On the public citation graph

Rigid-Docking Approaches to Explore Protein–Protein Interaction Space

https://doi.org/10.1007/10_2016_41

0 signed · 173 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 See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.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(20000501)39:2<178::aid-prot8>3.0.co;2-6openalex-snapshot

Protein docking using spherical polar Fourier correlations

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/jcc.23304openalex-snapshot

DOT2: Macromolecular docking with improved biophysical models

inferredcites →https://doi.org/10.1002/protopenalex-snapshot

A study on amino acid pairing at the N- and C-termini of helical segments in proteins

inferredcites →https://doi.org/10.1002/prot.10389openalex-snapshot

ZDOCK: An initial‐stage protein‐docking algorithm

inferredcites →https://doi.org/10.1002/prot.10391openalex-snapshot

Weighted geometric docking: Incorporating external information in the rotation‐translation scan

inferredcites →https://doi.org/10.1002/prot.10460openalex-snapshot

RDOCK: Refinement of rigid‐body protein docking predictions

inferredcites →https://doi.org/10.1002/prot.20573openalex-snapshot

Development and testing of an automated approach to protein docking

inferredcites →https://doi.org/10.1002/prot.21117openalex-snapshot

PIPER: An FFT‐based protein docking program with pairwise potentials

inferredcites →https://doi.org/10.1002/prot.21373openalex-snapshot

ZRANK: Reranking protein docking predictions with an optimized energy function

inferredcites →https://doi.org/10.1002/prot.21419openalex-snapshot

pyDock: Electrostatics and desolvation for effective scoring of rigid‐body protein–protein docking

inferredcites →https://doi.org/10.1002/prot.21495openalex-snapshot

FireDock: Fast interaction refinement in molecular docking

inferredcites →https://doi.org/10.1002/prot.21502openalex-snapshot

Integrating statistical pair potentials into protein complex prediction

inferredcites →https://doi.org/10.1002/prot.21600openalex-snapshot

Context shapes: Efficient complementary shape matching for protein–protein docking

inferredcites →https://doi.org/10.1002/prot.21920openalex-snapshot

A combination of rescoring and refinement significantly improves protein docking performance

inferredcites →https://doi.org/10.1002/prot.22550openalex-snapshot

PIE—Efficient filters and coarse grained potentials for unbound protein–protein docking

inferredcites →https://doi.org/10.1002/prot.22668openalex-snapshot

FiberDock: Flexible induced‐fit backbone refinement in molecular docking

inferredcites →https://doi.org/10.1002/prot.23192openalex-snapshot

Surface‐histogram: A new shape descriptor for protein‐protein docking

inferredcites →https://doi.org/10.1002/prot.24079openalex-snapshot

Multi‐LZerD: Multiple protein docking for asymmetric complexes

inferredcites →https://doi.org/10.1002/prot.24110openalex-snapshot

Scoring protein interaction decoys using exposed residues (SPIDER): A novel multibody interaction scoring function based on frequent geometric patterns of interfacial residues

inferredcites →https://doi.org/10.1002/prot.24115openalex-snapshot

Flexible protein docking refinement using pose‐dependent normal mode analysis

inferredcites →https://doi.org/10.1002/prot.24214openalex-snapshot

Improving ranking of models for protein complexes with side chain modeling and atomic potentials

inferredcites →https://doi.org/10.1002/prot.24252openalex-snapshot

CyClus: A fast, comprehensive cylindrical interface approximation clustering/reranking method for rigid‐body protein–protein docking decoys

inferredcites →https://doi.org/10.1002/prot.24314openalex-snapshot

Ranking multiple docking solutions based on the conservation of inter‐residue contacts

inferredcites →https://doi.org/10.1002/prot.24343openalex-snapshot

Sampling and scoring: A marriage made in heaven

inferredcites →https://doi.org/10.1002/prot.24354openalex-snapshot

Binding interface prediction by combining protein-protein docking results

inferredcites →https://doi.org/10.1002/prot.24369openalex-snapshot

A Markov‐chain model description of binding funnels to enhance the ranking of docked solutions

inferredcites →https://doi.org/10.1002/prot.24370openalex-snapshot

DockRank: Ranking docked conformations using partner‐specific sequence homology‐based protein interface prediction

inferredcites →https://doi.org/10.1002/prot.24403openalex-snapshot

How good is automated protein docking?

inferredcites →https://doi.org/10.1002/prot.24611openalex-snapshot

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

inferredcites →https://doi.org/10.1002/prot.24764openalex-snapshot

Native fold and docking pose discrimination by the same residue‐based scoring function

