Andrei T. Alexandrescu - Publications

University of Wisconsin, Madison, Madison, WI 

58 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2016 Harprecht C, Okifo O, Robbins KJ, Motwani T, Alexandrescu AT, Teschke CM. Contextual Role of a Salt-Bridge in the Phage P22 Coat Protein I-Domain. The Journal of Biological Chemistry. PMID 27006399 DOI: 10.1074/jbc.M116.716910  1
2016 Alexandrescu AT. Quenched Hydrogen Exchange NMR of Amyloid Fibrils. Methods in Molecular Biology (Clifton, N.J.). 1345: 211-22. PMID 26453215 DOI: 10.1007/978-1-4939-2978-8_14  1
2015 Newcomer RL, Fraser LC, Teschke CM, Alexandrescu AT. Mechanism of Protein Denaturation: Partial Unfolding of the P22 Coat Protein I-Domain by Urea Binding. Biophysical Journal. 109: 2666-77. PMID 26682823 DOI: 10.1016/j.bpj.2015.11.010  1
2015 Patil SM, Alexandrescu AT. Charge-Based Inhibitors of Amylin Fibrillization and Toxicity. Journal of Diabetes Research. 2015: 946037. PMID 26576438 DOI: 10.1155/2015/946037  1
2015 Tripler TN, Maciejewski MW, Teschke CM, Alexandrescu AT. NMR assignments for the insertion domain of bacteriophage CUS-3 coat protein. Biomolecular Nmr Assignments. 9: 333-6. PMID 25694158 DOI: 10.1007/s12104-015-9604-4  1
2014 Rizzo AA, Suhanovsky MM, Baker ML, Fraser LC, Jones LM, Rempel DL, Gross ML, Chiu W, Alexandrescu AT, Teschke CM. Multiple functional roles of the accessory I-domain of bacteriophage P22 coat protein revealed by NMR structure and CryoEM modeling. Structure (London, England : 1993). 22: 830-41. PMID 24836025 DOI: 10.1016/j.str.2014.04.003  1
2014 Jha S, Snell JM, Sheftic SR, Patil SM, Daniels SB, Kolling FW, Alexandrescu AT. pH dependence of amylin fibrillization. Biochemistry. 53: 300-10. PMID 24377660 DOI: 10.1021/bi401164k  1
2014 Sheftic SR, White E, Gage DJ, Alexandrescu AT. NMR structure of the HWE kinase associated response regulator Sma0114 in its activated state. Biochemistry. 53: 311-22. PMID 24364624 DOI: 10.1021/bi401497h  1
2013 Alexandrescu AT. Amide proton solvent protection in amylin fibrils probed by quenched hydrogen exchange NMR. Plos One. 8: e56467. PMID 23457571 DOI: 10.1371/journal.pone.0056467  1
2013 Rizzo AA, Fraser LC, Sheftic SR, Suhanovsky MM, Teschke CM, Alexandrescu AT. NMR assignments for the telokin-like domain of bacteriophage P22 coat protein. Biomolecular Nmr Assignments. 7: 257-60. PMID 22987227 DOI: 10.1007/s12104-012-9422-x  1
2012 Sheftic SR, Snell JM, Jha S, Alexandrescu AT. Inhibition of semen-derived enhancer of virus infection (SEVI) fibrillogenesis by zinc and copper. European Biophysics Journal : Ebj. 41: 695-704. PMID 22907203 DOI: 10.1007/s00249-012-0846-0  1
2012 Sheftic SR, Garcia PP, White E, Robinson VL, Gage DJ, Alexandrescu AT. Nuclear magnetic resonance structure and dynamics of the response regulator Sma0114 from Sinorhizobium meliloti. Biochemistry. 51: 6932-41. PMID 22880754 DOI: 10.1021/bi300922z  1
2011 Jha S, Patil SM, Gibson J, Nelson CE, Alder NN, Alexandrescu AT. Mechanism of amylin fibrillization enhancement by heparin. The Journal of Biological Chemistry. 286: 22894-904. PMID 21555785 DOI: 10.1074/jbc.M110.215814  1
2011 Patil SM, Mehta A, Jha S, Alexandrescu AT. Heterogeneous amylin fibril growth mechanisms imaged by total internal reflection fluorescence microscopy. Biochemistry. 50: 2808-19. PMID 21391619 DOI: 10.1021/bi101908m  1
2011 Croke RL, Patil SM, Quevreaux J, Kendall DA, Alexandrescu AT. NMR determination of pKa values in α-synuclein. Protein Science : a Publication of the Protein Society. 20: 256-69. PMID 21280118 DOI: 10.1002/pro.556  1
