| Year |
Citation |
Score |
| 2023 |
Seo D, Kammerer RA, Alexandrescu AT. Solution NMR assignments and structure for the dimeric kinesin neck domain. Biomolecular Nmr Assignments. 17: 301-307. PMID 37861970 DOI: 10.1007/s12104-023-10159-x |
0.347 |
|
| 2023 |
Rua AJ, Whitehead RD, Alexandrescu AT. NMR structure verifies the eponymous zinc finger domain of transcription factor ZNF750. Journal of Structural Biology: X. 8: 100093. PMID 37655311 DOI: 10.1016/j.yjsbx.2023.100093 |
0.301 |
|
| 2023 |
Rua AJ, Whitehead Iii RD, Alexandrescu AT. NMR structure verifies the eponymous zinc finger domain of transcription factor ZNF750. Journal of Structural Biology. 108003. PMID 37487847 DOI: 10.1016/j.jsb.2023.108003 |
0.308 |
|
| 2021 |
Kaplan AR, Olson R, Alexandrescu AT. Protein Yoga: Conformational Versatility of the Hemolysin II C-terminal Domain Detailed by NMR Structures for Multiple States. Protein Science : a Publication of the Protein Society. PMID 33733504 DOI: 10.1002/pro.4066 |
0.358 |
|
| 2020 |
Alexandrescu AT, Kaplan A, Tripler T, Teschke CM. NMR Structures of Closely Related Protein Conformations Biophysical Journal. 118: 23a. DOI: 10.1016/J.Bpj.2019.11.306 |
0.405 |
|
| 2019 |
Whitehead RD, Teschke CM, Alexandrescu AT. NMR Mapping of Disordered Segments from a Viral Scaffolding Protein Enclosed in a 23 MDa Procapsid. Biophysical Journal. 117: 1387-1392. PMID 31585705 DOI: 10.1016/J.Bpj.2019.08.038 |
0.444 |
|
| 2019 |
Newcomer RL, Schrad JR, Gilcrease EB, Casjens SR, Feig M, Teschke CM, Alexandrescu AT, Parent KN. The phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy. Elife. 8. PMID 30945633 DOI: 10.7554/Elife.45345 |
0.379 |
|
| 2019 |
Tripler TN, Kaplan AR, Alexandrescu AT, Teschke CM. Conservation and divergence of the I-domain inserted into the ubiquitous HK97 coat protein fold in the P22-like bacteriophages. Journal of Virology. PMID 30787158 DOI: 10.1128/Jvi.00007-19 |
0.434 |
|
| 2019 |
Newcomer RL, Schrad JR, Gilcrease EB, Casjens SR, Feig M, Teschke CM, Alexandrescu AT, Parent KN. Author response: The phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy Elife. DOI: 10.7554/Elife.45345.025 |
0.301 |
|
| 2018 |
Newcomer RL, Belato HB, Teschke CM, Alexandrescu AT. NMR assignments for monomeric phage L decoration protein. Biomolecular Nmr Assignments. PMID 30109462 DOI: 10.1007/S12104-018-9836-1 |
0.442 |
|
| 2018 |
Asthana S, Mallick B, Alexandrescu AT, Jha S. IAPP in type II diabetes: Basic research on structure, molecular interactions, and disease mechanisms suggests potential intervention strategies. Biochimica Et Biophysica Acta. PMID 29518374 DOI: 10.1016/J.Bbamem.2018.02.020 |
0.394 |
|
| 2018 |
Newcomer R, Belato H, Teschke C, Alexandrescu A. NMR assignments of Decorator, a phage-cementing 15 KDa monomer Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr27435 |
0.355 |
|
| 2017 |
Kaplan AR, Kaus K, De S, Olson R, Alexandrescu AT. NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold. Scientific Reports. 7: 3277. PMID 28607368 DOI: 10.1038/S41598-017-02917-4 |
0.499 |
|
| 2017 |
Kaplan AR, Brady MR, Maciejewski MW, Kammerer RA, Alexandrescu AT. NMR Structures of GCN4p are Largely Conserved when Ion Pairs are Disrupted at Acidic pH but Show a Relaxation of the Coiled Coil Superhelix. Biochemistry. PMID 28230348 DOI: 10.1021/Acs.Biochem.6B00634 |
0.445 |
|
| 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 |
0.454 |
|
| 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 |
0.424 |
|
| 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 |
0.469 |
|
| 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 |
0.768 |
|
| 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 |
0.367 |
|
| 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 |
0.426 |
|
| 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 |
0.786 |
|
| 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 |
0.433 |
|
| 2014 |
Kaplan AR, Maciejewski MW, Olson R, Alexandrescu AT. NMR assignments for the cis and trans forms of the hemolysin II C-terminal domain. Biomolecular Nmr Assignments. 8: 419-23. PMID 24234348 DOI: 10.1007/S12104-013-9530-2 |
0.431 |
|
| 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 |
0.45 |
|
| 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 |
0.429 |
|
| 2013 |
