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Emma Åberg
Researcher at Uppsala University
Publications - 7
Citations - 100
Emma Åberg is an academic researcher from Uppsala University. The author has contributed to research in topics: Transactivation & Protein domain. The author has an hindex of 4, co-authored 5 publications receiving 80 citations.
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Journal ArticleDOI
Emergence and evolution of an interaction between intrinsically disordered proteins
Greta Hultqvist,Emma Åberg,Carlo Camilloni,Carlo Camilloni,Gustav N. Sundell,Eva Andersson,Jakob Dogan,Jakob Dogan,Celestine N. Chi,Michele Vendruscolo,Per Jemth +10 more
TL;DR: Experiments together with molecular modeling using NMR chemical shifts suggest that new interactions involving intrinsically disordered proteins may evolve via a low-affinity complex which is optimized by modulating direct interactions as well as dynamics, while tolerating several potentially disruptive mutations.
Journal ArticleDOI
Evolution of the p53-MDM2 pathway.
TL;DR: The phylogenetic analysis of the p53/p63/p73 and MDM proteins from phyla that retain the interaction domains TAD and p 53/p 63/p 73BD built phylogenetic trees based on both vertebrate and invertebrate species.
Journal ArticleDOI
Binding Kinetics of the Intrinsically Disordered p53 Family Transactivation Domains and MDM2
TL;DR: The findings support an emerging picture of "conformational funneling" occurring in the initial stages of interactions involving IDPs and that these early binding events can rely on hydrophobic as well as charge-charge interactions.
Journal ArticleDOI
Targeting protein-protein interactions with trimeric ligands: high affinity inhibitors of the MAGUK protein family.
Klaus B. Nissen,Linda M. Haugaard-Kedström,Theis S. Wilbek,Line S. Nielsen,Emma Åberg,Anders S. Kristensen,Anders Bach,Per Jemth,Kristian Strømgaard +8 more
TL;DR: Novel inhibitors of the MAGUK proteins with exceptionally high affinity are provided, which can be used to further elucidate the therapeutic potential of these proteins.
Journal ArticleDOI
Molecular Details of a Coupled Binding and Folding Reaction between the Amyloid Precursor Protein and a Folded Domain
Thomas M T Jensen,Thomas M T Jensen,Christian R. O. Bartling,Andreas Karlsson,Emma Åberg,Linda M. Haugaard-Kedström,Kristian Strømgaard,Per Jemth +7 more
TL;DR: In this article, the interaction between the intrinsically disordered motif of amyloid precursor protein (APP) and the phosphotyrosine binding (PTB) domain of Mint2 was investigated.