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Molecular Biosystems|October 4, 2017
The Henipavirus V protein is a prevalently unfolded protein with a zinc-finger domain involved in binding to DDB1Edoardo Salladini, Vincent Delauzun, Sonia Longhi
International Journal of Molecular Sciences|December 29, 2020
Intrinsic Disorder in Plant Transcription Factor Systems: Functional ImplicationsEdoardo Salladini, Maria L M Jørgensen, Frederik F Theisen, et al.
Current Protocols|July 5, 2022
Exploring Manually Curated Annotations of Intrinsically Disordered Proteins with DisProtFederica Quaglia, András Hatos, Edoardo Salladini, et al.
Biochimica Et Biophysica Acta. General Subjects|July 21, 2018
Conformational response to charge clustering in synthetic intrinsically disordered proteinsGiulia Tedeschi, Edoardo Salladini, Carlo Santambrogio, et al.
The Journal of Biological Chemistry|December 28, 2020
αα-Hub domains and intrinsically disordered proteins: A decisive comboKatrine Bugge, Lasse Staby, Edoardo Salladini, et al.
Cell Communication and Signaling : CCS|January 7, 2021
Connecting the αα-hubs: same fold, disordered ligands, new functionsLasse Staby, Katrine Bugge, Rasmus Greve Falbe-Hansen, et al.
Scientific Reports|November 16, 2017
Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteinsKarama Hamdi, Edoardo Salladini, Darragh P O'Brien, et al.
The FEBS Journal|February 2, 2022
SARS-CoV-2 variants preferentially emerge at intrinsically disordered protein sites helping immune evasionFederica Quaglia, Edoardo Salladini, Marco Carraro, et al.
Scientific Reports|November 12, 2020
Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXSMarco Schiavina, Edoardo Salladini, Maria Grazia Murrali, et al.
The Journal of Biological Chemistry|April 22, 2022
αα-hub coregulator structure and flexibility determine transcription factor binding and selection in regulatory interactomesFrederik Friis Theisen, Edoardo Salladini, Rikke Davidsen, et al.
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