Publications Archive - Schepartz Laboratory at UC Berkeley

2025

Purification of Post-Transcriptionally Modified tRNAs for Enhanced Cell-Free Translation Systems

Kalb, E. M.; Alejo, J. L.; Dias-Fields, L.; Knudson, I.; Davisson, J. A.; Maldonado, E.; Chattrakun, K.; Lin, S.; Schepartz, A.; Zhang, S.; Blanchard, S.; Engelhart, A. E.; Adamala, K. P., bioRxiv 2025. https://doi.org/10.1101/2025.06.10.658963

Further Confirmation of the Structure of 3′-(2-Pyridyldithio)-3′-deoxyadenosine and 3′-Thio-3′-deoxyadenosine: Synthetic Convergence with Cordycepin

Dover, T. L.; Robins, J. G.; Mercado, B. Q.; Schepartz, A.; Miller, S. J., J. Org. Chem. 2025. https://doi.org/10.1021/acs.joc.5c00954.

Escherichia coli ribosomes support translation of (R) and (S) β2-hydroxyacids in vitro: a structural and biochemical study

Majumdar, C.; Kent, A.; Hamlish, N.; Zhu, C.; Fitzgerald, K.; Schepartz, A.; Cate, J., ChemRxiv 2025. https://doi.org/10.26434/chemrxiv-2025-d1896

Monitoring monomer-specific acyl-tRNA levels in cells with PARTI

Pressimone, M. A.; Schissel, C. K.; Goss, I. H.; Swenson, C. V.; Schepartz, A., Nucleic Acids Res. 2025, 53 (8). https://doi.org/10.1093/nar/gkaf327

Highlight: Selected as a “Breakthrough Publication”.

Hastened Fusion-Dependent Endosomal Escape Improves Activity of Delivered Enzyme Cargo

Vázquez-Maldonado, A.; Chen, T.; Rodriquez, D.; Zoltek, M.; Schepartz, A., ACS Cent. Sci. 2025. https://doi.org/10.1021/acscentsci.5c00012

Peptide Backbone Editing via Post-Translational O to C Acyl Shift

Schissel, C. K.; Roberts-Mataric, H.; Garcia, I. J.; Kang, H.; Mowzoon-Mogharrabi, R.; Francis, M. B.; Schepartz, A., J. Am. Chem. Soc. 2025. https://pubs.acs.org/doi/10.1021/jacs.4c14103

Highlight: Feature article in C&EN 2025 “A sequence-independent way to edit protein backbones” (https://cen.acs.org/synthesis/sequence-independent-way-edit-protein/103/web/2025/02)

Highlight: Feature article in APS 2025 “Backbone Editing” (https://americanpeptidesociety.org/aps-news/backbone-editing/)

Requirements for efficient endosomal escape by designed mini-proteins

Giudice, J.; Brauer, D. D.; Zoltek, M.; Vázquez Maldonado, A. L.; Kelly, M. & Schepartz, A., Nat. Chem. 2025, accepted in principle.

Chemo-ribosomal synthesis of atropisomeric and macrocyclic peptides with embedded quinolines

Knudson, I. J.; Dover, T. L.; Dilworth, D. A.; Paloutzian, C.; Cho, H.; Schepartz, A.; Miller, S. J., Nat. Chem. 2025, accepted in principle.

Packaged delivery of CRISPR-Cas9 ribonucleoproteins accelerates genome editing

Karp, H.; Zoltek, M.; Wasko, K. M.; Vazquez, A. L.; Brim, J.; Ngo, W.; Schepartz, A.; Doudna, J., Nucleic Acids Res 2025, in press.

Thioesters support efficient protein biosynthesis by the ribosome

Kent, A.†; Robins, J. G.†; Knudson, I. J.; Vance, J. T.; Solivan, A. C.; Hamlish, N. X.; Fitzgerald, K. A.; Schepartz, A., Miller, S. J.; Cate, J. M. D., ACS Cent Sci 2025. https://doi.org/10.1021/acscentsci.4c01698.

Highlight: Promiscuity in Nature Extends to Central Protein Biosynthetic Machinery, ACS Cent. Sci. 2025 (https://pubs.acs.org/doi/10.1021/acscentsci.5c00387)

Direct and quantitative analysis of tRNA acylation using intact tRNA liquid chromatography–mass spectrometry

Fricke, R.; Knudson, I. J.; Swenson, C. V.; Smaga, S.; Schepartz, A., Nat Protocol 2025. https://doi.org/10.1038/s41596-024-01086-9

2024

Sporadic distribution of a new archaeal genetic code with all TAG codons as pyrrolysine

Kivenson, V.; Peters, S. L.; Borrel, G.; Kivenson, A.; Roe, L. T.; Hamlish, N. X.; Fadhlaoui, K.; Schepartz, A., Gribaldo, S.; Hettich, R. L.; Banfield, J. F., BioRxiv, 2024. https://doi.org/10.1101/2024.09.30.615893

Nonenzymatic, prebiotic aminoacylation couples chirality of RNA and protein

Davisson, J. A.; Kalb, E. M.; Knudson, I. J.; Schepartz, A.; Engelhart, A. E.; Adamala, K. bioRxiv, 2024. https://doi.org/10.1101/2024.07.29.605638

β-Amino Acids Reduce Ternary Complex Stability and Alter the Translation Elongation Mechanism

Cruz-Navarrete, F. A.†; Griffin, W. C.†; Chan, Y.-C.†; Martin, M. I.; Alejo, J. L.; Brady, R. A.; Natchiar, S. K.; Knudson, I. J.; Altman, R. B.; Schepartz, A.; Miller, S. J.; Blanchard, S. C. ACS Cent. Sci, 2024. https://doi.org/10.1021/acscentsci.4c00314

A translation-independent directed evolution strategy to engineer aminoacyl-tRNA synthetases

C. Soni, N. Prywes, M. Hall, D. F. Savage, A. Schepartz, & A. Chatterjee, ACS Cent. Sci, 2024, 10, 1211–1220. https://doi.org/10.1021/acscentsci.3c01557

Incorporation of Multiple β2-Hydroxy Acids into a Protein In Vivo Using an Orthogonal Aminoacyl-tRNA Synthetase

N. X. Hamlish, A. M. Abramyan, B. Shah, Z. Zhang & A. Schepartz, ACS Cent. Sci, 2024, 10, 1044–1053. https://pubs.acs.org/doi/10.1021/acscentsci.3c01366