2011 Sheftic SR, Garcia PP, Robinson VL, Gage DJ, Alexandrescu AT. NMR assignments for the Sinorhizobium meliloti response regulator Sma0114. Biomolecular Nmr Assignments. 5: 55-8. PMID 20936511 DOI: 10.1007/s12104-010-9266-1  1
2009 Sheftic SR, Croke RL, LaRochelle JR, Alexandrescu AT. Electrostatic contributions to the stabilities of native proteins and amyloid complexes. Methods in Enzymology. 466: 233-58. PMID 21609864 DOI: 10.1016/S0076-6879(09)66010-9  1
2009 Guardino KM, Sheftic SR, Slattery RE, Alexandrescu AT. Relative stabilities of conserved and non-conserved structures in the OB-fold superfamily. International Journal of Molecular Sciences. 10: 2412-30. PMID 19564956 DOI: 10.3390/ijms10052412  1
2009 Patil SM, Xu S, Sheftic SR, Alexandrescu AT. Dynamic alpha-helix structure of micelle-bound human amylin. The Journal of Biological Chemistry. 284: 11982-91. PMID 19244249 DOI: 10.1074/jbc.M809085200  1
2008 Croke RL, Sallum CO, Watson E, Watt ED, Alexandrescu AT. Hydrogen exchange of monomeric alpha-synuclein shows unfolded structure persists at physiological temperature and is independent of molecular crowding in Escherichia coli. Protein Science : a Publication of the Protein Society. 17: 1434-45. PMID 18493022 DOI: 10.1110/ps.033803.107  1
2007 Matousek WM, Ciani B, Fitch CA, Garcia-Moreno B, Kammerer RA, Alexandrescu AT. Electrostatic contributions to the stability of the GCN4 leucine zipper structure. Journal of Molecular Biology. 374: 206-19. PMID 17920624 DOI: 10.1016/j.jmb.2007.09.007  1
2007 Watson E, Matousek WM, Irimies EL, Alexandrescu AT. Partially folded states of staphylococcal nuclease highlight the conserved structural hierarchy of OB-fold proteins. Biochemistry. 46: 9484-94. PMID 17661445 DOI: 10.1021/bi700532j  1
2007 Sallum CO, Kammerer RA, Alexandrescu AT. Thermodynamic and structural studies of carbohydrate binding by the agrin-G3 domain. Biochemistry. 46: 9541-50. PMID 17649979 DOI: 10.1021/bi7006383  1
2007 Steinmetz MO, Jelesarov I, Matousek WM, Honnappa S, Jahnke W, Missimer JH, Frank S, Alexandrescu AT, Kammerer RA. Molecular basis of coiled-coil formation. Proceedings of the National Academy of Sciences of the United States of America. 104: 7062-7. PMID 17438295 DOI: 10.1073/pnas.0700321104  1
2007 Ucci JW, Kobayashi Y, Choi G, Alexandrescu AT, Cole JL. Mechanism of interaction of the double-stranded RNA (dsRNA) binding domain of protein kinase R with short dsRNA sequences. Biochemistry. 46: 55-65. PMID 17198375 DOI: 10.1021/bi061531o  1
2005 Sallum CO, Martel DM, Fournier RS, Matousek WM, Alexandrescu AT. Sensitivity of NMR residual dipolar couplings to perturbations in folded and denatured staphylococcal nuclease. Biochemistry. 44: 6392-403. PMID 15850373 DOI: 10.1021/bi0473410  1
2005 Alexandrescu AT. Amyloid accomplices and enforcers. Protein Science : a Publication of the Protein Society. 14: 1-12. PMID 15576561 DOI: 10.1110/ps.04887005  1
2004 Matousek WM, Alexandrescu AT. NMR structure of the C-terminal domain of SecA in the free state. Biochimica Et Biophysica Acta. 1702: 163-71. PMID 15488768 DOI: 10.1016/j.bbapap.2004.08.012  1
2004 Alexandrescu AT. Strategy for supplementing structure calculations using limited data with hydrophobic distance restraints. Proteins. 56: 117-29. PMID 15162492 DOI: 10.1002/prot.20134  1
2004 Stetefeld J, Alexandrescu AT, Maciejewski MW, Jenny M, Rathgeb-Szabo K, Schulthess T, Landwehr R, Frank S, Ruegg MA, Kammerer RA. Modulation of agrin function by alternative splicing and Ca2+ binding. Structure (London, England : 1993). 12: 503-15. PMID 15016366 DOI: 10.1016/j.str.2004.02.001  1
