Author

A. A. Ibarra

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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Biochemistry· 3

Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Approach:biophysical modeling· 1 Approach:diffusion model· 1 Approach:experimental assay· 1 Organism:human· 1 Organism:non-human primate· 1 Organism:virus· 1

Frequent Co-Authors

A. J. Mulholland· 2 shared A. S. Oliveira· 2 shared R. B. Sessions· 2 shared A. D. Davidson· 1 shared A. J. Wilson· 1 shared C. Schaffitzel· 1 shared D. K. Shoemark· 1 shared D. Shoemark· 1 shared

Activity by Year

2020-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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2 shared papersBiochemistry

A. J. Mulholland

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Author profile →

3 papers

Recent·Most cited

Understanding p300-transcription factor interactions using sequence variation and hybridization

F. Hobor, Z. Hegedus, A. A. Ibarra, V. L. Petrovicz, G. J. Bartlett, R. B. Sessions, A. J. Wilson, T. A. Edwards

The paper investigates HIF-1 sequence variation tolerance using biochemical assays, showing that sequence changes are tolerated through disordered binding interactions.

bioRxiv · Dec 16, 2021Biochemistry

The fatty acid site is coupled to functional motifs in the SARS-CoV-2 spike protein and modulates spike allosteric behaviour

A. S. Oliveira, D. Shoemark, A. A. Ibarra, A. D. Davidson, I. Berger, C. Schaffitzel, A. J. Mulholland

This study uses molecular dynamics simulations to show that the fatty acid binding site in the SARS-CoV-2 spike protein influences distant functional regions and variant behavior.

Computational and Structural Biotechnology Journal · Dec 11, 2021Peer-reviewedBiochemistry

Simulations support the interaction of the SARS-CoV-2 spike protein with nicotinic acetylcholine receptors

A. S. Oliveira, A. A. Ibarra, I. Bermudez, L. Casalino, Z. Gaieb, D. K. Shoemark, T. Gallagher, R. B. Sessions, R. E. Amaro, A. J. Mulholland

The paper uses molecular simulations to show that the SARS-CoV-2 spike protein's Y674-R685 loop binds to nicotinic acetylcholine receptors, with specific interactions and conformational changes observed across different receptor subtypes.

bioRxiv · Jul 16, 2020Biochemistry