Author

S. P. Kordon

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

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Assay:structural biology· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:drug response / drug discovery· 1 Organism:human· 1 Organism:mouse· 1

Frequent Co-Authors

D. Arac· 3 shared J. Li· 3 shared K. Leon· 2 shared R. Sando· 2 shared S. J. Bandekar· 2 shared A. A. Kossiakoff· 1 shared B. Adams· 1 shared E. Dintzner· 1 shared

Activity by Year

2020-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 34 mutual co-author links

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3 shared papersBiochemistry

D. Arac

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3 papers

Recent·Most cited

Structural basis for regulation of CELSR1 by a compact module in its extracellular region

S. J. Bandekar, K. Garbett, S. P. Kordon, E. Dintzner, J. Li, T. Shearer, R. Sando, D. Arac

This study determines the structure of the CELSR1 extracellular region and shows how specific domains form a compact module to regulate cellular adhesion.

bioRxiv · Jan 26, 2024 · PreprintBiochemistry

Isoform- and ligand-specific modulation of the adhesion GPCR ADGRL3/Latrophilin3 by a synthetic binder

S. P. Kordon, P. Dutka, J. M. Adamska, S. J. Bandekar, K. Leon, B. Adams, J. Li, A. A. Kossiakoff, D. Arac

This study develops an antibody that specifically modulates ADGRL3 function without affecting ADGRL1, demonstrating isoform- and ligand-specific aGPCR modulation.

Nature Communications · Feb 6, 2023Peer-reviewedBiochemistry

Structure of the teneurin-latrophilin complex: Alternative splicing controls synapse specificity by a novel mechanism

J. Li, Y. Xie, S. Cornelius, X. Jiang, S. P. Kordon, R. Sando, M. Pan, K. Leon, T. C. Sudhof, M. Zhao, D. Arac

The paper reports the cryo-EM structure of the Tenm2-Lphn3 complex and shows how alternative splicing regulates synapse specificity by affecting access to the Lphn-binding site.

bioRxiv · Jan 13, 2020Biochemistry