Author

M. Khajehpour

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

Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Organism:bacteria (other)· 1 Approach:biophysical modeling· 1 Approach:experimental assay· 1

Frequent Co-Authors

G. Prehna· 2 shared N. R. Rutbeek· 2 shared D. Davidson· 1 shared H. Rezasoltani· 1 shared I. Asakereh· 1 shared M. Singh· 1 shared T. R. Patel· 1 shared

Activity by Year

2021-2024 · peak 1/yr

Co-Author Collaboration Network

7 top collaborators · 15 mutual co-author links

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2 shared papersBiochemistry

G. Prehna

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2 papers

Recent·Most cited

The Streptococcus phage protein paratox is an intrinsically disordered protein.

I. Asakereh, N. R. Rutbeek, M. Singh, D. Davidson, G. Prehna, M. Khajehpour

This paper shows that the phage protein paratox is intrinsically disordered in dilute solution but folds into a globular structure when bound to ComR or in the presence of stabilizing solutes.

Protein Science · May 27, 2024Peer-reviewedBiochemistry

Molecular mechanism of quorum sensing inhibition in Streptococcus by the phage protein paratox

N. R. Rutbeek, H. Rezasoltani, T. R. Patel, M. Khajehpour, G. Prehna

This study elucidates how the phage protein Prx inhibits quorum sensing in Streptococcus pyogenes by inducing conformational changes in the ComR receptor.

bioRxiv · Jun 3, 2021Biochemistry