Author

S. Katiyar

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 Evolutionary Biology· 1

Signature Assays, Organisms & Methods

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Research Focus:chromatin & epigenetic regulation· 3 Organism:human· 2 Approach:statistical model· 2 Organism:Arabidopsis· 1 Approach:experimental assay· 1 Approach:mechanistic / dynamical model· 1 Assay:protein sequence· 1 Assay:protein structure· 1

Frequent Co-Authors

D. P. Byrne· 3 shared N. Kannan· 3 shared S. Shrestha· 3 shared A. Venkat· 2 shared C. E. Eyers· 2 shared L. A. Daly· 2 shared P. Eyers· 2 shared W. Yeung· 2 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 40 mutual co-author links

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3 shared papersBiochemistry

D. P. Byrne

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Author profile →

3 papers

Recent·Most cited

Redox Regulation of Brain Selective Kinases BRSK1/2: Implications for Dynamic Control of the Eukaryotic AMPK family through Cys-based mechanisms

G. Bendzunas, D. P. Byrne, S. Shrestha, L. A. Daly, S. O. Oswald, S. Katiyar, A. Venkat, W. Yeung, C. E. Eyers, P. A. Eyers, N. Kannan

This study investigates how redox regulation via cysteine oxidation controls BRSK1/2 kinase activity, revealing conserved mechanisms that modulate catalytic function through disulfide bond formation and salt bridge disruption.

bioRxiv · Oct 5, 2023 · PreprintBiochemistry

Mechanistic and evolutionary insights into isoform-specific 'supercharging' in DCLK family kinases

A. Venkat, G. Watterson, D. P. Byrne, B. O. Boyle, S. Shrestha, N. Gravel, E. E. Fairweather, L. A. Daly, C. Bunn, W. Yeung, I. Aggarwal, S. Katiyar, C. E. Eyers, P. Eyers, N. Kannan

This study investigates how isoform-specific variations in DCLK family kinases affect autoregulation through structural and functional analyses.

bioRxiv · Mar 29, 2023Evolutionary Biology

A novel redox-active switch in Fructosamine-3-kinases expands the regulatory repertoire of the protein kinase superfamily

S. Shrestha, S. Katiyar, C. E. Sanz-Rodriguez, N. R. Kemppinen, H. W. Kim, R. Kadirvelraj, C. Panagos, N. Keyhaninejad, M. Colonna, P. Chopra, D. P. Byrne, G. J. Boons, E. V. Knaap, P. Eyers, A. S. Edison, , N. Kannan

This study identifies redox-sensitive cysteines in Fructosamine-3-kinases (FN3Ks) that regulate their activity and dimerization through disulfide bonds, revealing a novel redox regulatory mechanism in the protein kinase superfamily.

bioRxiv · Jan 13, 2020Biochemistry