On the public citation graph

Targeting the BH3 Domain Mediated Protein−Protein Interaction of Bcl-xL through Virtual Screening

https://doi.org/10.1021/ci1000373
0 signed · 114 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.
Claim with ORCID
Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What this work says

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

inferredcites →https://doi.org/10.1002/(sici)1097-0134(199602)24:2<227::aid-prot9>3.0.co;2-fopenalex-snapshot
Fitting an inhibitor into the active site of thermolysin: A molecular dynamics case study
inferredcites →https://doi.org/10.1002/(sici)1097-0134(19990501)35:2<153::aid-prot2>3.0.co;2-eopenalex-snapshot
Docking of flexible ligands to flexible receptors in solution by molecular dynamics simulation
inferredcites →https://doi.org/10.1002/anie.200461786openalex-snapshot
Strategies for Targeting Protein–Protein Interactions With Synthetic Agents
inferredcites →https://doi.org/10.1002/cmdc.200600004openalex-snapshot
Drugs Targeting Protein–Protein Interactions
inferredcites →https://doi.org/10.1002/cmdc.200700348openalex-snapshot
Discovery of VHR Phosphatase Inhibitors with Micromolar Activity based on Structure‐Based Virtual Screening
inferredcites →https://doi.org/10.1002/cmdc.200800104openalex-snapshot
Thiobarbiturates as Sirtuin Inhibitors: Virtual Screening, Free‐Energy Calculations, and Biological Testing
inferredcites →https://doi.org/10.1002/cmdc.200800301openalex-snapshot
Virtual Screening and Biological Characterization of Novel Histone Arginine Methyltransferase PRMT1 Inhibitors
inferredcites →https://doi.org/10.1002/cmdc.200800375openalex-snapshot
In Silico Screening for PTPN22 Inhibitors: Active Hits from an Inactive Phosphatase Conformation
inferredcites →https://doi.org/10.1002/cmdc.200900145openalex-snapshot
Discovery of Ligands for the Human Intestinal Di‐/Tripeptide Transporter (hPEPT1) Using a QSAR‐Assisted Virtual Screening Strategy
inferredcites →https://doi.org/10.1002/prot.10028openalex-snapshot
Automated docking to multiple target structures: Incorporation of protein mobility and structural water heterogeneity in AutoDock
inferredcites →https://doi.org/10.1002/prot.10085openalex-snapshot
Dissecting protein–protein recognition sites
inferredcites →https://doi.org/10.1002/prot.340190303openalex-snapshot
Molecular dynamics simulation of the docking of substrates to proteins
inferredcites →https://doi.org/10.1006/jmbi.1996.0776openalex-snapshot
Molecular docking to ensembles of protein structures 1 1Edited by B. Honig
inferredcites →https://doi.org/10.1007/s00005-006-0019-xopenalex-snapshot
Modulation of apoptosis signaling for cancer therapy
inferredcites →https://doi.org/10.1016/0022-2836(91)90859-5openalex-snapshot
“Soft docking”: Matching of molecular surface cubes
inferredcites →https://doi.org/10.1016/j.ab.2004.05.055openalex-snapshot
Development and optimization of a binding assay for the XIAP BIR3 domain using fluorescence polarization
inferredcites →https://doi.org/10.1016/j.bbamcr.2003.08.009openalex-snapshot
The role of Bcl-2 family members in tumorigenesis
inferredcites →https://doi.org/10.1016/j.bbamcr.2003.08.012openalex-snapshot
Structural biology of the Bcl-2 family of proteins
inferredcites →https://doi.org/10.1016/j.bioorg.2007.03.001openalex-snapshot
Structure-based discovery of a new class of Bcl-xL antagonists
inferredcites →https://doi.org/10.1016/j.bmc.2008.01.011openalex-snapshot
Structure-based virtual screening against SARS-3CLpro to identify novel non-peptidic hits
inferredcites →https://doi.org/10.1016/j.ccr.2004.07.011openalex-snapshot
Antiapoptotic BCL-2 is required for maintenance of a model leukemia
inferredcites →https://doi.org/10.1016/j.ceb.2006.10.008openalex-snapshot
Apoptosis in the treatment of cancer: a promise kept?
