AT SYRACUSE
69. W. Luo, H. Noguchi, C. Chen, Y. Nakamura, C. Homma, O. Zozulia, I. V. Korendovych, Y. Hiyamizu De novo designed peptides form highly catalytic ordered nanoarchitechture on graphite surface Nanoscale, 2022, 14, 8326-8331. DOI: 10.1039/D2NR01507B
68. S. Bhattacharya, E. Margheritis, K. Takahashi, A. Kulesha, A. D’Souza, I. Kim, J. H. Yoon, J. R. H. Tame, A. N. Volkov,* O. V. Makhlynets,* I. V. Korendovych* NMR-Guided Directed Evolution Nature 2022, DOI: 10.1038/s41586-022-05278-9
67. R. Batra, T. D. Loeffler, H. Chan, S. Srinivasan, H. Cui, I. V. Korendovych, V. Nanda, L. C. Palmer, L. A. Solomon, H. C. Fry, and S. KRS Sankaranarayanan Self-assembling Peptide Discovery: Overcoming Human Bias With Machine Learning Nature Chemistry, accepted DOI:10.21203/rs.3.rs-505801/v1
66. O. Zozulia, L. R. Marshall, I. Kim, E. M. Kohn, and I. V. Korendovych Self-Assembling Catalytic Peptide Nanomaterials Capable of Highly Efficient Peroxidase Activity Chem. Eur. J. 2021, 27, 5388 –5392 Has been selected as a feature article.
65. L. R. Marshall and I. V. Korendovych* Catalytic Amyloids – Is Misfolding Folding? Curr. Opin. Chem. Biol. 2021, 64, 145-153
64. Z. Lengyel-Zhand, L. R. Marshall, M. Jung, M-C. Kim, A. Kriews, O.V. Makhlynets, H.C. Fry, A. Geyer and I. V. Korendovych* Covalent Linkage and Macrocyclization Preserve and Enhance Synergistic Interactions in Catalytic Amyloids ChemBioChem 2021, 22, 585-591
63. L. R. Marshall, M. Jayachandran, Z. Lengyel‐Zhand, C. M. Rufo, A. Kriews, M.‐C. Kim, I.V. Korendovych* Synergistic Interactions Are Prevalent in Catalytic Amyloids. ChemBioChem 2020, 21, 9292-9297. Has been selected as a cover article.
62. O. Zozulia and I.V. Korendovych* Semi-Rationally Designed Peptides Self-Assemble and Bind Hemin to Promote Cyclopropanation. Angew. Chem. Int. Ed. 2020, 132, 8185-8129. doi:10.1002/ange.201916712
61. I.V. Korendovych and W.F. DeGrado* De novo Protein Design, a Retrospective. Quart. Rev. Biophys. 2020, 53, E3. doi:10.1017/S0033583519000131
60. O.V. Makhlynets* and I.V. Korendovych* A Single Amino Acid Enzyme. Nat. Catal. 2019, 2, 9265-9275. .
59. L.R. Marshall, O. Zozulia, Z. Lengyel, I.V. Korendovych* Minimalist Design of Protein Catalysts. ACS Catalysis, 2019, 9, 949-950.
58. M.A. Nolan, P.N. Basa, O. Zozulia, Z. Lengyel, R. Lebl, E.M. Kohn, S. Bhattacharya, I.V. Korendovych* Catalytic Nanoassemblies Formed by Short Peptides Promote Highly Enantioselective Transfer Hydrogenation. ACS Nano 2019, 13, 9292-9297.
57. E. Casselle, J.H. Yoon, J.J.L. Rempillo, Z. Lengyel, S. Bhattacharya, Y.S. Moroz, P. Tolbert, Alexander Volkov, M. Forconi, C. A. Castaneda, O.V. Makhlynets,* I.V. Korendovych* Enzymes Designed by Minimalist Approach Possess High Catalytic Promiscuity. ChemCatChem 2019, 11, 1425-1430. Has been selected as a cover article.
56. G. Ghirlanda* and I.V. Korendovych* The Many Facets of Protein Design: From Self-Assembled Materials to Vaccines. (Editorial) Curr. Opin. Struct. Biol. 2018, 51, iv-vi.
55. I.V. Korendovych* Rational and Semi-rational Protein Design. Meth. Mol. Biol., 2018, 1685, 15-23.
54. Z. Lengyel, C. M. Rufo, and I.V. Korendovych* Preparation and Screening of Catalytic Amyloid Assemblies. Meth. Mol. Biol. 2018, 1777, Ch. 16.
