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As of July 3, 2022 publications on this list were cited 3,634 times with ten having over 100 cites. Average citation per pub = 46.
*** – indicates papers with more than 100 citations in the list below
Andrei’s cumulative h-index = 35 for all years, i-index = 54 (source for wonderful metric statistics -> Google Scholar)

Publications (last updated July 3, 2022); Legend: Underlined = corresponding author

79) Mitchell, W., Tamucci, J.D., Ng, E.L., Liu, S., Birk, A.V., Szeto, H.H., May, E.R. Alexandrescu, A.T & Alder, N.N.(2022) “Structure Activity Relationships of Mitochondria-Targeted Tetrapeptide Pharmacological Compounds”, eLife, in press

78) Whitehead, R. D. III, Teschke, C.M., & Alexandrescu, A.T (2022) “Pulse-field gradient nuclear magnetic resonance of protein translational diffusion from native to non-native states”, Protein Sci 31, e4321.

77) Alexandrescu, A.T (2021) “To be or not to B-chromosome”, MCB Expressions 2020-2021.

76) Kaplan, A.R., Olson, R. & Alexandrescu, A.T (2021) “Protein yoga: conformational versatility of the hemolysin II C-terminal domain detailed by NMR structures for multiple states”, Protein Sci 30, 990-1005.

75) Dedeo, C.L., Teschke, C.M., & Alexandrescu, A.T (2020) “Keeping it together: structures, functions, and applications of viral decoration proteins”, Viruses 12 (Michael Rossmann Memorial Issue), 1163.

74) Whitehead, R. D. III, Teschke, C.M., & Alexandrescu, A.T (2019) “NMR mapping of disordered segments for a viral scaffolding protein enclosed in a 23 MDa procapsid”, Biophysics J. 117, 1387-1392.

73) Newcomer, R.L., Schrad, J.R., Gilcrease, E.B., Casjens, S.R., Feig, M., Teschke, C.M., Alexandrescu, A.T, & Parent K.N. (2019) “The phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy”, eLife 8: e45345.

72) Tripler, T.N., Kaplan, A.R., Alexandrescu, A.T, & Teschke, C.M. (2019) “Conservation and divergence of the I-domain inserted into the ubiquitous HK97 coat protein fold in the P22-like bacteriophages”, Journal of Virology 93, pii: e00007-19

71) Newcomer, R.L., Belato, H.B.,Teschke, C.M. & Alexandrescu, A.T. (2018) “NMR assignments for monomeric phage L decoration protein”, Biomol. NMR Assign. 12, 339-343.

70) Asthana, S., Mallick, B., Alexandrescu, A.T. & Jha, S. (2018) “IAPP in type II diabetes: Basic research on structure, molecular interactions, and disease mechanisms suggests potential intervention strategies”, BBA Biomembranes (special issue on Protein Aggregation) 1860, 1765-1782.

69) Kaplan, A.R, Kaus, K., De, S., Olson, R., & Alexandrescu, A.T. (2017) “NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold”, Scientific Reports 7, 3277.

68) Kaplan, A.R, Brady, M.R., Maciejewski, M.W., Kammerer, R.A., & Alexandrescu, A.T. (2017) “Nuclear Magnetic Resonance structures of GCN4p Are Largely Conserved When Ion Pairs Are Disrupted at Acidic pH but Show a Relaxation of the Coiled Coil Superhelix”, Biochemistry 56, 1604-1619.

67) Tripler, T.N., Teschke, C.M, & Alexandrescu, A.T. (2017) “NMR assignments for the insertion domain of bacteriophage Sf6 coat protein.”, Biomol. NMR Assign. 11, 35-38.

66) Harprecht, C., Okifo, O., Robbins, K.J., Motwani, T., Alexandrescu, A.T. & Teschke, C.M (2016) “Contextual role of a salt-bridge in the phage P22 coat protein I-domain.”, J. Biol. Chem. 291, 11359-11372.

65) Alexandrescu, A.T. (2016) “Quenched Hydrogen Exchange NMR of Amyloid Fibrils.” Methods in Mol. Biol. 1345, 211-222.