inferredcites →https://doi.org/10.1016/j.jmb.2009.04.033openalex-snapshot
Structural Basis for Bivalent Smac-Mimetics Recognition in the IAP Protein Family
inferredcites →https://doi.org/10.1016/j.molmed.2006.06.002openalex-snapshot
Targeted induction of apoptosis for cancer therapy: current progress and prospects
inferredcites →https://doi.org/10.1016/j.yexcr.2007.07.031openalex-snapshot
In vitro analysis of Bcl-2 proteins in mitochondria and endoplasmic reticulum: Similarities in anti-apoptotic functions and differences in regulation
inferredcites →https://doi.org/10.1016/s0006-2952(02)01148-6openalex-snapshot
Prospects for targeting the Bcl-2 family of proteins to develop novel cytotoxic drugs
inferredcites →https://doi.org/10.1016/s0009-2614(97)01074-9openalex-snapshot
Flexible docking of a ligand peptide to a receptor protein by multicanonical molecular dynamics simulation
inferredcites →https://doi.org/10.1016/s0026-895x(24)23192-8openalex-snapshot
Accommodating Protein Flexibility in Computational Drug Design,
inferredcites →https://doi.org/10.1016/s0092-8674(00)00008-8openalex-snapshot
Smac, a Mitochondrial Protein that Promotes Cytochrome c–Dependent Caspase Activation by Eliminating IAP Inhibition
inferredcites →https://doi.org/10.1016/s0092-8674(00)00009-xopenalex-snapshot
Identification of DIABLO, a Mammalian Protein that Promotes Apoptosis by Binding to and Antagonizing IAP Proteins
inferredcites →https://doi.org/10.1016/s0092-8674(00)81683-9openalex-snapshot
The Hallmarks of Cancer
inferredcites →https://doi.org/10.1016/s0092-8674(04)00046-7openalex-snapshot
Cell Death
inferredcites →https://doi.org/10.1016/s0361-090x(03)00067-9openalex-snapshot
Enhancing the efficacy of chemotherapeutic drugs by the suppression of antiapoptotic cellular defense
inferredcites →https://doi.org/10.1016/s0959-440x(02)00283-xopenalex-snapshot
Unraveling hot spots in binding interfaces: progress and challenges
inferredcites →https://doi.org/10.1016/s1093-3263(00)00036-xopenalex-snapshot
A method for including protein flexibility in protein-ligand docking: improving tools for database mining and virtual screening
inferredcites →https://doi.org/10.1016/s1359-6446(04)03069-7openalex-snapshot
Ligand efficiency: a useful metric for lead selection
inferredcites →https://doi.org/10.1016/s1367-5931(02)00341-1openalex-snapshot
Protein flexibility and drug design: how to hit a moving target
inferredcites →https://doi.org/10.1021/bi0619977openalex-snapshot
A Complete Structural Description of the Catalytic Cycle of Yeast Pyrophosphatase,
inferredcites →https://doi.org/10.1021/ci049714+openalex-snapshot
ZINC − A Free Database of Commercially Available Compounds for Virtual Screening
inferredcites →https://doi.org/10.1021/ja011239yopenalex-snapshot
A Novel Approach for Characterizing Protein Ligand Complexes: Molecular Basis for Specificity of Small-Molecule Bcl-2 Inhibitors
inferredcites →https://doi.org/10.1021/jm010468sopenalex-snapshot
Inhibition of Protein−Protein Association by Small Molecules: Approaches and Progress
inferredcites →https://doi.org/10.1021/jm030190zopenalex-snapshot
Discovery, Characterization, and Structure−Activity Relationships Studies of Proapoptotic Polyphenols Targeting B-Cell Lymphocyte/Leukemia-2 Proteins
inferredcites →https://doi.org/10.1021/jm0493717openalex-snapshot
Identification of Novel Parasitic Cysteine Protease Inhibitors Using Virtual Screening. 1. The ChemBridge Database
inferredcites →https://doi.org/10.1021/jm050540copenalex-snapshot
Novel Procedure for Modeling Ligand/Receptor Induced Fit Effects
inferredcites →https://doi.org/10.1021/jm0505765openalex-snapshot
