On the public citation graph

Discovery of binding proteins for a protein target using protein-protein docking-based virtual screening

https://doi.org/10.1002/prot.24611
0 signed · 66 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 See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.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(19990501)35:2<133::aid-prot1>3.0.co;2-nopenalex-snapshot
Effective energy function for proteins in solution
inferredcites →https://doi.org/10.1002/anie.201305963openalex-snapshot
Computational Design of Helical Peptides Targeting TNFα
inferredcites →https://doi.org/10.1002/jcc.21276openalex-snapshot
Protein–protein docking dealing with the unknown
inferredcites →https://doi.org/10.1002/jcc.21839openalex-snapshot
SDOCK: A global protein‐protein docking program using stepwise force‐field potentials
inferredcites →https://doi.org/10.1002/prot.10389openalex-snapshot
ZDOCK: An initial‐stage protein‐docking algorithm
inferredcites →https://doi.org/10.1002/prot.20560openalex-snapshot
Protein–protein docking benchmark 2.0: An update
inferredcites →https://doi.org/10.1002/prot.22106openalex-snapshot
Protein–protein docking benchmark version 3.0
inferredcites →https://doi.org/10.1002/prot.24009openalex-snapshot
Automatch: Target‐binding protein design and enzyme design by automatic pinpointing potential active sites in available protein scaffolds
inferredcites →https://doi.org/10.1006/jmbi.1997.1203openalex-snapshot
Modelling protein docking using shape complementarity, electrostatics and biochemical information 1 1Edited by J. Thornton
inferredcites →https://doi.org/10.1006/jmbi.1998.1843openalex-snapshot
Anatomy of hot spots in protein interfaces
inferredcites →https://doi.org/10.1016/b978-0-12-394292-0.00014-xopenalex-snapshot
Engineering Fibronectin-Based Binding Proteins by Yeast Surface Display
inferredcites →https://doi.org/10.1016/b978-0-12-396962-0.00007-0openalex-snapshot
Anticalins
inferredcites →https://doi.org/10.1016/j.biotechadv.2011.03.005openalex-snapshot
Longer action means better drug: Tuning up protein therapeutics
inferredcites →https://doi.org/10.1016/j.cbpa.2009.04.627openalex-snapshot
Engineered protein scaffolds as next-generation antibody therapeutics
inferredcites →https://doi.org/10.1016/j.cell.2012.03.016openalex-snapshot
Role of the Biomolecular Energy Gap in Protein Design, Structure, and Evolution
inferredcites →https://doi.org/10.1016/j.pharmthera.2007.10.001openalex-snapshot
Tumor necrosis factor antagonist mechanisms of action: A comprehensive review
inferredcites →https://doi.org/10.1016/j.sbi.2004.04.006openalex-snapshot
A structural perspective on protein–protein interactions
inferredcites →https://doi.org/10.1016/j.sbi.2009.07.005openalex-snapshot
Computational design of affinity and specificity at protein–protein interfaces
inferredcites →https://doi.org/10.1016/j.yexcr.2011.02.013openalex-snapshot
Introduction to current and future protein therapeutics: A protein engineering perspective
inferredcites →https://doi.org/10.1016/s0168-9525(00)02024-2openalex-snapshot
EMBOSS: The European Molecular Biology Open Software Suite
inferredcites →https://doi.org/10.1016/s0959-440x(02)00310-xopenalex-snapshot
Complexity and simplicity of ligand–macromolecule interactions: the energy landscape perspective
inferredcites →https://doi.org/10.1016/s1359-6446(02)02590-4openalex-snapshot
Optimization of protein therapeutics by directed evolution
inferredcites →https://doi.org/10.1021/ci0100144openalex-snapshot
Protocols for Bridging the Peptide to Nonpeptide Gap in Topological Similarity Searches
inferredcites →https://doi.org/10.1021/ci600426eopenalex-snapshot
Evaluating Virtual Screening Methods: Good and Bad Metrics for the “Early Recognition” Problem
inferredcites →https://doi.org/10.1021/ci900056copenalex-snapshot
Comparison of Several Molecular Docking Programs: Pose Prediction and Virtual Screening Accuracy
inferredcites →https://doi.org/10.1021/ci900463uopenalex-snapshot
Binding Energy Landscape Analysis Helps to Discriminate True Hits from High-Scoring Decoys in Virtual Screening
inferredcites →https://doi.org/10.1021/pr9009854openalex-snapshot
Are Scoring Functions in Protein−Protein Docking Ready To Predict Interactomes? Clues from a Novel Binding Affinity Benchmark
inferredcites →https://doi.org/10.1038/11354openalex-snapshot
Upregulation of RGS7 may contribute to tumor necrosis factor-induced changes in central nervous function
inferredcites →https://doi.org/10.1038/35059138openalex-snapshot
Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 Å
inferredcites →https://doi.org/10.1038/msb.2011.3openalex-snapshot
Towards the prediction of protein interaction partners using physical docking
inferredcites →https://doi.org/10.1038/nm939openalex-snapshot
TNF defined as a therapeutic target for rheumatoid arthritis and other autoimmune diseases
inferredcites →https://doi.org/10.1038/nrd2399openalex-snapshot
Protein therapeutics: a summary and pharmacological classification
inferredcites →https://doi.org/10.1038/nri1184openalex-snapshot
Signalling pathways of the TNF superfamily: a double-edged sword
inferredcites →https://doi.org/10.1038/nrm1859openalex-snapshot
Structural systems biology: modelling protein interactions
inferredcites →https://doi.org/10.1038/nsmb.1683openalex-snapshot
Crystal structure of TNFα complexed with a poxvirus MHC-related TNF binding protein
inferredcites →https://doi.org/10.1039/c005060copenalex-snapshot
Protein–protein docking tested in blind predictions: the CAPRI experiment
inferredcites →https://doi.org/10.1042/bst0391382openalex-snapshot
Towards structure-based protein drug design
inferredcites →https://doi.org/10.1073/pnas.0606198104openalex-snapshot
Nonnatural protein–protein interaction-pair design by key residues grafting
inferredcites →https://doi.org/10.1073/pnas.0709223105openalex-snapshot
Crystal structure and functional analysis of tetracenomycin ARO/CYC: Implications for cyclization specificity of aromatic polyketides
inferredcites →https://doi.org/10.1093/bioinformatics/btn334openalex-snapshot
Accelerating and focusing protein–protein docking correlations using multi-dimensional rotational FFT generating functions
inferredcites →https://doi.org/10.1111/febs.12056openalex-snapshot
Grafting of functional motifs onto protein scaffolds identified by PDB screening – an efficient route to design optimizable protein binders
inferredcites →https://doi.org/10.1126/science.1202617openalex-snapshot
Computational Design of Proteins Targeting the Conserved Stem Region of Influenza Hemagglutinin
inferredcites →https://doi.org/10.1126/science.257.5073.1078openalex-snapshot
Structure-Based Strategies for Drug Design and Discovery
inferredcites →https://doi.org/10.1142/s0219720009004461openalex-snapshot
IN SILICO SCREENING OF PROTEIN–PROTEIN INTERACTIONS WITH ALL-TO-ALL RIGID DOCKING AND CLUSTERING: AN APPLICATION TO PATHWAY ANALYSIS
inferredcites →https://doi.org/10.1186/1471-2105-10-225openalex-snapshot
A statistical framework to evaluate virtual screening
inferredcites →https://doi.org/10.1371/journal.pcbi.1000490openalex-snapshot
Pushing Structural Information into the Yeast Interactome by High-Throughput Protein Docking Experiments
inferredcites →https://doi.org/10.1523/jneurosci.1806-08.2008openalex-snapshot
Regulator of G-Protein Signaling 10 Promotes Dopaminergic Neuron Survival via Regulation of the Microglial Inflammatory Response
inferredcites →https://doi.org/10.2174/138161206778743655openalex-snapshot
Computational Protein Design: A Novel Path to Future Protein Drugs
inferredcites →https://doi.org/10.2174/138920308783565741openalex-snapshot
Recent Progress and Future Directions in Protein-Protein Docking

