Author

M. Iljina

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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Biophysics· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Assay:fluorescence / live-cell microscopy· 2 Research Focus:protein folding & dynamics· 2 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

G. Haran· 4 shared I. Riven· 4 shared H. Mazal· 2 shared A. Dayananda· 1 shared B. V. Adkar· 1 shared D. Levy· 1 shared D. Scheerer· 1 shared E. Shakhnovich· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 26 mutual co-author links

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4 shared papersBiophysics

G. Haran

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4 papers

Recent·Most cited

Single-molecule FRET probes allosteric effects on protein-translocating pore loops of a AAA+ machine

M. Iljina, H. Mazal, A. Dayananda, Z. Zhang, G. Stan, I. Riven, G. Haran

This study uses single-molecule FRET to show that ATP hydrolysis in ClpB's nucleotide binding domains allosterically controls pore loop dynamics, revealing long-range conformational changes essential for substrate translocation.

bioRxiv · Feb 2, 2023Biophysics

Allosteric communication between ligand binding domains modulates substrate inhibition in adenylate kinase

D. Scheerer, B. V. Adkar, S. Bhattacharyya, D. Levy, M. Iljina, I. Riven, O. Dym, G. Haran, E. Shakhnovich

This study investigates how AMP substrate inhibition in adenylate kinase is modulated by domain motions, showing that inhibitory concentrations of AMP increase domain closure and affect catalytic activity.

bioRxiv · Nov 21, 2022 · PreprintBiophysics

Ultrafast pore-loop dynamics in a AAA+ machine point to a Brownian-ratchet mechanism for protein translocation

H. A. Mazal, M. Iljina, I. Riven, G. Haran

The paper measures pore-loop dynamics in ClpB using single-molecule FRET, finding microsecond fluctuations and conformational changes linked to substrate binding and disaggregation activity, suggesting a Brownian-ratchet mechanism.

bioRxiv · Nov 19, 2020Biophysics

Single-molecule spectroscopy reveals dynamic allostery mediated by the substrate-binding domain of a AAA+ machine

M. Iljina, H. Mazal, P. Goloubinoff, I. Riven, G. Haran

This study uses single-molecule FRET to show the NTD of ClpB dynamically interacts with the MD, regulating ATPase and unfolding activity through allosteric signaling.

bioRxiv · Sep 13, 2020Biophysics