Identification of Novel Parasitic Cysteine Protease Inhibitors by Use of Virtual Screening. 2. The Available Chemical Directory
inferredcites →https://doi.org/10.1021/jm0507532openalex-snapshot
Discovery of a Potent Inhibitor of the Antiapoptotic Protein Bcl-x L from NMR and Parallel Synthesis
inferredcites →https://doi.org/10.1021/jm060460oopenalex-snapshot
Structure-Based Design of Potent Small-Molecule Inhibitors of Anti-Apoptotic Bcl-2 Proteins
inferredcites →https://doi.org/10.1021/jm061152topenalex-snapshot
Studies Leading to Potent, Dual Inhibitors of Bcl-2 and Bcl-xL
inferredcites →https://doi.org/10.1021/jm800669sopenalex-snapshot
Discovery of an Orally Bioavailable Small Molecule Inhibitor of Prosurvival B-Cell Lymphoma 2 Proteins
inferredcites →https://doi.org/10.1038/35037747openalex-snapshot
From bench to clinic with apoptosis-based therapeutic agents
inferredcites →https://doi.org/10.1038/35055085openalex-snapshot
Identification of small-molecule inhibitors of interaction between the BH3 domain and Bcl-xL
inferredcites →https://doi.org/10.1038/35055095openalex-snapshot
Antimycin A mimics a cell-death-inducing Bcl-2 homology domain 3
inferredcites →https://doi.org/10.1038/40901openalex-snapshot
X-linked IAP is a direct inhibitor of cell-death proteases
inferredcites →https://doi.org/10.1038/nature03579openalex-snapshot
An inhibitor of Bcl-2 family proteins induces regression of solid tumours
inferredcites →https://doi.org/10.1038/nrc2465openalex-snapshot
The TRAIL apoptotic pathway in cancer onset, progression and therapy
inferredcites →https://doi.org/10.1038/nrc991openalex-snapshot
Inhibiting the p53–MDM2 interaction: an important target for cancer therapy
inferredcites →https://doi.org/10.1038/nrd1063openalex-snapshot
Designing screens: how to make your hits a hit
inferredcites →https://doi.org/10.1038/nrd2656openalex-snapshot
The genetics of the p53 pathway, apoptosis and cancer therapy
inferredcites →https://doi.org/10.1038/sj.emboj.7601126openalex-snapshot
Bcl‐2 changes conformation to inhibit Bax oligomerization
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.c300138200openalex-snapshot
Identification of Chelerythrine as an Inhibitor of BclXL Function
inferredcites →https://doi.org/10.1074/jbc.m100655200openalex-snapshot
Bcl-2 Prevents Bax Oligomerization in the Mitochondrial Outer Membrane
inferredcites →https://doi.org/10.1074/jbc.m109939200openalex-snapshot
Bax and Bak Independently Promote Cytochrome cRelease from Mitochondria
inferredcites →https://doi.org/10.1074/jbc.m203392200openalex-snapshot
Association of Bax and Bak Homo-oligomers in Mitochondria
inferredcites →https://doi.org/10.1074/jbc.m400295200openalex-snapshot
Critical Upstream Signals of Cytochrome c Release Induced by a Novel Bcl-2 Inhibitor
inferredcites →https://doi.org/10.1089/108729002760220798openalex-snapshot
Oblimersen Bcl-2 Antisense: Facilitating Apoptosis in Anticancer Treatment
inferredcites →https://doi.org/10.1093/jnci/89.14.988openalex-snapshot
Promise and Problems of Bcl-2 Antisense Therapy
inferredcites →https://doi.org/10.1097/cad.0b013e32832ced78openalex-snapshot
Smac mimetics as new cancer therapeutics
inferredcites →https://doi.org/10.1111/j.1747-0285.2005.00327.xopenalex-snapshot
Use of an Induced Fit Receptor Structure in Virtual Screening
inferredcites →https://doi.org/10.1126/science.1066315openalex-snapshot
Glimpses of a Tiny RNA World
inferredcites →https://doi.org/10.1126/science.1098231openalex-snapshot
A Small Molecule Smac Mimic Potentiates TRAIL- and TNFα-Mediated Cell Death
