| Year |
Citation |
Score |
| 2019 |
Yuan CL, Shi EY, Srinivasan J, Ptak CP, Oswald RE, Nowak LM. Modulation of AMPA Receptor Gating by the Anticonvulsant Drug, Perampanel. Acs Medicinal Chemistry Letters. 10: 237-242. PMID 30891119 DOI: 10.1021/Acsmedchemlett.8B00322 |
0.425 |
|
| 2019 |
Shi EY, Yuan CL, Sipple MT, Srinivasan J, Ptak CP, Oswald RE, Nowak LM. Noncompetitive antagonists induce cooperative AMPA receptor channel gating. The Journal of General Physiology. PMID 30622133 DOI: 10.1085/Jgp.201812209 |
0.462 |
|
| 2016 |
Ptak CP, Ahmed AH, Oswald RE. Sensing Allosteric Modulator Binding to AMPA Receptors at the Glutamate-Binding Site Biophysical Journal. 110: 201a. DOI: 10.1016/j.bpj.2015.11.1122 |
0.366 |
|
| 2016 |
Ptak CP, Ahmed AH, Oswald RE. Sensing Allosteric Modulator Binding to AMPA Receptors at the Glutamate-Binding Site Biophysical Journal. 110: 201a. DOI: 10.1016/J.Bpj.2015.11.1122 |
0.374 |
|
| 2016 |
Poon K, Oswald RE, Nowak LM. Current recording and kinetic analyses for single AMPA receptors Neuromethods. 106: 257-272. DOI: 10.1007/978-1-4939-2812-5_17 |
0.583 |
|
| 2015 |
Oswald RE, Ahmed AH, Ptak CP, Martinez M. AMPA Receptor Structure, Function, and Dynamics Biophysical Journal. 108: 335a-336a. DOI: 10.1016/j.bpj.2014.11.1830 |
0.305 |
|
| 2015 |
Oswald RE, Ahmed AH, Ptak CP, Martinez M. AMPA Receptor Structure, Function, and Dynamics Biophysical Journal. 108: 335a-336a. DOI: 10.1016/J.Bpj.2014.11.1830 |
0.442 |
|
| 2014 |
Ptak CP, Hsieh CL, Lin YP, Maltsev AS, Raman R, Sharma Y, Oswald RE, Chang YF. NMR solution structure of the terminal immunoglobulin-like domain from the leptospira host-interacting outer membrane protein, LigB. Biochemistry. 53: 5249-60. PMID 25068811 DOI: 10.1021/Bi500669U |
0.68 |
|
| 2014 |
Martinez M, Ahmed AH, Loh AP, Oswald RE. Thermodynamics and mechanism of the interaction of willardiine partial agonists with a glutamate receptor: implications for drug development. Biochemistry. 53: 3790-5. PMID 24850223 DOI: 10.1021/bi500511m |
0.361 |
|
| 2014 |
Jenkins MA, Wells G, Bachman J, Snyder JP, Jenkins A, Huganir RL, Oswald RE, Traynelis SF. Regulation of GluA1 α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor function by protein kinase C at serine-818 and threonine-840. Molecular Pharmacology. 85: 618-29. PMID 24452473 DOI: 10.1124/Mol.113.091488 |
0.37 |
|
| 2014 |
Ptak CP, Hsieh CL, Weiland GA, Oswald RE. Role of stoichiometry in the dimer-stabilizing effect of AMPA receptor allosteric modulators. Acs Chemical Biology. 9: 128-33. PMID 24152170 DOI: 10.1021/Cb4007166 |
0.379 |
|
| 2013 |
Ahmed AH, Ptak CP, Fenwick MK, Hsieh CL, Weiland GA, Oswald RE. Dynamics of cleft closure of the GluA2 ligand-binding domain in the presence of full and partial agonists revealed by hydrogen-deuterium exchange. The Journal of Biological Chemistry. 288: 27658-66. PMID 23940029 DOI: 10.1074/Jbc.M113.495564 |
0.35 |
|
| 2013 |
Hsieh CL, Ptak CP, Maltsev AS, Oswald RE, Fu Chang Y. Structural Architecture of the Multi-Immunoglobulin-Like Domain Chain from Ligb Biophysical Journal. 104: 568a. DOI: 10.1016/J.Bpj.2012.11.3151 |
0.681 |
|
| 2013 |
Ptak CP, Healy LE, Hsieh CL, Oswald RE. Biophysical Studies on Glua2 Ligand-Binding Domain Dimerization in Solution Biophysical Journal. 104: 272a. DOI: 10.1016/J.Bpj.2012.11.1528 |
0.388 |
|
| 2013 |
Ptak CP, Healy LE, Hsieh CL, Oswald RE. Biophysical Studies on Glua2 Ligand-Binding Domain Dimerization in Solution Biophysical Journal. 104: 272a. DOI: 10.1016/j.bpj.2012.11.1528 |
0.306 |
|
| 2012 |
