Author

A. J. Darwin

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· 4 Biochemistry· 1

Signature Assays, Organisms & Methods

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Organism:bacteria (other)· 5 Approach:experimental assay· 5 Research Focus:cell type annotation· 4 Research Focus:protein folding & dynamics· 4 Assay:proteomics· 3 Research Focus:cell signaling & trafficking· 1 Assay:protein sequence· 1

Frequent Co-Authors

M. Wang· 2 shared A. Kovach· 1 shared B. Rimal· 1 shared D. Chakraborty· 1 shared D. Srivastava· 1 shared H. Li· 1 shared H.-C. Hsu· 1 shared J. Seo· 1 shared

Activity by Year

2018-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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2 shared papersMicrobiology

M. Wang

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5 papers

Recent·Most cited

An inhibitor/anti-inhibitor system controls the activity of lytic transglycosylase MltF in Pseudomonas aeruginosa

M. Wang, S. X. Ma, A. J. Darwin

This paper identifies an inhibitor/anti-inhibitor system in Pseudomonas aeruginosa that regulates the lytic transglycosylase MltF, affecting antibiotic resistance and cell wall homeostasis.

bioRxiv · Jul 28, 2023 · PreprintMicrobiology

Pseudomonas aeruginosa C-terminal processing protease CtpA assembles into a hexameric structure that requires activation by a spiral-shaped lipoprotein binding partner

H.-C. Hsu, M. Wang, A. Kovach, A. J. Darwin, H. Li

This paper reports the structure and function of Pseudomonas aeruginosa CtpA, showing it forms an inactive hexamer that requires the spiral-shaped lipoprotein LbcA for activation and substrate delivery.

bioRxiv · Aug 9, 2021Biochemistry

Direct and indirect interactions promote complexes of the lipoprotein LbcA, the CtpA protease and its substrates, and other cell wall proteins in Pseudomonas aeruginosa

D. Chakraborty, A. J. Darwin

This study identifies LbcA as a scaffold promoting CtpA protease activity and reveals its role in facilitating proteolysis and cell wall remodeling in Pseudomonas aeruginosa.

bioRxiv · Jul 29, 2021Microbiology

The C-terminus is critical for the degradation of substrates by the Pseudomonas aeruginosa CtpA protease

S. Chung, A. J. Darwin

This paper shows that CtpA protease requires both C-terminal-dependent cleavage and C-terminal-independent complex association for substrate degradation.

bioRxiv · Mar 31, 2020Microbiology

A proteolytic complex targets multiple cell wall hydrolases in Pseudomonas aeruginosa

D. Srivastava, J. Seo, B. Rimal, S. J. Kim, A. J. Darwin

This paper identifies CtpA and its partner LbcA as a proteolytic complex in Pseudomonas aeruginosa that degrades peptidoglycan cross-link hydrolases, regulating virulence and cell wall remodeling.

bioRxiv · May 2, 2018Microbiology