishing a degree of order: obtaining high-resolution NMR structures from molecular alignment
inferredcites →https://doi.org/10.1017/s096183680000331xopenalex-snapshot
Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies
inferredcites →https://doi.org/10.1021/bi00441a004openalex-snapshot
Overcoming the overlap problem in the assignment of proton NMR spectra of larger proteins by use of three-dimensional heteronuclear proton-nitrogen-15 Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1.beta.
inferredcites →https://doi.org/10.1021/bi00445a003openalex-snapshot
Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional carbon-13 labeling
inferredcites →https://doi.org/10.1021/ja00105a005openalex-snapshot
A Suite of Triple Resonance NMR Experiments for the Backbone Assignment of 15N, 13C, 2H Labeled Proteins with High Sensitivity
inferredcites →https://doi.org/10.1021/ja982592fopenalex-snapshot
Measurement of Residual Dipolar Couplings of Macromolecules Aligned in the Nematic Phase of a Colloidal Suspension of Rod-Shaped Viruses
inferredcites →https://doi.org/10.1023/a:1008392405740openalex-snapshot
Protein backbone angle restraints from searching a database for chemical shift and sequence homology
inferredcites →https://doi.org/10.1038/35037747openalex-snapshot
From bench to clinic with apoptosis-based therapeutic agents
inferredcites →https://doi.org/10.1038/369321a0openalex-snapshot
BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax
inferredcites →https://doi.org/10.1038/381335a0openalex-snapshot
X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death
inferredcites →https://doi.org/10.1038/4176openalex-snapshot
Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions
inferredcites →https://doi.org/10.1073/pnas.82.21.7439openalex-snapshot
Nucleotide sequence of a t(14;18) chromosomal breakpoint in follicular lymphoma and demonstration of a breakpoint-cluster region near a transcriptionally active locus on chromosome 18.
inferredcites →https://doi.org/10.1073/pnas.83.14.5214openalex-snapshot
Analysis of the structure, transcripts, and protein products of bcl-2, the gene involved in human follicular lymphoma.
inferredcites →https://doi.org/10.1073/pnas.91.9.3700openalex-snapshot
Targeted disruption of Bcl-2 alpha beta in mice: occurrence of gray hair, polycystic kidney disease, and lymphocytopenia.
inferredcites →https://doi.org/10.1073/pnas.97.13.7124openalex-snapshot
Structure-based discovery of an organic compound that binds Bcl-2 protein and induces apoptosis of tumor cells
inferredcites →https://doi.org/10.1074/jbc.272.49.30866openalex-snapshot
Dimerization Properties of Human BAD
inferredcites →https://doi.org/10.1089/cbr.1998.13.225openalex-snapshot
Bcl-2 and Drugs Used in the Treatment of Cancer: New Strategies of Biotherapy which should not be Underestimated
inferredcites →https://doi.org/10.1097/00001622-199901000-00014openalex-snapshot
Mechanisms of apoptosis avoidance in cancer
inferredcites →https://doi.org/10.1107/s0021889892009944openalex-snapshot
PROCHECK: a program to check the stereochemical quality of protein structures
inferredcites →https://doi.org/10.1126/science.275.5302.983openalex-snapshot
Structure of Bcl-x L -Bak Peptide Complex: Recognition Between Regulators of Apoptosis
inferredcites →https://doi.org/10.1126/science.281.5381.1322openalex-snapshot
The Bcl-2 Protein Family: Arbiters of Cell Survival
inferredcites →https://doi.org/10.1126/science.6093263openalex-snapshot
Cloning of the Chromosome Breakpoint of Neoplastic B Cells with the t(14;18) Chromosome Translocation
inferredcites →https://doi.org/10.1126/science.7878464openalex-snapshot
Apoptosis in the Pathogenesis and Treatment of Disease
inferredcites →https://doi.org/10.1126/science.7878471openalex-snapshot
Massive Cell Death of Immature Hematopoietic Cells and Neurons in Bcl-x-Deficient Mice
inferredcites →https://doi.org/10.1146/annurev.immunol.16.1.395openalex-snapshot
BCL-2 FAMILY: Regulators of Cell Death
inferredcites →https://doi.org/10.1182/blood.v81.11.3091.3091openalex-snapshot
High expression of bcl-2 protein in acute myeloid leukemia cells is associated with poor response to chemotherapy

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.3339906openalex-extracted
Allosteric Cross-Talk between the Hydrophobic Cleft and the BH4 Domain of Bcl-2 in Control of IP3R Activity
inferred← citeshttps://doi.org/10.1002/0470028637.met237openalex-snapshot
BAK
inferred← citeshttps://doi.org/10.1002/0471684228.egp01263openalex-snapshot
BCL 1, BCL 2, BCL 3, BCL 5, BCL 6 ( B ‐Cell Lymphoma)
