Ylva Ivarsson
Professor i biokemi vid Institutionen för kemi - BMC; Biokemi; Ivarsson grupp
- Telefon:
- 018-471 40 38
- E-post:
- Ylva.Ivarsson@kemi.uu.se
- Besöksadress:
- Husargatan 3
752 37 Uppsala - Postadress:
- Box 576
75123 Uppsala
- Akademiska meriter:
- FD, docent i biokemi
Mer information visas för dig som medarbetare om du loggar in.
Kort presentation
Ylva Ivarsson is a full professor of Biochemistry with a research team funded by the Swedish Research Council, the Swedish foundation for strategic research, EU Marie Curie ITN and others. The research of the group is interdisciplinary and combines biochemical and biophysical methods with bioinformatics and cell-based assays to study motif-based protein-protein interactions.
Visit the homepage of the group for more information
https://ivarssonlab.com/
Biografi
Denna text finns inte på svenska, därför visas den engelska versionen.
Ylva Ivarsson obtained her PhD in Biochemistry from Uppsala University in 2006. She moved to the University of Rome “La Sapienza” to study protein folding and misfolding in the group of Maurizio Brunori. After 2 ½ years in Italy she moved to the group of Pascale Zimmermann at the Catholic University of Leuven, Belgium, to study protein-phospholipid interactions. In February 2012 she transferred to the Donnelly Centre at the University of Toronto for a shared appointment between the groups of Sachdev Sidhu and Philip M Kim. During this stay, she developed a method called proteomic peptide phage display. Ylva was awarded a Young Investigator grant from the Swedish Research Council and started her independent lab in the Department of Chemistry, Uppsala University in July 2013. Since the start of the group she has recieved several prestigeous grants and was tenured in 2017. Her research interest is on the molecular interactions that underlie cellular signal transduction. In particular her group focus on mapping out interactions between modular domains and motifs found in the intrinsically disordered regions of the proteome.
Publikationer
Senaste publikationer
- Elucidation of Short Linear Motif-Based Interactions of the FERM Domains of Ezrin, Radixin, Moesin, and Merlin (2023)
- Motif-dependent binding on the intervening domain regulates O-GlcNAc transferase (2023)
- The next wave of interactomics (2023)
- Evaluation of affinity-purification coupled to mass spectrometry approaches for capture of short linear motif-based interactions (2023)
- Large‐scale phosphomimetic screening identifies phospho‐modulated motif‐based protein interactions (2023)
Alla publikationer
Artiklar
- Elucidation of Short Linear Motif-Based Interactions of the FERM Domains of Ezrin, Radixin, Moesin, and Merlin (2023)
- Motif-dependent binding on the intervening domain regulates O-GlcNAc transferase (2023)
- The next wave of interactomics (2023)
- Evaluation of affinity-purification coupled to mass spectrometry approaches for capture of short linear motif-based interactions (2023)
- Large‐scale phosphomimetic screening identifies phospho‐modulated motif‐based protein interactions (2023)
- Identification of motif-based interactions between SARS-CoV-2 protein domains and human peptide ligands pinpoint antiviral targets (2023)
- Large-scale phage-based screening reveals extensive pan-viral mimicry of host short linear motifs (2023)
- SLiM-binding pockets (2023)
- Proteome-scale mapping of binding sites in the unstructured regions of the human proteome (2022)
- ProP-PD for proteome-wide motif-mediated interaction discovery (2022)
- p Orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs (2022)
- Coupling to short linear motifs creates versatile PME-1 activities in PP2A holoenzyme demethylation and inhibition (2022)
- A Syntenin Inhibitor Blocks Endosomal Entry of SARS-CoV-2 and a Panel of RNA Viruses (2022)
- How viral proteins bind short linear motifs and intrinsically disordered domains (2022)
- Integrated analysis of Shank1 PDZ interactions with C-terminal and internal binding motifs (2021)
- A High-Affinity Peptide Ligand Targeting Syntenin Inhibits Glioblastoma (2021)
- Cytoplasmic short linear motifs in ACE2 and integrin beta(3) link SARS-CoV-2 host cell receptors to mediators of endocytosis and autophagy (2021)
- Large scale discovery of coronavirus-host factor protein interaction motifs reveals SARS-CoV-2 specific mechanisms and vulnerabilities (2021)
- Profiling calcium-dependent interactions between Sorcin and intrinsically disordered regions of human proteome (2020)
- Genetically Encoded Cyclic Peptide Phage Display Libraries (2020)
- Systematic Discovery of Short Linear Motifs Decodes Calcineurin Phosphatase Signaling (2020)
- Deciphering the Unexpected Binding Capacity of the Third PDZ Domain of Whirlin to Various Cochlear Hair Cell Partners (2020)
- Editorial overview (2019)
- Affinity and specificity of motif-based protein-protein interactions (2019)
