Author

M. Day

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· 2 Microbiology· 1 Pathology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Organism:human· 4 Research Focus:cell signaling & trafficking· 3 Research Focus:cell type annotation· 3 Assay:proteomics· 3 Approach:statistical model· 3 Approach:biophysical modeling· 2 Research Focus:chromatin & epigenetic regulation· 2

Frequent Co-Authors

A. Oliver· 3 shared L. H. Pearl· 3 shared A. Herbert· 1 shared A. W. Oliver· 1 shared B. Liu· 1 shared D. Boos· 1 shared D. J. Ingle· 1 shared E. Karanika· 1 shared

Activity by Year

2018-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 7 mutual co-author links

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3 shared papersBiochemistry

A. Oliver

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Author profile →

7 papers

Recent·Most cited

Centromere protection requires strict mitotic inactivation of the Bloom syndrome helicase complex

M. Fernandez-Casanas, E. Karanika, T. Olukoga, A. Herbert, U. Aliyaskarova, M. Day, K.-L. Chan

This study identifies a centromere protection pathway in human mitotic cells that relies on strict mitotic inactivation of the BTRR complex through phosphorylation and kinase regulation.

bioRxiv · May 21, 2024Cell Biology

Metabolomics and transcriptomics reveal the response mechanisms of Mikania micrantha to Puccinia spegazzinii infection

B. Liu, X. Ren, G. Zhang, Y. Gu, M. Jin, M. Day, H. Liu, W. Qian

This study investigates how Mikania micrantha responds to Puccinia spegazzinii infection using metabolomics and transcriptomics, identifying changes in metabolites and gene expression.

bioRxiv · Jun 10, 2022Pathology

Structure of the human RAD17-RFC clamp loader and 9-1-1 checkpoint clamp bound to a dsDNA-ssDNA junction

M. Day, A. Oliver, L. H. Pearl

The paper determines the structure of the human RAD17-RFC clamp loader complex bound to 9-1-1 and a dsDNA-ssDNA junction, explaining specificity and orientation mechanisms.

bioRxiv · Mar 11, 2022Biochemistry

Structural basis for recruitment of the CHK1 DNA damage kinase by the CLASPIN scaffold protein

M. Day, S. L. Parry-Morris, J. Houghton-Gisby, A. W. Oliver, L. H. Pearl

This study determines the crystal structure of CHK1 kinase domain bound to a CLASPIN motif, revealing its role as a scaffold for CHK1 activation by ATR.

bioRxiv · Oct 2, 2020Biochemistry

Informal genomic surveillance of regional distribution of Salmonella Typhi genotypes and antimicrobial resistance via returning travellers

D. J. Ingle, S. Nair, H. Hartman, P. M. Ashton, Z. A. Dyson, M. Day, J. Freedman, M. A. Chattaway, K. E. Holt, T. J. Dallman

This study uses whole-genome sequencing of Salmonella Typhi isolates from travelers to analyze genotype distribution and antimicrobial resistance patterns across regions.

bioRxiv · Jan 3, 2019Microbiology

Phosphorylation-mediated interactions with TOPBP1 couple 53BP1 and 9-1-1 to control the G1 DNA damage checkpoint

L. H. Pearl, N. Bigot, M. Day, R. A. Baldock, F. Z. Watts, A. Oliver

This study identifies a phosphorylation-dependent interaction between 53BP1 and TOPBP1 that is critical for the G1 DNA damage checkpoint by recruiting ATR and CHK1 to damage foci.

bioRxiv · Jan 2, 2019Cell Biology

N-terminal BRCT domains of the DNA damage checkpoint proteins TOPBP1/Rad4 display distinct specificities for phosphopeptide ligands

M. Day, M. Rappas, K. Ptasinska, D. Boos, A. Oliver, L. Pearl

The paper defines the specificity of N-terminal BRCT domains in TOPBP1/Rad4 for phosphopeptide ligands through structural and biochemical analysis of their interactions with various proteins.

bioRxiv · Jul 13, 2018Biochemistry