inferred← citeshttps://doi.org/10.1002/1521-3757(20011015)113:20<3922::aid-ange3922>3.0.co;2-8openalex-snapshot
Design and Evolution of a Miniature Bcl-2 Binding Protein
inferred← citeshttps://doi.org/10.1002/1521-3773(20011015)40:20<3806::aid-anie3806>3.0.co;2-bopenalex-snapshot
Design and Evolution of a Miniature Bcl-2 Binding Protein
inferred← citeshttps://doi.org/10.1002/1873-3468.13250openalex-snapshot
Probing the interaction of a quercetin bioconjugate with Bcl‐2 in living human cancer cells with in‐cell NMR spectroscopy
inferred← citeshttps://doi.org/10.1002/9780470249055openalex-snapshot
Preclinical Development Handbook
inferred← citeshttps://doi.org/10.1002/9780470571224.pse033openalex-snapshot
Protein–Protein Interactions
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0662openalex-snapshot
BAK
inferred← citeshttps://doi.org/10.1002/9783527845828.ch12openalex-snapshot
Small Molecule Inhibitors Targeting Protein–Protein Interactions in the BCL Protein
inferred← citeshttps://doi.org/10.1002/ange.200200558openalex-snapshot
Modulation von Protein‐Protein‐Wechselwirkungen mit niedermolekularen organischen Molekülen
inferred← citeshttps://doi.org/10.1002/ange.202011711openalex-snapshot
A Cerium Vanadate Nanozyme with Specific Superoxide Dismutase Activity Regulates Mitochondrial Function and ATP Synthesis in Neuronal Cells
inferred← citeshttps://doi.org/10.1002/anie.200200558openalex-snapshot
Modulation of Protein–Protein Interactions with Small Organic Molecules
inferred← citeshttps://doi.org/10.1002/anie.202011711openalex-snapshot
A Cerium Vanadate Nanozyme with Specific Superoxide Dismutase Activity Regulates Mitochondrial Function and ATP Synthesis in Neuronal Cells
inferred← citeshttps://doi.org/10.1002/bip.22839openalex-snapshot
Exploring the conformational and binding properties of unphosphorylated/phosphorylated monomeric and trimeric Bcl‐2 through docking and molecular dynamics simulations
inferred← citeshttps://doi.org/10.1002/cbic.201402639openalex-snapshot
Discovery of a Small‐Molecule pBcl‐2 Inhibitor that Overcomes pBcl‐2‐Mediated Resistance to Apoptosis
inferred← citeshttps://doi.org/10.1002/cmdc.200800246openalex-snapshot
Peptides and Peptide Mimics as Modulators of Apoptotic Pathways
inferred← citeshttps://doi.org/10.1002/cmdc.201000484openalex-snapshot
Discovery and Development of Thiazolo[3,2‐a]pyrimidinone Derivatives as General Inhibitors of Bcl‐2 Family Proteins
inferred← citeshttps://doi.org/10.1002/cmdc.201300159openalex-snapshot
Characterization of the Stereochemical Structures of 2H‐Thiazolo[3,2‐a]pyrimidine Compounds and Their Binding Affinities for Anti‐apoptotic Bcl‐2 Family Proteins
inferred← citeshttps://doi.org/10.1002/cmdc.201800321openalex-snapshot
Experimental Characterization of the Binding Affinities between Proapoptotic BH3 Peptides and Antiapoptotic Bcl‐2 Proteins
inferred← citeshttps://doi.org/10.1002/jcb.10573openalex-snapshot
Pro‐apoptotic activity of transiently expressed BCL‐2 occurs independent of BAX and BAK
inferred← citeshttps://doi.org/10.1002/jmr.2295openalex-snapshot
Biophysical basis of the promiscuous binding of B‐cell lymphoma protein 2 apoptotic repressor to BH3 ligands
inferred← citeshttps://doi.org/10.1002/med.70108openalex-snapshot
The Executioners of Mitochondrial Apoptosis: Structures, Mechanisms, and Therapeutic Advances of BAX, BAK, and BOK
inferred← citeshttps://doi.org/10.1002/mrc.1322openalex-snapshot
Structural studies of apoptosis and ion transport regulatory proteins in membranes
inferred← citeshttps://doi.org/10.1002/pro.329openalex-snapshot
Mcl‐1–Bim complexes accommodate surprising point mutations via minor structural changes
inferred← citeshttps://doi.org/10.1002/prot.22075openalex-snapshot
Anti‐apoptotic Bcl‐XL protein in complex with BH3 peptides of pro‐apoptotic Bak, Bad, and Bim proteins: Comparative molecular dynamics simulations
inferred← citeshttps://doi.org/10.1002/prot.24424openalex-snapshot
Intrinsically disordered regions in autophagy proteins
inferred← citeshttps://doi.org/10.1002/prot.24476openalex-snapshot
Antiapoptotic Bcl‐2 homolog CED‐9 in Caenorhabditis elegans: Dynamics of BH3 and CED‐4 binding regions and comparison with mammalian antiapoptotic Bcl‐2 proteins
inferred← citeshttps://doi.org/10.1002/psc.414openalex-snapshot
Peptides in apoptosis research
inferred← citeshttps://doi.org/10.1002/psc.686openalex-snapshot
Synthesis and secondary structure in membranes of the Bcl‐2 anti‐apoptotic domain BH4
inferred← citeshttps://doi.org/10.1002/psc.971openalex-snapshot
Tilted peptides: a structural motif involved in protein membrane insertion?
