Author

J. Lyons

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· 2 Cell Biology· 1 Plant Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Approach:statistical model· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:protein folding & dynamics· 2 Organism:Arabidopsis· 1 Organism:bacteria (other)· 1 Assay:bulk RNA-seq· 1 Assay:cryo-EM· 1

Frequent Co-Authors

C. M. T. Neumann· 2 shared P. Nissen· 2 shared A. Berroyer· 1 shared A. Eguskiza· 1 shared B. Ismail· 1 shared C. G. O'Brien· 1 shared C. Gallaher· 1 shared D. Focht· 1 shared

Activity by Year

2019-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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2 shared papersBiochemistry

C. M. T. Neumann

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Author profile →

4 papers

Recent·Most cited

Dual Mechanism of Action: Exosomes from Human iPSC-Cardiomyocytes and Mesenchymal Stem Cells Restore Injured Myocardium

E. Tzng, N. A. Bayardo, G. Ikeda, H. Takashima, J. Lyons, M. Bennett, C. G. O'Brien, P. C. Yang

This study shows that exosomes from human iPSC-cardiomyocytes and mesenchymal stem cells improve heart function after myocardial infarction in pigs, with distinct miRNA mechanisms.

bioRxiv · May 29, 2024 · PreprintCell Biology

Cryo-EM structure of the human NKCC1 transporter reveals mechanisms of ion coupling and specificity

C. M. T. Neumann, L. L. Rosenbaek, R. K. Flygaard, M. Habeck, J. L. Karlsen, Y. Wang, K. Lindorff-Larsen, H. H. Gad, R. Hartmann, J. Lyons, R. A. Fenton, P. Nissen

The paper presents a cryo-EM structure of human NKCC1, revealing ion binding sites and mechanisms of ion coupling and specificity.

bioRxiv · Nov 11, 2021Biochemistry

Role of transmembrane helix 6 in substrate recognition of the amino acid transporter MhsT

P. Nissen, M. Quick, R. Blunck, J. Lyons, C. M. T. Neumann, D. Focht, J. A. Javitch, A. Eguskiza, L. Malinauskaite, I. O. Schwarz

The paper investigates how the flexibility of a GMG motif in TM6 of MhsT enables substrate recognition of different amino acid sizes by shaping the binding site.

bioRxiv · Apr 3, 2020 · PreprintBiochemistry

Progress toward the identification and stacking of crucial domestication traits in pennycress

R. Chopra, E. B. Johnson, R. Emenecker, E. Cahoon, J. Lyons, D. J. Kliebenstein, E. Daniels, K. Dorn, M. Esfahanian, N. Folstad, K. Frels, M. McGinn, M. Ott, C. Gallaher, K. Altendorf, , M. D. Marks

This study identifies key domestication traits in pennycress and develops molecular markers to stack them into individual lines.

bioRxiv · Apr 16, 2019Plant Biology