53. O. Zozulia, M.A. Dolan and I.V. Korendovych* Catalytic Peptide Assemblies. Chem. Soc. Rev. 2018, 47, 3621-3639 DOI:10.1039/c8cs00080h
52. P. M. Gosavi, M. Jayachandran, J.J.L. Rempillo, C.M. Rufo, Y.S. Moroz, O. Zozulia, I.V. Korendovych* A Designed Enzyme Promotes Selective Post-translational Acylation. ChemBioChem, 2018, 19, 1605-1608. DOI:10.1002/cbic.201800196. Has been selected as a cover article.
51. Z. Lengyel, C.M. Rufo, Y.S. Moroz, O.V. Makhlynets, I.V. Korendovych* Copper-containing catalytic amyloids promote phosphoester hydrolysis and tandem reactions. ACS Cat., 2018, 8, 59-62. DOI:10.1021/acscatal.7b03323 Has been selected as a cover article for the first issue of 2018.
50. M. Lee, T. Wang, O. V. Makhlynets, Y. Wu, N. Polizzi, H. Wu, P. M. Gosavi, J. Stoehr, I. V. Korendovych, W. F. DeGrado, and M. Hong * Zinc-binding structure of a catalytic amyloid from solid-state NMR. Proc. Natl. Acad. Sci. U.S.A. 2017, 114, 6191-6196. DOI: 10.1073/pnas.1706179114
49. O.V. Makhlynets,* I.V. Korendovych* Finding a Silver Bullet in a Stack of Proteins. Biochemistry, 2017, 56, 6627-6628. DOI:10.1021/acs.biochem.7b01177
48. A. Li, B. Wang, A. Ilie, K.D. Dubey, G. Bange, I.V. Korendovych, S. Shaik, M.T. Reetz A Redox-mediated Kemp Eliminase. Nat. Commun., 2017, 8, 14876. DOI: 10.1038/ncomms14876.
47. M. Takacs, O.V. Makhlynets, P.L. Tolbert, I.V. Korendovych* Secretion of Functional Formate Dehydrogenase in Pichia Pastoris. Prot. Eng. Sel. Des.2017, 30, 279-284 DOI: 10.1093/protein/gzx010.
46. O.V. Makhlynets, I.V. Korendovych* Functional Frankensteins. (News and Views article). Nat. Chem. 2016, 8, 823-824. DOI: 10.1038/nchem.2603
45. P.M. Gosavi, I.V. Korendovych* Minimalist IR and Fluorescence Probes of Protein Function. Curr. Opin. Chem. Biol. 2016, 34, 103-139. DOI: 10.1016/j.cbpa.2016.08.010
44. O.V. Makhlynets,P.M. Gosavi, I.V. Korendovych* Short Peptides that Self-Assemble in the Presence of Copper are Capable of Oxygen Activation. Angew. Chem. Int. Ed. 2016, 55, 9017-9020DOI: 10.1002/anie.201602480
Featured as “Hot Paper”
43. O.V. Makhlynets,I.V. Korendovych* Minimalist Design of Allosterically Regulated Protein Catalysts. Meth. Enzymol. 2016, 580, 191-202. DOI:10.1016/bs.mie.2016.05.055
42. Y. Maeda, O.V. Makhlynets, H. Matsui* and I.V. Korendovych* Non-computational Design of Catalytic Peptides and Proteins through Rational and Combinatorial Approaches. (Invited Review) Ann. Rev. Biomed. Eng.2016, 18, 311-328DOI: 10.1146/annurev-bioeng-111215-024421.
41. Y.S. Moroz, T.T. Dunston, O.V. Makhlynets,O.V. Moroz, Y. Wu, J.H. Yoon, A.B. Olsen, J.M. McLaughlin, K.L. Mack, P.M. Gosavi, N.A.J. van Nuland, I.V. Korendovych* New Tricks For Old Proteins: Single Mutations in a Non-Enzymatic Protein Give Rise to Various Catalytic Activities. J. Am. Chem. Soc. 2015, 137, 14905-14911. DOI: 10.1021/jacs.5b07812.
Highlighted in JACS Spotlights.
