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Data‐driven docking: HADDOCK's adventures in CAPRI

https://doi.org/10.1002/prot.20563

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What this work says

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

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The impact of protein flexibility on protein–protein docking

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A calculation strategy for the structure determination of symmetric demers by 1H NMR

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A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform 1 1Edited by M. Yaniv

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The OPLS [optimized potentials for liquid simulations] potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin

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NMR structure of the bovine prion protein

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Cohesin-Dockerin Interaction in Cellulosome Assembly

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Structural Basis for Inhibition of Aspergillus niger Xylanase by Triticum aestivum Xylanase Inhibitor-I

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Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1

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SWISS-MODEL: an automated protein homology-modeling server

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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Data‐driven docking for the study of biomolecular complexes

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Structural requirements for low-pH-induced rearrangements in the envelope glycoprotein of tick-borne encephalitis virus

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Mapping of Functional Elements in the Stem-Anchor Region of Tick-Borne Encephalitis Virus Envelope Protein E

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Mutational Evidence for an Internal Fusion Peptide in Flavivirus Envelope Protein E

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Membrane Interactions of the Tick-Borne Encephalitis Virus Fusion Protein E at Low pH

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