55.  Gosavi PM, Jayachandran M, Rempillo JJL, Zozulia O, Makhlynets OV, Korendovych IV. A designed enzyme promotes selective post‐translational acylation. ChemBioChem, 2018, May 13. Has been selected as a cover article.

54.  Lengyel Z, Rufo CM, Moroz YS, Makhlynets OV, Korendovych IV. Copper-containing catalytic amyloids promote phosphoester hydrolysis and tandem reactions. ACS Catal, 2018, 8, 59–62. Has been selected as a cover article for the first issue of 2018.

52.  Lee M, Wang T, Makhlynets OV, Wu Y, Polizzi NF, Wu H, Gosavi PM, Stöhr J, Korendovych IV, DeGrado WF, Hong M. Zinc-binding structure of a catalytic amyloid from solid-state NMR. Proc Natl Acad Sci USA. 2017, 114(24), 6191-6196.

51.  Makhlynets OV*, Korendovych IV*. Finding a silver bullet in a stack of proteins. Biochemistry. 2017, 56, 6627–6628.

50.    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

49.    M. Takacs, O.V. Makhlynets, P.L. Tolbert, I.V. Korendovych* Secretion of Functional Formate Dehydrogenase in Pichia Pastoris. Prot. Eng. Des. Sel. 2017, 30, 279-284  DOI: 10.1093/protein/gzx010.

48.    O.V. Makhlynets, I.V. Korendovych* Functional Frankensteins. Nat. Chem. 2016, 8, 823-824. DOI: 10.1038/nchem.2603

47.    P.M. Gosavi, I.V. Korendovych Minimalist IR and Fluorescence Probes of Protein Function. Curr. Opin. Chem. Biol. 2016, 34, 103-109  DOI: 10.1016/j.cbpa.2016.08.010

46.    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, 9017-9020 DOI: 10.1002/anie.201602480

             Featured as “Hot Paper”

45.    O.V. Makhlynets, I.V. Korendovych* Minimalist Design of Allosterically Regulated Protein Catalysts. Meth. Enzymol. DOI:10.1016/bs.mie.2016.05.055

44.    I.V. Korendovych* (Semi)rational Protein Design. Meth. Mol. Biol. Accepted.

43.    Z. Lengyel, C.M. Rufo and I.V. Korendovych* Preparation and Screening of Catalytic Amyloid Assemblies. Meth. Mol. Biol. Accepted.

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. Annu. Rev. Biomed. Eng. 2016, 18, 311-328 DOI: 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 Nonenzymatic Protein Give Rise to Various Enzymatic Activities. DOI: 10.1021/jacs.5b07812 J. Am. Chem. Soc. 2015, 137, 14905.

             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. DOI: 10.1016/j.ab.2015.09.016 Anal. Biochem. 2016, 492, 76-81.

39.    O.V. Makhlynets, E.A. Raymond and I.V. Korendovych* Design of Allosterically Regulated Protein Catalysts. DOI: 10.1021/bi5015248 Biochemistry. 2015, 54, 1444-1456.

             Highlighted on the Biochemistry website.

38.    Z. 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. DOI: 10.1002/bip.22624Peptide Sci. 2015, 104, 384-394.

37.    P.M. Gosavi, Y.S. Moroz and I.V. Korendovych* ß-(1-Azulenyl)-L-Alanine – a Functional Probe for Determination of pKa of Histidine Residues. DOI: 10.1039/C4CC08720H Chem. Commun. 2015, 51, 5347-5350.

             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. DOI: 10.1007/s00726-014-1870-4. Amino Acids, 2015, 47, 213-216.

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. DOI: 10.1002/pro.2622 Protein Sci. 2015, 24, 561-570.

34.    I.V. Korendovych,* W.F. DeGrado Catalytic efficiency of Designed Catalytic Proteins.(invited review) DOI: 10.1016/ Curr. Opin. Struct. Biol., 2014, 27, 113-121.

33.    O. V. Makhlynets, I.V. Korendovych* Design of catalytically amplified sensors for small molecules. DOI:10.3390/biom4020402 Biomolecules, 2014, 4, 402-418.

              Highlighted as “New and Notable” in MDPI Magazine.

32.   C.M. Rufo, Y.S. Moroz, O.M. Moroz, J. Stohr, T.A. Smith, Z. Hu, W.F. DeGrado, I.V. Korendovych* Short peptides self-assemble to produce catalytic amyloids.DOI:10.1038/nchem.1894, Nature Chem2014, 6, 303-309.

            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. DOI:10.1002/ange.201302339 Angew. Chem. Int. Ed. 2013, 52, 6246-6249.

              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. DOI:10.1007/s00775-013-0985 J. Biol. Inorg. Chem. 2013, 18, 411-418.

28. Y.S. Moroz, W. Binder, P. Nygren, G.A. Caputo, I.V. Korendovych* Painting Proteins Blue: ß-(1-Azulenyl)-L-Alanine as a Probe for Studying Protein-Protein Interactions. DOI:10.1039/C2CC37550H Chem. Commun. 2013, 49, 490-492.

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. DOI:10.1371/journal.pone.0048875 PLoS One 2012, 7, e48875.


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.