Author

A. S. Oliveira

Primary ORCID profile (0009-0000-4798-7752 · 1 paper)Unclaimed ORCID profile · follow to get notified of new preprints

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Same name, identified by ORCID

A. S. OliveiraiD1 paper · Instituto Butantan

Biology Disciplines

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Biochemistry· 2

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 Organism:human· 1 Organism:non-human primate· 1 Organism:virus· 1

Frequent Co-Authors

A. A. Ibarra· 2 shared A. J. Mulholland· 2 shared A. D. Davidson· 1 shared C. Schaffitzel· 1 shared D. K. Shoemark· 1 shared D. Shoemark· 1 shared I. Berger· 1 shared I. Bermudez· 1 shared

Activity by Year

2020-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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2 shared papersBiochemistry

A. A. Ibarra

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2 papers

Recent·Most cited

BiochemistryComputational and Structural Biotechnology JournalPeer-reviewedDec 11, 2021

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. 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.

DOI 10.1016/j.csbj.2021.12.011

virusprotein structure

𝕏 PostBluesky

BiochemistrybioRxivJul 16, 2020

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

A. S. Oliveira, A. A. Ibarra, I. Bermudez…·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.

DOI 10.1016/j.bpj.2021.01.037

humannon-human primate

𝕏 PostBluesky