Author

J. J. Kohler

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· 3 Cell Biology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 4 Assay:proteomics· 4 Organism:human· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:cell type annotation· 2 Research Focus:cell-cell communication· 1 Research Focus:differential expression· 1

Frequent Co-Authors

P. Azadi· 2 shared R. S. R. Konada· 2 shared A. Boucher· 1 shared A. Broussard· 1 shared A. C. Ghorashi· 1 shared A. Florwick· 1 shared A. Kalimurthy· 1 shared A. M. Wands· 1 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 15 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

2 shared papersBiochemistry

P. Azadi

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Fucosylated glycoproteins and fucosylated glycolipids play opposing roles in cholera intoxication

A. C. Ghorashi, A. Boucher, S. A. Archer-hartmann, N. B. Murray, R. S. R. Konada, X. Zhang, C. Xing, P. Azadi, U. Yrlid, J. J. Kohler

This study identifies fucosylated glycoproteins and glycolipids as opposing factors in cholera toxin binding and intoxication in intestinal cells.

bioRxiv · Aug 2, 2023 · PreprintBiochemistry

Exo-enzymatic addition of diazirine-modified sialic acid to cell surfaces enables photocrosslinking of glycoproteins

N. Yarravarapu, R. S. R. Konada, N. Darabedian, N. J. Pedowtiz, S. N. Krishnamurthy, M. R. Pratt, J. J. Kohler

The paper introduces an exo-enzymatic method to add diazirine-modified sialic acid to cell surfaces, enabling UV-induced crosslinking of glycoproteins involved in glycan-mediated interactions.

bioRxiv · Oct 7, 2021Biochemistry

Mass spectrometric method for the unambiguous profiling of cellular dynamic glycosylation.

A. Shajahan, N. T. Supekar, H. Wu, A. M. Wands, G. Bhat, A. Kalimurthy, M. Matsubara, R. Ranzinger, J. J. Kohler, P. Azadi

This paper introduces a mass spectrometry-based method to directly detect non-natural sugars in glycopeptides, enabling the study of dynamic glycosylation without metabolic tagging.

bioRxiv · May 4, 2020Biochemistry

The human UDP-galactose 4’-epimerase (GALE) is required for cell surface glycome structure and function

A. Broussard, A. Florwick, C. Desbiens, N. Nischan, C. Robertson, Z. Guan, J. J. Kohler, L. Wells, M. Boyce

This study shows that GALE regulates nucleotide-sugar levels, affecting glycan structures and cell signaling, particularly in death receptor pathways.

bioRxiv · May 23, 2019Cell Biology