Publications

2017

20.
Rosenzweig, R; Sekhar, A; Nagesh, J; Kay, Le (2017). Promiscuous Binding by Hsp70 Results in Conformational Heterogeneity and Fuzzy Chaperone-Substrate Ensembles.  Elife. 6.  Abstract
19.
Sekhar, A; Nagesh, J; Rosenzweig, R; Kay, Le (2017). Conformational Heterogeneity in the Hsp70 Chaperone-Substrate Ensemble Identified from Analysis of NMR-Detected Titration Data.  Protein Science. 26:2207-2220.  Abstract
18.
Chojnacki, M; Mansour, W; Hameed, Ds; Singh, Rk; El Oualid, F; Rosenzweig, R; Nakasone, Ma; Yu, Zl; Glaser, F; Kay, Le; Fushman, D; Ovaa, H; Glickman, Mh (2017). Polyubiquitin-Photoactivatable Crosslinking Reagents For Mapping Ubiquitin Interactome Identify Rpn1 as a Proteasome Ubiquitin-Associating Subunit.  Cell Chemical Biology. 24:443-+.  Abstract
17.
Rosenzweig R, Sekhar A, Nagesh J, Kay Le. (2017). Promiscuous Binding by Hsp70 Results in Conformational Heterogeneity and Fuzzy Chaperone-Substrate Ensembles.  Elife. Jul 14:(6)e28030.

Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles.
Rosenzweig R, Sekhar A, Nagesh J, Kay LE.
Elife. 2017 Jul 14;6. pii: e28030. doi: 10.7554/eLife.28030.
PMID: 28708484

2016

16.

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.  J. Am. Chem. Soc. 138:(5) 1466-77.

15.
Sekhar, A; Rosenzweig, R; Bouvignies, G; Kay, Le (2016). Hsp70 Biases the Folding Pathways of Client Proteins.  Proceedings of the National Academy of Sciences of the United States of America. 113:E2794-E2801.  Abstract
14.

Sekhar A, Rosenzweig R, Bouvignies G, Kay L.E. (2016). Hsp70 Biases the Folding Pathways of Client Proteins.  Proc Natl Acad Sci USA. 113:(20) 2794-801.

2015

13.

Rosenzweig R, Farber P, Velyvis A, Rennella E, Latham M.P, Kay L.E. (2015). ClpB N-Terminal Domain Plays a Regulatory Role in Protein Disaggregation.  Proc Natl Acad Sci USA. 112:(50) 6872-81.

12.

Sekhar A, Rosenzweig R, Bouvignies G, Kay L.E. (2015). Mapping the Conformation of a Client Protein Through the Hsp70 Functional Cycle.  Proc Natl Acad Sci USA. 112:(33) 10395-400.

2014

11.
Rosenzweig R, Kay L.E. (2014). Bringing Dynamic Molecular Machines Into Focus by Methyl-Trosy NMR.  Annu Rev Biochem. 83:291-315.

2013

10.

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): 1080-3

2012

9.

Rosenzweig R, Bronner V, Fushman D, Glickman M.H.  (2012). Rpn1 and Rpn2 coordinate ubiquitin processing factors at the proteasome. J Biol Chem. 287 (18): 14659-71.

2011

8.

Deriziotis P, André 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 J. 30:(15) 3065-77.

7.

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.  J. Am Chem Soc. 133:(23) 9063-8.

2009

6.
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.  Mol Cell. 36:(6)1018-33.
5.
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.  J Mol Biol. 386:(5) 1204-11.

2008

4.
Rosenzweig R, Glickman M.H. (2008). Chaperone-Driven Proteasome Assembly.  Biochem Soc Trans. 36: 807-12.
3.

Rosenzweig R, Osmulski P.A, Gaczynska M, Glickman M.H. (2008). The Central Unit Within the 19S Regulatory Particle of the Proteasome.  Nat Struct Mol Biol. 15:(6) 573-80.

2.

Rosenzweig R, Glickman MH. (2008). Forging a proteasome alpha-ring with dedicated proteasome chaperones. Nat Struct Mol Biol. 5(3):218-20

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