64) Newcomer, R.L., Fraser, L.C.R., Teschke, C.M. & Alexandrescu, A.T. (2015) “Mechanism of protein denaturation: partial unfolding of the P22 coat protein I-domain by urea binding.”, Biophysical J. 109, 2666-2677.

63) Tripler, T.N., Maciejewski, M.W., Teschke, C.M. & Alexandrescu, A.T. (2015) “NMR assignments for the insertion domain of bacteriophage CUS-3 coat protein.” Biomolecular NMR Assignments 9, 333-336.

62) Patil S.M., & Alexandrescu, A.T. (2015) “Charge-based inhibitors of amylin fibrillization and totoxicity.” J. Diabetes Res., Article ID 946037.

61) Rizzo, A.A., Suhanovsky, M.M., Baker, M.L., Fraser, L.C.R., Jones, L.M., Rempel, D.L., Gross, M.L., Chiu, W., Alexandrescu, A.T. & Teschke, C.M. (2014) “Multiple functional roles of the accessory I-domain of bacteriophage P22 coat protein revealed by NMR structure and cryoEM modeling”. Structure 22, 830-841.

60) Sheftic, S.R., White, E., Gage, D.J. & Alexandrescu, A.T. (2014) “NMR structure of the HWE kinase associated response regulator Sma0114 in its activated state”. Biochemistry 53, 311-322.

***59) Jha, S., Snell, J.M., Sheftic, S.R., Patil S.M., Daniels, S.B., Kolling, F.W., & Alexandrescu, A.T. (2014) “pH dependence of amylin fibrillization”. Biochemistry 53, 300-310.

58) Kaplan, A.R., Maciejewski, M.W., Olson, R., & Alexandrescu, A.T. (2014) “NMR assignments for the cis and trans forms of the hemolysin II C-terminal domain”. Biomolecular NMR Assignments 8, 419-423.

57) Alexandrescu, A.T. (2013) “Amide proton protection in amylin fibrils probed by quenched hydrogen exchange NMR.” PLoS ONE 8, e56467.

56) Rizzo, A.A., Fraser, L.C.R., Sheftic, S.R., Suhanovsky, M.M., Teschke, C.M. & Alexandrescu, A.T. (2013) “NMR assignments for the telokin-like domain of bacteriophage P22 coat protein”. Biomolecular NMR Assignments 7, 257-260.

55) Sheftic, S.R., Garcia, P.P., White, E., Robinson, V.L., Gage, D. & Alexandrescu, A.T. (2012) “Nuclear Magnetic Resonance Structure and Dynamics of the Response Regulator Sma0114 from Sinorhizobium meliloti”. Biochemistry 51, 6932-6941.

54) Sheftic, S.R., Snell, J. M., Jha, S. & Alexandrescu, A.T. (2012) “Inhibition of Semen-derived Enhancer of Virus Infection (SEVI) fibrillogenesis by physiological zinc and copper concentrations”, European Biophysics Journal 41, 695-704.

53) Jha, S., Patil, S.M., Gibson, J., Nelson, C.E., Alder, N.N., Alexandrescu, A.T. (2011) “Mechanism of amylin fibrillization enhancement by heparin”. J. Biol. Chem. 286, 22894-22904.

52) Patil, S.M., Mehta, A., Jha, S. & Alexandrescu, A.T (2011) “Heterogeneous amylin fibril growth mechanisms imaged by Total Internal Reflection Fluorescence Microscopy”. Biochemistry 50, 2808-2819.

51) Croke, R.L., Patil, S.M., Queveraux, J., Kendall, D.A., & Alexandrescu, A.T (2011) “NMR Determination of pKa Values in a-synuclein”. Protein Science 20, 256-269.

50) Sheftic, S.R.,Garcia, P.P., Robinson, V.L., Gage, D.J, & Alexandrescu, A.T (2011) “NMR Assignments for the Sinorhizobium meliloti Response Regulator Sma0114″. Biomolecular NMR Assignments 5, 55-58.

49) Sheftic, S.R., Croke, R.L., LaRochelle, J.R., & Alexandrescu, A.T. (2009) “Electrostatic contributions ro the stabilities of native proteins and amyloid complexes”. Methods in Enzymology 466: 233-258.

