Author

D. R. Goodlett

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· 3 Organism:bacteria (other)· 2 Assay:metabolomics· 2 Organism:C. elegans· 1 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Approach:deep learning· 1 Organism:E. coli· 1

Frequent Co-Authors

A. Mikhael· 2 shared D. Smith· 2 shared H. Petrosova· 2 shared R. K. Ernst· 2 shared A. F. Azad· 1 shared A. M. Deutschbauer· 1 shared B. L. Oyler· 1 shared D. Hardie· 1 shared

Activity by Year

2022-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

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2 shared papersMicrobiology

A. Mikhael

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Lipid A double bond position determination using ozone and laser-induced dissociation

A. Mikhael, H. Petrosova, D. Smith, R. K. Ernst, D. R. Goodlett

This study determines the double bond position in Lipid A using ozone treatment on MALDI plates combined with tandem MS.

bioRxiv · Feb 15, 2024Microbiology

Structural Elucidation of Intact Rough-Type Lipopolysaccharides using Field Asymmetric Ion Mobility Spectrometry and Kendrick Mass Defect Plots

A. Mikhael, D. Hardie, D. Smith, H. Petrosova, R. K. Ernst, D. R. Goodlett

This paper uses FAIMS and Kendrick mass defect plots to characterize the structural diversity of R-type lipopolysaccharides from E. coli J5.

bioRxiv · Jun 21, 2023Biochemistry

Rickettsia typhi peptidoglycan mapping with data-dependent tandem mass spectrometry

B. L. Oyler, K. E. Rennoll-Bankert, V. I. Verhoeve, M. S. Rahman, A. F. Azad, J. J. Gillespie, D. R. Goodlett

This study maps the peptidoglycan structure of Rickettsia typhi using mass spectrometry, revealing muropeptide subunits with elongated alanine residues, similar to other Gram-negative bacteria.

bioRxiv · Mar 10, 2022 · PreprintMicrobiology

Caulobacter requires anionic sphingolipids and deactivation of fur to lose lipid A

J. J. Zik, S. H. Yoon, Z. Guan, G. S. Skidmore, R. R. Gudoor, K. M. Davies, A. M. Deutschbauer, D. R. Goodlett, E. A. Klein, K. R. Ryan

This study identifies that Caulobacter requires anionic sphingolipids and deactivation of Fur to survive without lipid A in its outer membrane.

bioRxiv · Jan 20, 2022 · PreprintMicrobiology