40. H. Zheng, I.V. Korendovych* and Y.-Y. Luk* Quantification of Alginate by Aggregation Induced by Calcium Ions and Fluorescent Polycations. Anal. Biochem. 2016, 492, 76-81. DOI:10.1016/j.ab.2015.09.016
39. O.V. Makhlynets, E.A. Raymond and I.V. Korendovych* Design of Allosterically Regulated Protein Catalysts. Biochemistry. 2015, 54, 1444-1456. DOI: 10.1021/bi5015248.
Highlighted on the Biochemistry website.
38. Ridgeway, A.L. Picciano, P.M. Gosavi, Y.S. Moroz, C.E. Angevine, A.E. Chavis, J. Reiner, I.V. Korendovych* and G.A. Caputo* Functional Characterization of a Melittin Analog Containing a Non-natural Tryptophan Analog. Biopolymers: Peptide Sci. 2015, 104, 384-394. DOI: 10.1002/bip.22624
37. P.M. Gosavi, Y.S. Moroz and I.V. Korendovych* ß-(1-Azulenyl)-L-Alanine – a Functional Probe for Determination of pKaof Histidine Residues. Chem. Commun. 2015, 51, 5347-5350. DOI: 10.1039/C4CC08720H
Invited paper for the 2015 Emerging Investigators Issue.
36. J. Shao, I.V. Korendovych and J. Broos* Biosynthetic Incorporation of the Azulene Moiety in Proteins with High Efficiency. Amino Acids, 2015, 47, 213-216. DOI: 10.1007/s00726-014-1870-4
35. E.A. Raymond,#K.L. Mack, J.H. Yoon, O.V. Moroz,^Y.S. Moroz^and I.V. Korendovych* Design of an Allosterically Regulated Retroaldolase. Protein Sci. 2015, 24, 561-570. DOI: 10.1002/pro.2622.
34. I.V. Korendovych,* W.F. DeGrado Catalytic Efficiency of Designed Catalytic Proteins. Curr. Opin. Struct. Biol. 2014, 27, 113-131. DOI: 10.1016/j.sbi.2014.06.006
33. O. V. Makhlynets,^I.V. Korendovych* Design of catalytically amplified sensors for small molecules. Biomolecules, 2014, 4,402-418.DOI:10.3390/biom4020402
Highlighted as “New and Notable” in MDPI Magazine.
32. C.M. Rufo, Y.S. Moroz, O.M. Moroz, J. Stöhr, T.A. Smith, Z. Hu, W.F. DeGrado, I.V. Korendovych*Short peptides self-assemble to produce catalytic amyloids. Nat. Chem. 2014, 6, 303-309. DOI:10.1038/nchem.1894
See News and Views in Nature Chem. 2014, 6, 273-274 DOI:10.1038/nchem.1904.
Featured in C&E News, 2014, 92(11), 34.
Featured in New Scientist.
Featured in Chemistry World.
Featured in Air and Space.
Featured on the SU website.
31. A. Ghosh, J. Wang, Y.S. Moroz, I.V. Korendovych, M. Zanni, W.F. DeGrado, F. Gai, R.M. Hochstrasser 2D IR Spectroscopy Reveals the Role of Water in the Binding of Channel-Blocking Drugs to the Influenza M2 Channel. DOI:10.1063/1.4881188 J. Chem. Phys.2014, 140, 235105.
30. O.V. Moroz, Y.S. Moroz, Y. Wu, A.B. Olsen, H. Cheng, K.L. Mack, J.M. McLaughlin, E.A. Raymond, K. Zhezherya, H. Roder, I.V. Korendovych* A Single Mutation in a Regulatory Protein Produces Evolvable Allosterically Regulated Catalyst of Unnatural Reaction. Angew. Chem. Int. Ed. 2013, 52,6246-6249. DOI: 10.1002/ange.201302339
Featured in C&E News 2013, 91(33), 26-27.
29. K.L. Mack, O.V. Moroz, Y.S. Moroz, A.B. Olsen, J.M. McLaughlin, I.V. Korendovych* Reprogramming EF-hands for Design of Catalytically Amplified Lanthanide Sensors. J. Biol. Inorg. Chem. 2013, 18, 411-418. DOI: 10.1007/s00775-013-0985-5
28. Y.S. Moroz, W. Binder, P. Nygren, G.A. Caputo, I.V. Korendovych* Painting Proteins Blue: ß-(1-Azulenyl)-L-Alanine as a Tryptophan Mimic for Studying Protein-Protein interactions.Chem. Commun.2013, 49, 490-492. DOI: 10.1039/C2CC37550H
27. J.I. Godfroy III, M.Roostan, Y.S. Moroz, I.V. Korendovych, H. Yin Isolated Toll-like Receptor Transmembrane Domains are Capable of Oligomerization.PLoS One2012, 7, e48875. DOI: 10.1371/journal.pone.0048875.
