Author

A. Laaksonen

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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Approach:statistical model· 4 Approach:deep learning· 2 Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Research Focus:cell type annotation· 1 Research Focus:differential expression· 1

Frequent Co-Authors

F. L. Barroso da Silva· 4 shared C. Correa Giron· 2 shared A. Neamtu· 1 shared C. C. Giron· 1 shared F. Mocci· 1 shared

Activity by Year

2020-2022 · peak 3/yr

Co-Author Collaboration Network

5 top collaborators · 5 mutual co-author links

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4 shared papersBiophysics

F. L. Barroso da Silva

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4 papers

Recent·Most cited

Electrostatic features for the Receptor binding domain of SARS-COV-2 wildtype and its variants. Compass to the severity of the future variants with the charge rule.

F. L. Barroso da Silva, C. C. Giron, A. Laaksonen

The paper analyzes electrostatic features of SARS-CoV-2 RBD variants to predict binding affinity and severity using a charge-based rule.

bioRxiv · Jun 16, 2022Biophysics

Differences between Omicron SARS-CoV-2 RBD and other variants in their ability to interact with cell receptors and monoclonal antibodies

C. Correa Giron, A. Laaksonen, F. L. Barroso da Silva

This paper uses simulations to compare Omicron and other SARS-CoV-2 variants' RBD interactions with ACE2 and mAbs, identifying binding affinities and potential therapeutic targets.

bioRxiv · Jan 29, 2022Biophysics

Towards an optimal monoclonal antibody with higher binding affinity to the receptor-binding domain of SARS-CoV-2 spike proteins from different variants

A. Neamtu, F. Mocci, A. Laaksonen, F. L. Barroso da Silva

The paper uses a multiscale computational protocol to design mAbs with higher binding affinity to SARS-CoV-2 spike protein RBD across variants, identifying candidates with improved performance against Omicron.

bioRxiv · Jan 4, 2022Biophysics

On the interactions of the receptor-binding domain of SARS-CoV-1 and SARS-CoV-2 spike proteins with monoclonal antibodies and the receptor ACE2

C. Correa Giron, A. Laaksonen, F. L. Barroso da Silva

This study maps electrostatic epitopes and interaction energies of SARS-CoV-1 and SARS-CoV-2 RBD proteins with antibodies and ACE2, showing higher ACE2 binding affinity for SARS-CoV-2 RBD.

bioRxiv · Apr 5, 2020Biophysics