HOPS-Dependent Endosomal Escape Demands Protein Unfolding

M. Zoltek, A. Vázquez, X. Zhang, N. Dadina, L. Lesiak, & A. Schepartz, ACS Cent. Sci, 2024. 10, 860-870. https://pubs.acs.org/doi/full/10.1021/acscentsci.4c00016

Minimization of the E. coli ribosome, aided and optimized by community science

T. Tangpradabkul, M. Z. Palo, J. Townley, K.B. Hsu, Eterna Participants, S. Smaga, R. Das & A. Schepartz, Nucleic Acids Res., 2024, 52, 1027–1042. https://doi.org/10.1093/nar/gkad1254

MAO–SiR is a tool for visualizing the inner workings of mitochondria

N. Dadina & A. Schepartz, Nat Chem Biol., 2024, 20, 15–16. https://doi.org/10.1038/s41589-023-01451-x

Long-term super-resolution inner mitochondrial membrane imaging with a lipid probe

S. Zheng, N. Dadina, D. Mozumdar, L. Lesiak, K.N. Martinez, E. W. Miller & A. Schepartz, Nat Chem Biol., 2024, 20, 83–92. https://doi.org/10.1038/s41589-023-01450-y

2023

High yield, low magnesium flexizyme reactions in a water-ice eutectic phase

J.A. Davisson, J.L. Alejo, M.Blank, E.M. Kalb, A. Prasad, I.J. Knudson, A. Schepartz, A.E. Engelhart & K.P. Adamala, bioRxiv, 2023. https://doi.org/10.1101/2023.12.03.569792

Backbone extension acyl rearrangements enable cellular synthesis of proteins with internal β2-peptide linkages

Roe, L.; Schissel, C. K.; Dover, T. L.; Shah, B.; Hamlish, N. X.; Zheng, S.; Dilworth, D. A.; Wong, N.; Zhang, Z.; Chatterjee, A.; Francis, M. B.; Miller, S. J.; Alanna Schepartz. bioRxiv. October 3, 2023, p 2023.10.03.560714. https://doi.org/10.1101/2023.10.03.560714.

A Bright, Photostable Dye that Enables Multicolor, Time Lapse, and SuperResolution Imaging of Acidic Organelles

Lesiak, L.; Dadina, N.; Zheng, S.; Schelvis, M.; Schepartz, A. ACS Cent. Sci., 2023

https://pubs.acs.org/doi/10.1021/acscentsci.3c01173

Atomistic simulations of the Escherichia coli ribosome provide selection criteria for translationally active substrates

Watson, Z. L.; Knudson, I. J.; Ward, F. R.; Miller, S. J.; Cate, J. H. D.; Schepartz, A.; Abramyan, A. M. Nat. Chem. 2023, 15 (7), 913–921. https://doi.org/10.1038/s41557-023-01226-w.

Aminobenzoic Acid Derivatives Obstruct Induced Fit in the Catalytic Center of the Ribosome

C. Majumdar, J.A. Walker, M.B. Francis, A. Schepartz & J.H.D. Cate, ACS Cent. Sci., 2023. https://doi.org/10.1021/acscentsci.3c00153

Expanding the substrate scope of PylRS enzymes to include non-⍺-amino acids in vitro and in vivo

Fricke, R.; Swenson, C. V.; Roe, L. T.; Hamlish, N. X.; Shah, B.; Zhang, Z.; Ficaretta, E.; Ad, O.; Smaga, S.; Gee, C. L.; Chatterjee, A.; Schepartz, A. Nat. Chem. 2023, 15 (7), 960–971. https://doi.org/10.1038/s41557-023-01224-y.

Dose-dependent nuclear delivery and transcriptional repression with a cell-penetrant MeCP2

Zhang, X.; Cattoglio, C.; Zoltek, M.; Vetralla, C.; Mozumdar, D.; Schepartz, A. ACS Cent. Sci. 2023, 9 (2), 277–288. https://doi.org/10.1021/acscentsci.2c01226.

2022

Suppression of p53 response by targeting p53-Mediator binding with a stapled peptide.

B. Allen, K. Quach, T. Jones, C. Levandowski, C. Ebmeier, J. Rubin, T. Read, R. Dowell, A. Schepartz & D. Taatjes, Cell Reports, 2022, 39, 110630. https://doi.org/10.1016/j.celrep.2022.110630

Redirecting RiPP Biosynthetic Enzymes to Proteins and Backbone-Modified Substrates.

J. A. Walker, N. Hamlish, A. Tytla, D. D. Brauer, M.B. Francis, and A. Schepartz, ACS Cent. Sci. 2022, 8, 473-483. https://doi.org/10.1021/acscentsci.1c01577

Targeted editing and evolution of engineered ribosomes in vivo by filtered editing.

F. Radford, S.D. Elliott, A. Schepartz, and F.J. Isaacs, Nat. Commun. 2022, 13, 180. https://doi.org/10.1038/s41467-021-27836-x

2021

Imaging organelle membranes in live cells at the nanoscale with lipid-based fluorescent probes.

N. Dadina, J. Tyson, S. Zheng, L. Lesiak, and A. Schepartz, Curr. Opin. Chem. Biol. 2021, 65, 154-162. https://doi.org/10.1016/j.cbpa.2021.09.003

Genetic code expansion in the engineered organism Vmax H2: high yield and exceptional fidelity.

S. Santiago González, O. Ad, B. Shah, Z. Zhang, X. Zhang, A. Chatterjee, and A. Schepartz, ACS Cent. Sci. 2021, 7 (9) 1500–1507. https://doi.org/10.1021/acscentsci.1c00499

Extremely bright, near-IR emitting spontaneously blinking fluorophores enable ratiometric multicolor nanoscopy in live cells.

J. Tyson, K. Hu, S. Zheng, P. Kidd, N. Dadina, L. Chu, D. Toomre, J. Bewersdorf, and A. Schepartz, ACS Cent. Sci. 2021, 7 (8) 1419–1426 https://doi.org/10.1021/acscentsci.1c00670

Highlight: Chosen for cover image.

Initiating protein synthesis with noncanonical monomers in vitro and in vivo.

J.M. Tharp, J.A. Walker, D. Söll, and A. Schepartz, Meth. Enzymol. 2021, 656, 495-519. https://doi.org/10.1016/bs.mie.2021.05.002

Cytosolic delivery of argininosuccinate synthetase using a cell-permeant miniature protein.