inferred← citeshttps://doi.org/10.1002/slct.202302948openalex-snapshot
Identification of Compounds Against Anti‐apoptotic Bcl‐2 Protein Using Docking Studies
inferred← citeshttps://doi.org/10.1006/abio.2001.5468openalex-snapshot
A Fluorescence Polarization Assay for the Identification of Inhibitors of the p53–DM2 Protein–Protein Interaction
inferred← citeshttps://doi.org/10.1007/0-387-23695-3_5openalex-snapshot
The Intrinsic (Mitochondrial) Death Pathway and New Cancer Therapeutics: Bcl-2 Family in Focus
inferred← citeshttps://doi.org/10.1007/1-4020-2217-4_2openalex-snapshot
The Bcl-2 Family
inferred← citeshttps://doi.org/10.1007/1-4020-3302-8_5openalex-snapshot
Targeting Oncogenes Which Regulate Apoptosis
inferred← citeshttps://doi.org/10.1007/3-540-28435-4_2openalex-snapshot
NMR of Membrane Proteins in Lipid Environments: the Bcl-2 Family of Apoptosis Regulators
inferred← citeshttps://doi.org/10.1007/978-1-4419-6327-7_8openalex-snapshot
Permeabilization of the Outer Mitochondrial Membrane by Bcl-2 Proteins
inferred← citeshttps://doi.org/10.1007/978-1-4419-6706-0_6openalex-snapshot
The Interplay between BCL-2 Family Proteins and Mitochondrial Morphology in the Regulation of Apoptosis
inferred← citeshttps://doi.org/10.1007/978-1-4614-9302-0_11openalex-snapshot
Structural Perspectives on BCL-2 Family of Proteins
inferred← citeshttps://doi.org/10.1007/978-1-4614-9302-0_4openalex-snapshot
Bcl-2 Family and Their Therapeutic Potential
inferred← citeshttps://doi.org/10.1007/978-1-4939-3581-9_16openalex-snapshot
Preparing Samples for Crystallization of Bcl-2 Family Complexes
inferred← citeshttps://doi.org/10.1007/978-1-59259-361-3_2openalex-snapshot
Bcl-2 Family Proteins
inferred← citeshttps://doi.org/10.1007/978-1-59259-361-3_6openalex-snapshot
The Mitochondrial Apoptosis Pathway
inferred← citeshttps://doi.org/10.1007/978-1-59745-474-2_15openalex-snapshot
Inhibitors of the Bcl-2 Protein Family as Sensitizers to Anticancer Agents
inferred← citeshttps://doi.org/10.1007/978-1-60327-381-7_2openalex-snapshot
The Bcl-2 Family Proteins
inferred← citeshttps://doi.org/10.1007/978-1-60761-314-5_9openalex-snapshot
Punching Holes in Membranes: How Oligomeric Pore-Forming Proteins and Lipids Cooperate to Form Aqueous Channels in Membranes
inferred← citeshttps://doi.org/10.1007/978-3-319-55539-3_10openalex-snapshot
New Insights on the Regulation of Programmed Cell Death by Bcl-2 Family Proteins at the Mitochondria: Physiological and Pathophysiological Implications
inferred← citeshttps://doi.org/10.1007/978-3-319-76858-8_7openalex-snapshot
Examining α-Helical Proteins
inferred← citeshttps://doi.org/10.1007/978-3-319-98304-2_7openalex-snapshot
Mathematical Modelling of the Interaction of BH3-Peptides with Full-Length Proteins, and Account of the Influence of Point Mutations on the Stability of the Formed Biological Complex on the Example of the Bcl-2 Family Proteins
inferred← citeshttps://doi.org/10.1007/978-3-642-16105-6_7openalex-snapshot
Membrane-Related Diseases
inferred← citeshttps://doi.org/10.1007/978-3-642-28965-1_7openalex-snapshot
The Discovery of Navitoclax, a Bcl-2 Family Inhibitor
inferred← citeshttps://doi.org/10.1007/s00018-018-2968-8openalex-snapshot
Structural disorder in the proteome and interactome of Alkhurma virus (ALKV)
inferred← citeshttps://doi.org/10.1007/s00204-014-1448-7openalex-snapshot
The mystery of BCL2 family: Bcl-2 proteins and apoptosis: an update
inferred← citeshttps://doi.org/10.1007/s00244-026-01200-wopenalex-snapshot
Bioaccumulation Patterns of Potentially Toxic Elements in Three Grouper Species from the Nizampatnam Coast, India: Multivariate Analysis and Risk Assessment
inferred← citeshttps://doi.org/10.1007/s00277-007-0288-4openalex-snapshot
A novel Bcl-2 small molecule inhibitor 4-(3-methoxy-phenylsulfannyl)-7-nitro-benzofurazan-3-oxide (MNB)-induced apoptosis in leukemia cells
inferred← citeshttps://doi.org/10.1007/s00441-001-0472-0openalex-snapshot
Bax and other pro-apoptotic Bcl-2 family "killer-proteins" and their victim the mitochondrion
inferred← citeshttps://doi.org/10.1007/s00894-003-0152-yopenalex-snapshot
A multimeric model for murine anti-apoptotic protein Bcl-2 and structural insights for its regulation by post-translational modification.
