2023
Atomistic simulations of the E. coli ribosome provide selection criteria for translationally active substrates
Z.L. Watson, I.Knudson, F.R. Ward, S.J. Miller, J.H.D. Cate, A. Schepartz & A.M. Abramyan, Nature Chem, accepted in principle. https://www.biorxiv.org/content/10.1101/2022.02.28.482149v3
Expanding the substrate scope of PylRS enzymes to include non-⍺-amino acids in vitro and in vivo
R. Fricke, C.V. Swenson, L.T. Roe, N. Hamlish, B. Shah, Z. Zhang, E. Ficaretta, O. Ad, S. Smaga, C.L. Gee, A. Chatterjee & A. Schepartz, Nature Chem, accepted in principle. https://www.biorxiv.org/content/10.1101/2022.02.28.482149v3
Dose-dependent nuclear delivery and transcriptional repression with a cell-penetrant MeCP2
X. Zhang, C. Cattoglio, M. Zoltek, C. Vetralla, D. Mozumdar & A. Schepartz, ACS Cent. Sci. 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.
Altered Specificity of DNA-Binding Proteins with Transition Metal Dimerization Domains.
B. Cuenoud & A. Schepartz, Science 1993, 259, 510-513.
Design of a Metallo-bZIP Peptide that Discriminates Between CRE and AP1 Target Sites: Selection Against AP1.
Cuenoud & A. Schepartz, Proc. Natl. Acad. Sci. USA 1993, 90, 1154-1159.
Protein-Cleavage Mapping: A New Tool for Drug Discovery and Protein Folding Studies.
Hayward & A. Schepartz, in Perspectives in Medicinal Chemistry, Testa, B., Kyburz, E., Fuhrer, W.; Giger, R., Eds., Verlag: Basel, 1993, p. 501-512.
1992
Conformation-Dependent Cleavage of Staphylococcal Nuclease with a Disulfide-Linked Iron Chelate.
M. Ermacora, J.M. Delfino, B. Cuenoud, A. Schepartz & R.O. Fox, Proc. Natl. Acad. Sci. USA 1992, 89, 6383-6387.
A New Strategy for Directed Protein Cleavage.
Cuenoud, T. Tarasow & A. Schepartz, Tetrahedron Lett. 1992, 33, 895-898.
Binding of Alkali Cations by Self-Assembling Ionophore Complexes of Ni(II).
M.W. Jones, N. Gupta, A. Schepartz & H. Thorpe, Inorg. Chem. 1992, 31, 1308-1310.
1991
A General Scheme for Incorporating Nonnatural Functionality into Peptides.
- Cuenoud & A. Schepartz, Tetrahedron Lett. 1991, 32, 3325-3328.
Polyether Tethered Oligonucleotide Probes.
S.T. Cload & A. Schepartz, J. Am. Chem. Soc. 1991, 113, 6324-6326.
Tethered Oligonucleotide Probes. A Strategy for the Recognition of Structured RNA.
P. Richardson & A. Schepartz, J. Am. Chem. Soc. 1991, 113, 5109-5111.
Synthesis of α-BOC-ɛ-EDTA-Lysine Tribenzyl Ester. An Amino Acid Analog Suitable for Solid Phase Peptide Synthesis.
- 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.