Author

G. K. Amarasinghe

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Microbiology· 3 Biochemistry· 2 Bioengineering· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 5 Research Focus:host-pathogen & immune response· 5 Organism:human· 2 Assay:proteomics· 2 Approach:biophysical modeling· 1 Approach:deep learning· 1 Research Focus:drug response / drug discovery· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

C. F. Basler· 2 shared D. W. Leung· 2 shared G. R. Bowman· 2 shared M. L. Gross· 2 shared S. Miersch· 2 shared A. B. Moyle· 1 shared A. Caruso· 1 shared A. Hachim· 1 shared

Activity by Year

2020-2021 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

2 shared papersBiochemistry

C. F. Basler

Mutual co-authors in cluster

Author profile →

6 papers

Recent·Most cited

Ultrapotent and Broad Neutralization of SARS-CoV-2 Variants by Modular, Tetravalent, Bi-paratopic Antibodies

S. Miersch, R. Saberianfar, C. Chen, N. Sharma, G. K. Amarasinghe, F. Caccuri, A. Zani, A. Caruso, G. Novelli, S. S. Sidhu

This study develops a tetravalent antibody format that neutralizes SARS-CoV-2 variants with high potency and breadth, surpassing conventional bivalent antibodies.

bioRxiv · Nov 2, 2021Bioengineering

Intrinsically disordered pathogen effector alters the STAT1 dimer to prevent recruitment of co-transcriptional activators CBP/p300

Z. Huang, H. Liu, J. Nix, C. R. Knoverek, G. R. Bowman, G. K. Amarasinghe, L. D. Sibley

This study identifies how the parasite Toxoplasma gondii uses the disordered protein TgIST to block STAT1-mediated gene expression by altering STAT1 dimer conformation and preventing activator recruitment.

bioRxiv · Aug 9, 2021 · PreprintMicrobiology

Characterization of SARS-CoV-2 N protein reveals multiple functional consequences of the C-terminal domain

C. Wu, A. J. Qavi, A. Hachim, N. Kavian, A. R. Cole, A. B. Moyle, N. D. Wagner, J. Sweeney-Gibbons, H. W. Rohrs, M. L. Gross, J. S. M. Peiris, C. F. Basler, C. W. Farnsworth, S. A. Valkenburg, G. K. Amarasinghe, D. W. Leung

This study characterizes the SARS-CoV-2 N protein, identifying domain-specific functions and highlighting the C-terminal domain's immunogenicity for diagnostic applications.

bioRxiv · Nov 30, 2020Biochemistry

Non-canonical proline-tyrosine interactions with multiple host proteins regulate Ebola virus infection

J. Batra, M. Anantpadma, G. I. Small, O. Shtanko, M. Zhang, D. Liu, C. G. Williams, N. Biedenkopf, S. Becker, M. L. Gross, D. W. Leung, R. A. Davey, G. K. Amarasinghe, N. J. Krogan, C. F. Basler

This study identifies non-canonical proline-tyrosine interactions in the Ebola virus VP30 protein that regulate viral replication by interacting with multiple host proteins.

bioRxiv · May 19, 2020Microbiology

Neutralizing antibody and soluble ACE2 inhibition of a replication-competent VSV-SARS-CoV-2 and a clinical isolate of SARS-CoV-2.

J. B. Case, P. W. Rothlauf, R. E. Chen, Z. Liu, H. Zhao, A. S. Kim, L.-M. Bloyet, Q. Zeng, S. Tahan, L. Droit, M. X. G. Ilagan, M. A. Tartell, G. K. Amarasinghe, J. P. Henderson, S. Miersch, , S. P. J. Whelan

This study develops two neutralization assays for SARS-CoV-2 using VSV and a clinical isolate, showing high concordance between monoclonal, polyclonal antibodies, and ACE2-Fc in neutralizing activity.

bioRxiv · May 18, 2020Microbiology

A cryptic pocket in Ebola VP35 allosterically controls RNA binding

M. A. Cruz, T. E. Frederick, U. L. Mallimadugula, S. Singh, N. Vithani, M. I. Zimmerman, J. R. Porter, K. E. Moeder, G. K. Amarasinghe, G. R. Bowman

This study identifies a cryptic pocket in Ebola VP35 that allosterically controls RNA binding, validated through simulations, experiments, and drug-like modifications.

bioRxiv · Feb 9, 2020Biochemistry