Rosenzweig R., Nillegoda N. B., Mayer M. P. & Bukau B. (2019). The Hsp70 chaperone network.  Nature Reviews Molecular Cell Biology. 20:(11)665-680.  Abstract
Mazal H., Iljina M., Barak Y., Elad N., Rosenzweig R., Goloubinoff P., Riven I. & Haran G. (2019). Tunable microsecond dynamics of an allosteric switch regulate the activity of a AAA+ disaggregation machine.  Nature Communications. 10:(1)  Abstract
Rina Rosenzweig, Nadinath B. Nillegoda, Matthias P. Mayer & Bernd Bukau (2019). The Hsp70 chaperone network.  Nat Rev Mol Cell Biol. . Jun 28.


Novakovic M., Cousin S. F., Jaroszewicz M. J., Rosenzweig R. & Frydman L. (2018). Looped-PROjected SpectroscopY (L-PROSY): A simple approach to enhance backbone/sidechain cross-peaks in 1H NMR.  Journal of Magnetic Resonance. 294:169-180.  Abstract
Sekhar A., Velyvis A., Zoltsman G., Rosenzweig R., Bouvignies G. & Kay L. E. (2018). Conserved conformational selection mechanism of Hsp70 chaperone-substrate interactions.  eLife. 7.  Abstract
Kampinga Hh, Andreasson C, Barducci A, Cheetham Me, Cyr D, Emanuelsson C, Genevaux P, Gestwicki Je, Goloubinoff P, Huerta-Cepas J, Kirstein J, Liberek K, Mayer Mp, Nagata K, Nillegoda Nb, Pulido P, Ramos C, De Los Rios P, Rospert S, Rosenzweig R, Sahi C, Taipale M, Tomiczek B, Ushioda R, Young Jc, Zimmermann R, Zylicz A, Zylicz M, Craig Ea, Marszalek J. (2018). Function, evolution, and structure of J-domain proteins.  Cell Stress Chaperones. Nov 26..


Sekhar A., Nagesh J., Rosenzweig R. & Kay L. E. (2017). Conformational heterogeneity in the Hsp70 chaperone-substrate ensemble identified from analysis of NMR-detected titration data.  Protein Science. 26:(11)2207-2220.  Abstract
Rosenzweig R., Sekhar A., Nagesh J. & Kay L. E. (2017). Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles.  eLife. 6.  Abstract
Chojnacki M., Mansour W., Hameed D. S., Singh R. K., El Oualid O. F., Rosenzweig R., Nakasone M. A., Yu Z., Glaser F., Kay L. E., Fushman D., Ovaa H. & Glickman M. H. (2017). Polyubiquitin-Photoactivatable Crosslinking Reagents for Mapping Ubiquitin Interactome Identify Rpn1 as a Proteasome Ubiquitin-Associating Subunit.  Cell Chemical Biology. 24:(4)443-457.  Abstract


Sekhar A., Rosenzweig R., Bouvignies G., Kay L. E., Raitsimring A., Otting G. & Graham B. (2016). Hsp70 biases the folding pathways of client proteins.  Proceedings of the National Academy of Sciences of the United States of America. 113:(20)E2794-E2801.  Abstract
Rosenzweig R. & Kay L. E. (2016). Solution NMR Spectroscopy Provides an Avenue for the Study of Functionally Dynamic Molecular Machines: The Example of Protein Disaggregation.  Journal of the American Chemical Society. 138:(5)1466-1477.  Abstract


Rosenzweig R., Farberd P., Velyvis A., Rennella E., Latham M. P. & Kay L. E. (2015). ClpB N-terminal domain plays a regulatory role in protein disaggregation.  Proceedings Of The National Academy Of Sciences Of The United States Of America-Biological Sciences. 112:(50)E6872-E6881.  Abstract
Sekhar A., Rosenzweig R., Bouvignies G. & Kay L. E. (2015). Mapping the conformation of a client protein through the Hsp70 functional cycle.  Proceedings Of The National Academy Of Sciences Of The United States Of America-Biological Sciences. 112:(33)10395-10400.  Abstract


Rosenzweig R. & Kay L. E. (2014). Bringing Dynamic Molecular Machines into Focus by Methyl-TROSY NMR.  Annual Review of Biochemistry, Vol 83. 291-315.  Abstract


Rosenzweig R., Moradi S., Zarrine-Afsar A., Glover J. R. & Kay L. E. (2013). Unraveling the Mechanism of Protein Disaggregation Through a ClpB-DnaK Interaction.  Science. 339:(6123)1080-1083.  Abstract


Rosenzweig R., Bronner V., Zhang D., Fushman D. & Glickman M. H. (2012). Rpn1 and Rpn2 coordinate ubiquitin processing factors at proteasome.  Journal of Biological Chemistry. 287:(18)14659-14671.  Abstract


Deriziotis P., Andre R., Smith D. M., Goold R., Kinghorn K. J., Kristiansen M., Nathan J. A., Rosenzweig R., Krutauz D., Glickman M. H., Collinge J., Goldberg A. L. & Tabrizi S. J. (2011). Misfolded PrP impairs the UPS by interaction with the 20S proteasome and inhibition of substrate entry.  EMBO Journal. 30:(15)3065-3077.  Abstract
Religa T. L., Ruschak A. M., Rosenzweig R. & Kay L. E. (2011). Site-directed methyl group labeling as an NMR probe of structure and dynamics in supramolecular protein systems: Applications to the proteasome and to the ClpP protease.  Journal of the American Chemical Society. 133:(23)9063-9068.  Abstract


Zhang D., Chen T., Ziv I., Rosenzweig R., Matiuhin Y., Bronner V., Glickman M. H. & Fushman D. (2009). Together, Rpn10 and Dsk2 Can Serve as a Polyubiquitin Chain-Length Sensor.  Molecular Cell. 36:(6)1018-1033.  Abstract
Effantin G., Rosenzweig R., Glickman M. H. & Steven A. C. (2009). Electron Microscopic Evidence in Support of alpha-Solenoid Models of Proteasomal Subunits Rpn1 and Rpn2.  Journal of Molecular Biology. 386:(5)1204-1211.  Abstract


Rosenzweig R. & Glickman M. H. (2008). Chaperone-driven proteasome assembly.  Biochemical Society Transactions. 36:807-812.  Abstract
Rosenzweig R., Osmulski P. A., Gaczynska M. & Glickman M. H. (2008). The central unit within the 19S regulatory particle of the proteasome.  Nature Structural & Molecular Biology. 15:(6)573-580.  Abstract
Rosenzweig R. & Glickman M. H. (2008). Forging a proteasome alpha-ring with dedicated proteasome chaperones.  Nature Structural & Molecular Biology. 15:(3)218-220.  Abstract