Author

T. Panchenko

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· 2 Immunology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Assay:proteomics· 4 Research Focus:host-pathogen & immune response· 3 Organism:human· 3 Research Focus:benchmarking· 1 Assay:ChIP-seq· 1 Research Focus:chromatin & epigenetic regulation· 1 Approach:machine learning (classical)· 1

Frequent Co-Authors

A. Koide· 3 shared K. W. Teng· 3 shared L. A. Romero· 3 shared S. Koide· 3 shared T. Hattori· 3 shared K. A. Stapleford· 2 shared M. I. Samanovic· 2 shared M. J. Mulligan· 2 shared

Activity by Year

2019-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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3 shared papersImmunology

A. Koide

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Author profile →

4 papers

Recent·Most cited

Two-dimensional multiplexed assay for rapid and deep SARS-CoV-2 serology profiling and for machine learning prediction of neutralization capacity

A. Koide, T. Panchenko, C. Wang, S. A. Thannickal, L. A. Romero, K. W. Teng, F.-Z. Li, P. Akkapeddi, A. D. Corrado, J. Caro, C. Diefenbach, M. I. Samanovic, M. J. Mulligan, T. Hattori, K. A. Stapleford, , S. Koide

This paper introduces a 2D-MBBA assay for SARS-CoV-2 serology profiling and uses machine learning to predict neutralization capacity from antibody profiles.

bioRxiv · Aug 3, 2021 · PreprintImmunology

The ACE2-binding interface of SARS-CoV-2 Spike inherently deflects immune recognition

T. Hattori, A. Koide, T. Panchenko, L. A. Romero, K. W. Teng, T. Tada, N. R. Landau, S. Koide

This study investigates antibody targeting of the ACE2-binding interface of SARS-CoV-2 Spike, finding that only a small fraction of RBD-binding antibodies target this region, suggesting it is less immunogenic.

bioRxiv · Nov 3, 2020Biochemistry

High titers of multiple antibody isotypes against the SARS-CoV-2 spike receptor-binding domain and nucleoprotein associate with better neutralization.

M. G. Noval, M. E. Kaczmarek, A. Koide, B. A. Rodriguez-Rodriguez, P. Louie, T. Tada, T. Hattori, T. Panchenko, L. A. Romero, K. W. Teng, A. Bazley, M. de Vries, M. I. Samanovic, J. N. Weiser, I. Aifantis, , K. A. Stapleford

The paper assesses neutralization capacity and antibody titers against SARS-CoV-2 antigens in recovered healthcare workers, finding that high titers of multiple isotypes correlate with neutralization.

bioRxiv · Aug 15, 2020 · PreprintMicrobiology

Phosphorylation of the ancestral histone variant H3.3 amplifies stimulation-induced transcription

A. Armache, S. Yang, L. E. Robbins, C. Durmaz, A. W. Daman, J. Q. Jeong, A. Martinez de Paz, A. Ravishankar, T. Arslan, S. Lin, T. Panchenko, B. A. Garcia, S. Hake, H. Li, C. D. Allis, S. Z. Josefowicz

The paper identifies phosphorylation of H3.3S31 in response to pathogen sensing in macrophages and shows its role in recruiting SETD2 to enhance transcription of inflammatory genes.

bioRxiv · Oct 17, 2019 · PreprintBiochemistry