48) Guardino, K.M., Sheftic, S.R., Slattery, R.E., & Alexandrescu, A.T. (2009) “Hallmarks of conserved and non-conserved structures in the OB-fold superfamily”. Int. J. Mol. Sci. 10, 2412-2430.

*** 47) Patil, S.M., Xu, S., Sheftic, S.R., & Alexandrescu, A.T. (2009) “Dynamic alpha-helix structure of micelle-bound human amylin”, J Biol Chem, 284, 11982-11991.

46) Alexandrescu, A.T. & Croke, R.L. (2008) “NMR of amyloidogenic proteins”, in Protein Misfolding (O’Doherty C.B., and Byrne, A.C. eds.) Nova Publishers, Hauppauge, NY. ISBN 978-1-60456-881-3

*** 45) Croke, R.L., Sallum, C.O., Watson, E., Watt, E.D., & Alexandrescu, A.T. (2008) “Hydrogen exchange of monomeric alpha-synuclein shows unfolded structure persists at physiological temperature and is independent of molecular crowding in Escherichia coli.” Protein Sci. 17, 1434-1445.

44) Matousek, W.M., Ciani, B., Fitch, C.A., Garcia-Moreno E., B., Kammerer, R.A. & Alexandrescu, A.T. (2007) “Electrostatic contributions to the stability of the GCN4 leucine zipper structure”, J Mol Biol., 374, 206-219

43) Sallum, C.O., Kammerer, R.A., & Alexandrescu, A.T. (2007) “Thermodynamic and structural studies of carbohydrate binding by the agrin-G3 domain”, Biochemistry, 46, 9541-9550.

42) Watson, E., Matousek, W.M., Irimies, E.L. & Alexandrescu, A.T. (2007) “Partially folded states of staphylococcal nuclease highlight the conserved structural hierarchy of OB-fold proteins”, Biochemistry, 46, 9484-9494.

*** 41) Steinmetz, M.O, Jelesarov, I., Matousek, W.M., Honnappa, S., Jahnke, W., Missimer, J.H., Frank, S., Alexandrescu, A.T. & Kammerer, R.A. (2007) “Molecular basis of coiled coil formation”. Proc. Natl. Acad., USA. 104, 7062-7067.

40) Ucci, J.W., Kobayashi, Y., Choi, G. & Alexandrescu, A.T., Cole, J.L. (2007) “Mechanism of interaction of the double-stranded RNA (dsRNA) binding domain of protein kinase R with short dsRNA sequences”. Biochemistry 46, 55-65.

39) Sallum, C.O., Martel, D.M., Fournier, R.S., Matousek, W.M & Alexandrescu, A.T. (2005) “Sensitivity of NMR residual dipolar couplings to perturbations in folded and unfolded staphylococcal nuclease”. Biochemistry 44, 6392-6403.

*** 38) Alexandrescu, A.T. (2005) “Amyloid accomplices and enforcers”. Protein Science 14, 1-12.

37) Matousek, W.M., & Alexandrescu, A.T. (2004) “NMR structure of the C-terminal domain of SecA in the free state”. Biochem. Biophys. Acta 1702, 163-171.

36) Alexandrescu, A.T. (2004) “Strategy for supplementing structure calculations using limited data with hydrophobic distance restraints”. Proteins 56, 117-129.

35) Stetefeld, J., Alexandrescu A. T., Maciejewski, M. W., Jenny, M., Rathgeb-Szabo, K., Schulthess, T., Landwehr, R., Frank, S., Ruegg, M.A., & Kammerer, R.A. (2004) “Modulation of agrin function by alternative splicing and Ca2+ binding”. Structure 12, 503-515.

34) Alexandrescu, A.T., & Kammerer, R.A. (2003) “Structure and disorder in the ribonuclease S-peptide probed by NMR residual dipolar couplings”. Protein Sci. 12, 2132-2140.

33) Alexandrescu, A.T., Snyder, D.R., & Abildgaard, F. (2001) “NMR of hydrogen bonding in cold shock protein A and an analysis of the influence of crystallographic resolution on comparisons of hydrogen bond lengths”. Protein Sci. 10, 1856-1868.

