Browsing by Author "Olivieri, Cristina"

Now showing 1 - 6 of 6
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    Analysis of the kinetics of binding of Protein Kinase A Inhibitor alpha (PKIa) to cAMP-dependent protein kinase a catalytic subunit (PKA-C)
    (2020-04-17) Li, Geoffrey; Muretta, Joseph; Olivieri, Cristina; vegli001@umn.edu; Veglia, Gianluigi
    TR-FRET raw data used for the analysis of the binding kinetic for full-length protein kinase inhibitor (PKIa) to ATP-saturated cAMP-dependent protein kinase A (PKA-C). The experiments are part of a publication on eLIFE: "Multi-state Recognition Pathway of the Intrinsically Disordered Protein Kinase Inhibitor by Protein Kinase A", where we investigated the structural and kinetics changed that PKIa undergoes upon interaction with PKA-C
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    Binding interaction between PKA-C and RKIP and its mutant P74L
    (2022-01-03) Olivieri, Cristina; Veglia, Gianluigi; vegli001@umn.edu; Veglia, Gianluigi; University of Minnesota, BMBB Department, Structural Biology Division, Professor Gianluigi Veglia Lab
    Kinetical and structural characterization of the interaction between the RAF kinase inhibitor (RKIP) and the cAMP-dependent protein kinase A (PKA-C) by interferometry and nuclear magnetic resonance (NMR) spectroscopy analysis. Together with the analysis performed by Dr. Marsha Rosner's laboratory (University of Chicago), these studies are part of a paper that has been sent to the PNAS journal.
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    Changes in protein kinase A conformational entropy by ATP-competitive inhibitors
    (2022-05-09) Olivieri, Cristina; Veglia, Gianluigi; vegli001@umn.edu; Veglia, Gianluigi; University of Minnesota, BMBB Department, Structural Biology Division, Professor Gianluigi Veglia Lab
    NMR characterization of the structural and dynamic changes of the catalytic subunit of cAMP-dependent protein kinase A (PKA-C) in complex with balanol and H89, two ATP-competitive inhibitors. This study aims to unveil how these two inhibitors affect the PKA-C structure and dynamics and how these changes govern the enzyme binding cooperativity and conformational dynamic. These data are part of a paper that has been sent to a peer-review paper.
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    Proton and amide chemical shift list files of wild-type cAMP-dependent protein kinase a (PKA-C) and the chimeric mutant (PKA-JC) and MATLab scripts for the chemical shift analysis
    (2020-11-23) Veglia, Gianluigi; Olivieri, Cristina; Walker, Caitlin; Veliparambil Subrahmanian, Manu; vegli001@umn.edu; Veglia, Gianluigi; University of Minnesota, BMBB Department, Structural Biology Division, Professor Gianluigi Veglia Lab
    Proton and amide chemical shift list files of wild-type cAMP-dependent protein kinase a (PKA-C) and the chimeric mutant (PKA-JC) and MatLab scripts used for the CHESCA and CONCISE analysis. The chemical shift lists were obtained using standard NMR experiments (1H-15N -TROSY-HSQC). The MatLab scripts were used for the CHESCA and CONCISE analysis of the amide chemical shift. These files are part of a publication on Communication biology: "Defective Internal Allosteric Network Imparts Dysfunctional ATP/Substrate Binding Cooperativity in Oncogenic Chimera of Protein Kinase A"
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    The role of the αC-β4 loop in regulating cooperativity interaction in Protein Kinase A
    (2024-02-19) Olivieri, Cristina; Veglia, Gianluigi; Veliparambil Subrahmanian, Manu; Wang, Yingjie; vegli001@umn.edu; Veglia, Gianluigi; Veglia Lab
    This investigation examines the cooperative modulation of Protein Kinase A (PKA) activity by ATP and substrates, with a specialized focus on the enzyme's catalytic subunit (PKA-C), utilizing NMR-restrained molecular dynamics simulations complemented by advanced Markov Model analysis. Herein, we deposit chemical shift datasets for the PKA-C mutant F100A, both in its apo form and in complex with nucleotides and inhibitors, and activity assay data providing a comprehensive insight into the enzyme's allosteric regulation mechanisms.
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    Steady-state coupled enzyme assays using standard peptides of cAMP-dependent protein kinase a catalytic subunit (PKA-C) and its chimeric mutant (PKA-CJ)
    (2020-11-23) Olivieri, Cristina; vegli001@umn.edu; Veglia, Gianluigi
    Steady-state coupled enzyme assays using standard peptide substrates (Kempite, CREB, and KSR1) of cAMP-dependent protein kinase A (PKA-C) and its chimeric mutant (PKA-JC)