Author

I. Deshpande

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· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein structure prediction· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:drug response / drug discovery· 1 Organism:human· 1 Assay:protein structure· 1 Assay:proteomics· 1

Frequent Co-Authors

A. Manglik· 2 shared G. E. Merz· 2 shared H. T. Kratochvil· 2 shared J. Liang· 2 shared N. Hoppe· 2 shared A. A. Anand· 1 shared A. Aimon· 1 shared A. C. Thwin· 1 shared

Activity by Year

2020-2024 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 26 mutual co-author links

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2 shared papersBiochemistry

A. Manglik

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Author profile →

4 papers

Recent·Most cited

GPR161 structure uncovers the redundant role of sterol-regulated ciliary cAMP signaling in the Hedgehog pathway

N. Hoppe, S. Harrison, S.-H. Hwang, Z. Chen, M. Karelina, I. Deshpande, C.-M. Suomivuori, V. R. Palicharla, S. P. Berry, P. Tschaikner, D. Regele, D. F. Covey, E. Stefan, D. S. Marks, J. Reiter, , A. Manglik

The paper determines the cryo-EM structure of active GPR161 bound to Gs, revealing sterol binding and its role in ciliary cAMP signaling, while showing that sterol binding is not essential for Hedgehog pathway suppression.

Nature Structural & Molecular Biology · Feb 7, 2024Peer-reviewedBiochemistry

Fragment binding to the Nsp3 macrodomain of SARS-CoV-2 identified through crystallographic screening and computational docking

M. Schuller, G. J. Correy, S. Gahbauer, D. Fearon, T. Wu, R. E. Diaz, I. D. Young, L. Carvalho Martins, D. H. Smith, U. Schulze-Gahmen, T. W. Owens, I. Deshpande, G. E. Merz, A. C. Thwin, J. T. Biel, , Smi

The paper identifies new chemical fragments binding to the SARS-CoV-2 Nsp3 macrodomain through crystallographic screening and computational docking, validating their binding with biophysical techniques.

bioRxiv · Nov 24, 2020Biochemistry

An ultra-potent synthetic nanobody neutralizes SARS-CoV-2 by locking Spike into an inactive conformation

M. Schoof, B. Faust, R. A. Saunders, S. Sangwan, V. V. Rezelj, N. Hoppe, M. Boone, C. Billesboelle, C. Puchades, C. M. Azumaya, H. T. Kratochvil, M. Zimanyi, I. Deshpande, J. Liang, S. Dickinson, , Barile-H

This paper develops a potent synthetic nanobody that neutralizes SARS-CoV-2 by locking its Spike protein in an inactive conformation, enabling aerosol delivery as a prophylactic or therapeutic agent.

bioRxiv · Aug 8, 2020Biochemistry

Smoothened Transduces Hedgehog Signals via Activity-Dependent Sequestration of PKA Catalytic Subunits

C. D. Arveseth, J. T. Happ, D. S. Hedeen, J.-F. Zhu, J. L. Capener, D. K. Shaw, I. Deshpande, J. Liang, J. Xu, S. L. Stubben, I. B. Nelson, M. F. Walker, N. J. Krogan, D. J. Grunwald, R. Hüttenhain, , B. R. Myers

This study reveals that Smoothened (SMO) activates GLI transcription factors by sequestering PKA catalytic subunits at the membrane, bypassing traditional GPCR signaling mechanisms.

bioRxiv · Jul 1, 2020Biochemistry