Author

K. A. Black

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Biochemistry· 2 Microbiology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Organism:bacteria (other)· 1 Research Focus:cell signaling & trafficking· 1 Assay:cryo-EM· 1 Assay:electrophysiology· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Assay:metabolomics· 1

Frequent Co-Authors

A. Glukhova· 1 shared A. Periasamy· 1 shared A. Wardak· 1 shared B. J. Smith· 1 shared C. V. Robinson· 1 shared D. Amador-Noguez· 1 shared D. Laver· 1 shared D. M. Stevenson· 1 shared

Activity by Year

2021-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

1 shared paperBiochemistry

A. Glukhova

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Cryo-EM structures of human arachidonate 12S-Lipoxygenase (12-LOX) bound to endogenous and exogenous inhibitors

J. I. Mobbs, K. A. Black, M. Tran, H. Venugopal, T. R. Holman, M. Holinstat, D. M. Thal, A. Glukhova

This study determines the cryo-EM structures of human 12-LOX, revealing its oligomeric states, catalytic mechanism, and inhibitor binding, which informs drug development.

bioRxiv · Mar 10, 2023Biochemistry

Listeria monocytogenes GlmR is an accessory uridyltransferase essential for cytosolic survival and virulence

D. Pensinger, K. V. Gutierrez, H. B. Smith, W. J. B. Vincent, D. M. Stevenson, K. A. Black, K. M. Perez-Medina, J. P. Dillard, K. Y. Rhee, D. Amador-Noguez, T. N. Huynh, J.-D. Sauer

This study identifies GlmR as an accessory uridyltransferase essential for Listeria monocytogenes cytosolic survival and virulence by synthesizing UDP-GlcNAc.

bioRxiv · Oct 27, 2021 · PreprintMicrobiology

Ion currents through Kir potassium channels are gated by anionic lipids.

R. Jin, S. He, K. A. Black, O. B. Clarke, D. Wu, J. R. Bolla, P. Johnson, A. Periasamy, A. Wardak, P. Czabotar, P. M. Colman, C. V. Robinson, D. Laver, B. J. Smith, J. M. Gulbis

The paper shows anionic lipids gate potassium conduction through Kir channels by interacting with the internal gate via fatty acyl tails.

bioRxiv · Sep 21, 2021Biochemistry