Author

J. K. K. Low

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· 4 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Organism:human· 3 Assay:protein structure· 2 Research Focus:protein structure prediction· 2 Assay:proteomics· 2 Research Focus:cell type annotation· 1 Assay:CRISPR screen· 1 Approach:deep learning· 1

Frequent Co-Authors

J. P. Mackay· 3 shared K. Patel· 2 shared R. J. Payne· 2 shared A. Aggarwal· 1 shared A. E. Whitten· 1 shared A. J. Cole· 1 shared A. J. Oakley· 1 shared A. Norman· 1 shared

Activity by Year

2018-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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3 shared papersBiochemistry

J. P. Mackay

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Author profile →

5 papers

Recent·Most cited

Cross-linking mass spectrometry discovers, evaluates, and validates the experimental and predicted structural proteome

T. K. Bartolec, X. Vazquez-Campos, A. Norman, C. Luong, R. J. Payne, M. R. Wilkins, J. P. Mackay, J. K. K. Low

The paper combines cross-linking mass spectrometry with AI-based structure prediction to discover and validate protein and complex structures at proteome scale.

bioRxiv · Nov 16, 2022 · PreprintBiochemistry

Fibroblast-expressed LRRC15 suppresses SARS-CoV-2 infection and controls antiviral and antifibrotic transcriptional programs.

L. Loo, M. A. Waller, C. L. Moreno, A. J. Cole, A. O. Stella, O.-T. Pop, A.-K. Jochum, O. H. Ali, C. E. Denes, Z. Hamoudi, F. Chung, A. Aggarwal, J. K. K. Low, K. Patel, R. Siddique, , G. G. Neely

This study identifies LRRC15 as a host factor that suppresses SARS-CoV-2 infection and regulates antiviral and antifibrotic transcriptional programs in fibroblasts.

bioRxiv · Nov 9, 2021 · PreprintCell Biology

Unique Protein Interaction Networks Define The Chromatin Remodeling Module of The NuRD Complex

M. Sharifi Tabar, C. Giardina, Y. Feng, H. Francis, H. Moghaddassani, J. K. K. Low, J. P. Mackay, C. G. Bailey, J. E. J. Rasko

The paper identifies paralogue-specific protein interactions of the MGCC module in the NuRD complex, revealing mechanisms for functional specificity and integration into other complexes.

bioRxiv · Jan 27, 2021Biochemistry

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

Identification of a novel tetrameric structure for human apolipoprotein-D

C. S. Kielkopf, J. K. K. Low, Y.-F. Mok, S. Bhatia, T. Palasovski, A. J. Oakley, A. E. Whitten, B. Garner, S. H. J. Brown

This study identifies a tetrameric structure of human apolipoprotein-D in breast cyst fluid, contrasting with its monomeric or higher-order forms in other biological fluids.

bioRxiv · May 31, 2018Biochemistry