Author

C. M. T. Neumann

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Biochemistry· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:bacteria (other)· 2 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Research Focus:protein structure prediction· 2 Approach:statistical model· 2 Research Focus:cell signaling & trafficking· 1 Assay:cryo-EM· 1

Frequent Co-Authors

P. Nissen· 4 shared D. Focht· 2 shared J. Lyons· 2 shared A. Eguskiza· 1 shared E. Meldgaard Hogh Quistgaard· 1 shared H. H. Gad· 1 shared I. O. Schwarz· 1 shared J. A. Javitch· 1 shared

Activity by Year

2020-2022 · peak 2/yr

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10 top collaborators · 23 mutual co-author links

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4 shared papersBiochemistry

P. Nissen

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4 papers

Recent·Most cited

Variations of a theme - crystal forms of the amino acid transporter MhsT

C. M. T. Neumann, D. Focht, S. Trampari, J. A. Lyons, P. Nissen

The paper reports on the crystallization of MhsT with different substrates, revealing varied crystal packing arrangements and challenges in structure determination due to crystal imperfections.

bioRxiv · May 3, 2022Biochemistry

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

The crystal structure of the Ca2+-ATPase 1 from Listeria monocytogenes reveals a pump primed for dephosphorylation

S. Basse Hansen, M. Dyla, C. M. T. Neumann, E. Meldgaard Hogh Quistgaard, J. Lauwring Andersen, M. Kjaergaard, P. Nissen

The paper presents crystal structures of LMCA1, revealing its primed state for dephosphorylation and a single Ca2+-binding site, with insights into its transport mechanism.

bioRxiv · Jun 23, 2020Biochemistry

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