2003 Alexandrescu AT, Kammerer RA. Structure and disorder in the ribonuclease S-peptide probed by NMR residual dipolar couplings. Protein Science : a Publication of the Protein Society. 12: 2132-40. PMID 14500871 DOI: 10.1110/ps.03164403  1
2001 Alexandrescu AT, Maciejewski MW, Rüegg MA, Engel J, Kammerer RA. 1H, 13C and 15N backbone assignments for the C-terminal globular domain of agrin. Journal of Biomolecular Nmr. 20: 295-6. PMID 11519755 DOI: 10.1023/A:1011256008944  1
2001 Alexandrescu AT, Snyder DR, Abildgaard F. 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 Science : a Publication of the Protein Society. 10: 1856-68. PMID 11514676 DOI: 10.1110/ps.14301  1
2001 Jaravine VA, Alexandrescu AT, Grzesiek S. Observation of the closing of individual hydrogen bonds during TFE-induced helix formation in a peptide. Protein Science : a Publication of the Protein Society. 10: 943-50. PMID 11316874 DOI: 10.1110/ps.48501  1
2001 Alexandrescu AT. An NMR-based quenched hydrogen exchange investigation of model amyloid fibrils formed by cold shock protein A. Pacific Symposium On Biocomputing. Pacific Symposium On Biocomputing. 67-78. PMID 11262979  1
2001 Kammerer RA, Jaravine VA, Frank S, Schulthess T, Landwehr R, Lustig A, Garcia-Echeverria C, Alexandrescu AT, Engel J, Steinmetz MO. An intrahelical salt bridge within the trigger site stabilizes the GCN4 leucine zipper. The Journal of Biological Chemistry. 276: 13685-8. PMID 11134036 DOI: 10.1074/jbc.M010492200  1
2000 Jaravine VA, Rathgeb-Szabo K, Alexandrescu AT. 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 : a Publication of the Protein Society. 9: 290-301. PMID 10716181 DOI: 10.1110/ps.9.2.290  1
2000 Alexandrescu AT, Lamour FP, Jaravine VA. NMR evidence for progressive stabilization of native-like structure upon aggregation of acid-denatured LysN. Journal of Molecular Biology. 295: 239-55. PMID 10623523 DOI: 10.1006/jmbi.1999.3354  1
1999 Alexandrescu AT, Rathgeb-Szabo K. An NMR investigation of solution aggregation reactions preceding the misassembly of acid-denatured cold shock protein A into fibrils. Journal of Molecular Biology. 291: 1191-206. PMID 10518954 DOI: 10.1006/jmbi.1999.3039  1
1999 Alexandrescu AT, Jaravine VA, Dames SA, Lamour FP. 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. Journal of Molecular Biology. 289: 1041-54. PMID 10369781 DOI: 10.1006/jmbi.1999.2813  1
1999 Dames SA, Kammerer RA, Moskau D, Engel J, Alexandrescu AT. Contributions of the ionization states of acidic residues to the stability of the coiled coil domain of matrilin-1. Febs Letters. 446: 75-80. PMID 10100618 DOI: 10.1016/S0014-5793(99)00186-6  1
1998 Alexandrescu AT, Rathgeb-Szabo K. NMR assignments for acid-denatured cold shock protein A. Journal of Biomolecular Nmr. 11: 461-2. PMID 9691289  1
1998 Alexandrescu AT, Rathgeb-Szabo K, Rumpel K, Jahnke W, Schulthess T, Kammerer RA. 15N backbone dynamics of the S-peptide from ribonuclease A in its free and S-protein bound forms: toward a site-specific analysis of entropy changes upon folding. Protein Science : a Publication of the Protein Society. 7: 389-402. PMID 9521116 DOI: 10.1002/pro.5560070220  1
1997 Wiltscheck R, Kammerer RA, Dames SA, Schulthess T, Blommers MJ, Engel J, Alexandrescu AT. Heteronuclear NMR assignments and secondary structure of the coiled coil trimerization domain from cartilage matrix protein in oxidized and reduced forms. Protein Science : a Publication of the Protein Society. 6: 1734-45. PMID 9260286 DOI: 10.1002/pro.5560060814  1
