Author

I. Galleano

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 3 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Research Focus:cell type annotation· 1 Assay:electrophysiology· 1 Research Focus:host-pathogen & immune response· 1 Organism:mouse· 1 Assay:proteomics· 1

Frequent Co-Authors

K. K. Khoo· 2 shared S. A. Heusser· 2 shared S. A. Pless· 2 shared A. S. Madsen· 1 shared C. A. Olsen· 1 shared C. B. Borg· 1 shared C. Lund· 1 shared C. Moreno-Yruela· 1 shared

Activity by Year

2017-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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2 shared papersBiophysics

K. K. Khoo

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4 papers

Recent·Most cited

Protein semisynthesis underscores role of a conserved lysine in activation and desensitization of acid-sensing ion channels

D. Sarkar, I. Galleano, S. A. Heusser, S. Y. Ou, G. R. Uzun, K. K. Khoo, G. J. v. d. H. van Noort, J. S. Harrison, S. A. Pless

This study uses semisynthesis to investigate the role of a conserved lysine in ASIC1a function, showing its importance in activation and desensitization.

bioRxiv · Jan 23, 2023Biophysics

Functional crosstalk between phosphorylation and disease-causing mutations in the cardiac sodium channel Nav1.5

I. Galleano, H. Harms, K. Choudhury, K. K. Khoo, L. Delemotte, S. A. Pless

This paper investigates how phosphorylation and disease-causing mutations interact in Nav1.5, showing that mutations can amplify phosphorylation's impact on channel function and drug sensitivity.

bioRxiv · Dec 11, 2020Biophysics

Mechanism and site of action of big dynorphin on ASIC1a

C. B. Borg, N. Braun, S. A. Heusser, Y. Bay, D. Weis, I. Galleano, C. Lund, W. Tian, L. M. Haugaard-Kedstroem, E. P. Bennett, T. Lynagh, K. Stromgaard, J. Andersen, S. Pless

This study identifies the binding site and mechanism of big dynorphin on ASIC1a, revealing the acidic pocket as the interaction site and highlighting its potential for therapeutic development.

Proceedings of the National Academy of Sciences · Mar 12, 2020Peer-reviewedBiophysics

Histone Deacetylase 11 is an ε-N-Myristoyllysine Hydrolase

C. Moreno-Yruela, I. Galleano, A. S. Madsen, C. A. Olsen

This study identifies HDAC11 as an ε-N-myristoyllysine hydrolase, showing it efficiently cleaves long-chain acyl modifications and is insensitive to common HDAC inhibitors but inhibited by macrocyclic hydroxamic acid peptides.

bioRxiv · Nov 1, 2017Biochemistry