Search Results - "Galleano, Iacopo"

Correction to A Continuous, Fluorogenic Sirtuin 2 Deacylase Assay: Substrate Screening and Inhibitor Evaluation by Galleano, Iacopo, Schiedel, Matthias, Jung, Manfred, Madsen, Andreas S, Olsen, Christian A

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Using protein semi-synthesis to identify proton-sensing residues in an acid-sensing ion channel by Sarkar, Debayan, Galleano, Iacopo, Pless, Stephan A.

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Functional cross-talk between phosphorylation and disease-causing mutations in the cardiac sodium channel Nav1.5 by Galleano, Iacopo, Harms, Hendrik, Choudhury, Koushik, Khoo, Keith, Delemotte, Lucie, Pless, Stephan Alexander

“…The voltage-gated sodium channel Nav1.5 initiates the cardiac action potential. Alterations of its activation and inactivation properties due to mutations can…”
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Targeting Sirtuins: Substrate Specificity and Inhibitor Design by Rajabi, Nima, Galleano, Iacopo, Madsen, Andreas S, Olsen, Christian A

“…Lysine residues across the proteome are modified by posttranslational modifications (PTMs) that significantly enhance the structural and functional diversity…”
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Functional cross-talk between phosphorylation and disease-causing mutations in the cardiac sodium channel Na v 1.5 by Galleano, Iacopo, Harms, Hendrik, Choudhury, Koushik, Khoo, Keith, Delemotte, Lucie, Pless, Stephan Alexander

“…The voltage-gated sodium channel Na 1.5 initiates the cardiac action potential. Alterations of its activation and inactivation properties due to mutations can…”
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A Semi-Synthetic Approach to Engineer Ligand- and Voltage-Gated Ion Channels in Live Cells by Khoo, Keith K., Galleano, Iacopo, Pless, Stephan A.

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Characterizing Conformational Changes of ASIC1a During Gating and Peptide Modulation by Heusser, Stephanie A., Sheikh, Zeshan P., Borg, Christian B., Galleano, Iacopo, Pless, Stephan A.

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Interplay of Nav1.5 Disease-Causing Mutations and Phosphorylation Revealed by Protein Semi-Synthesis and Molecular Dynamics Simulations by Galleano, Iacopo, Harms, Hendrik, Choudhury, Koushik, Khoo, Keith K., Delemotte, Lucie, Pless, Stephan A.

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Functional cross-talk between phosphorylation and disease-causing mutations in the cardiac sodium channel Na(v)1.5 by Galleano, Iacopo, Harms, Hendrik, Choudhury, Koushik, Khoo, Keith, Delemotte, Lucie, Pless, Stephan Alexander

“…The voltage-gated sodium channel Nav1.5 initiates the cardiac action potential. Alterations of its activation and inactivation properties due to mutations can…”
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A Continuous, Fluorogenic Sirtuin 2 Deacylase Assay: Substrate Screening and Inhibitor Evaluation by Galleano, Iacopo, Schiedel, Matthias, Jung, Manfred, Madsen, Andreas S, Olsen, Christian A

“…Sirtuins are important regulators of lysine acylation, which is implicated in cellular metabolism and transcriptional control. This makes the sirtuin class of…”
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Mechanism and site of action of big dynorphin on ASIC1a by Borg, Christian B., Braun, Nina, Heusser, Stephanie A., Bay, Yasmin, Weis, Daniel, Galleano, Iacopo, Lund, Camilla, Tian, Weihua, Haugaard-Kedström, Linda M., Bennett, Eric P., Lynagh, Timothy, Strømgaard, Kristian, Andersen, Jacob, Pless, Stephan A.

“…Acid-sensing ion channels (ASICs) are proton-gated cation channels that contribute to neurotransmission, as well as initiation of pain and neuronal death…”
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Mechanism and Binding Site of the ASIC1A-Big Dynorphin Interaction by Borg, Christian B., Braun, Nina, Heusser, Stephanie A., Bay, Yasmin, Weis, Daniel, Galleano, Iacopo, Lund, Camilla, Tian, Weihua, Haugaard-Kedström, Linda M., Bennett, Eric P., Lynagh, Timothy, Strømgaard, Kristian, Andersen, Jacob, Pless, Stephan A.

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Protein semisynthesis underscores the role of a conserved lysine in activation and desensitization of acid-sensing ion channels by Sarkar, Debayan, Galleano, Iacopo, Heusser, Stephanie Andrea, Ou, Sofie Yuewei, Uzun, Gül Refika, Khoo, Keith K, van der Heden van Noort, Gerbrand Jan, Harrison, Joseph Scott, Pless, Stephan Alexander

“…Acid-sensing ion channels (ASICs) are trimeric ion channels that open a cation-conducting pore in response to proton binding. Excessive ASIC activation during…”
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