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/10.1007/978-3-642-34123-6_16openalex-snapshot

Improvement of the Protein–Protein Docking Prediction by Introducing a Simple Hydrophobic Interaction Model: An Application to Interaction Pathway Analysis

inferredcites →https://doi.org/10.1007/bf00994018openalex-snapshot

Support-Vector Networks

inferredcites →https://doi.org/10.1007/s00726-009-0295-yopenalex-snapshot

Predicting protein–protein interactions from sequence using correlation coefficient and high-quality interaction dataset

inferredcites →https://doi.org/10.1016/j.bpj.2015.06.048openalex-snapshot

A Structural View of Negative Regulation of the Toll-like Receptor-Mediated Inflammatory Pathway

inferredcites →https://doi.org/10.1016/j.cbpa.2007.08.033openalex-snapshot

Virtual screening strategies in drug discovery

inferredcites →https://doi.org/10.1016/j.crvi.2004.03.006openalex-snapshot

On proteins, grids, correlations, and docking

inferredcites →https://doi.org/10.1016/j.drudis.2014.02.005openalex-snapshot

Search strategies and evaluation in protein–protein docking: principles, advances and challenges

inferredcites →https://doi.org/10.1016/j.jmb.2007.05.022openalex-snapshot

Inference of Macromolecular Assemblies from Crystalline State

inferredcites →https://doi.org/10.1016/j.jmb.2008.05.042openalex-snapshot

Conformer Selection and Induced Fit in Flexible Backbone Protein–Protein Docking Using Computational and NMR Ensembles

inferredcites →https://doi.org/10.1016/j.jmb.2008.08.002openalex-snapshot

Identification of Protein Interaction Partners and Protein–Protein Interaction Sites

inferredcites →https://doi.org/10.1016/j.jmb.2015.07.016openalex-snapshot

Updates to the Integrated Protein–Protein Interaction Benchmarks: Docking Benchmark Version 5 and Affinity Benchmark Version 2

inferredcites →https://doi.org/10.1016/j.jsb.2012.02.002openalex-snapshot

Enriching the human apoptosis pathway by predicting the structures of protein–protein complexes

inferredcites →https://doi.org/10.1016/j.sbi.2011.03.013openalex-snapshot

Challenges for the prediction of macromolecular interactions

inferredcites →https://doi.org/10.1016/j.sbi.2012.04.004openalex-snapshot

Constructing structural networks of signaling pathways on the proteome scale

inferredcites →https://doi.org/10.1016/j.sbi.2012.12.003openalex-snapshot

Low-resolution structural modeling of protein interactome

inferredcites →https://doi.org/10.1016/j.sbi.2013.06.017openalex-snapshot

Scoring functions for protein–protein interactions

inferredcites →https://doi.org/10.1016/j.sbi.2013.11.005openalex-snapshot

Template-based structure modeling of protein–protein interactions

inferredcites →https://doi.org/10.1016/j.semcancer.2013.05.003openalex-snapshot

The structural network of inflammation and cancer: Merits and challenges

inferredcites →https://doi.org/10.1016/j.str.2014.07.009openalex-snapshot

Assessing the Applicability of Template-Based Protein Docking in the Twilight Zone

inferredcites →https://doi.org/10.1016/s0022-2836(03)00670-3openalex-snapshot

Protein–Protein Docking with Simultaneous Optimization of Rigid-body Displacement and Side-chain Conformations

inferredcites →https://doi.org/10.1021/ci100353eopenalex-snapshot

Scoring by Intermolecular Pairwise Propensities of Exposed Residues (SIPPER): A New Efficient Potential for Protein−Protein Docking

inferredcites →https://doi.org/10.1021/ci200528dopenalex-snapshot

Recognizing Pitfalls in Virtual Screening: A Critical Review

inferredcites →https://doi.org/10.1021/ci600342eopenalex-snapshot

Optimizing Fragment and Scaffold Docking by Use of Molecular Interaction Fingerprints

inferredcites →https://doi.org/10.1021/ci800310fopenalex-snapshot

Improving the Accuracy of an Affinity Prediction Method by Using Statistics on Shape Complementarity between Proteins

inferredcites →https://doi.org/10.1021/ja026939xopenalex-snapshot

HADDOCK: A Protein−Protein Docking Approach Based on Biochemical or Biophysical Information

inferredcites →https://doi.org/10.1021/jm030331xopenalex-snapshot

Structural Interaction Fingerprint (SIFt): A Novel Method for Analyzing Three-Dimensional Protein−Ligand Binding Interactions