32) Alexandrescu, A.T., Maciejewski, M.W., Rüegg, M.A., Engel, J., & Kammerer, R.A. (2001) “1H, 13C and 15N backbone assignments for the C-terminal globular domain of agrin”. J. Biomol. NMR 20, 295-296.

31) Jaravine, V.A., Alexandrescu A. T., & Grzesiek, S. (2001) “Observation of the closing of individual hydrogen bonds during TFE-induced helix formation in a peptide”. Protein Science 10, 943-950.

30) Kammerer, R.A., Jaravine, V.A., Frank, S., Schulthess, T., Landwehr, R., Lustig, A., Garcia-Echeveria, C., Alexandrescu, A.T., Engel, J., & Steinmetz, M.O. (2001) “An interhelical salt bridge within the trigger site stabilizes the GCN4 leucine zipper”. J. Biol. Chem. 276, 13685-13688.

29) Alexandrescu, A.T. (2001) “An NMR-based quenched hydrogen exchange investigation of model amyloid fibrils formed by the protein CspA”. Pac. Symp. Biocomput. 6, 67-78.

28) Alexandrescu, A.T., Jaravine, V.A., & Lamour, F.P. (2000) “NMR evidence for progressive stabilization of native-like structure upon aggregation of acid denatured LysN”. J. Mol. Biol. 295, 239-255.

27) Jaravine, V.A., Rathgeb-Szabo, K., & Alexandrescu, A.T. (2000) “Microscopic stability of cold shock protein A examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxide”. Protein Science 9, 290-301.

26) Alexandrescu, A.T., & Rathgeb-Szabo, K. (1999) “An NMR investigation of solution aggregation reactions preceding the misassembly of acid denatured cold shock protein A into fibrils”. J. Mol. Biol. 291, 1191-1206.

25) Alexandrescu, A.T., Jaravine, V.A., Dames, S.A. & Lamour, F.P. (1999) “NMR hydrogen exchange of the OB-fold protein LysN as a function of denaturant: The most conserved elements of structure are the most stable to unfolding”. J. Mol. Biol. 289, 1041-1054.

24) Dames, S.A., Kammerer, Moskau, D., Engel, J. & Alexandrescu, A.T. (1999) “Contributions of the ionization states of acidic residues to the stability of the coiled coil domain of matrilin-1”. FEBS Lett. 446, 75-80.

23) Dames, S.A., Wiltscheck, R., Kammerer, R.A., Engel, J., & Alexandrescu, A.T. (1998) “NMR structure of a parallel homotrimeric coiled coil”. Nature Struct. Biol. 5, 687-691.

22) Alexandrescu, A.T., & Rathgeb-Szabo, K. (1998) “NMR assignments for acid-denatured cold shock protein A”. J. Biomol. NMR 11, 461-462.

21) Alexandrescu, A.T., Rathgeb-Szabo, K., Rumpel, K., Jahnke, W., Schulthess, T., & Kammerer, R.A. (1998) “15N backbone dynamics of the S-Peptide from Ribonuclease A in its free and S-Protein bound forms: Towards a site-specific analysis of entropy changes upon folding”. Protein Science 7, 389-402.

20) Wiltscheck, R., Kammerer, R.A., Dames, S.A., Schulthess, T., Blommers, M.J.J., Engel, J., & Alexandrescu, A.T. (1997) “Heteronuclear NMR assignments and secondary structure of the coiled coil trimerization domain from cartilage matrix protein in oxidized and reduced forms”. Protein Science 6, 1734-1745.

19) Alexandrescu, A.T., Dames, S.A., & Wiltscheck, R. (1996) “A fragment of staphylococcal nuclease with an OB-fold structure shows hydrogen-exchange protection factors in the range reported for ‘Molten Globules'”. Protein Science 5, 1942-1946.

18) Alexandrescu, A.T., Jahnke, W., Wiltscheck, R., & Blommers, M.J.J (1996) “Accretion of structure in staphylococcal nuclease: An 15N NMR relaxation study”. J. Mol. Biol. 260, 570-587.

17) Alexandrescu, A. T., Gittis, A., Abeygunawardana, C., & Shortle, D. (1995) “NMR structure of a stable “OB-fold” sub-domain isolated from staphylococcal nuclease”. J. Mol. Biol. 250, 134-143.

