R
Rina Rosenzweig
Researcher at Weizmann Institute of Science
Publications - 40
Citations - 2370
Rina Rosenzweig is an academic researcher from Weizmann Institute of Science. The author has contributed to research in topics: Chaperone (protein) & Chemistry. The author has an hindex of 20, co-authored 33 publications receiving 1704 citations. Previous affiliations of Rina Rosenzweig include Technion – Israel Institute of Technology & University of Toronto.
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The Hsp70 chaperone network
TL;DR: Recent advances that have increased the understanding of the molecular mechanisms and working principles of the Hsp70 network are described, and new opportunities for the development of chemical compounds that modulate disease-related HSp70 activities are offered.
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Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction.
TL;DR: Bacterial protein disaggregation elucidated via a combined biochemical methyl–transverse relaxation–optimized spectroscopy nuclear magnetic resonance approach and an atomic-resolution model for the ClpB-DnaK complex, which is verified by mutagenesis and functional assays.
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Bringing Dynamic Molecular Machines into Focus by Methyl-TROSY NMR
Rina Rosenzweig,Lewis E. Kay +1 more
TL;DR: Methyl-TROSY (transverse relaxation optimized spectroscopy) NMR is highlighted, which enables the study of such large systems, and it is shown how this emerging technique contributes to an understanding of cellular function and the role of molecular plasticity in regulating an array of biochemical activities.
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The central unit within the 19S regulatory particle of the proteasome
TL;DR: A previously unknown functional unit is described within the 19S of the 26S proteasome, comprising two subunits, Rpn1 and Rpn2, which physically link the site of substrate recruitment with the sites of proteolysis.
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Rpn1 and Rpn2 coordinate ubiquitin processing factors at proteasome.
TL;DR: By binding multiple ubiquitin-processing factors simultaneously, Rpn1 is uniquely suited to coordinate substrate recruitment, deubiquitination, and movement toward the catalytic core, and consequently it influences substrate residency time and commitment to degradation.