S.L. Knox, R. Wissner, S. Piszkiewicz, and A. Schepartz, ACS Cent. Sci. 2021, 7 (4) 641–649. https://doi.org/10.1021/acscentsci.0c01603

Genetic encoding of three distinct noncanonical amino acids using reprogrammed initiator and nonsense codons.

J.M. Tharp, O. Vargas-Rodriguez, A. Schepartz, and D. Söll. ACS Chem. Biol. 2021, 16 (4) 766–774. https://doi.org/10.1021/acschembio.1c00120

Allosteric inhibition of the epidermal growth factor receptor.

J.K.L. Sinclair, W.E. Robertson, D. Mozumdar, K. Quach, and A. Schepartz. Biochemistry 2021, 60 (7) 500–512. https://doi.org/10.1021/acs.biochem.0c00978

2020

Structure of the bacterial ribosome at 2 Å resolution.

Z.L. Watson, F.R. Ward, R. Méheust, O. Ad, A. Schepartz, J.F. Banfield, and J.H. Cate, eLife 2020, 9:e60482. https://www.ncbi.nlm.nih.gov/pubmed/32924932

Discrete coiled coil rotamers form within the EGFRvIII juxtamembrane domain.

D. Mozumdar, A. Doerner, J. Zhang, D. Rafizadeh, and A. Schepartz, Biochemistry 2020, 59 (41) 3965-3972. https://doi.org/10.1021/acs.biochem.0c00641

Two-color nanoscopy of organelles for extended times with HIDE probes.

L. Chu, J. Tyson, J.E. Shaw, F. Rivera-Molina, A.J. Koleske, A. Schepartz, and D.K. Toomre, Nat. Commun. 2020, 11 (1), 4271. https://doi.org/10.1038/s41467-020-17859-1

RNA sectors and allosteric function within the ribosome.

A.S. Walker, W.P. Russ, R. Ranganathan, and A. Schepartz, Proc. Natl. Acad. Sci. 2020, 117 (33) 19879-19887. https://doi.org/10.1073/pnas.1909634117

Quantification of protein delivery in live cells using fluorescence correlation spectroscopy.

S.L. Knox, A. Steinauer, G. Alpha-Cobb, A. Trexler, E. Rhoades, and A. Schepartz, Meth. Enzymol. 2020, 641, 477-505. https://doi.org/10.1016/bs.mie.2020.05.007

Endosome motility defects revealed at super-resolution in live cells using HIDE probes.

A. Gupta, F. Rivera-Molina, Z. Xi, D. Toomre, and A. Schepartz, Nat. Chem. Bio. 2020, 16 (4), 408-414. https://doi.org/10.1038/s41589-020-0479-z

Initiation of protein synthesis with non‐canonical amino acids in vivo.

J.M. Tharp, O. Ad, K. Amikura, F.R. Ward, E.M. Garcia, J.H.D. Cate, A. Schepartz, and D. Söll, Angew. Chem. 2020, 59 (8) 3122-3126. https://doi.org/10.1002/anie.201914671

2019

Dan Kahne: Winner of the 2019 Gordon Hammes Lectureship

A. Schepartz, Biochemistry 2019, 58, 3407.

Defects in the assembly of ribosomes selected for β-amino acid incorporation.

F.R. Ward, Z.L. Watson, O. Ad, A. Schepartz, and J.H.D. Cate, Biochemistry 2019, 58 (45) 4494-4504. https://doi.org/10.1021/acs.biochem.9b00746

Translation of diverse aramid- and 1,3-dicarbonyl-peptides by wild type ribosomes in vitro.

O. Ad, K.S. Hoffmann, A.G. Cairns, A.L. Featherston, S.J. Miller, D. Söll, and A. Schepartz, ACS Cent. Sci. 2019 5 (7) 1289-1294. https://doi.org/10.1021/acscentsci.9b00460

GEM-NET: Lessons in multi-institution teamwork using collaboration software.

S.G. Gaffney, O. Ad, S. Smaga, Z. Zhang, A. Schepartz, & J.P. Townsend, ACS Cent. Sci. 2019, 5 (7) 1159-1169. https://doi.org/10.1021/acscentsci.9b00111

Labeling strategies matter for super-resolution microscopy: A comparison between Halo- and SNAP-Tags.

R.S. Erdmann, S.W. Baguley, J.H. Richens, R.F. Wissner, Z. Xi, E.S. Allgeyer, S. Zhong, A.D. Thompson, N. Lowe, R. Butler, J. Bewersdorf, J.E. Rothman, D. St Johnston, A. Schepartz, and D. Toomre. Cell Chem Biol 2019, 26, 584–592. https://doi.org/10.1016/j.chembiol.2019.01.003

HOPS-dependent endosomal fusion required for efficient cytosolic delivery of therapeutic peptides and small proteins.

A. Steinauer, J.R. LaRochelle, S.L. Knox, R.F. Wissner, S. Berry, and A. Schepartz, Proc. Natl. Acad. Sci. USA 2019, 116 (2) 512. https://doi.org/10.1073/pnas.1812044116

2018

Special Issue on Discovering New Tools.

Schepartz. Biochemistry 2018, 57, 4605.

Synthesis and Biological Evaluation of an Indazole-Based Selective Protein Arginine Deiminase 4 (PAD4) Inhibitor.

Tjin, R. Wissner, H. Jamali, A. Schepartz, & J. Ellman, ACS Med Chem Lett 2018, 9, 1013.

Pushing the limits of solid-phase synthesis with continuous flow.

A.J. Mijalis, A. Steinauer, A. Schepartz, & B.L. Pentalute, Science of Synthesis: Flow Chemistry, Section 12, 2018, in press. DOI: 10.1055/sos-SD-228-00230

Fluorescence correlation spectroscopy reveals efficient cytosolic delivery of protein cargo by cell-permeant miniature proteins.

R.F. Wissner, A. Steinauer, S.L. Knox, A.D. Thompson, & A. Schepartz, ACS Cent. Sci. 2018, 4 (10) 1379-1393. https://doi.org/10.1021/acscentsci.8b00446

Introducing the Future of Biochemistry.

Schepartz. Biochemistry 2018, 57, 1.

Mechanism of allosteric coupling into and through the plasma membrane by EGFR.

J.K.L. Sinclair, A.S. Walker, A.E. Doerner, and A. Schepartz, Cell Chem. Biol. 2018, 25 (7) 857-870. https://doi.org/10.1016/j.chembiol.2018.04.005

Rapid phenolic O-glycosylation of small molecules and complex unprotected peptides in aqueous solvent.

