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Rubinstein Lab
Rubinstein Lab


Representative publications

Ripstein, Z. A., Huang, R., Augustyniak R, Kay, L. E., and Rubinstein, J. L. (2017). Structure of a AAA+ unfoldase in the process of unfolding substrate. eLife 10.7554/eLife.25754  

Punjani, A., Rubinstein, J. L., Fleet, D. J., Brubaker, M.A. (2017). Algorithmic innovation removes the computational bottleneck in cryo-EM. Nature Methods, Nature Methods 14, 290-6.

Mazhab-Jafari, M.T., Rohou, A., Schmidt, C., Bueler, S.A., Benlekbir, S., Robinson, C.V., and Rubinstein, J.L. (2016). Atomic model for the membrane-embedded VO motor of a eukaryotic V-ATPase. Nature 539, 118-122.

Wilson, M.D., Benlekbir, S., Fradet-Turcotte, A., Sherker, A., Julien, J.-P., McEwan, A., Noordermeer, S.M., Sicheri, F., Rubinstein, J.L. and Durocher, D. (2016). The structural basis of modified nucleosome recognition by 53BP1. Nature 536, 100-3.

Huang, R., Ripstein, Z.A., Augustyniak, R., Kay L.E, and Rubinstein, J.L. (2016). Unfolding the mechanism of the AAA+ unfoldase VAT by a combined cryo-EM solution NMR study. PNAS 113(29), E4190–E4199.

Schep, D.G, Zhao, J., Rubinstein, J. L. (2016). Models for the a subunits of the T. thermophilus V/A-ATPase and S. cerevisiae V-ATPase by cryo-EM and evolutionary covariance. Proc Natl Acad Sci U S A. 2016 Mar 7. pii: 201521990. [Epub ahead of print].

Zhou, A., Rohou, A., Schep, D.G., Bason, J.V., Montgomery, M.G., Walker, J.E., Grigorieff, N., Rubinstein, J. L. (2015). Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM. eLife e10180 [BioRxiv:11 Aug 2015]

Rubinstein, J. L., and Brubaker, M. A. (2015). Alignment of cryo-EM movies of individual particles by optimization of image translations. J Struct Biol 192, 188-95. [ArXiv:1409.6789]

Zhao, J., Benlekbir, S., and Rubinstein, J. L. (2015). Cryo-EM observation of rotational states in a eukaryotic V-ATPase. Nature 521, 241-5.

Smith, M.T. J., Rubinstein, J. L. (2014). Beyond blob-ology. Science 345, 617-9.

Marr, C. R., Benlekbir, S., and Rubinstein, J.L. (2014). Fabrication of carbon films with ~500 nm holes for cryo-EM with a direct detector device. Journal of Structural Biology 185, 42-7.

Benlekbir, S., Bueler, S. A., and Rubinstein, J. L. (2012).  Structure of the vacuolar-type ATPase from Saccharomyces cerevisiae at 11 Å resolution.  Nature Structural and Molecular Biology 19, 1356-62

Baker, L. A., Watt, I. N., Runswick, M. J., Walker, J. E., and Rubinstein, J. L. (2012).  The arrangement of subunits in intact mammalian mitochondrial ATP synthase determined by cryo-EM. Proceedings of the National Academy of Sciences (USA) 109, 11675-80.

Lau, W. C. Y., and Rubinstein, J. L. (2012). Sub-nanometer resolution structure of the intact T. thermophilus H+-driven ATP synthase.   Nature 481, 214-8.

A detailed list of Dr. Rubinstein's publications is available on PubMed. »»