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/10.1038/35075138openalex-snapshot

Lethality and centrality in protein networks

inferredcites →https://doi.org/10.1038/47056openalex-snapshot

Protein interaction maps for complete genomes based on gene fusion events

inferredcites →https://doi.org/10.1038/82360openalex-snapshot

A network of protein–protein interactions in yeast

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/nature11503openalex-snapshot

Structure-based prediction of protein–protein interactions on a genome-wide scale

inferredcites →https://doi.org/10.1038/nbt0108-69openalex-snapshot

Protein-protein interaction networks and biology—what's the connection?

inferredcites →https://doi.org/10.1038/nmeth.2259openalex-snapshot

Flaws in evaluation schemes for pair-input computational predictions

inferredcites →https://doi.org/10.1038/nmeth.2289openalex-snapshot

Interactome3D: adding structural details to protein networks

inferredcites →https://doi.org/10.1038/nprot.2010.32openalex-snapshot

The HADDOCK web server for data-driven biomolecular docking

inferredcites →https://doi.org/10.1038/nprot.2011.367openalex-snapshot

Predicting protein-protein interactions on a proteome scale by matching evolutionary and structural similarities at interfaces using PRISM

inferredcites →https://doi.org/10.1038/nrd1549openalex-snapshot

Docking and scoring in virtual screening for drug discovery: methods and applications

inferredcites →https://doi.org/10.1038/srep13128openalex-snapshot

The Architecture of the TIR Domain Signalosome in the Toll-like Receptor-4 Signaling Pathway

inferredcites →https://doi.org/10.1039/c005060copenalex-snapshot

Protein–protein docking tested in blind predictions: the CAPRI experiment

inferredcites →https://doi.org/10.1039/c4ib00136bopenalex-snapshot

An improved interolog mapping-based computational prediction of protein–protein interactions with increased network coverage

inferredcites →https://doi.org/10.1039/c4mb00219aopenalex-snapshot

Viral proteins that bridge unconnected proteins and components in the human PPI network

inferredcites →https://doi.org/10.1073/pnas.0607879104openalex-snapshot

Predicting protein–protein interactions based only on sequences information

inferredcites →https://doi.org/10.1073/pnas.1101440108openalex-snapshot

Structural principles within the human-virus protein-protein interaction network

inferredcites →https://doi.org/10.1073/pnas.1200678109openalex-snapshot

Templates are available to model nearly all complexes of structurally characterized proteins

inferredcites →https://doi.org/10.1073/pnas.141236298openalex-snapshot

Genes linked by fusion events are generally of the same functional category: A systematic analysis of 30 microbial genomes

inferredcites →https://doi.org/10.1073/pnas.89.6.2195openalex-snapshot

Molecular surface recognition: determination of geometric fit between proteins and their ligands by correlation techniques.

inferredcites →https://doi.org/10.1093/bib/bbt047openalex-snapshot

Evaluating template-based and template-free protein-protein complex structure prediction

inferredcites →https://doi.org/10.1093/bioinformatics/19.1.161openalex-snapshot

InterPreTS: protein Interaction Prediction through Tertiary Structure

inferredcites →https://doi.org/10.1093/bioinformatics/btg371openalex-snapshot

ClusPro: an automated docking and discrimination method for the prediction of protein complexes

inferredcites →https://doi.org/10.1093/bioinformatics/bth483openalex-snapshot

Predicting protein–protein interactions using signature products

inferredcites →https://doi.org/10.1093/bioinformatics/bti1016openalex-snapshot

Kernel methods for predicting protein-protein interactions

inferredcites →https://doi.org/10.1093/bioinformatics/btl661openalex-snapshot

Structure-based evaluation ofin silicopredictions of protein–protein interactions using Comparative Docking

inferredcites →https://doi.org/10.1093/bioinformatics/btp447openalex-snapshot

FRODOCK: a new approach for fast rotational protein–protein docking

inferredcites →https://doi.org/10.1093/bioinformatics/btq444openalex-snapshot

Ultra-fast FFT protein docking on graphics processors

inferredcites →https://doi.org/10.1093/bioinformatics/btq483openalex-snapshot

Simple sequence-based kernels do not predict protein–protein interactions

inferredcites →https://doi.org/10.1093/bioinformatics/btr514openalex-snapshot

Revisiting the negative example sampling problem for predicting protein–protein interactions