Alexandrescu AT, Jha S, Snell JM, Sheftic SR. The pH-Dependence of Amylin Fibrillization Biophysical Journal. 104: 360a. DOI: 10.1016/J.Bpj.2012.11.1998 |
0.497 |
|
| 2013 |
Sheftic S, Alexandrescu A. NMR Structure and Dynamics of the Response Regulator Sma0114 from Sinorhizobium Meliloti Biophysical Journal. 104: 225a. DOI: 10.1016/J.Bpj.2012.11.1268 |
0.415 |
|
| 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 |
0.408 |
|
| 2012 |
Alexandrescu AT, Jha S, Patil SM, Gibson J, Alder NN, Nelson CE. Effects of Heparin on Amylin Fibrillization Biophysical Journal. 102: 243a. DOI: 10.1016/J.Bpj.2011.11.1338 |
0.772 |
|
| 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 |
0.776 |
|
| 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 |
0.742 |
|
| 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 |
0.72 |
|
| 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 |
0.421 |
|
| 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 |
0.746 |
|
| 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 |
0.415 |
|
| 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 |
0.78 |
|
| 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 |
0.732 |
|
| 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 |
0.477 |
|
| 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 |
0.458 |
|
| 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 |
0.336 |
|
| 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 |
0.402 |
|
| 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 |
0.468 |
|
| 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 |
0.377 |
|
| 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 |
0.441 |
|
| 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 |
0.411 |
|
| 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 |
0.385 |
|
| 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 |
0.432 |
|
| 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 |
0.34 |
|
| 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 |
0.358 |
|
| 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 |
0.349 |
|
| 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 |
0.398 |
|
| 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 |
0.341 |
|
| 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 |
0.461 |
|
| 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 |
0.441 |
|
| 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 |
0.46 |
|
| 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 |
0.41 |
|
| 1998 |
Dames SA, Kammerer RA, Wiltscheck R, Engel J, Alexandrescu AT. NMR structure of a parallel homotrimeric coiled coil. Nature Structural Biology. 5: 687-91. PMID 9699631 DOI: 10.1038/90444 |
0.477 |
|
| 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 |
0.441 |
|
| 1998 |
Alexandrescu A, Rathgeb-Szabo K. Acid Denatured Cold Shock Protein A (CspA) Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr4107 |
0.301 |
|
| 1998 |
Wiltscheck R, Kammerer R, Dames S, Schulthess T, Blommers M, Engel J, Alexandrescu A. Alpha-Helical Coiled Coil Trimerization Domain of Chicken Cartilage Matrix Protein (Oxidized) Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr4055 |
0.357 |
|
| 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 |
0.485 |
|
| 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 |
0.433 |
|
| 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 |
0.431 |
|
| 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 |
0.409 |
|
| 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 |
0.467 |
|
| 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 |
0.399 |
|
| 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 DOI: 10.1021/Bi00171A004 |
0.522 |
|
| 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 |
0.421 |
|
| 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 |
0.38 |
|
| 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 |
0.445 |
|
| 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 |
0.412 |
|
| 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 |
0.66 |
|
| 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 |
0.677 |
|
| 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 |
0.568 |
|
| 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 [Erratum to document cited in CA110(5):36063b] Biochemistry. 28: 3628-3628. DOI: 10.1021/Bi00434A075 |
0.438 |
|
| 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 |
0.571 |
|
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