Stephen E. Miller, Ph.D.

Early Discovery Biochemistry Genentech, Inc., San Francisco, CA, United States 
"Stephen Miller"
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Miller SE, Schneider JP. (2020) The effect of turn residues on the folding and cell-penetrating activity of β-hairpin peptides and applications toward protein delivery. Peptide Science (Hoboken, N.J.). 112
Miller SE, Tsuji K, Abrams RPM, et al. (2020) Uncoupling the Folding-Function Paradigm of Lytic Peptides to Deliver Impermeable Inhibitors of Intracellular Protein-Protein Interactions. Journal of the American Chemical Society
Miller SE, Yamada Y, Patel N, et al. (2019) Electrostatically Driven Guanidinium Interaction Domains that Control Hydrogel-Mediated Protein Delivery In Vivo. Acs Central Science. 5: 1750-1759
Miller SE, Schneider JP. (2019) The effect of turn residues on the folding and cell‐penetrating activity of β‐hairpin peptides and applications toward protein delivery Peptide Science. 112
Nagarkar RP, Miller SE, Zhong S, et al. (2018) Dynamic Protein Folding at the Surface of Stimuli-Responsive Peptide Fibrils. Protein Science : a Publication of the Protein Society
Medina SH, Michie MS, Miller SE, et al. (2017) Fluorous Phase-Directed Peptide Assembly Affords Nano-Peptisomes Capable of Ultrasound-Triggered Cellular Delivery. Angewandte Chemie (International Ed. in English)
Medina SH, Miller SE, Keim AI, et al. (2016) An Intrinsically Disordered Peptide Facilitates Non-Endosomal Cell Entry. Angewandte Chemie (International Ed. in English)
Miller SE, Thomson PF, Arora PS. (2014) Synthesis of hydrogen-bond surrogate α-helices as inhibitors of protein-protein interactions. Current Protocols in Chemical Biology. 6: 101-16
Miller SE, Watkins AM, Kallenbach NR, et al. (2014) Effects of side chains in helix nucleation differ from helix propagation. Proceedings of the National Academy of Sciences of the United States of America. 111: 6636-41
Miller SE, Kallenbach NR, Arora PS. (2012) Reversible α-helix formation controlled by a hydrogen bond surrogate. Tetrahedron. 68: 4434-4437
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