inferred← citeshttps://doi.org/10.1007/s00894-011-1201-6openalex-snapshot
Molecular dynamics simulations of the Bcl-2 protein to predict the structure of its unordered flexible loop domain
inferred← citeshttps://doi.org/10.1007/s00894-016-2940-1openalex-snapshot
Mapping the intrinsically disordered properties of the flexible loop domain of Bcl-2: a molecular dynamics simulation study
inferred← citeshttps://doi.org/10.1007/s10495-006-5702-1openalex-snapshot
Cell death regulation by B-cell lymphoma protein
inferred← citeshttps://doi.org/10.1007/s10495-007-0722-zopenalex-snapshot
A tale of two mitochondrial channels, MAC and PTP, in apoptosis
inferred← citeshttps://doi.org/10.1007/s10495-009-0389-8openalex-snapshot
Oligomerization of membrane-bound Bcl-2 is involved in its pore formation induced by tBid
inferred← citeshttps://doi.org/10.1007/s10495-012-0780-8openalex-snapshot
Enhanced heterodimerization of Bax by Bcl-2 mutants improves irradiated cell survival
inferred← citeshttps://doi.org/10.1007/s10495-016-1283-9openalex-snapshot
Alpha 5/6 helix domains together with N-terminus determine the apoptotic potency of the Bcl-2 family proteins
inferred← citeshttps://doi.org/10.1007/s10822-011-9439-8openalex-snapshot
Biosensor-based small molecule fragment screening with biolayer interferometry
inferred← citeshttps://doi.org/10.1007/s10930-022-10046-9openalex-snapshot
Multi-catalytic Sites Inhibition of Bcl2 Induces Expanding of Hydrophobic Groove: A New Avenue Towards Waldenström Macroglobulinemia Therapy
inferred← citeshttps://doi.org/10.1007/s11010-011-0729-1openalex-snapshot
Deletion mutational analysis of BMRP, a pro-apoptotic protein that binds to Bcl-2
inferred← citeshttps://doi.org/10.1007/s12094-026-04526-yopenalex-snapshot
Targeting protein–protein interactions in the BCL-2 family: opportunities for precision oncology
inferred← citeshttps://doi.org/10.1007/s12247-025-10345-5openalex-snapshot
Evaluation of the Neuroprotective Efficacies and Related Mechanisms of Cirsimaritin in MPTP-Induced Parkinson in Mice with Following the Molecular Docking Studies
inferred← citeshttps://doi.org/10.1007/s13206-019-3306-4openalex-snapshot
Molecular Docking-assisted Protein Chip Screening of Inhibitors for Bcl-2 Family Protein-protein Interaction to Discover Anticancer Agents by Fragment-based Approach
inferred← citeshttps://doi.org/10.1016/b978-0-12-374920-8.00312-xopenalex-snapshot
3.9 Intrinsically Disordered Proteins
inferred← citeshttps://doi.org/10.1016/b978-0-443-45105-8.00010-xopenalex-snapshot
Venetoclax: An oral selective Bcl-2 inhibitor approved for chronic lymphocytic leukemia (CLL)
inferred← citeshttps://doi.org/10.1016/bs.ai.2024.02.004openalex-snapshot
The regulation of the apoptotic pore—An immunological tightrope walk
inferred← citeshttps://doi.org/10.1016/j.ab.2003.07.014openalex-snapshot
High-throughput methods to detect dimerization of Bcl-2 family proteins
inferred← citeshttps://doi.org/10.1016/j.ab.2003.12.034openalex-snapshot
Discovery of novel inhibitors of Bcl-xL using multiple high-throughput screening platforms
inferred← citeshttps://doi.org/10.1016/j.addr.2007.06.004openalex-snapshot
Delivery of drugs and macromolecules to mitochondria☆
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2003.07.001openalex-snapshot
There is more to life and death than mitochondria: Bcl-2 proteins at the endoplasmic reticulum
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2003.08.009openalex-snapshot
The role of Bcl-2 family members in tumorigenesis
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2003.08.012openalex-snapshot
Structural biology of the Bcl-2 family of proteins
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2003.09.006openalex-snapshot
Bcl-2 family members: intracellular targeting, membrane-insertion, and changes in subcellular localization
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2003.10.010openalex-snapshot
Shooting at survivors: Bcl-2 family members as drug targets for cancer
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2003.11.001openalex-snapshot
Viral Bcl-2 homologs and their role in virus replication and associated diseases
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2008.10.015openalex-snapshot
Targeting Bcl-2 based on the interaction of its BH4 domain with the inositol 1,4,5-trisphosphate receptor
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2012.12.016openalex-snapshot
IP3, a small molecule with a powerful message
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2015.03.012openalex-snapshot
Emerging understanding of Bcl-2 biology: Implications for neoplastic progression and treatment
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2021.118987openalex-snapshot
It's time to die: BH3 mimetics in solid tumors
inferred← citeshttps://doi.org/10.1016/j.bbamem.2004.07.001openalex-snapshot
On the role of lipid in colicin pore formation
inferred← citeshttps://doi.org/10.1016/j.bbamem.2009.09.006openalex-snapshot
