Author

M. A. Lemmon

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 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:human· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Organism:Drosophila· 1 Assay:fluorescence / live-cell microscopy· 1 Research Focus:host-pathogen & immune response· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

A. Kiyatkin· 2 shared C. Hu· 2 shared S. E. Stayrook· 2 shared A. Li· 1 shared A. Sommer· 1 shared C. A. Leche· 1 shared C. M. Smith· 1 shared D. J. Schodt· 1 shared

Activity by Year

2021-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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2 shared papersBiophysics

A. Kiyatkin

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Distinct interactions stabilize EGFR dimers and higher-order oligomers in cell membranes

K. C. Mudumbi, E. A. Burns, D. J. Schodt, Z. O. Petrova, A. Kiyatkin, L. W. Kim, E. M. Mangiacapre, I. Ortiz-Caraveo, H. R. Ortiz, C. Hu, K. D. Ashtekar, K. A. Lidke, D. Lidke, M. A. Lemmon

This study investigates how EGFR dimers and higher-order oligomers form and interact in cell membranes using SPT and FRET, revealing the role of the tyrosine kinase domain in oligomerization.

bioRxiv · Apr 10, 2023Biophysics

Phosphatidylserine binding regulates TIM-3 effects on T cell receptor signaling

C. M. Smith, A. Li, N. Krishnamurthy, M. A. Lemmon

This study shows TIM-3 promotes NF-κB signaling and IL-2 secretion in Jurkat cells through phosphatidylserine binding, clarifying its role as a co-stimulatory receptor.

bioRxiv · May 7, 2021 · PreprintBiochemistry

Glioblastoma mutations impair ligand discrimination by EGFR

C. Hu, C. A. Leche, A. Kiyatkin, S. E. Stayrook, K. M. Ferguson, M. A. Lemmon

This study shows that GBM mutations in EGFR disrupt ligand discrimination by altering dimer structure and stability, leading to aberrant signaling.

bioRxiv · May 4, 2021 · PreprintBiochemistry

ROR and RYK extracellular region structures suggest that receptor tyrosine kinases have distinct WNT-recognition modes

F. Shi, J. M. Mendrola, J. B. Sheetz, N. Wu, A. Sommer, K. F. Speer, J. N. Noordermeer, Z.-Y. Kan, K. Perry, S. W. Englander, S. E. Stayrook, L. G. Fradkin, M. A. Lemmon

The paper presents crystal structures of Drosophila ROR and RYK orthologs, revealing distinct WNT-recognition mechanisms through their extracellular domains.

bioRxiv · Apr 29, 2021Biochemistry