Author

H. Mazal

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· 3

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 2 Assay:fluorescence / live-cell microscopy· 2 Research Focus:protein folding & dynamics· 2 Approach:deep learning· 1 Approach:statistical model· 1

Frequent Co-Authors

G. Haran· 2 shared I. Riven· 2 shared M. Iljina· 2 shared A. Dayananda· 1 shared F.-F. Wieser· 1 shared G. Stan· 1 shared P. Goloubinoff· 1 shared V. Sandoghdar· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

9 top collaborators · 19 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 papersBiophysics

G. Haran

Mutual co-authors in cluster

Author profile →

3 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

Deciphering a hexameric protein complex with Angstrom optical resolution

H. Mazal, F.-F. Wieser, V. Sandoghdar

This paper introduces polarCOLD, a method combining partial labeling and polarization encoding to achieve Angstrom-resolution 3D structure determination of protein complexes.

bioRxiv · Nov 18, 2021Biophysics

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