T.J. Wadzinski, A. Steinauer, L. Hie, G. Pelletier, A. Schepartz, and S.J. Miller, Nat. Chem. 2018, 10, 644-652. https://doi.org/10.1038/s41557-018-0041-8

Highlights: Hitting the sweet spot, Nat. Chem.; Stop Ignoring the Sugars, Science

Foldamers wave to the ribosome.

A. Schepartz, Nat. Chem. 2018, 10, 377-379. https://doi.org/10.1038/s41557-018-0036-5

Unique arginine array improves cytosolic localization of hydrocarbon-stapled peptides.

Quach, J. LaRochelle. X-H. Li, E. Rhoades, A. Schepartz, Bioorg Med Chem 2018, 26,1197-1202.

2017

The ecstasy and agony of assay interference compounds.

Aldrich et al, J. Med, Chem. 2017, 60, 2165-2178.

Long-term live-cell STED nanoscopy of primary and cultured cells with the plasma membrane HIDE probe Dil-SiR.

A.D. Thompson, M.H. Omar, F. Rivera-Molina, Z. Xi, A.J. Koleske, D. Toomre, and A. Schepartz, Angew. Chem. 2017, 56 (35) 10408-10412. https://doi.org/10.1002/anie.201704783

Long time-lapse nanoscopy with spontaneously blinking membrane probes.

H. Takakura, Y. Zhang, R.S. Erdmann, A.D. Thompson, Y. Lin, B. McNellis, F. Rivera-Molina, S.N. Uno, M. Kamiya, Y. Urano, J.E. Rothman, J. Bewersdorf, A. Schepartz, and D. Toomre, Nat. Biotechnol. 2017, 35, 773-780. https://doi.org/10.1038/nbt.3876

Highlight: Nanoscopic imaging that lasts, Nat. Methods

STED imaging of Golgi dynamics with CerSiR: a two-component, photostable, high-density lipid probe for live cells.

R.S. Erdmann, D. Toomre, & A. Schepartz, Super-Resolution Microscopy: Methods and Protocols. 2017, in press.

A novel physiological role for ARF1 in the formation of bi-directional tubules from the Golgi.

Bottanelli, N. Kilian, A.M. Ernst, F. Molina-Rivera, L.K. Schroeder, E.B. Kromann, M.D. Lessard, R.S. Erdmann, A. Schepartz, D. Baddeley, J. Bewersdorf, D. Toomre, & J.E. Rothman, Mol. Biol. Cell. 2017, 28, 1676-1687.

2016

Building on 50 years of excellence where chemistry meets life science.

Schepartz, Biochemistry 2016, 55, 4997.

Rotamer-restricted fluorogenicity of the bis-arsenical ReAsH.

A.S. Walker, P.R. Rablen, and A. Schepartz, J. Am. Chem. Soc. 2016, 138 (22) 7143-50. https://doi.org/10.1021/jacs.6b03422

Highlight: Chosen for cover image.

β-peptide bundles: design. build. analyze. biosynthesize.

P.S. Wang and A. Schepartz, Chem. Commun. 2016, 52, 7420-32. https://doi.org/10.1039/C6CC01546H

In vivo biosynthesis of a β-amino acid-containing protein.

C.M. Czekster, W.E. Robertson, A.S. Walker, D. Söll, and A. Schepartz, J. Am. Chem. Soc. 2016, 138 (16) 5194-5197. https://doi.org/10.1021/jacs.6b01023

Aqueous glycosylation of unprotected sucrose employing glycosyl fluorides in the presence of calcium ion and trimethylamine.

Pelletier, A. Zwicker, C. Allen, A. Schepartz, & S. Miller, J. Am. Chem. Soc.2016, 138, 3175–3182.

Two-colour live-cell nanoscale imaging of intracellular targets.

F. Bottanelli, E.B. Kromann, E.S. Allgeyer, R.S. Erdmann, S.W. Baguley, G. Sirinakis, A. Schepartz, D. Baddeley, D.K. Toomre, J.E. Rothman, and J. Bewersdorf, Nat. Commun. 2016, 7, 10778. https://doi.org/10.1038/ncomms10778

Highlight: F1000Prime

2015

Discovery and characterization of a peptide that enhances endosomal escape of delivered proteins in vitro and in vivo.

Li, Y. Tao, Y. Shu, J.R. LaRochelle, A. Steinauer, D. Thompson, A. Schepartz, Z.-Y. Chen, & D. Liu, J. Am. Chem. Soc. 2015, 137, 14084-93.

Improved carbohydrate recognition in water with an electrostatically enhanced β-peptide bundle.

M.S. Melicher, A.S. Walker, J. Shen, S.J. Miller, & A. Schepartz, Org. Lett. 2015, 17, 4718-21.

Growth factor identity is encoded by discrete coiled-coil rotamers in the EGFR juxtamembrane region.

A. Doerner, R. Scheck, and A. Schepartz, Chem. Biol. 2015, 22 (6) 776-784. https://doi.org/10.1016/j.chembiol.2015.05.008

Highlight: Dialing in EGFR Signaling, Chem. Biol.

Structural differences between wild-type and double mutant EGFR modulated by third-generation kinase inhibitors.

M.A. Lowder, A.E. Doerner, and A. Schepartz, J. Am. Chem. Soc. 2015, 137 (20) 6456-9. https://doi.org/10.1021/jacs.5b02326

Highlight: Drug-Resistant EGFR May Have “Achilles Heel”, SciTechDaily

Fluorescence correlation spectroscopy reveals highly efficient cytosolic delivery of certain penta-arg proteins and stapled peptides.

J.R. LaRochelle, G.B. Cobb, A. Steinauer, E. Rhoades, and A. Schepartz, J. Am. Chem. Soc. 2015, 137 (7) 2536-2541. https://doi.org/10.1021/ja510391n

2014

Positive allostery in metal ion binding by a cooperatively folded β-peptide bundle.

J.P. Miller, M.S. Melicher, & A. Schepartz, J. Am. Chem. Soc. 2014, 136, 14726-9.

Influence of macrocyclization on allosteric, juxtamembrane-derived, stapled peptide inhibitors of EGFR.

J.K. Sinclair & A. Schepartz, Org. Lett. 2014, 16, 4916-9.

Inhibiting epidermal growth factor receptor at a distance.

