Ivarsson Group

Molecular interactions in cell function and dysfunction
We focus on interactions between linear motifs and peptide binding domains and aim to contribute with novel insights into the human protein-protein interaction networks in health and diseases. In addition, we explore the interplay between protein-protein and protein-phospholipid interactions. Our research is interdisciplinary and combines biochemical and biophysical methods with bioinformatics and cell-based assays.
Group members
Publications
Part of Biology Direct, 2025
- DOI for Elucidation of short linear motif‑based interactions of the MIT and rhodanese domains of the ubiquitin‑specific protease 8
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Defining short linear motif binding determinants by phage display-based deep mutational scanning
Part of Protein Science, 2025
- DOI for Defining short linear motif binding determinants by phage display-based deep mutational scanning
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Part of Biochimica et Biophysica Acta - Proteins and Proteomics, 2025
Part of Nature Communications, 2025
- DOI for High-throughput investigation of cyclin docking interactions reveals the complexity of motif binding determinants
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Part of Archives of Biochemistry and Biophysics, 2025
Part of Structure, 2024
Exploring the short linear motif-mediated protein-protein interactions of CrkL through ProP-PD
Part of Biochemical and Biophysical Research Communications - BBRC, 2024
Proteome-scale characterisation of motif-based interactome rewiring by disease mutations
Part of Molecular Systems Biology, p. 1025-1048, 2024
- DOI for Proteome-scale characterisation of motif-based interactome rewiring by disease mutations
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Part of Nature Communications, 2024
- DOI for ASXLs binding to the PHD2/3 fingers of MLL4 provides a mechanism for the recruitment of BAP1 to active enhancers
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Motif-dependent binding on the intervening domain regulates O-GlcNAc transferase
Part of Nature Chemical Biology, p. 1423-1431, 2023
Large-scale phage-based screening reveals extensive pan-viral mimicry of host short linear motifs
Part of Nature Communications, 2023
- DOI for Large-scale phage-based screening reveals extensive pan-viral mimicry of host short linear motifs
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Part of Biochemistry, p. 1594-1607, 2023
- DOI for Elucidation of Short Linear Motif-Based Interactions of the FERM Domains of Ezrin, Radixin, Moesin, and Merlin
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SLiM-binding pockets: an attractive target for broad-spectrum antivirals
Part of TIBS -Trends in Biochemical Sciences. Regular ed., p. 420-427, 2023
- DOI for SLiM-binding pockets: an attractive target for broad-spectrum antivirals
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Part of Nature Communications, 2023
- DOI for Identification of motif-based interactions between SARS-CoV-2 protein domains and human peptide ligands pinpoint antiviral targets
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Part of Analytical Biochemistry, 2023
- DOI for Evaluation of affinity-purification coupled to mass spectrometry approaches for capture of short linear motif-based interactions
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Large‐scale phosphomimetic screening identifies phospho‐modulated motif‐based protein interactions
Part of Molecular Systems Biology, 2023
- DOI for Large‐scale phosphomimetic screening identifies phospho‐modulated motif‐based protein interactions
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Part of Current opinion in structural biology, 2023
- DOI for The next wave of interactomics: Mapping the SLiM-based interactions of the intrinsically disordered proteome
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Part of eLIFE, 2022
- DOI for Coupling to short linear motifs creates versatile PME-1 activities in PP2A holoenzyme demethylation and inhibition
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A Syntenin Inhibitor Blocks Endosomal Entry of SARS-CoV-2 and a Panel of RNA Viruses
Part of Viruses, 2022
- DOI for A Syntenin Inhibitor Blocks Endosomal Entry of SARS-CoV-2 and a Panel of RNA Viruses
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Part of Biochemical Journal, p. 1-22, 2022
- DOI for p Orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs
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Proteome-scale mapping of binding sites in the unstructured regions of the human proteome
Part of Molecular Systems Biology, 2022
- DOI for Proteome-scale mapping of binding sites in the unstructured regions of the human proteome
