Author

A. Shonhai

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· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Organism:E. coli· 1 Organism:plant (other)· 1 Assay:protein structure· 1

Frequent Co-Authors

T. Zininga· 3 shared A. Arowolo· 1 shared A. Burger· 1 shared C. M. Lebepe· 1 shared I. Achilonu· 1 shared I. Kursula· 1 shared J. Vahokoski· 1 shared N. Nemukondeni· 1 shared

Activity by Year

2019-2020 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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3 shared papersBiochemistry

T. Zininga

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Author profile →

3 papers

Recent·Most cited

Biophysical characterization of the human K0513 protein

N. Nemukondeni, A. Arowolo, A. Shonhai, T. Zininga, A. Burger

This study characterizes the structure and function of the human K0513 protein using bioinformatics and biophysical methods, revealing its potential role in cancer signaling pathways.

bioRxiv · Jun 18, 2020 · PreprintBiochemistry

Comparative characterisation of Plasmodium falciparum Hsp70-1 relative to E. coli DnaK reveals functional specificity of the parasite chaperone

C. M. Lebepe, P. R. Matambanadzo, X. H. Makhoba, I. Achilonu, T. Zininga, A. Shonhai

This study compares the structure and function of Plasmodium falciparum Hsp70-1 with E. coli DnaK and a chimeric protein, showing functional specificity of the parasite chaperone.

bioRxiv · Mar 9, 2020Biochemistry

Biophysical analysis of Plasmodium falciparum Hsp70-Hsp90 organizing protein (PfHop) reveals a monomer that is characterised by folded segments connected by flexible linkers

A. Shonhai, S. Makumire, T. Zininga, J. Vahokoski, I. Kursula

This study characterizes the structure and thermal stability of PfHop, a Plasmodium falciparum protein involved in Hsp70-Hsp90 complex formation, revealing it as a monomeric protein with folded segments and flexible linkers.

bioRxiv · Dec 5, 2019Biochemistry