J.K. Sinclair, E.V. Denton, & A. Schepartz, J. Am. Chem. Soc. 2014, 136, 11232-11235. Highlights: F1000 Prime (http://f1000.com/prime/718512057); SciBX (http://www.nature.com/scibx/journal/v7/n35/full/scibx.2014.1036.html)

Interactions of AsCy3 with cysteine-rich peptides.

S.C. Alexander & A. Schepartz, Org. Lett. 2014, 16, 3824-3827.

Hochaufgelöste Visualisierung des Golgi-Apparats in lebenden Zellen mit einem bioorthogonalen Ceramid.

R.S. Erdmann, H. Takakura, A.D. Thompson, F. Rivera-Molina, E.S. Allgeyer, J. Bewersdorf, D.K. Toomre, & A. Schepartz, Angew. Chem. Weinheim. Bergstr. Ger. 2014, 126, 10407-12.

Super-resolution imaging of the Golgi in live cells with a bio-orthogonal ceramide probe.

R.S. Erdmann, H. Takakura, A.D. Thompson, F. Rivera-Molina, E.S. Allgeyer, J. Bewersdorf, D.K. Toomre, & A. Schepartz, Angew. Chem. Int. Ed. Engl. 2014, 53, 10242-6. Highlight: Chosen as a “Hot Paper”.

Chemistry and the BRAIN initiative.

A.M. Andrews, A. Schepartz, J.V. Sweedler, & P.S. Weiss, J. Am. Chem. Soc. 2014, 136, 1-2.

Design and high-resolution structure of a β3-peptide bundle catalyst.

P.S.P. Wang, J.B. Nguyen, & A. Schepartz, J. Am. Chem. Soc. 2014, 136, 6810-6813.

2013

Improved assays for determining the cytosolic access of peptides, proteins, and their mimetics.

J.M. Holub, J.R. LaRochelle, J.S. Appelbaum, & A. Schepartz, Biochemistry 2013, 52, 9036-9046.

Combined lewis acid and bronstead acid-mediated reactivity of glycosyl trichloroacetimidate donors.

N.D. Gould, C.L. Allen, B.C. Nam, A. Schepartz, & S.J. Miller, Carbohydr. Res. 2013, 382, 36-42.

A β-peptide agonist of the GLP-1 receptor, a class B GPCR.

E.V. Denton, C.J. Craig, R.L. Pongratz, J.S. Appelbaum, A.E. Doerner, A. Narayanan, G.I. Shulman, G.W. Cline, & A. Schepartz, Org. Lett. 2013, 15, 5318-5321.

A β-boronopeptide bundle of known structure as a vehicle for polyol recognition.

M.S. Melicher, J. Chu, A.S. Walker, S.J. Miller, R.H.G. Baxter, & A. Schepartz, Org. Lett. 2013, 15, 5048-5051.

Remodeling a β-peptide bundle.

M.A. Molski, J.L. Goodman, F-C. Chou, D. Baker, R. Das, & A. Schepartz, RSC Chem. Sci. 2013, 4, 319-324.

2012

Arginine topology controls escape of minimally cationic proteins from early endosomes to the cytoplasm.

J.S. Appelbaum, J.M. LaRochelle, B.A. Smith, D.M. Balkin, J.M. Holub, & A. Schepartz, Chem. Bio. 2012,19, 819-830.

Bipartite tetracysteine display reveals allosteric control of ligand-specific EGFR activation.

R.A. Scheck, M.A. Lowder, J.S. Appelbaum, & A. Schepartz, ACS Chem. Bio. 2012, 7, 1367-1376. Highlight: Faculty of 1000: http://f1000.com/prime/717993412

Relationship between side-chain branching and stoichiometry in β3-peptide bundles.

P.S. Wang, C.J. Craig, & A. Schepartz, Tetrahedron 2012, 68, 4342-4345.

Rewiring kinase specificity with a synthetic adaptor protein.

E.M. Hobert & A. Schepartz, J. Am. Chem. Soc. 2012, 134, 3976-3978. Highlight: Angew. Chem. 2012 (doi: 10.1002/anie.201203345)

2011

Visualizing protein partnerships in living cells and organisms.

M.A. Lowder, J.S. Appelbaum, E.M. Hobert, & A. Schepartz, Curr. Opin. Chem. Biol. 2011, 15, 781-788.

Molecular imaging: sine labore nihil.

A. Schepartz & R.L. Gonzalez Jr., Curr. Opin. Chem. Biol. 2011, 15, 749-751.

Surveying protein structure and function using bis-arsenical small molecules.

R.A. Scheck & A. Schepartz, Acc. Chem. Res. 2011, 44, 654-665.

Enhancing β3-peptide bundle stability by design.

C.J. Craig, J.L. Goodman, & A. Schepartz, ChemBioChem 2011, 12, 1035-1038.

2010

Direct visualization of protein association in living cells with complex-edited electron microscopy.

R.J. Dexter & A. Schepartz, Angew. Chem. 2010, 49, 7952-7954.

β-Peptide bundles with fluorous cores.

M.A. Molski, J.L. Goodman, C.J. Craig, H. Meng, K. Kumar, & A. Schepartz, J. Am. Chem. Soc. 2010, 132, 3658-3659.

Visualizing tyrosine kinase activity with bipartite tetracysteine display.

Visualizing tyrosine kinase activity with bipartite tetracysteine display. S. Ray-Saha & A. Schepartz, ChemBioChem 2010, 11, 2089-2091 95.

β-Peptide bundles with fluorous cores.

M.A. Molski, J.L. Goodman, C.J. Craig, H. Meng, K. Kumar, & A. Schepartz, J. Am. Chem. Soc. 2010, 132, 3658-3659.

Bridged β3-peptide inhibitors of p53-hDM2 complexation: Correlation between affinity and cell permeability.

A.D. Bautista, J.S. Appelbaum, C.J. Craig, J. Michel, & A. Schepartz, J. Am. Chem. Soc. 2010, 132, 2904-2906.

2009

Bipartite tetracysteine display requires site flexibility for ReAsH coordination.

J.L. Goodman, D.B. Fried, & A. Schepartz, ChemBioChem 2009, 10, 1644-1647.

In silico improvement of β3-peptide inhibitors of p53•hDM2 and p53•hDMX.

Michel, E.A. Harker, J. Tirado-Rives, W.L. Jorgensen, & A. Schepartz, J. Am. Chem. Soc. 2009, 131, 6356-6357. Highlight: Nature Chem. 2009 (doi:10.1038/nchem.243)

Cell-permeable β-peptide inhibitors of p53•hDM2 complexation.