16) Wang, Y., Alexandrescu, A. T., & Shortle, D. (1995) “Initial studies of the equilibrium folding pathway of staphylococcal nuclease”. Philos. Trans. R. Soc. Lond. B Biol. Sci. 348, 27-34.

*** 15) Alexandrescu, A. T., & Shortle, D. (1994) “Backbone dynamics of a highly disordered 131 residue fragment of staphylococcal nuclease”. J. Mol. Biol. 242, 527-546.

*** 14) Alexandrescu, A. T., Abeygunawardana, C., & Shortle, D. (1994) “Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: A heteronuclear NMR study”. Biochemistry 33, 1063-1072.

13) Smith, L., Alexandrescu, A. T., Pitkeathly, M. & Dobson, C. M. (1994) “Solution structure of a peptide fragment of human alpha-lactalbumin in trifluoroethanol: a model for local structure in the molten globule”. Structure 2, 703-712.

*** 12) Alexandrescu, A. T., Ng, Y-L., & Dobson, C. M. (1994) “Characterization of a TFE-induced partially folded state of alpha-lactalbumin”. J. Mol. Biol. 235, 587-599.

*** 11) Alexandrescu, A. T., Evans, P. A., Pitkeathly, M., & Dobson, C. M. (1993) “Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: A two-dimensional NMR study”. Biochemistry 32, 1707-1718.

10) Alexandrescu, A. T., Broadhurst, W., Wormald, C., Chyan, C.-L., Baum, J., & Dobson, C. M. (1992) “1H-NMR assignments and local environments of aromatic residues in bovine, human and guinea pig variants of alpha-lactalbumin”. European Journal of Biochemistry 210, 699-709.

9) Alexandrescu, A. T., Drendel, W. & Sundaralingam, M. (1991) “A highly propeller twisted adenine-adenine base pair in 8-tertiary butyl adenine”. Acta Crystallographica C47, 1041-1044.

8) Alexandrescu, A. T., Loh, S. N., & Markley, J. L. (1990) “Chemical exchange spectroscopy based on carbon-13 NMR. Applications to enzymology and protein folding”. Journal of Magnetic Resonance 87, 523-535.

7) Markley, J. L., Seavey, B. R., Alexandrescu, A. T., Darba, P., Hinck, A. P., Loh, S. N., McNemar, C. W., Mooberry, E. S., Oh, B. H., et al. (1990) “Multinuclear magnetic resonance spectroscopy of proteins: Information content, data extraction and analysis, and database design”. Protein Eng. Proc. Int. Conf. Protein Eng. Editor: Ikehara, M., 285-290.

6) Alexandrescu, A. T., Hinck, A. P. & Markley, J. L. (1990) “Coupling between local structure and global stability of a protein: Mutants of staphylococcal nuclease”. Biochemistry 29, 4516-4525.

5) Alexandrescu, A. T. (1990) “Nuclear magnetic resonance spectroscopy of staphylococcal nuclease: Effects of solution conditions and sequence changes on conformational forms”. Ph.D. Thesis, University of Wisconsin-Madison.

4) Alexandrescu, A. T., Ulrich, E. L., & Markley, J. L. (1989) “Hydrogen – 1 NMR evidence for three interconverting forms of staphylococcal nuclease: Effects of mutations and solution conditions on their distribution”. Biochemistry 28, 204-212.

3) Alexandrescu, A. T., Mills, D. A., Ulrich, E. L., Chinami, M. & Markley, J. L. (1988) “NMR assignments of the four histidines of staphylococcal nuclease in native and denatured states”. Biochemistry 27, 2158-2165.

2) Grissom, C.B., Alexandrescu A.T., Ulrich, E.L., Mills, D.A., & Markley, J.L. (1986) “Multinuclear magnetic resonance and kinetic studies of single amino-acid replacements in staphylococcal nuclease”. Federation Proceedings 45, 1915-1915.

*** 1) Barton, J. K., Basile, L. A., Danishefsky, A., & Alexandrescu, A. (1984) “Chiral probes for the handedness of DNA helices: Enantiomers of Tris(4,7-diphenyl phenanthroline) Ruthenium(II)”. Proc. Natl. Acad. Sci. U.S.A. 81, 1961-1965.