inferredcites →https://doi.org/10.1093/bioinformatics/btt038openalex-snapshot

SwarmDock: a server for flexible protein–protein docking

inferredcites →https://doi.org/10.1093/bioinformatics/btt262openalex-snapshot

pyDockWEB: a web server for rigid-body protein–protein docking using electrostatics and desolvation scoring

inferredcites →https://doi.org/10.1093/bioinformatics/btu097openalex-snapshot

ZDOCK server: interactive docking prediction of protein–protein complexes and symmetric multimers

inferredcites →https://doi.org/10.1093/bioinformatics/btu532openalex-snapshot

MEGADOCK 4.0: an ultra–high-performance protein–protein docking software for heterogeneous supercomputers

inferredcites →https://doi.org/10.1093/bioinformatics/btu580openalex-snapshot

Protein–protein binding affinity prediction from amino acid sequence

inferredcites →https://doi.org/10.1093/bioinformatics/btu594openalex-snapshot

CCharPPI web server: computational characterization of protein–protein interactions from structure

inferredcites →https://doi.org/10.1093/bioinformatics/btu837openalex-snapshot

CONSRANK: a server for the analysis, comparison and ranking of docking models based on inter-residue contacts

inferredcites →https://doi.org/10.1093/nar/28.1.235openalex-snapshot

The Protein Data Bank

inferredcites →https://doi.org/10.1093/nar/gkh086openalex-snapshot

The Database of Interacting Proteins: 2004 update

inferredcites →https://doi.org/10.1093/nar/gki481openalex-snapshot

PatchDock and SymmDock: servers for rigid and symmetric docking

inferredcites →https://doi.org/10.1093/nar/gki585openalex-snapshot

PRISM: protein interactions by structural matching

inferredcites →https://doi.org/10.1093/nar/gkl206openalex-snapshot

GRAMM-X public web server for protein-protein docking

inferredcites →https://doi.org/10.1093/nar/gkn159openalex-snapshot

Using support vector machine combined with auto covariance to predict protein–protein interactions from protein sequences

inferredcites →https://doi.org/10.1093/nar/gkn216openalex-snapshot

The RosettaDock server for local protein-protein docking

inferredcites →https://doi.org/10.1093/nar/gkn218openalex-snapshot

HOMCOS: a server to predict interacting protein pairs and interacting sites by homology modeling of complex structures

inferredcites →https://doi.org/10.1093/nar/gkn892openalex-snapshot

Human Protein Reference Database--2009 update

inferredcites →https://doi.org/10.1093/nar/gkp1026openalex-snapshot

The Negatome database: a reference set of non-interacting protein pairs

inferredcites →https://doi.org/10.1093/nar/gkq311openalex-snapshot

HexServer: an FFT-based protein docking server powered by graphics processors

inferredcites →https://doi.org/10.1093/nar/gkr930openalex-snapshot

MINT, the molecular interaction database: 2012 update

inferredcites →https://doi.org/10.1093/nar/gks1231openalex-snapshot

PrePPI: a structure-informed database of protein–protein interactions

inferredcites →https://doi.org/10.1093/nar/gkt1079openalex-snapshot

Negatome 2.0: a database of non-interacting proteins derived by literature mining, manual annotation and protein structure analysis

inferredcites →https://doi.org/10.1093/nar/gkt1115openalex-snapshot

The MIntAct project—IntAct as a common curation platform for 11 molecular interaction databases

inferredcites →https://doi.org/10.1093/nar/gku1204openalex-snapshot

The BioGRID interaction database: 2015 update

inferredcites →https://doi.org/10.1093/nar/gku397openalex-snapshot

PRISM: a web server and repository for prediction of protein–protein interactions and modeling their 3D complexes

inferredcites →https://doi.org/10.1093/nar/gku989openalex-snapshot

UniProt: a hub for protein information

inferredcites →https://doi.org/10.1093/protein/14.2.105openalex-snapshot

Protein docking using continuum electrostatics and geometric fit

inferredcites →https://doi.org/10.1109/tcbb.2009.57openalex-snapshot

$F^2$Dock: Fast Fourier Protein-Protein Docking

inferredcites →https://doi.org/10.1109/tcbb.2012.149openalex-snapshot

SP-Dock: Protein-Protein Docking Using Shape and Physicochemical Complementarity

inferredcites →https://doi.org/10.1126/science.285.5428.751openalex-snapshot

Detecting Protein Function and Protein-Protein Interactions from Genome Sequences

inferredcites →https://doi.org/10.1142/s0219720008003904openalex-snapshot

DEVELOPMENT OF AN AFFINITY EVALUATION AND PREDICTION SYSTEM BY USING THE SHAPE COMPLEMENTARITY CHARACTERISTIC BETWEEN PROTEINS