PREVIOUS WORK
26. S.J. Shandler, I.V. Korendovych, D.T. Moore, K.B. Dupont-Smith, C.N. Streu, R.I. Litvinov, P.C. Billings, F. Gai, J.S. Bennett, W.F. DeGrado Computational design of a beta–peptide that targets transmembrane helices. J. Am. Chem. Soc. 2011, 133, 12378-12381.
25. I.V. Korendovych, S.J. Shandler, G. Montalvo, W.F. DeGrado. Environment and sequence-dependence of helical type in membrane-spanning peptides composed of beta3-amino acids. Org. Lett. 2011, 13, 3474-3477.
24. A. Remorino, I.V. Korendovych, Y. Wu, W.F. DeGrado, R.M. Hochstrasser. Residue specific vibrational echoes yield three dimensional structures of a transmembrane protein. Science 2011, 332, 1206-1209.
Highlighted as Editor’s Choice in Sci. Signal. 2011, 4, ec161
23. I.V. Korendovych, D.W. Kulp, Y. Wu, H. Cheng, H. Roder, W.F. DeGrado. Design of a Switchable Eliminase. Proc. Natl. Acad. Sci. U.S.A. 2011, 108, 6823-6827.
22. H. Jo, R.M. Culik, I.V. Korendovych, W.F. DeGrado, F. Gai. Selective Incorporation of Nitrile-Based Infrared Probes into Proteins via Cysteine Alkylation. Biochemistry 2010, 49, 10354-10356.
21. I.V. Korendovych, Y.H. Kim, A.H. Ryan, J.D. Lear, W.F. DeGrado, S.J. Shandler. Computational Design of a beta-peptide Oligomer. Org. Lett. 2010, 12, 5142-5145.
20. I.V. Korendovych, A. Senes, Y.H. Kim, J.D. Lear, H.C. Fry, M.J. Therien, J.K. Blasie, F.A. Walker, W.F. DeGrado De novo Design and Molecular Assembly of a Transmembrane Diporphyrin-binding Protein Complex. J. Am. Chem. Soc. 2010, 132, 15516-15518.
19. J.Y. Yang, S.-Y. Liu, I.V. Korendovych, E.V. Rybak-Akimova, D.G. Nocera. Hangman Salen Platforms Containing Dibenzofuran Scaffolds. ChemSusChem 2008, 1, 941-949.
18. I.V. Korendovych, M. Cho, O.V. Makhlynets, P. Butler, R.J. Staples, E.V. Rybak-Akimova. Anion and Carboxylic Acid Binding to Monotopic and Ditopic Amidopyridine Macrocycles. J. Org. Chem. 2008, 73, 4771-4782. Selected as a cover article of the issue.
17.I.V. Korendovych, S.V. Kryatov, E.V. Rybak-Akimova. Dioxygen Activation at Non-Heme Iron: Insights from Rapid Kinetic Studies. Acc. Chem. Res. 2007, 40, 510-521.
16.I.V. Korendovych, O.P. Kryatova, W.M. Reiff, E.V. Rybak-Akimova. Iron(II) Complexes with Amide-Containing Macrocycles as Non-Heme Porphyrin Analogues. Inorg. Chem. 2007, 46, 4197-4211.
15. I.V. Korendovych, R.A. Roesner, E.V. Rybak-Akimova. Molecular Recognition of Neutral and Charged Guests Using Metallomacrocyclic Hosts. Adv. Inorg. Chem. 2007, 59, 109-173.
14. A. Company, L. Gómez, R. Mas-Ballesté, I.V. Korendovych, X. Ribas, A. Poater, T. Parella, X. Fontrodona, J. Benet-Buchholz, M. Solà, L. Que Jr, E.V. Rybak-Akymova, M. Costas Fast O2 Binding at Dicopper Complexes Containing Schiff Base Dinucleating Ligands. Inorg. Chem. 2007, 46, 4997–5012.
13. I.V. Korendovych, M. Cho, P. Butler, R.J. Staples, E.V. Rybak-Akimova. Anion Binding to Monotopic and Ditopic Macrocyclic Amides. Org. Lett. 2006, 8, 3171-3174.
