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165 results on '"Rosenzweig, Rina"'

3. Assessing site-specific enhancements imparted by hyperpolarized water in folded and unfolded proteins by 2D HMQC NMR

Author

Szekely, Or, Olsen, Gregory Lars, Novakovic, Mihajlo, Rosenzweig, Rina, and Frydman, Lucio

Subjects
Physics - Chemical Physics, Physics - Biological Physics
Abstract

Hyperpolarized water can be a valuable aid in protein NMR, leading to amide group 1H polarizations that are orders of magnitude larger than their thermal counterparts. Suitable procedures can exploit this to deliver 2D 1H-15N correlations with good resolution and enhanced sensitivity. These enhancements depend on the exchange rates between the amides and the water, thereby yielding diagnostic information about solvent accessibility. This study applied this HyperW method to four proteins exhibiting a gamut of exchange behaviors: PhoA4, an unfolded 122-residue fragment; barstar, a fully folded ribonuclease inhibitor; R17, a 13.3 kDa system possessing folded and unfolded forms under slow interconversion; and drkN SH3, a protein domain whose folded and unfolded forms interchange rapidly and with temperature-dependent population ratios. For PhoA4 HyperW sensitivity enhancements were larger than 300-fold, as expected for an unfolded protein sequence. Though fully folded barstar also exhibited substantial enhancements; these, however, were not uniform, and according to CLEANEX experiments reflected the solvent-exposed residues. R17 showed the expected superposition of 100-fold enhancements for its unfolded form, coexisting with more modest folded counterparts. Unexpected, however, was the behavior of drkN SH3, for which HyperW enhanced the unfolded but even more certain folded protein sites. These preferential enhancements were repeatedly and reproducibly observed; a number of explanations including three-site exchange magnetization transfers between water, unfolded and folded states; cross-correlated relaxation processes from hyperpolarized structural waters and labile sidechain protons; and the possibility that faster solvent exchange rates characterize certain folded sites over their unfolded counterparts are considered to account for them.

Published
2020

5. Function, evolution, and structure of J-domain proteins

Author

Kampinga, Harm H, Andreasson, Claes, Barducci, Alessandro, Cheetham, Michael E, Cyr, Douglas, Emanuelsson, Cecilia, Genevaux, Pierre, Gestwicki, Jason E, Goloubinoff, Pierre, Huerta-Cepas, Jaime, Kirstein, Janine, Liberek, Krzysztof, Mayer, Matthias P, Nagata, Kazuhiro, Nillegoda, Nadinath B, Pulido, Pablo, Ramos, Carlos, De los Rios, Paolo, Rospert, Sabine, Rosenzweig, Rina, Sahi, Chandan, Taipale, Mikko, Tomiczek, Bratłomiej, Ushioda, Ryo, Young, Jason C, Zimmermann, Richard, Zylicz, Alicja, Zylicz, Maciej, Craig, Elizabeth A, and Marszalek, Jaroslaw

Subjects
Biochemistry and Cell Biology, Biological Sciences, Underpinning research, 1.1 Normal biological development and functioning, Generic health relevance, Animals, Disease, Evolution, Molecular, HSP70 Heat-Shock Proteins, Humans, Protein Aggregates, Protein Domains, Protein Refolding, Heat shock protein 70, J-domain proteins, 8-stranded -sandwich domain, 8-stranded β-sandwich domain, Biochemistry & Molecular Biology, Biochemistry and cell biology
Abstract

Hsp70 chaperone systems are very versatile machines present in nearly all living organisms and in nearly all intracellular compartments. They function in many fundamental processes through their facilitation of protein (re)folding, trafficking, remodeling, disaggregation, and degradation. Hsp70 machines are regulated by co-chaperones. J-domain containing proteins (JDPs) are the largest family of Hsp70 co-chaperones and play a determining role functionally specifying and directing Hsp70 functions. Many features of JDPs are not understood; however, a number of JDP experts gathered at a recent CSSI-sponsored workshop in Gdansk (Poland) to discuss various aspects of J-domain protein function, evolution, and structure. In this report, we present the main findings and the consensus reached to help direct future developments in the field of Hsp70 research.

Published
2019

15. Bacterial adaptation to cold: Conservation of a short J‐domain co‐chaperone and its protein partners in environmental proteobacteria

Author

Weber, Lana, primary, Gilat, Atar, additional, Maillot, Nathanael, additional, Byrne, Deborah, additional, Arnoux, Pascal, additional, Giudici‐Orticoni, Marie‐Thérèse, additional, Méjean, Vincent, additional, Ilbert, Marianne, additional, Genest, Olivier, additional, Rosenzweig, Rina, additional, and Dementin, Sébastien, additional

Published
2023
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28. NudC guides client transfer between the Hsp40/70 and Hsp90 chaperone systems

Author

Biebl, Maximilian M., primary, Delhommel, Florent, additional, Faust, Ofrah, additional, Zak, Krzysztof M., additional, Agam, Ganesh, additional, Guo, Xiaoyan, additional, Mühlhofer, Moritz, additional, Dahiya, Vinay, additional, Hillebrand, Daniela, additional, Popowicz, Grzegorz M., additional, Kampmann, Martin, additional, Lamb, Don C., additional, Rosenzweig, Rina, additional, Sattler, Michael, additional, and Buchner, Johannes, additional

Published
2022
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33. Meet the authors: Guy Zoltsman and Rina Rosenzweig.