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/10.1145/2506583.2506693openalex-snapshot

MEGADOCK-GPU

inferredcites →https://doi.org/10.1155/2014/147648openalex-snapshot

Protein-Protein Interaction Detection: Methods and Analysis

inferredcites →https://doi.org/10.1186/1471-2105-10-407openalex-snapshot

Protein-protein docking using region-based 3D Zernike descriptors

inferredcites →https://doi.org/10.1186/1471-2105-10-419openalex-snapshot

Critical assessment of sequence-based protein-protein interaction prediction methods that do not require homologous protein sequences

inferredcites →https://doi.org/10.1186/1471-2105-11-144openalex-snapshot

Large-scale prediction of protein-protein interactions from structures

inferredcites →https://doi.org/10.1186/1471-2105-11-236openalex-snapshot

Analysis of protein-protein docking decoys using interaction fingerprints: application to the reconstruction of CaM-ligand complexes

inferredcites →https://doi.org/10.1186/1471-2105-12-289openalex-snapshot

Bio::Homology::InterologWalk - A Perl module to build putative protein-protein interaction networks through interolog mapping

inferredcites →https://doi.org/10.1186/1471-2105-12-36openalex-snapshot

ASPDock: protein-protein docking algorithm using atomic solvation parameters model

inferredcites →https://doi.org/10.1186/1471-2105-14-286openalex-snapshot

The scoring of poses in protein-protein docking: current capabilities and future directions

inferredcites →https://doi.org/10.1186/1471-2105-15-213openalex-snapshot

Homology-based prediction of interactions between proteins using Averaged One-Dependence Estimators

inferredcites →https://doi.org/10.1186/1471-2105-8-s10-s8openalex-snapshot

A new pairwise kernel for biological network inference with support vector machines

inferredcites →https://doi.org/10.1186/1471-2164-15-s4-s2openalex-snapshot

The structural network of Interleukin-10 and its implications in inflammation and cancer

inferredcites →https://doi.org/10.1186/1751-0473-8-18openalex-snapshot

MEGADOCK 3.0: a high-performance protein-protein interaction prediction software using hybrid parallel computing for petascale supercomputing environments

inferredcites →https://doi.org/10.1186/1752-0509-9-s1-s6openalex-snapshot

Protein-protein docking on hardware accelerators: comparison of GPU and MIC architectures

inferredcites →https://doi.org/10.1186/1753-6561-7-s7-s6openalex-snapshot

Highly precise protein-protein interaction prediction based on consensus between template-based and de novo docking methods

inferredcites →https://doi.org/10.1186/1756-0500-3-145openalex-snapshot

PRED_PPI: a server for predicting protein-protein interactions based on sequence data with probability assignment

inferredcites →https://doi.org/10.1186/2046-1682-5-7openalex-snapshot

Arbitrary protein−protein docking targets biologically relevant interfaces

inferredcites →https://doi.org/10.1186/gb-2006-7-11-120openalex-snapshot

How complete are current yeast and human protein-interaction networks?

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/10.1371/journal.pcbi.1003369openalex-snapshot

Protein-Protein Interactions in a Crowded Environment: An Analysis via Cross-Docking Simulations and Evolutionary Information

inferredcites →https://doi.org/10.1371/journal.pcbi.1003470openalex-snapshot

The Structural Pathway of Interleukin 1 (IL-1) Initiated Signaling Reveals Mechanisms of Oncogenic Mutations and SNPs in Inflammation and Cancer

inferredcites →https://doi.org/10.1371/journal.pone.0017695openalex-snapshot

CPORT: A Consensus Interface Predictor and Its Performance in Prediction-Driven Docking with HADDOCK

inferredcites →https://doi.org/10.1371/journal.pone.0024657openalex-snapshot

Accelerating Protein Docking in ZDOCK Using an Advanced 3D Convolution Library

inferredcites →https://doi.org/10.1371/journal.pone.0030938openalex-snapshot

SPPS: A Sequence-Based Method for Predicting Probability of Protein-Protein Interaction Partners

inferredcites →https://doi.org/10.1371/journal.pone.0051304openalex-snapshot

Computational Prediction of Protein-Protein Interactions in Leishmania Predicted Proteomes