What points at this work

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

inferred← citeshttps://doi.org/10.1002/pro.4322openalex-snapshot
Tertiary motifs as building blocks for the design of protein‐binding peptides
inferred← citeshttps://doi.org/10.1007/10_2016_41openalex-snapshot
Rigid-Docking Approaches to Explore Protein–Protein Interaction Space
inferred← citeshttps://doi.org/10.1007/978-3-030-69984-0_53openalex-snapshot
High-Performance Cloud Computing for Exhaustive Protein–Protein Docking
inferred← citeshttps://doi.org/10.1016/j.omtn.2023.06.013openalex-snapshot
PPM1H is down-regulated by ATF6 and dephosphorylates p-RPS6KB1 to inhibit progression of hepatocellular carcinoma
inferred← citeshttps://doi.org/10.1016/j.tifs.2026.105751openalex-snapshot
Advancing food science through molecular docking: Methods, applications, and future perspectives
inferred← citeshttps://doi.org/10.1017/qrd.2022.16openalex-snapshot
Towards design of drugs and delivery systems with the Martini coarse-grained model
inferred← citeshttps://doi.org/10.1017/qrd.2022.16.pr1openalex-snapshot
Review: Towards design of drugs and delivery systems with the Martini coarse-grained model — R0/PR1
inferred← citeshttps://doi.org/10.1017/qrd.2022.16.pr2openalex-snapshot
Review: Towards design of drugs and delivery systems with the Martini coarse-grained model — R0/PR2
inferred← citeshttps://doi.org/10.1017/qrd.2022.16.pr3openalex-snapshot
Review: Towards design of drugs and delivery systems with the Martini coarse-grained model — R0/PR3
inferred← citeshttps://doi.org/10.1017/qrd.2022.16.pr4openalex-snapshot
Recommendation: Towards design of drugs and delivery systems with the Martini coarse-grained model — R0/PR4
inferred← citeshttps://doi.org/10.1017/qrd.2022.16.pr5openalex-snapshot
Recommendation: Towards design of drugs and delivery systems with the Martini coarse-grained model — R1/PR5
inferred← citeshttps://doi.org/10.1039/c9md00473dopenalex-snapshot
Discovery and characterization of a novel peptide inhibitor against influenza neuraminidase
inferred← citeshttps://doi.org/10.1088/1674-1056/25/1/018702openalex-snapshot
Computational design of proteins with novel structure and functions
inferred← citeshttps://doi.org/10.1093/bioinformatics/btu532openalex-snapshot
MEGADOCK 4.0: an ultra–high-performance protein–protein docking software for heterogeneous supercomputers
inferred← citeshttps://doi.org/10.1155/bri/7191508openalex-snapshot
In Silico Bioprospection of Daniellia oliveri– Based Products as Quorum Sensing Modulators of Escherichia coli SdiA
inferred← citeshttps://doi.org/10.48550/arxiv.2105.03617openalex-snapshot
MEGADOCK-GUI: a GUI-based complete cross-docking tool for exploring protein-protein interactions
inferred← citeshttps://doi.org/10.70675/4a8eec9czf145z472fza6c0z16e66489d796openalex-snapshot
Développement d’une méthode in silico pour caractériser le potentiel d’interaction des surfaces protéiques dans un environnement encombré
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.