1996 Alexandrescu AT, Dames SA, Wiltscheck R. A fragment of staphylococcal nuclease with an OB-fold structure shows hydrogen-exchange protection factors in the range reported for "molten globules". Protein Science : a Publication of the Protein Society. 5: 1942-6. PMID 8880922 DOI: 10.1002/pro.5560050924  1
1996 Alexandrescu AT, Jahnke W, Wiltscheck R, Blommers MJ. Accretion of structure in staphylococcal nuclease: an 15N NMR relaxation study. Journal of Molecular Biology. 260: 570-87. PMID 8759321 DOI: 10.1006/jmbi.1996.0422  1
1995 Wang Y, Alexandrescu AT, Shortle D. Initial studies of the equilibrium folding pathway of staphylococcal nuclease. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 348: 27-34. PMID 7770483 DOI: 10.1098/rstb.1995.0042  1
1995 Alexandrescu AT, Gittis AG, Abeygunawardana C, Shortle D. NMR structure of a stable "OB-fold" sub-domain isolated from staphylococcal nuclease. Journal of Molecular Biology. 250: 134-43. PMID 7608966 DOI: 10.1006/jmbi.1995.0365  1
1994 Alexandrescu AT, Ng YL, Dobson CM. Characterization of a trifluoroethanol-induced partially folded state of alpha-lactalbumin. Journal of Molecular Biology. 235: 587-99. PMID 8289283 DOI: 10.1006/jmbi.1994.1015  1
1994 Alexandrescu AT, Abeygunawardana C, Shortle D. Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: a heteronuclear NMR study. Biochemistry. 33: 1063-72. PMID 8110737  1
1994 Smith LJ, Alexandrescu AT, Pitkeathly M, Dobson CM. Solution structure of a peptide fragment of human alpha-lactalbumin in trifluoroethanol: a model for local structure in the molten globule. Structure (London, England : 1993). 2: 703-12. PMID 7994570 DOI: 10.1016/S0969-2126(00)00071-X  1
1994 Alexandrescu AT, Shortle D. Backbone dynamics of a highly disordered 131 residue fragment of staphylococcal nuclease. Journal of Molecular Biology. 242: 527-46. PMID 7932708 DOI: 10.1006/jmbi.1994.1598  1
1993 Alexandrescu AT, Evans PA, Pitkeathly M, Baum J, Dobson CM. Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: a two-dimensional NMR study. Biochemistry. 32: 1707-18. PMID 8439536 DOI: 10.1021/bi00058a003  1
1992 Alexandrescu AT, Broadhurst RW, Wormald C, Chyan CL, Baum J, Dobson CM. 1H-NMR assignments and local environments of aromatic residues in bovine, human and guinea pig variants of alpha-lactalbumin. European Journal of Biochemistry / Febs. 210: 699-709. PMID 1483454 DOI: 10.1111/j.1432-1033.1992.tb17471.x  1
1990 Alexandrescu AT, Hinck AP, Markley JL. Coupling between local structure and global stability of a protein: mutants of staphylococcal nuclease. Biochemistry. 29: 4516-25. PMID 2372535 DOI: 10.1021/bi00471a003  1
1990 Alexandrescu AT, Loh SN, Markley JL. Chemical exchange spectroscopy based on carbon-13 NMR. Applications to enzymology and protein folding Journal of Magnetic Resonance (1969). 87: 523-535. DOI: 10.1016/0022-2364(90)90309-W  1
1989 Alexandrescu AT, Ulrich EL, Markley JL. Hydrogen-1 NMR evidence for three interconverting forms of staphylococcal nuclease: effects of mutations and solution conditions on their distribution. Biochemistry. 28: 204-11. PMID 2706243 DOI: 10.1021/bi00427a028  1
1988 Alexandrescu AT, Mills DA, Ulrich EL, Chinami M, Markley JL. NMR assignments of the four histidines of staphylococcal nuclease in native and denatured states. Biochemistry. 27: 2158-65. PMID 3288282 DOI: 10.1021/bi00406a051  1
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