Author

T. P. Schrank

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

Cell Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Assay:bulk RNA-seq· 2 Organism:human· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:drug response / drug discovery· 1 Approach:experimental assay· 1 Approach:genetic perturbation / CRISPR· 1 Research Focus:host-pathogen & immune response· 1 Assay:proteomics· 1

Frequent Co-Authors

D. Goldfarb· 2 shared K. M. Lapak· 2 shared M. B. Major· 2 shared M. J. Agajanian· 2 shared A. E. Hale· 1 shared A. Horani· 1 shared A. L. Bailey· 1 shared B. E. Weissman· 1 shared

Activity by Year

2019-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 36 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 papersMicrobiology

D. Goldfarb

Mutual co-authors in cluster

Author profile →

2 papers

Recent·Most cited

Systematic analysis of SARS-CoV-2 infection of an ACE2-negative human airway cell

M. Puray-Chavez, K. M. Lapak, T. P. Schrank, J. L. Elliott, D. P. Bhatt, M. J. Agajanian, R. Jasuja, D. Q. Lawson, K. Davis, P. W. Rothlauf, H. Jo, N. Lee, K. Tenneti, J. E. Eschbach, C. Shema Mugisha, , S. B. Kutluay

This study identifies H522 cells as ACE2-negative human cells permissive to SARS-CoV-2 infection, revealing alternative receptor usage and host response mechanisms.

bioRxiv · Mar 1, 2021Microbiology

Gain-of-function genetic screen of the kinome reveals BRSK2 as an inhibitor of the NRF2 transcription factor

T. Y. Tamir, B. M. Bowman, M. J. Agajanian, D. Goldfarb, T. P. Schrank, T. Stohrer, A. E. Hale, P. F. Siesser, S. J. Weir, R. M. Murphy, K. M. LaPak, B. E. Weissman, N. J. Moorman, M. B. Major

The paper identifies BRSK2 as a negative regulator of NRF2 by inhibiting protein synthesis through mTOR downregulation, suggesting it as a potential therapeutic target for NRF2-related diseases.

bioRxiv · Nov 5, 2019Cell Biology