Author

K. E. McNally

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 Cell Biology· 1

Signature Assays, Organisms & Methods

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Assay:proteomics· 4 Research Focus:cell signaling & trafficking· 3 Approach:experimental assay· 3 Approach:deep learning· 1 Research Focus:development & morphogenesis· 1 Organism:E. coli· 1 Organism:human· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

E. Derivery· 2 shared M. D. Healy· 2 shared P. J. Cullen· 2 shared A. Bittleston· 1 shared A. Broerman· 1 shared A. P. Walker· 1 shared B. Collins· 1 shared B. M. Collins· 1 shared

Activity by Year

2021-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

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2 shared papersBiochemistry

E. Derivery

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Mechanism and regulation of cargo entry into the Commander recycling pathway

R. Butkovic, A. P. Walker, M. D. Healy, K. E. McNally, M. Liu, K. Kato, B. M. Collins, P. J. Cullen

The paper identifies the mechanism by which SNX17 cargo is selected for entry into the Commander recycling pathway through direct binding to the Retriever sub-complex.

bioRxiv · Jan 10, 2024 · PreprintCell Biology

Elongator is a microtubule polymerase selective for poly-glutamylated tubulin

V. J. Planelles-Herrero, M. Genova, A. Bittleston, K. E. McNally, G. Degliesposti, M. M. Magiera, C. Janke, E. Derivery

This paper identifies Elongator's role in stabilizing microtubules by selectively binding polyglutamylated tubulin, contributing to cell fate determination during asymmetric division.

bioRxiv · May 10, 2023 · PreprintBiochemistry

De novo design of modular peptide binding proteins by superhelical matching

K. Wu, H. Bai, Y.-T. Chang, R. Redler, K. E. McNally, W. Sheffler, T. Brunette, D. R. Hicks, T. E. Morgan, T. J. Stevens, A. Broerman, I. Goreshnik, M. DeWitt, C. M. Chow, Y. Shen, , D. Baker

This paper introduces a method to design modular peptide binding proteins that bind repeating peptide sequences with high specificity and affinity.

bioRxiv · Nov 14, 2022 · PreprintBiochemistry

Proteomic identification and structural basis for the interaction between sorting nexin SNX17 and PDLIM family proteins

M. D. Healy, J. Sacharz, K. E. McNally, C. McConville, V. Tillu, R. J. Hall, M. Chilton, P. J. Cullen, M. Mobli, R. Ghai, D. A. Stroud, B. Collins

The paper identifies the structural basis of the interaction between SNX17 and PDLIM family proteins, revealing a specific PDZ binding motif and unique electrostatic contacts.

bioRxiv · Jul 29, 2021Biochemistry