Author

J. Garnett

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· 3 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Organism:bacteria (other)· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1

Frequent Co-Authors

A. Fornili· 3 shared K. Richardson· 2 shared N. Cianciotto· 2 shared R. Shaw· 2 shared S. Rehman· 2 shared T. Portlock· 2 shared A. Antonovic· 1 shared A. Oregioni· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 34 mutual co-author links

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3 shared papersMicrobiology

A. Fornili

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

The Legionella collagen-like protein employs a unique binding mechanism for the recognition of host glycosaminoglycans

S. Rehman, A. Antonovic, I. McIntire, H. Zheng, L. Cleaver, C. Adams, T. Portlock, K. Richardson, R. Shaw, A. Oregioni, G. Mastroianni, S. Whittaker, G. Kelly, A. Fornili, N. Cianciotto, J. Garnett

This study determines the crystal structure of Legionella collagen-like protein and reveals its unique binding mechanism for sulphated glycosaminoglycans.

bioRxiv · Dec 10, 2023 · PreprintMicrobiology

N4BP1 is dimerization-dependent linear ubiquitin reader regulating TNFR1 signalling through linear ubiquitin binding and Caspase-8-mediated processing

K. W. Kliza, W. Song, I. Pinzuti, S. Schaubeck, S. Kunzelmann, D. Kuntin, A. Fornili, A. Pandini, K. Hofmann, J. Garnett, B. Stieglitz, K. Husnjak

This study identifies N4BP1 as a dimerization-dependent linear ubiquitin reader that regulates TNFR1 signaling by modulating NF-κB and apoptosis pathways.

bioRxiv · Nov 2, 2021 · PreprintBiochemistry

Discovery of a new Neisseria gonorrhoeae Type IV pilus assembly factor, TfpC

L. I. Hu, S. Yin, E. A. Ozer, L. Sewell, S. Rehman, J. Garnett, H. S. SEIFERT

This paper identifies TfpC as a new Neisseria gonorrhoeae protein essential for stabilizing Type IV pili in their extended form, with orthologs in other bacteria.

bioRxiv · Sep 26, 2020Microbiology

Structure and functional analysis of the Legionella chitinase ChiA reveals a novel mechanism of metal-dependent mucin degradation

K. Richardson, L. Grigoryeva, P. Corsini, R. White, R. Shaw, T. Portlock, B. Dorgan, A. Fornili, N. Cianciotto, J. Garnett

This study characterizes the structure and function of Legionella pneumophila's chitinase ChiA, revealing its role in mucin degradation and bacterial pathogenesis.

PLOS Pathogens · May 4, 2020Peer-reviewedMicrobiology