Structure assembly of Bcl-xL through α5–α5 and α6–α6 interhelix interactions in lipid membranes
inferred← citeshttps://doi.org/10.1016/j.bbamem.2011.10.007openalex-snapshot
Interaction of the full-length Bax protein with biomimetic mitochondrial liposomes: A small-angle neutron scattering and fluorescence study
inferred← citeshttps://doi.org/10.1016/j.bbamem.2015.09.013openalex-snapshot
Assembling the puzzle: Oligomerization of α-pore forming proteins in membranes
inferred← citeshttps://doi.org/10.1016/j.bbapap.2012.12.003openalex-snapshot
Utilization of protein intrinsic disorder knowledge in structural proteomics
inferred← citeshttps://doi.org/10.1016/j.bbrc.2005.09.023openalex-snapshot
Molecular characterization of FK-506 binding protein 38 and its potential regulatory role on the anti-apoptotic protein Bcl-2
inferred← citeshttps://doi.org/10.1016/j.bbrc.2005.12.201openalex-snapshot
Direct interaction of Bcl-2 proteins with tubulin
inferred← citeshttps://doi.org/10.1016/j.bbrc.2007.07.122openalex-snapshot
Oligomerization of BH4-truncated Bcl-xL in solution
inferred← citeshttps://doi.org/10.1016/j.bbrc.2011.04.054openalex-snapshot
Interaction of a putative BH3 domain of clusterin with anti-apoptotic Bcl-2 family proteins as revealed by NMR spectroscopy
inferred← citeshttps://doi.org/10.1016/j.bbrc.2012.02.113openalex-snapshot
Structural insights into the dual-targeting mechanism of Nutlin-3
inferred← citeshttps://doi.org/10.1016/j.bbrc.2013.12.054openalex-snapshot
Targeting of p53 peptide analogues to anti-apoptotic Bcl-2 family proteins as revealed by NMR spectroscopy
inferred← citeshttps://doi.org/10.1016/j.bbrc.2014.01.130openalex-snapshot
Structural basis for the conserved binding mechanism of MDM2-inhibiting peptides and anti-apoptotic Bcl-2 family proteins
inferred← citeshttps://doi.org/10.1016/j.bbrc.2017.11.129openalex-snapshot
Structural basis for the interaction between DJ-1 and Bcl-XL
inferred← citeshttps://doi.org/10.1016/j.biocel.2009.05.001openalex-snapshot
Mitochondrial outer-membrane permeabilization and remodelling in apoptosis
inferred← citeshttps://doi.org/10.1016/j.biochi.2011.05.013openalex-snapshot
Bax: Addressed to kill
inferred← citeshttps://doi.org/10.1016/j.biopha.2018.05.126openalex-snapshot
Apoptosis-inducing effects and growth inhibitory of a novel chalcone, in human hepatic cancer cells and lung cancer cells
inferred← citeshttps://doi.org/10.1016/j.bmc.2006.12.020openalex-snapshot
Development of selective inhibitors for anti-apoptotic Bcl-2 proteins from BHI-1
inferred← citeshttps://doi.org/10.1016/j.bmc.2012.05.079openalex-snapshot
Structure-based design of rhodanine-based acylsulfonamide derivatives as antagonists of the anti-apoptotic Bcl-2 protein
inferred← citeshttps://doi.org/10.1016/j.bmc.2025.118364openalex-snapshot
Employing a drug repurposing strategy to identify B-cell lymphoma-2 (BCL-2) inhibitors with anticancer potential: An in silico and in vitro based study
inferred← citeshttps://doi.org/10.1016/j.bmcl.2008.10.113openalex-snapshot
Tetrahydroisoquinoline amide substituted phenyl pyrazoles as selective Bcl-2 inhibitors
inferred← citeshttps://doi.org/10.1016/j.bmcl.2009.01.071openalex-snapshot
Atropisomeric small molecule Bcl-2 ligands: Determination of bioactive conformation
inferred← citeshttps://doi.org/10.1016/j.bmcl.2011.11.101openalex-snapshot
Design, synthesis, and activity evaluation of broad-spectrum small-molecule inhibitors of anti-apoptotic Bcl-2 family proteins: Characteristics of broad-spectrum protein binding and its effects on anti-tumor activity
inferred← citeshttps://doi.org/10.1016/j.bmcl.2017.11.023openalex-snapshot
Discovery of Mcl-1 inhibitors based on a thiazolidine-2,4-dione scaffold
inferred← citeshttps://doi.org/10.1016/j.bmcl.2019.126682openalex-snapshot
Discovery and optimization of covalent Bcl-xL antagonists
inferred← citeshttps://doi.org/10.1016/j.bpj.2022.10.041openalex-snapshot
Domain-specific insight into the recognition of BH3-death motifs by the pro-survival Bcl-2 protein
inferred← citeshttps://doi.org/10.1016/j.brainres.2024.148991openalex-snapshot
Differential toxic and antiepileptic features of Vigabatrin raceme and its enantiomers
inferred← citeshttps://doi.org/10.1016/j.canlet.2007.01.018openalex-snapshot
Exploitation of drug-induced Bcl-2 overexpression for restoring normal apoptosis function: A promising new approach to the treatment of multidrug resistant cancer
inferred← citeshttps://doi.org/10.1016/j.canlet.2009.09.016openalex-snapshot
Aloe-emodin induces apoptosis of human nasopharyngeal carcinoma cells via caspase-8-mediated activation of the mitochondrial death pathway
inferred← citeshttps://doi.org/10.1016/j.compbiolchem.2022.107736openalex-snapshot
Remote communication between unstructured and structured regions of Bcl-2 tunes its ligand binding capacity: Mechanistic insights
inferred← citeshttps://doi.org/10.1016/j.cplett.2017.10.030openalex-snapshot