inferredcites →https://doi.org/10.1371/journal.pone.0051307openalex-snapshot

Protein-Protein Docking with F2Dock 2.0 and GB-Rerank

inferredcites →https://doi.org/10.1371/journal.pone.0063906openalex-snapshot

Serverification of Molecular Modeling Applications: The Rosetta Online Server That Includes Everyone (ROSIE)

inferredcites →https://doi.org/10.1371/journal.pone.0069365openalex-snapshot

Re-Docking Scheme for Generating Near-Native Protein Complexes by Assembling Residue Interaction Fingerprints

inferredcites →https://doi.org/10.1529/biophysj.108.135814openalex-snapshot

DARS (Decoys As the Reference State) Potentials for Protein-Protein Docking

inferredcites →https://doi.org/10.2147/aabc.s3646openalex-snapshot

The development of an affinity evaluation and prediction system by using protein–protein docking simulations and parameter tuning

inferredcites →https://doi.org/10.2174/092986612800191080openalex-snapshot

Predicting Protein-Protein Interactions by Combing Various Sequence- Derived Features into the General Form of Chou’s Pseudo Amino Acid Composition

inferredcites →https://doi.org/10.2174/09298665113209990050openalex-snapshot

MEGADOCK: An All-to-All Protein-Protein Interaction Prediction System Using Tertiary Structure Data

inferredcites →https://doi.org/10.2174/09298665113209990066openalex-snapshot

Protein-protein Interaction Network Prediction by Using Rigid-Body Docking Tools: Application to Bacterial Chemotaxis

inferredcites →https://doi.org/10.2174/138920308783565741openalex-snapshot

Recent Progress and Future Directions in Protein-Protein Docking

inferredcites →https://doi.org/10.2197/ipsjtbio.3.10openalex-snapshot

Improved Prediction Method for Protein Interactions Using Both Structural and Functional Characteristics of Proteins

inferredcites →https://doi.org/10.3390/ijms11103623openalex-snapshot

SwarmDock and the Use of Normal Modes in Protein-Protein Docking

inferredcites →https://doi.org/10.3390/ijms15023220openalex-snapshot

Prediction of Protein–Protein Interaction with Pairwise Kernel Support Vector Machine

What points at this work

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

inferred← citeshttps://doi.org/10.1007/978-1-0716-3985-6_1openalex-snapshot

Docking Foundations: From Rigid to Flexible Docking

inferred← citeshttps://doi.org/10.1007/978-3-030-58356-9_2openalex-snapshot

Society of “Citizen Science through Dancing”

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/b978-0-12-816386-3.00071-5openalex-snapshot

Molecular Imaging of Protein–Protein Interactions and Protein Folding

inferred← citeshttps://doi.org/10.1016/j.compbiolchem.2018.06.005openalex-snapshot

Docking techniques in pharmacology: How much promising?

inferred← citeshttps://doi.org/10.1016/j.csbj.2025.05.009openalex-snapshot

Multimeric protein interaction and complex prediction: Structure, dynamics and function

inferred← citeshttps://doi.org/10.1016/j.lwt.2025.117753openalex-snapshot

Identification of a novel umami peptides from fermented Bighead carp and its umami mechanism via molecular dynamic simulation

inferred← citeshttps://doi.org/10.1016/j.molstruc.2025.142044openalex-snapshot

Molecular docking technology drives multidimensional applications of microbial natural products

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/10.1021/acs.jafc.2c08646openalex-snapshot

Modification of a Novel Umami Octapeptide with Trypsin Hydrolysis Sites via Homology Modeling and Molecular Docking

inferred← citeshttps://doi.org/10.1186/s12859-018-2073-xopenalex-snapshot

MEGADOCK-Web: an integrated database of high-throughput structure-based protein-protein interaction predictions

inferred← citeshttps://doi.org/10.2174/1570159x20666220830105350openalex-snapshot

Virtual Screening-Based Drug Development for the Treatment of Nervous System Diseases

inferred← citeshttps://doi.org/10.2174/9789815223019124010014openalex-snapshot

Warp and Woof of Drug Designing and Development: An In-Silico Approach

inferred← citeshttps://doi.org/10.3390/ijms242015239openalex-snapshot

The Molecular Docking of MAX Fungal Effectors with Plant HMA Domain-Binding Proteins

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/e211ffb4z6d6fz476ez9441z34c4cdf8d79aopenalex-snapshot

Fragment-based modelling of protein-RNA complexes for protein design

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.