Sibylle Brenner

Brenner, S., F. Berger, L. Rao, M. P. Nicholas, and A. Gennerich. Force production of human cytoplasmic dynein is limited by its processivity. 2020. Sci. Adv. 6:eaaz4295. PDF

Nicholas, M. P., F. Berger, L. Rao, S. Brenner, C. Cho, and A. Gennerich. Cytoplasmic dynein regulates its attachment to microtubules via nucleotide state-switched mechanosensing at multiple AAA domains. 2015. Proc. Natl. Acad. Sci. USA 112:6371–6376. PDF

Nicholas, M. P.*, P. Hook*, S. Brenner, C. Lazar, R. B. Vallee#, and A. Gennerich#. Control of cytoplasmic dynein force production and processivity by its C-terminal domain. 2015. Nat. Commun. 6:6206 (*: co-first authors; #: co-corresponding authors). PDF

Rao, L.*, E. M. Romes*, M. P. Nicholas, S. Brenner, T. Ashutosh, A. Gennerich#, and K. C. Slep#. The yeast dynein Dyn2–Pac11 complex is a dynein dimerization/processivity factor: structural and single-molecule characterization. 2013. Mol. Biol. Cell (*: co-first authors; #: co-corresponding authors). PDF

Leferink, N. G., C. R. Pudney, S. Brenner, D. J. Heyes, R. R. Eady, S. S. Hasnain, S. Hay, S. E. Rigby, and N. S. Scrutton. Gating mechanisms for biological electron transfer: integrating structure with biophysics reveals the nature of redox control in cytochrome P450 reductase and copper-dependent nitrite reductase. 2011. FEBS Lett. 586:578–584. PDF

Hay, S., S. Brenner, B. Khara, A. M. Quinn, S. E. Rigby, and N. S. Scrutton. Nature of the energy landscape for gated electron transfer in a dynamic redox protein. 2010. J. Am. Chem. Soc. 132:9738–9745. PDF

Brenner, S., D. J. Heyes, S. Hay, M. A. Hough, R. R. Eady, S. S. Hasnain, and N. S. Scrutton. Demonstration of proton-coupled electron transfer in copper-containing nitrite reductases. 2009. J. Biol. Chem. 284:25973–25983. PDF

Brenner, S., S. Hay, and N. S. Scrutton. Ionic strength dependence of the heating time in T-Jump instrument TJ-64. 2009. Hi-Tech Scientific AN.020.T64.

Wohlgemuth, I., S. Brenner, M. Beringer, and M. V. Rodnina. Modulation of the rate of peptidyl transfer on the ribosome by the nature of substrates. 2008. J. Biol. Chem. 283:32229–32235. PDF

Brenner, S., S. Hay, A. W. Munro, and N. S. Scrutton. Inter-flavin electron transfer in cytochrome P450 reductase — effects of solvent and pH identify hidden complexity in mechanism. 2008. FEBS J. 275:4540–4557. PDF

Brenner, S., S. Hay, H. M. Girvan, A. W. Munro, and N. S. Scrutton. Conformational dynamics of the cytochrome P450 BM3/N-palmitoylglycine complex: the proposed “proximal-distal” transition probed by temperature-jump spectroscopy. 2007. J. Phys. Chem. B 111:7879–7886. PDF

Brenner, S., S. Hay, and N. S. Scrutton. Temperature calibration of T-Jump instrument TJ-64 using Tris/Phenol Red. 2006. Hi-Tech Scientific AN.019.T64.