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.7878464openalex-snapshot
Apoptosis in the Pathogenesis and Treatment of Disease
inferredcites →https://doi.org/10.1158/0008-5472.can-04-0945openalex-snapshot
Breast Cancer Cells Can Evade Apoptosis-Mediated Selective Killing by a Novel Small Molecule Inhibitor of Bcl-2
inferredcites →https://doi.org/10.1177/1087057104265290openalex-snapshot
High-Throughput Screening: Searching for Higher Productivity
inferredcites →https://doi.org/10.1242/jcs.03293openalex-snapshot
Outcomes of p53 activation - spoilt for choice
inferredcites →https://doi.org/10.1358/dof.2007.032.03.1084808openalex-snapshot
Obatoclax Mesylate
inferredcites →https://doi.org/10.1385/1-59259-851-x:043openalex-snapshot
Resistance to Apoptosis in Cancer Therapy
inferredcites →https://doi.org/10.1517/14728222.11.10.1299openalex-snapshot
TRAIL in cancer therapy: present and future challenges
inferredcites →https://doi.org/10.2174/1381612043382747openalex-snapshot
TNF-Related Apoptosis-Inducing Ligand (TRAIL): A Potential Candidate for Combined Treatment of Hematological Malignancies
inferredcites →https://doi.org/10.2174/156802607780906735openalex-snapshot
Protein-Protein Interaction Inhibitors: Small Molecules from Screening Techniques
inferredcites →https://doi.org/10.2174/157489208783478676openalex-snapshot
Small-Molecule Inhibitors of Bcl-2 Family Proteins as Therapeutic Agents in Cancer
inferredcites →https://doi.org/10.2174/187152009789124628openalex-snapshot
Recent Advances in Validating MDM2 as a Cancer Target

What points at this work

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

inferred← citeshttps://doi.org/10.1002/cmdc.201700572openalex-snapshot
Mimicking Intermolecular Interactions of Tight Protein–Protein Complexes for Small‐Molecule Antagonists
inferred← citeshttps://doi.org/10.1007/82_2010_93openalex-snapshot
Small-Molecule Inhibitors of IL-2/IL-2R: Lessons Learned and Applied
inferred← citeshttps://doi.org/10.1007/s11030-018-9856-xopenalex-snapshot
Identification of molecular features necessary for selective inhibition of B cell lymphoma proteins using machine learning techniques
inferred← citeshttps://doi.org/10.1016/b978-0-12-818549-0.00016-9openalex-snapshot
Miscellaneous small- molecule and biological approaches to targeted cancer therapy
inferred← citeshttps://doi.org/10.1016/b978-0-444-62649-3.00011-9openalex-snapshot
Other Nonbiological Approaches to Targeted Cancer Chemotherapy
inferred← citeshttps://doi.org/10.1016/b978-1-60805-865-5.50004-6openalex-snapshot
Recent advances in the discovery and development of protein- protein interaction modulators by virtual screening
inferred← citeshttps://doi.org/10.1016/j.bmc.2014.09.047openalex-snapshot
Design, synthesis and structure–activity relationship studies of morpholino-1H-phenalene derivatives that antagonize Mcl-1/Bcl-2
inferred← citeshttps://doi.org/10.1016/j.cbi.2016.03.006openalex-snapshot
Discovery of new selective cytotoxic agents against Bcl-2 expressing cancer cells using ligand-based modeling
inferred← citeshttps://doi.org/10.1016/j.cbpa.2011.02.021openalex-snapshot
The role of computational methods in the identification of bioactive compounds
inferred← citeshttps://doi.org/10.1016/j.ejmech.2013.01.045openalex-snapshot
Novel IKKβ inhibitors discovery based on the co-crystal structure by using binding-conformation-based and ligand-based method
inferred← citeshttps://doi.org/10.1016/j.tips.2013.04.007openalex-snapshot
Targeting protein–protein interactions as an anticancer strategy
inferred← citeshttps://doi.org/10.1021/acs.jcim.2c00920openalex-snapshot