E.A. Harker & A. Schepartz, ChemBioChem 2009, 10, 990-993.

Identification of a β3-peptide HIV fusion inhibitor with improved potency in live cells.

A.D. Bautista, O.M. Stephens, L. Wang, R.A. Domaoal, K.S. Anderson, & A. Schepartz, Bioorg. Med. Chem. Lett. 2009, 19, 3736-3738.

β-peptides with improved affinity for hDM2 and hDMX.

E.A. Harker, D.S. Daniels, D.A. Guarracino & A. Schepartz, Bioorg. Med. Chem. 2009, 17, 2038-2046.

Selective recognition of protein tetraserine motifs with a cell-permeable, pro-fluorescent bis-boronic acid.

T.L. Halo, J. Appelbaum, E.M. Hobert, D.M. Balkin, & A. Schepartz, J. Am. Chem. Soc. 2009, 131, 438-439. Highlight: Faculty of 1000 Biology: http://www.f1000biology.com/article/id/1144997/evaluation

2008

Tetrameric β3-peptide bundles.

J.L. Goodman, M.A. Molski, J. Qui, & A. Schepartz, ChemBioChem 2008, 9, 1576-1578.

Minimally cationic cell-permeable miniature proteins via alpha-helical arginine display.

Smith, D.S. Daniels, A. Coplin, G. Jordan, & L. McGregor, & A. Schepartz, J. Am. Chem. Soc. 2008, 130, 2948-2949.

Toward β-amino acid proteins: Design, synthesis, and characterization of a fifteen kilodalton β-peptide tetramer.

E.J. Petersson & A. Schepartz, J. Am. Chem. Soc. 2008, 130, 821-823.

2007

Biophysical and structural characterization of a robust octameric β-peptide bundle.

J.L. Goodman, D.S. Daniels, J.X. Qiu, E.J. Petersson & A. Schepartz, J. Am. Chem. Soc. 2007, 129, 14746-14751.

Intrinsically cell-permeable miniature proteins based on a minimal cationic PPII motif.

D.S. Daniels & A. Schepartz, J. Am. Chem. Soc. 2007, 129, 14578-14579. Highlight: Chem. Eng. News 2007, 85, 43; Highlight: Faculty of 1000 Biology: http://www.f1000biology.com/article/id/1097219/evaluation

Engineering a monomeric miniature protein.

A.M. Hodges & A. Schepartz, J. Am. Chem. Soc. 2007, 129, 11024-11025.

Miniature protein ligands for EVH1 domains: Interplay between affinity, specificity, and cell motility.

J.H. Holtzman, D. Golemi-Kotra, K. Woronowicz & A. Schepartz, Biochemistry 2007, 46, 13541-13553.

Surveying protein conformation and association in live cells with small-molecule fluorescence.

Luedtke, R. Dexter, D. Fried & A. Schepartz, Nat. Chem. Biol. 2007, 3, 779-784. . Highlight: Science 2007, 318, 1217; Highlight: Nat. Methods 2008, 5, 6-7

Biophysical characterization of a β-peptide bundle: Comparison to natural proteins.

E.J. Petersson, C. Craig, D.S. Daniels, J.X. Qiu, & A. Schepartz, J. Am. Chem. Soc. 2007, 129, 1532-1533.

High resolution structure of a β-peptide bundle.

D.S. Daniels, E.J. Petersson, J.X. Qiu, & A. Schepartz, J. Am. Chem. Soc. 2007, 129, 1532-1533. Highlight: Chem. Eng. News 2007, 85(6), 7; Highlight: Chem. Eng. News 2007, 85(52), 13-19; Highlight: Faculty of 1000 Biology: http://www.f1000biology.com/article/id/1071733/evaluation

2006

Encodable activators of Src family kinases.

C.D. Zellefrow, J.S. Griffiths, S. Saha, A.M. Hodges, J.L. Goodman, J. Paulk, J.A. Kritzer & A. Schepartz, J. Am. Chem. Soc. 2006, 128, 16506-16507.

Toward β-amino acid proteins: A cooperatively folded β-peptide quaternary Structure.

J.X. Qiu, E.J. Petersson, E.E. Matthews & A. Schepartz, J. Am. Chem. Soc. 2006, 128, 11338-11339.

Relationship between salt-bridge identity and 14-helix stability of β3-peptides in aqueous buffer.

D.A. Guarracino, H.R. Chiang, T.N. Banks, J.D. Lear, M.E. Hodsdon & A. Schepartz, Org Lett. 2006, 8, 807-810.

Miniature protein inhibitors of the p53•hDM2 interaction.

J.A. Kritzer, R. Zutshi, M. Cheah, F.A. Ran, R. Webman, T.M. Wonjirad & A. Schepartz, ChemBioChem 2006, 7, 29-31.

2005

A Rapid Library Screen for Tailoring β-peptide Structure and Function.

J.A. Kritzer, N.W. Luedtke, E. Harker, & A Schepartz, J. Am. Chem. Soc. 2005, 127, 14584-14585. Highlight: Faculty of 1000: http://www.f1000biology.com/article/id/1028774/evaluation

Inhibiting HIV Fusion with a β-Peptide Foldamer.

O.M. Stephens, S. Kim, B.D. Welch, M.E. Hodsdon, M.S. Kay & A. Schepartz, J. Am. Chem. Soc. 2005, 127, 13126-13127.

Increasing the kinase specificity of K252a by protein surface recognition.

T.L. Schneider, R.S. Mathew, K.P. Rice, K. Tamaki, J.L. Wood & A. Schepartz, Org. Lett. 2005, 7, 1695-1698.

Relationship between folding and function in a sequence-specific miniature DNA-binding protein.

Yang & A. Schepartz, Biochemistry 2005, 44, 7469-7478.

Solution Structure of a β-peptide Ligand for hDM2.

J.A. Kritzer, M.E. Hodsdon & A. Schepartz, J. Am. Chem. Soc. 2005, 127, 4118-4119.

Dephosphorylation of Phosphopeptides by Cerium(IV) and Other Lanthanide Ions.

N.W. Luedtke & A. Schepartz, Chem. Comm. 2005, 43, 5426-5428.

β-peptide inhibitors of protein-protein interactions.

J.A. Kritzer, O.M. Stephens, D.A. Guarracino. S.K. Reznik & A. Schepartz, Bio. Med. Chem. 2005, 13, 11-16.

