Author

I. T. Cadby

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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Microbiology· 5 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:protein folding & dynamics· 3 Organism:bacteria (other)· 2 Organism:E. coli· 2 Assay:protein structure· 2 Assay:structural biology· 2 Research Focus:cell type annotation· 1 Approach:genetic perturbation / CRISPR· 1

Frequent Co-Authors

A. L. Lovering· 5 shared R. W. Meek· 3 shared A. F. Cunningham· 2 shared G. Kritikos· 2 shared M. Banzhaf· 2 shared S.-S. Chng· 2 shared Z.-S. Chong· 2 shared A. Wilson· 1 shared

Activity by Year

2018-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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5 shared papersMicrobiology

A. L. Lovering

Mutual co-authors in cluster

Author profile →

6 papers

Recent·Most cited

The structure of the OmpA/Pal protein of Anaplasma phagocytophilum

I. T. Cadby

The paper presents crystal structures of the OmpA-like protein from Anaplasma phagocytophilum, revealing amino acid insertions that confer flexibility, which may be relevant for host-pathogen interactions and vaccine development.

bioRxiv · Jun 15, 2023 · PreprintMicrobiology

Asymmetric peptidoglycan editing generates the curvature of predatory bacteria, optimizing invasion and replication within a spherical prey niche

E. J. Banks, M. Valdivia-Delgado, J. Biboy, A. Wilson, I. T. Cadby, W. Vollmer, C. Lambert, A. L. Lovering, R. E. Sockett

The paper identifies Bd1075 as a peptidoglycan-editing enzyme in Bdellovibrio bacteriovorus that generates asymmetric curvature, enhancing invasion and replication within spherical prey.

bioRxiv · Jun 24, 2021 · PreprintMicrobiology

Structures of Bdellovibrio bacteriovorus phosphoglucose isomerase reveal novel rigidity in the active site of a selected subset of enzymes upon substrate binding.

R. W. Meek, I. T. Cadby, A. L. Lovering

The paper presents the structures of Bdellovibrio bacteriovorus phosphoglucose isomerase, revealing a novel mechanism of substrate binding that does not require induced-fit conformational changes.

bioRxiv · Mar 26, 2021Biochemistry

Structure-function characterization of the conserved regulatory mechanism of the Escherichia coli M48 metalloprotease BepA

J. A. Bryant, I. T. Cadby, Z.-S. Chong, Y. R. Sevastsyanovich, F. C. Morris, A. F. Cunningham, G. Kritikos, R. W. Meek, M. Banzhaf, S.-S. Chng, A. L. Lovering, I. R. Henderson

The paper presents the crystal structure of E. coli BepA, an M48 metalloprotease, and shows that its active site plug regulates function and is conserved across the family.

bioRxiv · Jul 30, 2020Microbiology

Structure-function analysis of the Escherichia coli β-barrel assembly enhancing protease BepA suggests a role for a self-inhibitory state

J. Bryant, I. T. Cadby, Z.-S. Chong, Y. Sevastsyanovich, F. Morris, A. F. Cunningham, G. Kritikos, R. W. Meek, M. Banzhaf, S.-S. Chng, I. Henderson, A. L. Lovering

This study presents the crystal structure of BepA, a protease involved in LptD folding, and shows its auto-regulation and role in maintaining outer membrane lipid asymmetry.

bioRxiv · Jul 2, 2019 · PreprintMicrobiology

The hydrolase LpqI primes mycobacterial peptidoglycan recycling.

P. J. Moynihan, I. T. Cadby, N. Veerapen, M. Jankute, M. Crosatti, G. Mukamolova, A. L. Lovering, G. S. Besra

This study shows that Mycobacterium tuberculosis and M. bovis BCG recycle peptidoglycan via the LpqI enzyme, which is essential for amino sugar recycling and affects antimicrobial resistance.

bioRxiv · Jul 4, 2018Microbiology