Author

A. Tennenhouse

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· 1 Bioengineering· 1 Immunology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Assay:proteomics· 2 Approach:deep learning· 1 Research Focus:drug response / drug discovery· 1 Research Focus:protein design· 1 Assay:protein structure· 1

Frequent Co-Authors

A. Mechaly· 2 shared E. Epstein· 2 shared O. Mazor· 2 shared R. Alcalay· 2 shared S. J. Fleishman· 2 shared A. Barnea· 1 shared A. Ben-David· 1 shared A. Noronha· 1 shared

Activity by Year

2021-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 31 mutual co-author links

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Curved chords = mutual co-authorship

2 shared papersBiochemistry

A. Mechaly

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Reliable energy-based antibody humanization and stabilization

A. Tennenhouse, L. Khmelnitsky, R. Khalaila, N. Yeshaya, A. Noronha, M. Lindzen, E. Makowski, I. Zaretsky, Y. Fridmann Sirkis, Y. Galon-Wolfenson, P. M. Tessier, J. Abramson, Y. Yarden, D. Fass, S. J. Fleishman

The paper introduces CUMAb, a computational method for humanizing antibodies that improves stability and binding by systematically grafting CDRs onto human frameworks and ranking designs using Rosetta simulations.

bioRxiv · Aug 14, 2022Bioengineering

Isolation and characterization of a highly specific monoclonal antibody targeting the botulinum neurotoxin type E exposed SNAP-25 neoepitope

A. Mechaly, E. Diamant, R. Alcalay, A. Ben-David, E. Dor, A. Torgeman, A. Barnea, M. Girshengorn, L. Levin, E. Epstein, A. Tennenhouse, s. Fleishman, R. Zichel, O. Mazor

This paper isolates a highly specific monoclonal antibody that detects the BoNT/E-cleaved SNAP-25 neoepitope with ultra-high affinity and no cross-reactivity.

bioRxiv · Sep 16, 2021 · PreprintBiochemistry

The neutralization potency of anti-SARS-CoV-2 therapeutic human monoclonal antibodies is retained against novel viral variants

E. Makdasi, A. Zvi, R. Alcalay, T. Noy-Porat, E. Peretz, A. Mechaly, Y. Levy, E. Epstein, T. Chitlaru, A. Tennenhouse, M. Aftalion, D. Gur, N. Paran, H. Tamir, O. Zimhony, , R. Rosenfeld

This study evaluates the neutralization potency of four SARS-CoV-2 mAbs against spike mutations and two variants of concern, finding that MD65 and BL6 retain effectiveness against B.1.1.7 and B.1.351.

bioRxiv · Apr 1, 2021Immunology