Author

K. D. Patel

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· 2 Immunology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Assay:structural biology· 2 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:host-pathogen & immune response· 1 Organism:mouse· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1

Frequent Co-Authors

A. M. Gulick· 1 shared B. Pal· 1 shared C. A. Thomson· 1 shared C. A. Townsend· 1 shared E. M. Mercer· 1 shared E. van Tilburg Bernardes· 1 shared G. S. Patil· 1 shared H. R. Ramay· 1 shared

Activity by Year

2021-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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1 shared paperBiochemistry

A. M. Gulick

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Antibiotic-induced Malassezia spp. expansion in infants promotes early-life immune dysregulation and airway inflammation in mice

E. van Tilburg Bernardes, M. W. Gutierrez, W. N. T. Nguyen, E. M. Mercer, H. R. Ramay, T. Glatthardt, C. A. Thomson, T. Halim, N. Gopalakrishnan, K. Kalbfleish, K. D. Patel, K. D. McCoy, S. B. Freedman, M. C. Arrieta

bioRxiv · Apr 24, 2024 · PreprintImmunology

The structure of the monobactam-producing thioesterase domain of SulM forms a unique complex with the upstream carrier protein domain

K. D. Patel, R. A. Oliver, M. S. Lichstrahl, R. Li, C. A. Townsend, A. M. Gulick

The paper determines the structure of the thioesterase domain of SulM and its complex with the upstream carrier protein domain, revealing a constrained active site for β-lactam formation.

bioRxiv · Apr 6, 2024Biochemistry

A universal pocket in FAALs ensures redirection of fatty acid pool away from CoA-based activation

G. S. Patil, P. Kinatukara, S. Mondal, S. Shambhavi, K. D. Patel, S. Pramanik, N. Dubey, S. Narasimhan, M. K. Madduri, B. Pal, R. S. Gokhale, R. Sankaranarayanan

The paper identifies a unique binding pocket in FAALs that allows them to selectively use holo-ACP over CoA, enabling CoA-independent fatty acid activation and lipid biosynthesis.

bioRxiv · May 4, 2021Biochemistry