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ProP-PD for proteome-wide motif-mediated interaction discovery
Part of TIBS -Trends in Biochemical Sciences. Regular ed., p. 547-548, 2022
- DOI for ProP-PD for proteome-wide motif-mediated interaction discovery
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How viral proteins bind short linear motifs and intrinsically disordered domains
Part of Essays in Biochemistry, p. 935-944, 2022
A High-Affinity Peptide Ligand Targeting Syntenin Inhibits Glioblastoma
Part of Journal of Medicinal Chemistry, p. 1423-1434, 2021
Integrated analysis of Shank1 PDZ interactions with C-terminal and internal binding motifs
Part of Current Research in Structural Biology, p. 41-50, 2021
- DOI for Integrated analysis of Shank1 PDZ interactions with C-terminal and internal binding motifs
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Part of Nature Communications, 2021
- DOI for Large scale discovery of coronavirus-host factor protein interaction motifs reveals SARS-CoV-2 specific mechanisms and vulnerabilities
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Part of Science Signaling, 2021
Identification of Cellular Protein-Protein Interactions
Part of INHIBITORS OF PROTEIN-PROTEIN INTERACTIONS, p. 1-39, Royal Society of Chemistry, 2021
Identification of PDZ Interactions by Proteomic Peptide Phage Display
Part of PDZ Mediated Interactions, p. 41-60, Springer Nature, 2021
Genetically Encoded Cyclic Peptide Phage Display Libraries
Part of ACS CENTRAL SCIENCE, p. 336-338, 2020
- DOI for Genetically Encoded Cyclic Peptide Phage Display Libraries
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Part of Journal of Molecular Biology, p. 5920-5937, 2020
Part of Biochimica et Biophysica Acta - General Subjects, 2020
Systematic Discovery of Short Linear Motifs Decodes Calcineurin Phosphatase Signaling
Part of Molecular Cell, p. 342-+, 2020
A Consensus Binding Motif for the PP4 Protein Phosphatase
Part of Molecular Cell, p. 953-964000000, 2019
Editorial overview: Folding and binding
Part of Current opinion in structural biology, p. 139-140, 2019
Systematic identification of recognition motifs for the hub protein LC8
Part of Life Science Alliance, 2019
- DOI for Systematic identification of recognition motifs for the hub protein LC8
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Affinity and specificity of motif-based protein-protein interactions
Part of Current opinion in structural biology, p. 26-33, 2019
- DOI for Affinity and specificity of motif-based protein-protein interactions
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Part of Biochemistry, p. 66-71, 2018
- DOI for The Sign of Nuclear Magnetic Resonance Chemical Shift Difference as a Determinant of the Origin of Binding Selectivity: Elucidation of the Position Dependence of Phosphorylation in Ligands Binding to Scribble PDZ1
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Proteome‐wide analysis of phospho‐regulated PDZ domain interactions
Part of Molecular Systems Biology, 2018
- DOI for Proteome‐wide analysis of phospho‐regulated PDZ domain interactions
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High-throughput discovery of functional disordered regions
Part of Molecular Systems Biology, 2018
Uncovering Novel Substrates and Functions for the Calcineurin Phosphatase in Human Cells
Part of The FASEB Journal, 2017
Part of Molecular Biology of the Cell, p. 3727-3727, 2017
Part of Molecular Biology of the Cell, p. 3727-3727, 2017
A novel role for the Calcineurin phosphatase at the nuclear pore
Part of Molecular Biology of the Cell, p. 3727-3727, 2017
PP2A-B' holoenzyme substrate recognition, regulation and role in cytokinesis
Part of Cell Discovery, 2017
- DOI for PP2A-B' holoenzyme substrate recognition, regulation and role in cytokinesis
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Part of The FEBS Journal, p. 485-498, 2017
- DOI for Discovery of short linear motif-mediated interactions through phage display of intrinsically disordered regions of the human proteome
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Uncovering novel substrates and functions for the calcineurin phosphatase in human cells.
Part of Molecular Biology of the Cell, 2016
Part of Scientific Reports, 2016
- DOI for Improved affinity at the cost of decreased specificity: a recurring theme in PDZ-peptide interactions.
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Frizzled 7 and PIP2 binding by syntenin PDZ2 domain supports Frizzled 7 trafficking and signalling
Part of Nature Communications, 2016
- DOI for Frizzled 7 and PIP2 binding by syntenin PDZ2 domain supports Frizzled 7 trafficking and signalling
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Pooled screening for antiproliferative inhibitors of protein-protein interactions.
Part of Nature Chemical Biology, p. 275-281, 2016