Binding of anti-apoptotic Bcl-2 with different BH3 peptides: A molecular dynamics study
inferred← citeshttps://doi.org/10.1016/j.csbj.2023.07.017openalex-snapshot
Structural basis of the specificity and interaction mechanism of Bmf binding to pro-survival Bcl-2 family proteins
inferred← citeshttps://doi.org/10.1016/j.drudis.2014.11.002openalex-snapshot
Splice variants in the proteome: a promising and challenging field to targeted drug discovery
inferred← citeshttps://doi.org/10.1016/j.drudis.2015.11.008openalex-snapshot
BH4 domain of Bcl-2 as a novel target for cancer therapy
inferred← citeshttps://doi.org/10.1016/j.drudis.2020.02.002openalex-snapshot
Impact of the Protein Data Bank on antineoplastic approvals
inferred← citeshttps://doi.org/10.1016/j.ejmech.2017.10.021openalex-snapshot
Dual or multi-targeting inhibitors: The next generation anticancer agents
inferred← citeshttps://doi.org/10.1016/j.febslet.2005.01.053openalex-snapshot
The flexible loop of Bcl‐2 is required for molecular interaction with immunosuppressant FK‐506 binding protein 38 (FKBP38)
inferred← citeshttps://doi.org/10.1016/j.febslet.2005.05.015openalex-snapshot
Structural conservation of residues in BH1 and BH2 domains of Bcl‐2 family proteins
inferred← citeshttps://doi.org/10.1016/j.insi.2025.100143openalex-snapshot
Deciphering the mutagenicity-related toxicity of acrylamide food toxin using computational toxicology, in-silico molecular docking/MD-simulations and bioinformatics
inferred← citeshttps://doi.org/10.1016/j.jbc.2025.110712openalex-snapshot
Inhibition of anti-apoptotic BCL2 overcomes adaptive resistance to co-targeting of the protein kinase FAK and MEK in GNAQ-driven uveal melanoma
inferred← citeshttps://doi.org/10.1016/j.jconrel.2015.03.036openalex-snapshot
Mitochondrial biology, targets, and drug delivery
inferred← citeshttps://doi.org/10.1016/j.jmb.2003.08.007openalex-snapshot
Solution Structure of the BHRF1 Protein From Epstein-Barr Virus, a Homolog of Human Bcl-2
inferred← citeshttps://doi.org/10.1016/j.jmb.2007.06.069openalex-snapshot
Molecular Basis of Bcl-xL’s Target Recognition Versatility Revealed by the Structure of Bcl-xL in Complex with the BH3 Domain of Beclin-1
inferred← citeshttps://doi.org/10.1016/j.jmb.2009.09.023openalex-snapshot
Reconstitution and Engineering of Apoptotic Protein Interactions on the Bacterial Cell Surface
inferred← citeshttps://doi.org/10.1016/j.jmb.2011.12.015openalex-snapshot
Ligand Binding and Membrane Insertion Compete with Oligomerization of the BclXL Apoptotic Repressor
inferred← citeshttps://doi.org/10.1016/j.jmb.2013.10.026openalex-snapshot
From DARPins to LoopDARPins: Novel LoopDARPin Design Allows the Selection of Low Picomolar Binders in a Single Round of Ribosome Display
inferred← citeshttps://doi.org/10.1016/j.jmb.2015.05.015openalex-snapshot
Locating Herpesvirus Bcl-2 Homologs in the Specificity Landscape of Anti-Apoptotic Bcl-2 Proteins
inferred← citeshttps://doi.org/10.1016/j.jmb.2019.06.010openalex-snapshot
Predicting Protein–Protein Interfaces that Bind Intrinsically Disordered Protein Regions
inferred← citeshttps://doi.org/10.1016/j.jmgm.2016.12.006openalex-snapshot
Binding affinity of pro-apoptotic BH3 peptides for the anti-apoptotic Mcl-1 and A1 proteins: Molecular dynamics simulations of Mcl-1 and A1 in complex with six different BH3 peptides
inferred← citeshttps://doi.org/10.1016/j.jnutbio.2015.12.019openalex-snapshot
Gamma-tocotrienol acts as a BH3 mimetic to induce apoptosis in neuroblastoma SH-SY5Y cells
inferred← citeshttps://doi.org/10.1016/j.jsb.2012.10.015openalex-snapshot
Poxvirus antagonism of innate immunity by Bcl-2 fold proteins
inferred← citeshttps://doi.org/10.1016/j.mitoco.2023.08.001openalex-snapshot
Structure-destabilizing mutations unleash an intrinsic perforation activity of antiapoptotic Bcl-2 in the mitochondrial membrane enabling apoptotic cell death
inferred← citeshttps://doi.org/10.1016/j.molcel.2006.10.014openalex-snapshot
The X-Ray Structure of a BAK Homodimer Reveals an Inhibitory Zinc Binding Site
inferred← citeshttps://doi.org/10.1016/j.molcel.2010.10.019openalex-snapshot
BH3-Triggered Structural Reorganization Drives the Activation of Proapoptotic BAX
inferred← citeshttps://doi.org/10.1016/j.molcel.2015.01.014openalex-snapshot
Inhibition of Pro-Apoptotic BAX by a Noncanonical Interaction Mechanism
inferred← citeshttps://doi.org/10.1016/j.molcel.2021.03.014openalex-snapshot
Structure of detergent-activated BAK dimers derived from the inert monomer
inferred← citeshttps://doi.org/10.1016/j.molstruc.2023.136298openalex-snapshot
Molecular docking, synthesis and evaluation of the antimicrobial, antiproliferative, and antioxidant properties of β-lactam bisindoles
inferred← citeshttps://doi.org/10.1016/j.molstruc.2024.139171openalex-snapshot
Multitargeted molecular docking and dynamics simulation studies of thiazolidinones synthesised from (R)-carvone against specific tumour protein markers: Synthesis, spectroscopic characterization and in-silico study
