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The targets of CAPRI Rounds 13–19
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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.116openalex-snapshot
Thermodynamic characterization of two homologous protein complexes: Associations of the semaphorin receptor plexin‐B1 RhoGTPase binding domain with Rnd1 and active Rac1
inferredcites →https://doi.org/10.1002/prot.10381openalex-snapshot
CAPRI: A Critical Assessment of PRedicted Interactions
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.22818openalex-snapshot
Docking and scoring protein interactions: CAPRI 2009
inferredcites →https://doi.org/10.1016/j.jmb.2003.12.073openalex-snapshot
A Dissection of Specific and Non-specific Protein–Protein Interfaces
inferredcites →https://doi.org/10.1016/j.jmb.2007.03.077openalex-snapshot
Structural Basis for the Bifunctionality of the U5 snRNP 52K Protein (CD2BP2)
inferredcites →https://doi.org/10.1016/j.jmb.2008.03.055openalex-snapshot
Experimental and Computational Analyses of the Energetic Basis for Dual Recognition of Immunity Proteins by Colicin Endonucleases
inferredcites →https://doi.org/10.1016/j.jmb.2008.05.034openalex-snapshot
Structural and Mutational Analyses of the Interaction between the Barley α-Amylase/Subtilisin Inhibitor and the Subtilisin Savinase Reveal a Novel Mode of Inhibition
inferredcites →https://doi.org/10.1016/j.molcel.2005.10.025openalex-snapshot
Molecular Basis for Bacterial Class I Release Factor Methylation by PrmC
inferredcites →https://doi.org/10.1016/j.str.2004.10.018openalex-snapshot
When Monomers Are Preferred: A Strategy for the Identification and Disruption of Weakly Oligomerized Proteins
inferredcites →https://doi.org/10.1016/j.str.2007.10.025openalex-snapshot
Structure of the Yeast tRNA m7G Methylation Complex
inferredcites →https://doi.org/10.1016/s0969-2126(03)00076-5openalex-snapshot
Design of Stable α-Helical Arrays from an Idealized TPR Motif
inferredcites →https://doi.org/10.1017/s0033583508004708openalex-snapshot
Protein–protein interaction and quaternary structure
inferredcites →https://doi.org/10.1021/ja070153nopenalex-snapshot
Molecular Mimicry Enables Competitive Recruitment by a Natively Disordered Protein
inferredcites →https://doi.org/10.1038/emboj.2009.209openalex-snapshot
The structural basis of Arf effector specificity: the crystal structure of ARF6 in a complex with JIP4
inferredcites →https://doi.org/10.1038/nature04510openalex-snapshot
How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP
inferredcites →https://doi.org/10.1038/sj.emboj.7601634openalex-snapshot
Structural basis for ARF1‐mediated recruitment of ARHGAP21 to Golgi membranes
inferredcites →https://doi.org/10.1073/pnas.0503525102openalex-snapshot
Structural basis of the Sir1–origin recognition complex interaction in transcriptional silencing
inferredcites →https://doi.org/10.1073/pnas.0611173104openalex-snapshot
Evidence for a dual binding mode of dockerin modules to cohesins
inferredcites →https://doi.org/10.1073/pnas.0910756107openalex-snapshot
The structural and energetic basis for high selectivity in a high-affinity protein-protein interaction
inferredcites →https://doi.org/10.1074/jbc.m109.022095openalex-snapshot
The Ternary Structure of the Double-headed Arrowhead Protease Inhibitor API-A Complexed with Two Trypsins Reveals a Novel Reactive Site Conformation
inferredcites →https://doi.org/10.1074/jbc.m109.056275openalex-snapshot
Structure and Function of the Intracellular Region of the Plexin-B1 Transmembrane Receptor
inferredcites →https://doi.org/10.1107/s090744490603575xopenalex-snapshot
Macromolecular recognition in the Protein Data Bank
inferredcites →https://doi.org/10.1242/jcs.02369openalex-snapshot
Centaurin-α1 interacts directly with kinesin motor protein KIF13B
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1002/prot.23082openalex-snapshot
SymmRef: A flexible refinement method for symmetric multimers
inferred← citeshttps://doi.org/10.1002/prot.24075openalex-snapshot
A protein‐RNA docking benchmark (II): Extended set from experimental and homology modeling data
inferred← citeshttps://doi.org/10.1002/prot.24083openalex-snapshot
A protein–RNA docking benchmark (I): Nonredundant cases
inferred← citeshttps://doi.org/10.1002/prot.24115openalex-snapshot
Flexible protein docking refinement using pose‐dependent normal mode analysis
inferred← citeshttps://doi.org/10.1002/prot.24314openalex-snapshot
Ranking multiple docking solutions based on the conservation of inter‐residue contacts
inferred← citeshttps://doi.org/10.1002/prot.24423openalex-snapshot
Using a consensus approach based on the conservation of inter‐residue contacts to rank CAPRI models
inferred← citeshttps://doi.org/10.1002/prot.24428openalex-snapshot
Docking, scoring, and affinity prediction in CAPRI
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/10.1002/wcms.45openalex-snapshot
Prediction of protein binding sites and hot spots
inferred← citeshttps://doi.org/10.1007/978-1-4939-2425-7_1openalex-snapshot
Structural Basis of Protein-Protein Interactions
inferred← citeshttps://doi.org/10.1007/978-1-4939-3572-7_5openalex-snapshot
Classification and Exploration of 3D Protein Domain Interactions Using Kbdock
inferred← citeshttps://doi.org/10.1007/978-94-007-5285-6_6openalex-snapshot
Prediction of Protein-Protein Binding Interfaces
inferred← citeshttps://doi.org/10.1007/s00894-011-1157-6openalex-snapshot
Application of information theory to feature selection in protein docking
inferred← citeshttps://doi.org/10.1016/j.sbi.2017.10.006openalex-snapshot
The computational prediction of protein assemblies
inferred← citeshttps://doi.org/10.1016/j.str.2011.04.006openalex-snapshot
Protein-Protein Complex Structure Predictions by Multimeric Threading and Template Recombination
inferred← citeshttps://doi.org/10.1016/j.str.2018.10.001openalex-snapshot
Sampling Native-like Structures of RNA-Protein Complexes through Rosetta Folding and Docking
inferred← citeshttps://doi.org/10.1016/j.ymeth.2016.11.001openalex-snapshot
Structural and energy determinants in protein-RNA docking
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/10.1039/c005060copenalex-snapshot
Protein–protein docking tested in blind predictions: the CAPRI experiment
inferred← citeshttps://doi.org/10.1074/jbc.m110.197053openalex-snapshot
Structural Basis of Rnd1 Binding to Plexin Rho GTPase Binding Domains (RBDs)
inferred← citeshttps://doi.org/10.1093/nar/gks535openalex-snapshot
PRince: a web server for structural and physicochemical analysis of Protein-RNA interface
inferred← citeshttps://doi.org/10.1186/1471-2105-13-228openalex-snapshot
Protein-DNA docking with a coarse-grained force field
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.pone.0074443openalex-snapshot
Optimizing Scoring Function of Protein-Nucleic Acid Interactions with Both Affinity and Specificity
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
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