Predicting the Likelihood of Molecules to Act as Modulators of Protein–Protein Interactions
inferred← citeshttps://doi.org/10.1021/acs.jcim.7b00181openalex-snapshot
A Computational Investigation of Small-Molecule Engagement of Hot Spots at Protein–Protein Interaction Interfaces
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.0c02227openalex-snapshot
Decision Making in Structure-Based Drug Discovery: Visual Inspection of Docking Results
inferred← citeshttps://doi.org/10.1021/acsomega.5c11622openalex-snapshot
Revealing the Binding Mechanism of Gossypol on Bcl-2 via Funnel Metadynamics Simulations
inferred← citeshttps://doi.org/10.1021/ci1004916openalex-snapshot
Inhibitors of SARS-3CL pro : Virtual Screening, Biological Evaluation, and Molecular Dynamics Simulation Studies
inferred← citeshttps://doi.org/10.1021/ci100501dopenalex-snapshot
Rational Design of New Class of BH3-Mimetics As Inhibitors of the Bcl-xL Protein
inferred← citeshttps://doi.org/10.1021/ci200029yopenalex-snapshot
Identification of Novel Malarial Cysteine Protease Inhibitors Using Structure-Based Virtual Screening of a Focused Cysteine Protease Inhibitor Library
inferred← citeshttps://doi.org/10.1021/ci400332eopenalex-snapshot
From Determinants of RUNX1/ETO Tetramerization to Small-Molecule Protein–Protein Interaction Inhibitors Targeting Acute Myeloid Leukemia
inferred← citeshttps://doi.org/10.1038/nrd.2016.29openalex-snapshot
Small molecules, big targets: drug discovery faces the protein–protein interaction challenge
inferred← citeshttps://doi.org/10.1039/9781849735377-00319openalex-snapshot
Computational Strategies and Challenges for Targeting Protein–Protein Interactions with Small Molecules
inferred← citeshttps://doi.org/10.1039/c2mb25195gopenalex-snapshot
Screening efficient BH3-mimetics to hBcl-B by means of peptidodynmimetic method
inferred← citeshttps://doi.org/10.1074/jbc.m117.809137openalex-snapshot
Structure-based virtual screening identifies a small-molecule inhibitor of the profilin 1–actin interaction
inferred← citeshttps://doi.org/10.11606/d.9.2016.tde-17022016-103150openalex-snapshot
Potenciais candidatos a novos antineoplásicos: síntese e avaliação da atividade antitumoral de análogos da queleritrina planejados por simplificação molecular
inferred← citeshttps://doi.org/10.1371/journal.pone.0054397openalex-snapshot
Behavior of Solvent-Exposed Hydrophobic Groove in the Anti-Apoptotic Bcl-XL Protein: Clues for Its Ability to Bind Diverse BH3 Ligands from MD Simulations
inferred← citeshttps://doi.org/10.2174/0929867324666170712115411openalex-snapshot
Rational Drug Design of Antineoplastic Agents Using 3D-QSAR, Cheminformatic, and Virtual Screening Approaches
inferred← citeshttps://doi.org/10.2174/138161212799436386openalex-snapshot
From Laptop to Benchtop to Bedside: Structure-based Drug Design on Protein Targets
inferred← citeshttps://doi.org/10.2174/138955712802762202openalex-snapshot
In silico Methods for Designing Antagonists to Anti-apoptotic Members of Bcl-2 Family Proteins
inferred← citeshttps://doi.org/10.22159/ajpcr.2017.v10i4.16269openalex-snapshot
IN SILICO DOCKING STUDIES OF GALLIC ACID STRUCTURAL ANALOGUES AS BCL-XL INHIBITOR IN CANCER
inferred← citeshttps://doi.org/10.3389/fmed.2026.1925157openalex-snapshot
Targeting BCL-XL-mediated apoptotic resistance in lung cancer: in silico and in vitro identification of bioactive inhibitors from Ailanthus excelsa chloroform extract
inferred← citeshttps://doi.org/10.4155/fmc.13.204openalex-snapshot
Structure-Based Design of Small-Molecule Protein–Protein Interaction Modulators: The Story so Far
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.