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The targets of CAPRI rounds 20–27

https://doi.org/10.1002/prot.24375
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What this work says

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

inferredcites →https://doi.org/10.1002/pro.580openalex-snapshot
A structure‐based benchmark for protein–protein binding affinity
inferredcites →https://doi.org/10.1002/prot.22106openalex-snapshot
Protein–protein docking benchmark version 3.0
inferredcites →https://doi.org/10.1002/prot.22726openalex-snapshot
Self-association of TPR domains: Lessons learned from a designed, consensus-based TPR oligomer
inferredcites →https://doi.org/10.1002/prot.22774openalex-snapshot
The targets of CAPRI Rounds 13–19
inferredcites →https://doi.org/10.1002/prot.23200openalex-snapshot
Critical assessment of methods of protein structure prediction (CASP)—round IX
inferredcites →https://doi.org/10.1002/prot.24356openalex-snapshot
Community-wide evaluation of methods for predicting the effect of mutations on protein-protein interactions
inferredcites →https://doi.org/10.1007/s00018-012-1184-1openalex-snapshot
Structural basis of bacterial defense against g-type lysozyme-based innate immunity
inferredcites →https://doi.org/10.1016/j.jmb.2010.09.048openalex-snapshot
Design, Production and Molecular Structure of a New Family of Artificial Alpha-helicoidal Repeat Proteins (αRep) Based on Thermostable HEAT-like Repeats
inferredcites →https://doi.org/10.1016/j.jmb.2011.09.031openalex-snapshot
Community-Wide Assessment of Protein-Interface Modeling Suggests Improvements to Design Methodology
inferredcites →https://doi.org/10.1016/j.jmb.2012.01.019openalex-snapshot
Structure of the Ultra-High-Affinity Colicin E2 DNase–Im2 Complex
inferredcites →https://doi.org/10.1016/j.molcel.2011.03.010openalex-snapshot
A De Novo Protein Binding Pair By Computational Design and Directed Evolution
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/nbt.2214openalex-snapshot
Optimization of affinity, specificity and function of designed influenza inhibitors using deep sequencing
inferredcites →https://doi.org/10.1073/pnas.0807948105openalex-snapshot
Structural consequences of effector protein complex formation in a diiron hydroxylase
inferredcites →https://doi.org/10.1093/nar/gkr176openalex-snapshot
Mechanism of activation of methyltransferases involved in translation by the Trm112 ‘hub’ protein
inferredcites →https://doi.org/10.1107/s0907444904011679openalex-snapshot
PRODRG: a tool for high-throughput crystallography of protein–ligand complexes
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/10.1371/journal.pone.0071512openalex-snapshot
Selection of Specific Protein Binders for Pre-Defined Targets from an Optimized Library of Artificial Helicoidal Repeat Proteins (alphaRep)
inferredcites →https://doi.org/10.2210/pdb4ak1/pdbopenalex-snapshot
Structure of BT4661, a SusE-like surface located polysaccharide binding protein from the Bacteroides thetaiotaomicron heparin utilisation locus

What points at this work

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

inferred← citeshttps://doi.org/10.1002/jcc.24679openalex-snapshot
Residue‐centric modeling and design of saccharide and glycoconjugate structures
inferred← citeshttps://doi.org/10.1002/jmr.2471openalex-snapshot
Improvements, trends, and new ideas in molecular docking: 2012–2013 in review
inferred← citeshttps://doi.org/10.1002/prot.25212openalex-snapshot
Predicting protein conformational changes for unbound and homology docking: learning from intrinsic and induced flexibility
inferred← citeshttps://doi.org/10.1007/978-1-0716-3985-6_12openalex-snapshot
Challenges of Protein-Protein Docking of the Membrane Proteins
inferred← citeshttps://doi.org/10.1007/978-1-4939-0366-5_12openalex-snapshot
Modeling Protein–Protein Complexes Using the HADDOCK Webserver “Modeling Protein Complexes with HADDOCK”
inferred← citeshttps://doi.org/10.1007/978-1-4939-1465-4_18openalex-snapshot
Information-Driven Structural Modelling of Protein–Protein Interactions
inferred← citeshttps://doi.org/10.1007/978-1-4939-2425-7_1openalex-snapshot
Structural Basis of Protein-Protein Interactions
inferred← citeshttps://doi.org/10.1016/j.abb.2014.05.010openalex-snapshot
Evolution of protein interactions: From interactomes to interfaces
inferred← citeshttps://doi.org/10.1016/j.pbiomolbio.2014.05.004openalex-snapshot
Prediction and redesign of protein–protein interactions
inferred← citeshttps://doi.org/10.1021/acs.jcim.5c01029openalex-snapshot
Exploring Protein–Protein Docking Tools: Comprehensive Insights into Traditional and Deep-Learning Approaches
inferred← citeshttps://doi.org/10.1093/nar/gky427openalex-snapshot
SWISS-MODEL: homology modelling of protein structures and complexes
inferred← citeshttps://doi.org/10.1186/s12859-024-05991-4openalex-snapshot
A comprehensive survey of scoring functions for protein docking models
inferred← citeshttps://doi.org/10.1371/journal.pcbi.1004018openalex-snapshot
Protein-Protein Docking with Dynamic Residue Protonation States
inferred← citeshttps://doi.org/10.1371/journal.pone.0154923openalex-snapshot
Addressing the Role of Conformational Diversity in Protein Structure Prediction
inferred← citeshttps://doi.org/10.1385/1-59259-762-9:003openalex-snapshot
Structural Basis of Protein–Protein Interactions
inferred← citeshttps://doi.org/10.3389/fmolb.2021.647915openalex-snapshot
Protein Docking Model Evaluation by Graph Neural Networks
inferred← citeshttps://doi.org/10.4018/978-1-5225-0115-2.ch007openalex-snapshot
Protein-Protein Docking
inferred← citeshttps://doi.org/10.4018/978-1-5225-1762-7.ch042openalex-snapshot
Protein-Protein Docking
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