Author

L. Malinauskaite

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· 1 Biophysics· 1

Signature Assays, Organisms & Methods

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

Frequent Co-Authors

A. Eguskiza· 1 shared A. Kotecha· 1 shared A. R. Aricescu· 1 shared A. Sente· 1 shared C. M. T. Neumann· 1 shared D. Focht· 1 shared D. Karia· 1 shared D. Y. Chirgadze· 1 shared

Activity by Year

2020-2020 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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1 shared paperBiochemistry

A. Eguskiza

Mutual co-authors in cluster

Author profile →

2 papers

Recent·Most cited

Single-particle cryo-EM at atomic resolution

T. Nakane, A. Kotecha, A. Sente, G. McMullan, S. Masiulis, P. M. G. E. Brown, I. T. Grigoras, L. Malinauskaite, T. Malinauskas, J. Miehling, L. Yu, D. Karia, E. V. Pechnikova, E. de Jong, J. Keizer, , S. Scheres

This paper demonstrates achieving atomic resolution cryo-EM structures for membrane proteins and apo-ferritin using advanced hardware, enabling detailed structural analysis and hydrogen bonding visualization.

Nature · Oct 21, 2020Peer-reviewedBiophysics

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