Author

Zoltsman, Guy and Rosenzweig, Rina

Abstract

We talk to first and last authors Guy Zoltsman and Rina Rosenzweig about their paper, "A unique chaperoning mechanism in Class A JDPs recognizes and stabilizes mutant p53," how every result may be important in the right context, and the importance to Rina that her lab is an encouraging and collaborative place. [ABSTRACT FROM AUTHOR]

Published
2024
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38. Function, evolution, and structure of J-domain proteins

Author

Kampinga, Harm H., Andreasson, Claes, Barducci, Alessandro, Cheetham, Michael E., Cyr, Douglas, Emanuelsson, Cecilia, Genevaux, Pierre, Gestwicki, Jason E., Goloubinoff, Pierre, Huerta-Cepas, Jaime, Kirstein, Janine, Liberek, Krzysztof, Mayer, Matthias P., Nagata, Kazuhiro, Nillegoda, Nadinath B., Pulido, Pablo, Ramos, Carlos, De los Rios, Paolo, Rospert, Sabine, Rosenzweig, Rina, Sahi, Chandan, Taipale, Mikko, Tomiczek, Bratlomiej, Ushioda, Ryo, Young, Jason C., Zimmermann, Richard, Zylicz, Alicja, Zylicz, Maciej, Craig, Elizabeth A., Marszalek, Jaroslaw, Kampinga, Harm H., Andreasson, Claes, Barducci, Alessandro, Cheetham, Michael E., Cyr, Douglas, Emanuelsson, Cecilia, Genevaux, Pierre, Gestwicki, Jason E., Goloubinoff, Pierre, Huerta-Cepas, Jaime, Kirstein, Janine, Liberek, Krzysztof, Mayer, Matthias P., Nagata, Kazuhiro, Nillegoda, Nadinath B., Pulido, Pablo, Ramos, Carlos, De los Rios, Paolo, Rospert, Sabine, Rosenzweig, Rina, Sahi, Chandan, Taipale, Mikko, Tomiczek, Bratlomiej, Ushioda, Ryo, Young, Jason C., Zimmermann, Richard, Zylicz, Alicja, Zylicz, Maciej, Craig, Elizabeth A., and Marszalek, Jaroslaw

Abstract

Hsp70 chaperone systems are very versatile machines present in nearly all living organisms and in nearly all intracellular compartments. They function in many fundamental processes through their facilitation of protein (re)folding, trafficking, remodeling, disaggregation, and degradation. Hsp70 machines are regulated by co-chaperones. J-domain containing proteins (JDPs) are the largest family of Hsp70 co-chaperones and play a determining role functionally specifying and directing Hsp70 functions. Many features of JDPs are not understood; however, a number of JDP experts gathered at a recent CSSI-sponsored workshop in Gdansk (Poland) to discuss various aspects of J-domain protein function, evolution, and structure. In this report, we present the main findings and the consensus reached to help direct future developments in the field of Hsp70 research.

Published
2019
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39. Function, evolution, and structure of J-domain proteins

Author

Kampinga, Harm H., primary, Andreasson, Claes, additional, Barducci, Alessandro, additional, Cheetham, Michael E., additional, Cyr, Douglas, additional, Emanuelsson, Cecilia, additional, Genevaux, Pierre, additional, Gestwicki, Jason E., additional, Goloubinoff, Pierre, additional, Huerta-Cepas, Jaime, additional, Kirstein, Janine, additional, Liberek, Krzysztof, additional, Mayer, Matthias P., additional, Nagata, Kazuhiro, additional, Nillegoda, Nadinath B., additional, Pulido, Pablo, additional, Ramos, Carlos, additional, De los Rios, Paolo, additional, Rospert, Sabine, additional, Rosenzweig, Rina, additional, Sahi, Chandan, additional, Taipale, Mikko, additional, Tomiczek, Bratłomiej, additional, Ushioda, Ryo, additional, Young, Jason C., additional, Zimmermann, Richard, additional, Zylicz, Alicja, additional, Zylicz, Maciej, additional, Craig, Elizabeth A., additional, and Marszalek, Jaroslaw, additional

Published
2018
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48. Solution NMR Spectroscopy Provides an Avenue for the Study of Functionally Dynamic Molecular Machines: The Example of Protein Disaggregation.

Author

Rosenzweig, Rina and Kay, Lewis E.

Subjects
*NUCLEAR magnetic resonance spectroscopy, *MOLECULAR machinery (Technology), *PROTEIN structure, *CLUSTERING of particles, *SOLUTION (Chemistry), *MOLECULAR chaperones
Abstract

Solution-based NMR spectroscopy has been an important tool for studying the structure and dynamics of relatively small proteins and protein complexes with aggregate molecular masses under approximately 50 kDa. The development of new experiments and labeling schemes, coupled with continued improvements in hardware, has significantly reduced this size limitation, enabling atomic-resolution studies of molecular machines in the 1 MDa range. In this Perspective, some of the important advances are highlighted in the context of studies of molecular chaperones involved in protein disaggregation. New insights into the structural biology of disaggregation obtained from NMR studies are described, focusing on the unique capabilities of the methodology for obtaining atomic-resolution descriptions of dynamic systems. [ABSTRACT FROM AUTHOR]

Published
2016
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