Author

G. Zenkeviciute

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 Cancer Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 2 Research Focus:drug response / drug discovery· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1 Assay:structural biology· 1

Frequent Co-Authors

L. Itzhaki· 2 shared A. H. A. Parret· 1 shared A. T. Tuukkanen· 1 shared C. S. Verma· 1 shared C. T. Chaton· 1 shared D. Eisenberg· 1 shared D. Freire· 1 shared D. Spring· 1 shared

Activity by Year

2018-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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2 shared papersCancer Biology

L. Itzhaki

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Development of Constrained Peptide Inhibitors Targeting an Oncogenic E3 Ubiquitin Ligase

G. Zenkeviciute, W. Xu, J. Iegre, H. Seki, Y. S. Tan, P. J. Rowling, F. Ferrer, C. S. Verma, D. Spring, H. Laman, L. Itzhaki

This study develops macrocyclic peptides that inhibit the Skp2-p27 interaction by binding to SCFSkp2/Cks1, reducing cell proliferation in breast cancer cells.

bioRxiv · Apr 27, 2023 · PreprintCancer Biology

Nanobodies restore stability to cancer-associated mutants of tumor suppressor protein p16INK4a

O. Burbidge, M. W. Pastok, S. L. Hodder, G. Zenkeviciute, M. E. Noble, J. A. Endicott, L. Itzhaki

This paper shows nanobodies stabilize p16INK4a mutants and restore their function by binding to a site distinct from CDK6, enabling ternary complex formation.

bioRxiv · Jul 1, 2021Biochemistry

Structural variability of EspG chaperones from mycobacterial ESX-1, ESX-3 and ESX-5 type VII secretion systems

A. T. Tuukkanen, D. Freire, S. Chan, M. A. Arbing, R. W. Reed, T. J. Evans, G. Zenkeviciute, J. Kim, S. Kahng, M. R. Sawaya, C. T. Chaton, M. Wilmanns, D. Eisenberg, A. H. A. Parret, K. V. Korotkov

The paper reports crystal and SAXS structures of EspG chaperones from mycobacterial ESX systems, revealing structural variability and potential substrate binding modes.

bioRxiv · Oct 13, 2018Biochemistry