12. I.V. Korendovych, O.V. Makhlynets, S.K. Buzak, M.M. Flook, S.V. Kryatov, T.E. Haas, E.V. Rybak-Akimova. (1R,2R)-(+)-4,4′-Di-tert-butyl-2,2′-[1,2-diphenylethane-1,2-diylbis(nitrilomethylidyne)]diphenol. Acta Cryst. 2006 E62, o1240-o1242.
11. I.V. Korendovych, S.V. Kryatov, W.M. Reiff, E.V. Rybak-Akimova. Diiron(II) mu-aqua mu-hydroxo Model for Non-Heme Iron Sites in Proteins. Inorg. Chem. 2005, 44, 8656-8658.
10. S. V. Kryatov, S. Taktak, I. V. Korendovych, E. V. Rybak-Akimova, J. Kaizer, S. Torelli, Xiaopeng Shan, S. Mandal, V. L. MacMurdo, A. Mairata i Payeras, L. Que, Jr. Dioxygen Binding to Complexes with FeII2(mu-OH)2 Cores: Steric Control of Activation Barriers and O2-Adduct Formation. Inorg. Chem. 2005, 44, 85 – 99
9. I.V. Korendovych, R.J. Staples, W.M. Reiff, E.V. Rybak-Akimova. A New High-spin Iron(III) Complex with a Pentadentate Macrocyclic Amidopyridine Ligand: A Change From Slow Single Ion Paramagnetic Relaxation to Long Range Anti-ferromagnetic Order in a Hydrogen-bonded Network. Inorg. Chem. 2004, 43, 3930-3941.
8. O.P. Kryatova, I.V. Korendovych, E.V. Rybak-Akimova Complexes of benzo-15-crown-5 with protonated primary amines and diamines. Tetrahedron, 2004, 60, 4579-4588.
7. I.V. Korendovych, E.V. Rybak-Akimova Chloro{2,2′-[(1S,2S)-1,2-diphenyl-1,2-ethanediylbis(nitrilomethylidyne)]diphenolato-k4 O,N,N’,O’}(ethanol-kO)manganese(III). Acta Cryst. 2004 C60, m82-m84.
6. A. M. Herrera, G. V. Kalayda, J. S. Disch, J. P. Wikstrom, I. V. Korendovych, R. J. Staples, C. F. Campana, A. Y. Nazarenko, T. E. Haas, E. V. Rybak-Akimova Reactions at the Azomethine C=N Bonds in the Nickel(II) and Copper(II) Complexes of Pyridine-containing Schiff-base Macrocyclic Ligands. Dalton. Trans. 2003, 4482-4492.
5. I.V. Korendovych, E.V. Rybak-Akimova (-)-(1S,2S)-N,N‘-Bis(salicylidene)-1,2-diphenyl-1,2-ethanediamine. Acta Cryst. 2003 E59, o1498-o1500.
4. O.P. Kryatova, I.V. Korendovych, E.V. Rybak-Akimova Proton-induced Supramolecular Dimerization of Aminomethylenebenzo-15-crown-5 Accompanied by Covalent Dimerization of Cyanoborohydride Anion. Tetrahedron Letters 2003, 44, 4251-4255.
3. A.I. Brusilovets, I.V. Korendovich, T. Lis, O.V. Manoilenko Reactions of N,N,N1-tris(trimethylsily)amide and N,N-bis(trimethylsilyl)-N’-tert-butylamide Imidophosphenic Acid with Titanium and Zirconium Tetrabenzyls. Ukrainskii Khimicheskii Zhurnal (Russian Edition) 2003, 69, 92-94.
2. V.V. Trachevskii, A.I. Brusilovets, I.V. Korendovich, V.G. Bdzhola, I.G. Ryabokon Reactions of Molybdenum(V) Oxychloride with Diimidophosphenic Acid N,N,N’,N”-tetrakis(trimethylsily)amide and Thiophosphenic Acid N,N-bis(trimethylsilyl)amide and N’-tert-butylimide. Ukrainskii Khimicheskii Zhurnal (Russian Edition) 2002, 68, 14-18.
1. A.I. Brusilovets, I.V. Korendovich Reactions of niobium, tantalum, tin, and zirconium alkoxides with N’-(1,1-dimethylethyl)-N,N-bis(trimethylsilyl)phosphenimidothioic amide. Ukrainskii Khimicheskii Zhurnal (Russian Edition) 1997, 63, 84-88.