Inbal Riven
Affiliations: | Weizmann Institute of Science, Rehovot, Israel |
Google:
"Inbal Riven"Mean distance: 15.66 (cluster 32) | S | N | B | C | P |
BETA: Related publications
See more...
Publications
|
You can help our author matching system! If you notice any publications incorrectly attributed to this author, please sign in and mark matches as correct or incorrect. |
| Liebermann DG, Jungwirth J, Riven I, et al. (2023) From Microstates to Macrostates in the Conformational Dynamics of GroEL: A Single-Molecule Förster Resonance Energy Transfer Study. The Journal of Physical Chemistry Letters. 6513-6521 |
| Riven I, Mazal H, Iljina M, et al. (2022) Fast dynamics shape the function of the AAA+ machine ClpB:Lessons from single-molecule FRET spectroscopy. The Febs Journal |
| Mazal H, Iljina M, Barak Y, et al. (2019) Tunable microsecond dynamics of an allosteric switch regulate the activity of a AAA+ disaggregation machine. Nature Communications. 10: 1438 |
| Kantaev R, Riven I, Goldenzweig A, et al. (2018) Manipulating the Folding Landscape of a Multi-Domain Protein. The Journal of Physical Chemistry. B |
| Aviram HY, Pirchi M, Barak Y, et al. (2018) Two states or not two states: Single-molecule folding studies of protein L. The Journal of Chemical Physics. 148: 123303 |
| Mazal H, Aviram H, Riven I, et al. (2017) Effect of ligand binding on a protein with a complex folding landscape. Physical Chemistry Chemical Physics : Pccp |
| Ozer E, Chemla Y, Schlesinger O, et al. (2016) In-vitro suppression of two different stop codons. Biotechnology and Bioengineering |
| Cohen SS, Riven I, Cortajarena AL, et al. (2015) Probing the Molecular Origin of Native-State Flexibility in Repeat Proteins. Journal of the American Chemical Society. 137: 10367-73 |
| Cohen SS, Riven I, Cortajarena AL, et al. (2015) Probing the molecular origin of native-state flexibility in repeat proteins Journal of the American Chemical Society. 137: 10367-10373 |
| Pirchi M, Ziv G, Riven I, et al. (2011) Single-molecule fluorescence spectroscopy maps the folding landscape of a large protein. Nature Communications. 2: 493 |