Author

S. Shivakumaraswamy

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· 4

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 3 Assay:proteomics· 2 Organism:bacteria (other)· 1 Research Focus:cell type annotation· 1 Organism:E. coli· 1 Organism:plant (other)· 1 Approach:statistical model· 1

Frequent Co-Authors

A. Roeselova· 2 shared D. Balchin· 2 shared H. Balaram· 2 shared S. Howell· 2 shared A. Bellur· 1 shared A. Pajak· 1 shared D. Joshi· 1 shared F.-U. Hartl· 1 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 23 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

A. Roeselova

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Mechanism of chaperone coordination during cotranslational protein folding in bacteria

A. Roeselova, S. L. Maslen, S. Shivakumaraswamy, G. A. Pellowe, S. Howell, D. Joshi, J. Redmond, S. Kjaer, M. Skehel, D. Balchin

The paper investigates how chaperones coordinate during cotranslational protein folding in bacteria, showing they create a protected space for maturation without destabilizing intermediates.

Molecular Cell · Jul 1, 2024Peer-reviewedBiochemistry

Resolving chaperone-assisted protein folding on the ribosome at the peptide level

T. E. Wales, A. Pajak, A. Roeselova, S. Shivakumaraswamy, S. Howell, F.-U. Hartl, J. R. Engen, D. Balchin

This study uses HDX-MS to map the cotranslational folding pathway of E. coli dihydrofolate reductase, revealing structured intermediates and chaperone interactions on the ribosome.

bioRxiv · Sep 23, 2022Biochemistry

Mechanistic insights into the functioning of GMP synthetase: a two-subunit, allosterically regulated, ammonia tunnelling enzyme

S. Shivakumaraswamy, S. Kumar, A. Bellur, S. D. Polisetty, H. Balaram

This paper presents a mechanistic model of MjGMPS, a two-subunit GMP synthetase, using biochemical experiments, crystal structures, and cross-linking mass spectrometry to elucidate ammonia tunneling and allostery.

bioRxiv · Feb 27, 2022 · PreprintBiochemistry

Helices on interdomain interface couple catalysis in the ATPPase domain with allostery in Plasmodium falciparum GMP synthetase

S. Shivakumaraswamy, N. Pandey, L. Ballut, S. Violot, N. Aghajari, H. Balaram

This study identifies helices at the interdomain interface of Plasmodium falciparum GMP synthetase that couple ATPPase catalysis with GATase activation through domain crosstalk.

bioRxiv · Feb 11, 2020Biochemistry