Author

L. J. Walport

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· 5

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:drug response / drug discovery· 3 Assay:proteomics· 3 Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Assay:protein structure· 2 Approach:deep learning· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

H. Suga· 4 shared K. Patel· 3 shared R. J. Payne· 3 shared T. Passioura· 3 shared A. Norman· 2 shared J. P. Mackay· 2 shared P. Solomon· 2 shared A. J. Powell· 1 shared

Activity by Year

2019-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 28 mutual co-author links

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4 shared papersBiochemistry

H. Suga

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5 papers

Recent·Most cited

mRNA display in cell lysates enables identification of cyclic peptides targeting the BRD3 extraterminal domain

C. A. Hurd, J. Bush, A. J. Powell, L. J. Walport

The paper describes a method to identify cyclic peptides targeting the BRD3 extraterminal domain using mRNA display in cell lysates, expanding the scope of target proteins for screening.

bioRxiv · Mar 20, 2024Biochemistry

A cyclic peptide toolkit reveals mechanistic principles of peptidylarginine deiminase IV (PADI4) regulation

M. T. Bertran, R. Walmsley, T. F. M. Cummings, I. Aramburu, D. J. Benton, J. Assalaarachchi, M. Chasampalioti, T. Swanton, D. Joshi, S. Federico, H. Okkenhaug, L. Yu, D. Oxley, S. Walker, V. Papayannopoulos, , L. J. Walport

The paper develops cyclic peptide modulators of PADI4 and reveals their mechanism of action and cellular activity.

bioRxiv · Dec 12, 2023Biochemistry

mRNA display reveals a class of high-affinity bromodomain-binding motifs that are not found in the human proteome

J. K. Low, K. Patel, P. Solomon, A. Norman, P. Pachl, N. Jones, R. J. Payne, T. Passioura, H. Suga, L. J. Walport, J. Mackay

The paper uses mRNA display to identify high-affinity bromodomain-binding motifs not present in the human proteome, revealing novel binding modes and suggesting evolutionary pressure against strong binders.

bioRxiv · May 17, 2023Biochemistry

Discovery and characterization of cyclic peptides selective for the C-terminal bromodomains of BET family proteins

C. Franck, K. Patel, L. J. Walport, M. T. Christie, A. Norman, T. Passioura, R. J. Payne, H. Suga, J. P. Mackay

The paper discovers and characterizes cyclic peptides that selectively bind to the C-terminal bromodomains of BET family proteins, showing high potency and paralogue-specificity.

bioRxiv · Dec 25, 2022Biochemistry

Cyclic peptides can engage a single binding pocket through multiple, entirely divergent modes

K. Patel, L. J. Walport, J. L. Walshe, P. Solomon, J. K. K. Low, D. H. Tran, K. S. Mouradian, A. P. G. Silva, L. Wilkinson-White, J. M. Matthews, J. M. Guss, R. J. Payne, T. Passioura, H. Suga, J. P. Mackay

The paper identifies high-affinity, specific cyclic peptide inhibitors of BET bromodomains using RaPID screening, revealing diverse binding modes and structures.

bioRxiv · Nov 21, 2019Biochemistry