Binding mode and transcriptional activation potential of high affinity ligands for the CBP KIX domain.

H.M. Volkman, S.E. Rutledge, and A. Schepartz, J. Am. Chem. Soc. 2005, 127, 4649-4658.

Paralog-selective ligands for Bcl-2 proteins.

A.C. Gemperli, S.E. Rutledge, A. Maranda & A. Schepartz, J. Am. Chem. Soc. 2005, 127, 1596-1597.

Relationship between side chain structure and 14-helix stability of β3-peptides in water.

J.A. Kritzer, J. Tirado-Rives, S.A. Hart, J.D. Lear, W.L. Jorgensen, & A. Schepartz, J. Am. Chem. Soc. 2005, 127, 167-178.

2004

Helical β-peptide inhibitors of the p53-hDM2 interaction.

J.A. Kritzer, J.D. Lear, M. Hodsdon & A. Schepartz, J. Am. Chem. Soc. 2004, 126, 9468-9469.

High affinity, paralog-specific recognition of the Mena EVH1 domain by a miniature protein.

Golemi-Kotra, R. Mahaffy, M.J. Footer, J.H. Holtzman, T.D. Pollard, J.A. Theriot & A. Schepartz, J. Am. Chem. Soc. 2004, 126, 4.

2003

Molecular recognition of protein surfaces: High affinity ligands for the CBP KIX domain.

S.E. Rutledge, H. M. Volkman & A. Schepartz, J. Am. Chem. Soc. 2003, 125, 14336.

Helix macrodipole control of β3-peptide 14-helix stability in water.

S.A. Hart, A.B.F. Bahadoor, E.E. Matthews, & A. Schepartz, J. Am. Chem. Soc. 2003, 125, 4022.

Miniature Homeodomains: High specificity without an N-terminal arm.

J.K. Montclare & A. Schepartz, J. Am. Chem. Soc. 2003, 125, 3416.

2002

A View to a Kill: Ligands for Bcl-2 family proteins.

S.E. Rutledge, J.W. Chin & A. Schepartz, Curr. Op. Chem. Biol. 2002, 6, 479-485.

Gal4-VP16 and Gal4-AH increase the orientational and axial specificity of TATA box recognition by TBP.

A.R. Kays & A. Schepartz, Biochemistry 2002, 41, 3147-3155. Highlight: Faculty of 1000: http://www.f1000biology.com/article/id/1006604/evaluation

2001

Electrostatic Control of Half-Site Spacing Preferences by the cyclic AMP Response Element Binding Protein CREB.

J.K. Montclare, L.S. Sloan & A. Schepartz, Nucl. Acids Res. 2001, 29, 3311-3319.

Design and evolution of a miniature Bcl-2 binding protein.

J.W. Chin & A. Schepartz, Angew. Chem. Int. Ed. Eng. 2001, 40, 3806-3809. Highlight: Science 2001, 291, 2049.

Effects of nucleic acids and polyanions on dimer formation and DNA binding by dimeric transcription factors.

J.J. Kohler & A. Schepartz, Bioorg. Med. Chem. 2001, 9, 2435-2443.

Methodology for optimizing functional miniature proteins based on avian pancreatic polypeptide using phage display.

J.W. Chin, R.M. Grotzfeld, M.A. Fabian & A. Schepartz, Bioorg. Med. Chem. Lett. 2001, 11, 1501-1505.

Hepatitis B Virus protein pX enhances monomer assembly pathway of bZIP•DNA complexes.

T.L. Schneider & A. Schepartz, Biochemistry 2001, 40, 2835-2843.

A Roller Coaster Ride of Thrills.

Schepartz, Chem. Eng. News 2001,125th Anniversary Issue.

Kinetic Preference for Oriented DNA Binding by the Yeast TATA-Binding Protein TBP.

Liu & A. Schepartz, Biochemistry 2001, 40, 6257-6266.

Kinetic studies of Fos•Jun•DNA complex formation: DNA binding prior to dimerization.

J.J. Kohler & A. Schepartz, Biochemistry 2001, 40, 130-142.

Concerted evolution of structure and function in a miniature protein.

J.W. Chin & A. Schepartz, J. Am. Chem. Soc. 2001, 123, 2929-2930.

Hepatitis B virus X protein activates transcription by bypassing CREB phosphorylation, not by stabilizing bZIP-DNA complexes.

M.K. Pflum, D. Hall, T.L. Schneider, & A. Schepartz, Biochemistry 2001, 40, 693-703.

2000

Virtually unidirectional binding of TBP to the AdMLP TATA box within quaternary complex with TFIIA and TFIIB.

A.R. Kays & A. Schepartz, Chem. Biol. 2000, 7, 601-610.

1999

Gene Regulation: Protein escorts to the transcription ball.

J.W. Chin, J.J. Kohler, T.L. Schneider & A. Schepartz, Curr. Biol. 1999, 9, R929-R932.

DNA specificity enhanced by sequential binding of protein monomers.

J.J. Kohler, S.J. Metallo, T.L. Schneider & A. Schepartz, Proc. Natl. Acad. Sci. USA 1999, 96, 11735-11739.

Highly specific DNA recognition by a designed, miniature protein.

N.J. Zondlo & A. Schepartz, J. Am. Chem. Soc. 1999, 121, 6938-6939.

1998

Polarity of transcription on Pol II and archaeal promoters: where is the “one-way sign” and how is it read?

F.T. Tsai, O. Littlefield, P.F. Kosa, J. M. Cox, A. Schepartz & P.B. Sigler, Cold Spring Harb. Symp. Quant. Biol. 1998, 63, 53-61.

At the chemistry-biology interface.

Schepartz & P.S. Kim, Curr. Op. Chem. Biol. 1998, 2, 9-10.

Preinitiation complex assembly: Potentially a bumpy path.

J.M. Cox, A.R. Kays, J.F. Sanchez & A. Schepartz, Curr. Op. Chem. Biol. 1998, 2, 11-17.

Sequence determinants of the intrinsic bend in the cyclic AMP response element.

L.S. Sloan & A. Schepartz, Biochemistry 1998, 37, 7113-7118.

1997

Mechanism of DNA Binding Enhancement by the Hepatitis B Virus Protein X.

C.R. Palmer, L.D. Gegnas, A. Schepartz, Biochemistry 1997, 36, 15349-15355.