inferred← citeshttps://doi.org/10.1016/j.molstruc.2025.144061openalex-snapshot
One pot-synthesis, crystal structure , DFT studies, in silico molecular docking studies of Novel Mannich bases from p-methoxythymol
inferred← citeshttps://doi.org/10.1016/j.nurt.2009.11.001openalex-snapshot
Mitochondrial Damage: A Target for New Therapeutic Horizons
inferred← citeshttps://doi.org/10.1016/j.pep.2008.04.005openalex-snapshot
High-yield expression and purification of soluble forms of the anti-apoptotic Bcl-xL and Bcl-2 as TolAIII-fusion proteins
inferred← citeshttps://doi.org/10.1016/j.pep.2011.02.003openalex-snapshot
Expression and purification of full-length anti-apoptotic Bcl-2 using cell-free protein synthesis
inferred← citeshttps://doi.org/10.1016/j.pep.2019.02.004openalex-snapshot
Bax to the future – A novel, high-yielding approach for purification and expression of full-length Bax protein for structural studies
inferred← citeshttps://doi.org/10.1016/j.pep.2020.105628openalex-snapshot
A novel recombinant expression and purification approach for the full-length anti-apoptotic membrane protein Bcl-2
inferred← citeshttps://doi.org/10.1016/j.preteyeres.2017.01.002openalex-snapshot
BAX to basics: How the BCL2 gene family controls the death of retinal ganglion cells
inferred← citeshttps://doi.org/10.1016/j.pt.2013.12.005openalex-snapshot
Apoptosis in schistosomes: toward novel targets for the treatment of schistosomiasis
inferred← citeshttps://doi.org/10.1016/j.sbi.2005.10.003openalex-snapshot
Regulation of apoptosis: uncovering the binding determinants
inferred← citeshttps://doi.org/10.1016/j.str.2009.09.005openalex-snapshot
Structural Basis for Targeting of Human RNA Helicase DDX3 by Poxvirus Protein K7
inferred← citeshttps://doi.org/10.1016/j.tcb.2003.11.005openalex-snapshot
Bcl-w(edding) with mitochondria
inferred← citeshttps://doi.org/10.1016/j.ultras.2013.11.009openalex-snapshot
The effects of Ce6-mediated sono-photodynamic therapy on cell migration, apoptosis and autophagy in mouse mammary 4T1 cell line
inferred← citeshttps://doi.org/10.1016/j.yexcr.2009.01.009openalex-snapshot
Prosurvival Bcl-2 proteins stabilize pancreatic mitochondria and protect against necrosis in experimental pancreatitis
inferred← citeshttps://doi.org/10.1016/s0006-2952(02)01148-6openalex-snapshot
Prospects for targeting the Bcl-2 family of proteins to develop novel cytotoxic drugs
inferred← citeshttps://doi.org/10.1016/s0014-5793(03)00872-xopenalex-snapshot
Conversion of Bfl‐1, an anti‐apoptotic Bcl‐2 family protein, to a potent pro‐apoptotic protein by fusion with green fluorescent protein (GFP)
inferred← citeshttps://doi.org/10.1016/s0065-7743(05)40016-0openalex-snapshot
Inhibitors of Anti-apoptotic Proteins for Cancer Therapy
inferred← citeshttps://doi.org/10.1016/s0076-6879(08)01622-4openalex-snapshot
Chapter 22 Synthesis and Biophysical Characterization of Stabilized α‐Helices of BCL‐2 Domains
inferred← citeshttps://doi.org/10.1016/s0079-6565(02)00049-3openalex-snapshot
NMR screening techniques in drug discovery and drug design
inferred← citeshttps://doi.org/10.1016/s0092-8674(04)00162-xopenalex-snapshot
Conversion of Bcl-2 from Protector to Killer by Interaction with Nuclear Orphan Receptor Nur77/TR3
inferred← citeshttps://doi.org/10.1016/s0161-5890(02)00252-3openalex-snapshot
The Bcl-2 protein family: sensors and checkpoints for life-or-death decisions
inferred← citeshttps://doi.org/10.1016/s0163-7258(02)00339-xopenalex-snapshot
Regulation of cardiac myocyte cell death
inferred← citeshttps://doi.org/10.1016/s1046-5928(02)00016-5openalex-snapshot
Soluble expression in Escherichia coli, purification and characterization of a human TF-1 cell apoptosis-related protein TFAR19
inferred← citeshttps://doi.org/10.1016/s1074-5521(02)00247-8openalex-snapshot
The Chemical Biology of Apoptosis
inferred← citeshttps://doi.org/10.1016/s1074-7613(03)00234-6openalex-snapshot
The Structure of a Bcl-xL/Bim Fragment Complex
inferred← citeshttps://doi.org/10.1016/s1359-6446(04)03358-6openalex-snapshot
Monitor – chemistry
inferred← citeshttps://doi.org/10.1016/s1367-5931(02)00352-6openalex-snapshot
A view to a kill: ligands for Bcl-2 family proteins
inferred← citeshttps://doi.org/10.1016/s1567-1356(03)00143-0openalex-snapshot
Yeast as a tool to study Bax/mitochondrial interactions in cell death
inferred← citeshttps://doi.org/10.1021/acs.biochem.0c00661openalex-snapshot
Computational Design of BH3-Mimetic Peptide Inhibitors That Can Bind Specifically to Mcl-1 or Bcl-X L : Role of Non-Hot Spot Residues
inferred← citeshttps://doi.org/10.1021/acs.biochem.2c00709openalex-snapshot
Innate Conformational Dynamics Drive Binding Specificity in Anti-Apoptotic Proteins Mcl-1 and Bcl-2
inferred← citeshttps://doi.org/10.1021/acs.bioconjchem.0c00363openalex-snapshot
Biocompatible and Rapid Cyclization of Peptides with 2,4-Difluoro-6-hydroxy-1,3,5-benzenetricarbonitrile for the Development of Cyclic Peptide Libraries
