Author

S. Vahidi

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

Biophysics· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Organism:bacteria (other)· 2 Assay:cryo-EM· 2 Approach:biophysical modeling· 1 Research Focus:protein folding & dynamics· 1 Research Focus:protein structure prediction· 1 Assay:structural biology· 1

Frequent Co-Authors

J. L. Rubinstein· 3 shared L. E. Kay· 2 shared Z. A. Ripstein· 2 shared A. K. Mittermaier· 1 shared A. L. Goldberg· 1 shared A. Plourde· 1 shared E. Rennella· 1 shared J. B. Juravsky· 1 shared

Activity by Year

2019-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 27 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

3 shared papersBiophysics

J. L. Rubinstein

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Structure of mycobacterial respiratory Complex I

Y. Liang, A. Plourde, S. A. Bueler, J. Liu, P. Brzezinski, S. Vahidi, J. L. Rubinstein

The paper determines the structure of mycobacterial Complex I using cryoEM, revealing its composition and interactions with menaquinone and a unique lipid.

bioRxiv · Oct 4, 2022Biochemistry

An allosteric switch regulates Mycobacterium tuberculosis ClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR

S. Vahidi, Z. A. Ripstein, J. B. Juravsky, E. Rennella, A. L. Goldberg, A. K. Mittermaier, J. L. Rubinstein, L. E. Kay

This paper identifies an allosteric switch in Mycobacterium tuberculosis ClpP1P2 protease that regulates its activity through conformational changes, revealed by cryo-EM and methyl-TROSY NMR.

Proceedings of the National Academy of Sciences · Mar 2, 2020Peer-reviewedBiophysics

A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery

Z. A. Ripstein, S. Vahidi, W. A. Houry, J. L. Rubinstein, L. E. Kay

This study presents cryo-EM structures of the ClpXP complex from Neisseria meningitidis, revealing how ATP hydrolysis couples substrate unfolding and proteolysis.

bioRxiv · Dec 8, 2019Biophysics