Induced DNA bending by the Zn2Cys6 binuclear cluster protein PUT3.

Hoffmann & A. Schepartz, Bio. Med. Chem. Lett. 1997, 7, 2049-2054.

Kinetics and Mechanism of RNA Binding by Triplex Tethered Oligonucleotide Probes.

A.C. Moses & A. Schepartz, J. Am. Chem. Soc. 1997, 119, 11591-11597.

The role of a basic amino acid cluster in target site selection and nonspecific binding of bZIP peptides to DNA.

S.J. Metallo, D.N. Paolella, & A. Schepartz, Nucl. Acids Res. 1997, 25, 2967-2972.

Bidirectional Binding of TBP to the TATA Box.

J.M. Cox, M.H. Hayward, J.F. Sanchez, L.D. Gegnas, S. van der Zee, J.H. Dennis, P.B. Sigler, & A. Schepartz, Proc. Natl. Acad. Sci. USA 1997, 94, 13475-13480.

Electrostatic Mechanism for DNA Bending by bZIP Proteins.

D.N. Paolella, Y. Liu & A. Schepartz, Biochemistry 1997, 36, 10033-10038.

Inhibition of Rev•RRE Complexation by Triplex Tethered Oligonucleotide Probes.

A.C. Moses, S.W. Huang & A. Schepartz, Bioorg. Med. Chem. 1997, 5, 1123-1129.

Certain bZIP Proteins Bind DNA Sequentially as Monomers and Dimerize on the DNA.

S.J. Metallo & A. Schepartz, Nat. Str. Biol. 1997, 4, 115-117.

1996

Triplex Tethered Oligonucleotide Probes.

A.C. Moses & A. Schepartz, J. Am. Chem. Soc. 1996, 118, 10896-10897.

1995

Conformation of Tax-response elements in the human T-cell leukemia virus type I promoter.

J.M. Cox, L.S. Sloan & A. Schepartz, Chem. Biol. 1995, 2, 819-826.

Studies on the Formation of Protein•DNA Interfaces: DNA Specificity and Straightening by CREB.

M.K. Hamm & A. Schepartz, Bio. Med. Chem. Lett. 1995, 5, 1621-1626.

DNA Bending and Binding by Metallo-Peptide Models of bZIP Proteins.

C.R. Palmer, L.S. Sloan, J.C. Adrian, Jr., B. Cuenoud, D.N. Paolella & A. Schepartz, J. Am. Chem. Soc. 1995, 117, 8899-8907.

Mechanism of DNA Binding Enhancement by the HTLV-I Transactivator Tax.

A.M. Baranger, C.R. Palmer, M.K. Hamm, H. A. Giebler, A. Brauweiler, J.K. Nyborg, & A. Schepartz, Nature 1995, 376, 606-608.

Convenient Syntheses of Reagents for Cleavage Mapping Experiments.

M. H. Hayward, J. C. Adrian, Jr. & A. Schepartz, J. Org. Chem. 1995, 60, 3924-3927.

Nonspecific DNA Bending and the Specificity of Protein•DNA Interactions.

Schepartz, Science 1995, 269, 988-989.

Peptide Models of bZIP Proteins: Quantitative Analysis of DNA Affinity and Specificity.

S.J. Metallo & A. Schepartz, Tech. Protein Chem. 1995, 6, 385-391.

Mechanistic Studies on the Formation of bZIP•DNA Interfaces: A Simple Example of Supramolecular Stereochemistry.

D.N. Paolella, C.R. Palmer, S.J. Metallo & A. Schepartz, in Supramolecular Stereochemistry, J. Siegel, Ed. NATO Adv. Ser. 1995, 83-90.

1994

A Uniquely Modified RNA: Site-Specific Introduction of a Single RNA Cleavage Agent into the M1 Ribozyme.

P.L. Richardson, M.L. Gross, R.D. Smith, K.J. Light-Wahl, & A. Schepartz, Bio. Med. Chem. Lett. 1994, 4, 2133-2138.

Distribution of Labor Among CRE-BP1 bZIP Segments in the Control of DNA Affinity and Specificity.

S.J. Metallo & A. Schepartz, Chem. Biol. 1994, 1, 143-152.

Mapping Regions in Eukaryotic Ribosomes that are Accessible to Methidiumpropyl- EDTA•Fe(II) and EDTA•Fe(II).

Han, A. Schepartz, M. Pelligrini & P.B. Dervan, Biochemistry 1994, 33, 9831-9844.

DNA Targets for Certain bZIP Proteins Distinguished by an Intrinsic Bend.

D.N. Paolella, C.R. Palmer & A. Schepartz, Science 1994, 264, 1130-1133.

Selection of Structure-Specific Inhibitors of the HIV Rev–Rev Response Element Complex.

S.T. Cload & A. Schepartz, J. Am. Chem. Soc. 1994, 116, 437-443.

1993

A Kinetic and Thermodynamic Analysis of RNA Binding by Tethered Oligonucleotide Probes: Alternative Structures and Conformational Changes.

S.T. Cload, P.L. Richardson, Y. Huang & A. Schepartz, J. Am. Chem. Soc. 1993, 115, 5005-5014.

1991

A General Scheme for Incorporating Nonnatural Functionality into Peptides.

Cuenoud & A. Schepartz, Tetrahedron Lett. 1991, 32, 3325-3328.

Cuenoud & A. Schepartz, Tetrahedron 1991, 47, 2535-2542.

1990

Site-Specific Cleavage of the Protein Calmodulin Using a Trifluoperazine-Based Affinity Reagent.

Schepartz & B. Cuenoud, J. Am. Chem. Soc. 1990, 112, 3247-3249.

1989

Self-Assembling Ionophores.

Schepartz & J.P. McDevitt, J. Am. Chem. Soc. 1989, 111, 5976-5977.

1987

On the Mechanism of Catalysis by the Enzyme Carboxypeptidase A.

Breslow & A. Schepartz, Chem. Lett. 1987, 1-4.

Hydrolysis of an Amide in a Carboxypeptidase Model Using Co(III) and Bifunctional Catalysts.

Schepartz & R. Breslow, J. Am. Chem. Soc. 1987, 109, 1814-1826.

1983

Substituent Effect on the Electrochemical Oxidation of Arylmethyl Anions. 3. Effect of Methyl Substitution on Diarylmethyl Anions.

Bank, A. Schepartz, P. Giammateo, J. Zubieta, J. Org. Chem. 1983, 48, 3548-3564.