Author

T. Shafi

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· 3 Microbiology· 1

Signature Assays, Organisms & Methods

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Assay:cryo-EM· 3 Approach:experimental assay· 3 Research Focus:protein structure prediction· 3 Organism:Drosophila· 1 Research Focus:drug response / drug discovery· 1 Organism:human· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

A. Barbieri· 2 shared R. C. Ford· 2 shared R. F. Collins· 2 shared A. M. Brzozowski· 1 shared A. Siebert· 1 shared C. M. Viola· 1 shared H. T. Jenkins· 1 shared N. Thonghin· 1 shared

Activity by Year

2018-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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2 shared papersBiochemistry

A. Barbieri

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Author profile →

4 papers

Recent·Most cited

Structural Conservation of Insulin/IGF Signalling Axis at the Insulin Receptors Level in Drosophila and Humans

C. M. Viola, O. Frittmann, H. T. Jenkins, T. Shafi, P. De Meyts, A. M. Brzozowski

This study presents the cryoEM structure of the Drosophila insulin receptor (dmIR) complex with DILP5, showing structural homology to human IRs and dmIR-specific features.

bioRxiv · Feb 17, 2023 · PreprintBiochemistry

Structure of ABCB1/P-glycoprotein bound to the CFTR potentiator ivacaftor.

A. Barbieri, N. Thonghin, T. Shafi, S. M. Prince, R. F. Collins, R. C. Ford

This study determines the structure of ABCB1/P-glycoprotein bound to ivacaftor and compares it to the drug-free state to understand binding mechanisms and conformational changes.

bioRxiv · Jun 11, 2021 · PreprintBiochemistry

Kite-shaped molecules block SARS-CoV-2 cell entry at a post-attachment step

S.-W. Chan, T. Shafi, R. Ford

The paper screens FDA-approved compounds to find SARS-CoV-2 inhibitors, identifying kite-shaped molecules that block viral entry after attachment.

bioRxiv · May 29, 2021Microbiology

Novel features in the structure of P-glycoprotein (ABCB1) in the post-hydrolytic state as determined at 7.9A resolution

N. Thongin, R. F. Collins, A. Barbieri, T. Shafi, A. Siebert, R. C. Ford

This study reports novel structural features of P-glycoprotein in the post-hydrolytic state using cryo-EM at 7.9Å resolution, revealing conformational changes and implications for drug transport and resistance.

bioRxiv · Apr 25, 2018Biochemistry