inferred← citeshttps://doi.org/10.1021/acs.jafc.9b01203openalex-snapshot
Characterization and Inception of a Triterpenoid Astrakurkurol, as a Cytotoxic Molecule on Human Hepatocellular Carcinoma Cells, Hep3B
inferred← citeshttps://doi.org/10.1021/acs.jcim.2c01408openalex-snapshot
Integrating Protein Interaction Surface Prediction with a Fragment-Based Drug Design: Automatic Design of New Leads with Fragments on Energy Surfaces
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.0c01290openalex-snapshot
Targeting the Allosteric Pathway That Interconnects the Core-Functional Scaffold and the Distal Phosphorylation Sites for Specific Dephosphorylation of Bcl-2
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.1c00690openalex-snapshot
Structure-Based Optimization of 3-Phenyl-N-(2-(3-phenylureido)ethyl)thiophene-2-sulfonamide Derivatives as Selective Mcl-1 Inhibitors
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.5c02670openalex-snapshot
Design, Synthesis, and Evaluation of Phenylpyrrole Derivatives as Small-Molecule Activators of BAX
inferred← citeshttps://doi.org/10.1021/acschembio.5c00913openalex-snapshot
Avoiding Mitochondrial Apoptosis by the Bcl-2-Driven Bax Oligomerization on Membrane Surfaces
inferred← citeshttps://doi.org/10.1021/acschembio.8b00421openalex-snapshot
High-Throughput Screens To Identify Autophagy Inducers That Function by Disrupting Beclin 1/Bcl-2 Binding
inferred← citeshttps://doi.org/10.1021/acsomega.2c07779openalex-snapshot
Anticancer Activities of Re(I) Tricarbonyl and Its Imidazole-Based Ligands: Insight from a Theoretical Approach
inferred← citeshttps://doi.org/10.1021/acsomega.9b00611openalex-snapshot
Establishing Drug Discovery and Identification of Hit Series for the Anti-apoptotic Proteins, Bcl-2 and Mcl-1
inferred← citeshttps://doi.org/10.1021/bi0503192openalex-snapshot
Modulation of the Membrane Orientation and Secondary Structure of the C-Terminal Domains of Bak and Bcl-2 by Lipids
inferred← citeshttps://doi.org/10.1021/bi052332sopenalex-snapshot
Structural Model of the BCL-w−BID Peptide Complex and Its Interactions with Phospholipid Micelles,
inferred← citeshttps://doi.org/10.1021/bi061577hopenalex-snapshot
NMR Structural Investigation of the Mitochondrial Outer Membrane Protein VDAC and Its Interaction with Antiapoptotic Bcl-xL
inferred← citeshttps://doi.org/10.1021/bi100029kopenalex-snapshot
Identification of Core Structural Residues in the Sequentially Diverse and Structurally Homologous Bcl-2 Family of Proteins
inferred← citeshttps://doi.org/10.1021/cb500259eopenalex-snapshot
Direct Binding of Bcl-2 Family Proteins by Quercetin Triggers Its Pro-Apoptotic Activity
inferred← citeshttps://doi.org/10.1021/cr4004049openalex-snapshot
Small Molecule Modulators of Protein–Protein Interactions: Selected Case Studies
inferred← citeshttps://doi.org/10.1021/ja0441211openalex-snapshot
Paralog-Selective Ligands for Bcl-2 Proteins
inferred← citeshttps://doi.org/10.1021/jacs.5b05896openalex-snapshot
α/β-Peptide Foldamers Targeting Intracellular Protein–Protein Interactions with Activity in Living Cells
inferred← citeshttps://doi.org/10.1021/jacs.9b11875openalex-snapshot
Condensation of 2-((Alkylthio)(aryl)methylene)malononitrile with 1,2-Aminothiol as a Novel Bioorthogonal Reaction for Site-Specific Protein Modification and Peptide Cyclization
inferred← citeshttps://doi.org/10.1021/jm010016fopenalex-snapshot
Discovery of Small-Molecule Inhibitors of Bcl-2 through Structure-Based Computer Screening
inferred← citeshttps://doi.org/10.1021/jm050754uopenalex-snapshot
Discovery and Structure−Activity Relationship of Antagonists of B-Cell Lymphoma 2 Family Proteins with Chemopotentiation Activity in Vitro and in Vivo
inferred← citeshttps://doi.org/10.1021/jm060460oopenalex-snapshot
Structure-Based Design of Potent Small-Molecule Inhibitors of Anti-Apoptotic Bcl-2 Proteins
inferred← citeshttps://doi.org/10.1021/jm060968ropenalex-snapshot
Structure−Activity Relationship Studies of Ethyl 2-Amino-6-bromo-4-(1-cyano-2-ethoxy-2-oxoethyl)-4H-chromene-3-carboxylate (HA 14-1), an Antagonist for Antiapoptotic Bcl-2 Proteins To Overcome Drug Resistance in Cancer
inferred← citeshttps://doi.org/10.1021/jm061152topenalex-snapshot
Studies Leading to Potent, Dual Inhibitors of Bcl-2 and Bcl-xL
inferred← citeshttps://doi.org/10.1021/jm061400lopenalex-snapshot
Pyrogallol-Based Molecules as Potent Inhibitors of the Antiapoptotic Bcl-2 Proteins
inferred← citeshttps://doi.org/10.1021/jm070383copenalex-snapshot
Structure-Based Design of Flavonoid Compounds As a New Class of Small-Molecule Inhibitors of the Anti-apoptotic Bcl-2 Proteins
inferred← citeshttps://doi.org/10.1021/jm3010306openalex-snapshot
Structure-Based Discovery of BM-957 as a Potent Small-Molecule Inhibitor of Bcl-2 and Bcl-xL Capable of Achieving Complete Tumor Regression
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