- Systematic identification of recognition motifs for the hub protein LC8 (2019)
- A Consensus Binding Motif for the PP4 Protein Phosphatase (2019)
- High-throughput discovery of functional disordered regions (2018)
- Proteome‐wide analysis of phospho‐regulated PDZ domain interactions (2018)
- The Sign of Nuclear Magnetic Resonance Chemical Shift Difference as a Determinant of the Origin of Binding Selectivity (2018)
- Investigating the phospho-regulation of ER shaping protein RTN1A (Reticulon-1A) by the Calcineurin phosphatase. (2017)
- Discovery of short linear motif-mediated interactions through phage display of intrinsically disordered regions of the human proteome (2017)
- Mapping the human calcineurin phosphatase signaling network through global identification of short linear motifs that mediate substrate recognition (2017)
- A novel role for the Calcineurin phosphatase at the nuclear pore (2017)
- Uncovering Novel Substrates and Functions for the Calcineurin Phosphatase in Human Cells (2017)
- PP2A-B' holoenzyme substrate recognition, regulation and role in cytokinesis (2017)
- Frizzled 7 and PIP2 binding by syntenin PDZ2 domain supports Frizzled 7 trafficking and signalling (2016)
- Proteomic peptide phage display uncovers novel interactions of the PDZ1-2 supramodule of syntenin (2016)
- Improved affinity at the cost of decreased specificity (2016)
- Pooled screening for antiproliferative inhibitors of protein-protein interactions. (2016)
- Let There Be Light! (2016)
- Uncovering novel substrates and functions for the calcineurin phosphatase in human cells. (2016)
- High-throughput methods for identification of protein-protein interactions involving short linear motifs (2015)
- Selectivity of Aggregation-Determining Interactions (2015)
- Structural basis of Sorcin-mediated calcium-dependent signal transduction (2015)
- A Structural Portrait of the PDZ Domain Family (2014)
- The Development and Characterization of a Peptide-Based Syntenin Inhibitor (2014)
- Large-scale interaction profiling of PDZ domains through proteomic peptide-phage display using human and viral phage peptidomes (2014)
- Interaction Analysis through Proteomic Phage Display (2014)
- A ZO-1/α5β1-integrin complex regulates cytokinesis downstream of PKCε in NCI-H460 cells plated on fibronectin (2013)
- Prevalence, specificity and determinants of lipid-interacting PDZ domains from an in-cell screen and in vitro binding experiments (2013)
- Syndecan-syntenin-ALIX regulates the biogenesis of exosomes (2012)
- Plasticity of PDZ domains in ligand recognition and signaling (2012)
- Syntenin, a syndecan adaptor and an Arf6 phosphatidylinositol 4,5-bisphosphate effector, is essential for epiboly and gastrulation cell movements in zebrafish (2012)
- Extensions of PSD-95/discs large/ZO-1 (PDZ) domains influence lipid binding and membrane targeting of syntenin-1 (2012)
- Misregulated alternative splicing of BIN1 is associated with T tubule alterations and muscle weakness in myotonic dystrophy (2011)
- Cooperative phosphoinositide and peptide binding by PSD-95/discs large/ZO-1 (PDZ) domain of polychaetoid, Drosophila zonulin (2011)
- Structural diversity of PDZ-lipid interactions (2010)
- Structural characterization of a misfolded intermediate populated during the folding process of a PDZ domain (2010)
- Engineered symmetric connectivity of secondary structure elements highlights malleability of protein folding pathways (2009)
- Folding and stability of globular proteins and implications for function (2009)
- Folding and misfolding in a naturally occurring circularly permuted PDZ domain (2008)
- Mechanisms of protein folding (2008)
- The folding pathway of an engineered circularly permuted PDZ domain (2008)
- Mechanism of Na(+) binding to thrombin resolved by ultra-rapid kinetics (2007)
- Identification and characterization of protein folding intermediates (2007)
- Engineering the enantioselectivity of glutathione transferase by combined active-site mutations and chemical modifications (2007)
- An on-pathway intermediate in the folding of a PDZ domain (2007)
- Regio- and enantioselectivity in epoxide conjugations are modulated by residue 210 in Mu class glutathione transferases (2006)
- Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution (2006)
- Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution (2006)
- Regio- and enantioselectivities in epoxide conjugations are modulated by residue 210 in Mu class glutathione transferases. (2005)
- Exploring the importance of an active site residue on the stereo and regio selectivity of Mu class glutathione transferases (2005)
- Identification of residues in glutathione transferase capable of driving functional diversification in evolution (2003)
- Tick-borne flaviviruses recruits the pro viral factor NUP153 to the replication site
- Evaluation of affinity-purification coupled to mass spectrometry approaches for capture of short linear motif-based interactions
Kapitel