Ahmed AH, Hamada M, Shinada T, Ohfune Y, Weerasinghe L, Garner PP, Oswald RE. The structure of (-)-kaitocephalin bound to the ligand binding domain of the (S)-α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)/glutamate receptor, GluA2. The Journal of Biological Chemistry. 287: 41007-13. PMID 23076153 DOI: 10.1074/jbc.M112.416362 |
0.427 |
|
| 2012 |
Holley SM, Ahmed AH, Srinivasan J, Murthy SE, Weiland GA, Oswald RE, Nowak LM. The loss of an electrostatic contact unique to AMPA receptor ligand binding domain 2 slows channel activation. Biochemistry. 51: 4015-27. PMID 22512472 DOI: 10.1021/Bi3001837 |
0.489 |
|
| 2011 |
Ahmed AH, Wang S, Chuang HH, Oswald RE. Mechanism of AMPA receptor activation by partial agonists: disulfide trapping of closed lobe conformations. The Journal of Biological Chemistry. 286: 35257-66. PMID 21846932 DOI: 10.1074/jbc.M111.269001 |
0.414 |
|
| 2011 |
Poon K, Ahmed AH, Nowak LM, Oswald RE. Mechanisms of modal activation of GluA3 receptors. Molecular Pharmacology. 80: 49-59. PMID 21464198 DOI: 10.1124/Mol.111.071688 |
0.67 |
|
| 2011 |
Ahmed AH, Wang S, Chuang H, Oswald RE. Studies of the Mechanism of AMPA Receptor Activation using Disulfide Trapping Biophysical Journal. 100: 24a. DOI: 10.1016/j.bpj.2010.12.336 |
0.306 |
|
| 2011 |
Ahmed AH, Wang S, Chuang H, Oswald RE. Studies of the Mechanism of AMPA Receptor Activation using Disulfide Trapping Biophysical Journal. 100: 24a. DOI: 10.1016/j.bpj.2010.12.336 |
0.306 |
|
| 2011 |
Holley SM, Srinivasan J, Ahmed AH, Oswald RE, Nowak LM. An Ampa Receptor Unique Asp-Lys Salt-Bridge has a Role in Channel Function Biophysical Journal. 100: 258a. DOI: 10.1016/J.Bpj.2010.12.1626 |
0.458 |
|
| 2011 |
Holley SM, Srinivasan J, Ahmed AH, Oswald RE, Nowak LM. An Ampa Receptor Unique Asp-Lys Salt-Bridge has a Role in Channel Function Biophysical Journal. 100: 258a. DOI: 10.1016/j.bpj.2010.12.1626 |
0.352 |
|
| 2010 |
Poon K, Nowak LM, Oswald RE. Characterizing single-channel behavior of GluA3 receptors. Biophysical Journal. 99: 1437-46. PMID 20816055 DOI: 10.1016/J.Bpj.2010.06.058 |
0.647 |
|
| 2010 |
Ahmed AH, Ptak CP, Oswald RE. Molecular mechanism of flop selectivity and subsite recognition for an AMPA receptor allosteric modulator: structures of GluA2 and GluA3 in complexes with PEPA. Biochemistry. 49: 2843-50. PMID 20199107 DOI: 10.1021/Bi1000678 |
0.438 |
|
| 2010 |
Ahmed AH, Oswald RE. Piracetam defines a new binding site for allosteric modulators of alpha-amino-3-hydroxy-5-methyl-4-isoxazole-propionic acid (AMPA) receptors. Journal of Medicinal Chemistry. 53: 2197-203. PMID 20163115 DOI: 10.1021/jm901905j |
0.386 |
|
| 2010 |
Wang S, Poon K, Oswald RE, Chuang HH. Distinct modulations of human capsaicin receptor by protons and magnesium through different domains. The Journal of Biological Chemistry. 285: 11547-56. PMID 20145248 DOI: 10.1074/Jbc.M109.058727 |
0.634 |
|
| 2010 |
Maltsev AS, Oswald RE. Hydrophobic side chain dynamics of a glutamate receptor ligand binding domain. The Journal of Biological Chemistry. 285: 10154-62. PMID 20110365 DOI: 10.1074/jbc.M109.088641 |
0.752 |
|
| 2010 |
Fenwick MK, Oswald RE. On the mechanisms of alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) receptor binding to glutamate and kainate. The Journal of Biological Chemistry. 285: 12334-43. PMID 20110361 DOI: 10.1074/Jbc.M109.086371 |
0.473 |
|
| 2010 |
Ptak CP, Ahmed AH, Fenwick MK, Maltsev A, Oswald RE. Exploring the Role of Positive Allosteric Modulators in Stabilizing the GluR2 Ligand-Binding Domain Dimer Biophysical Journal. 98: 609a. DOI: 10.1016/J.Bpj.2009.12.3323 |
0.731 |
|
| 2009 |
Ptak CP, Ahmed AH, Oswald RE. Probing the allosteric modulator binding site of GluR2 with thiazide derivatives. Biochemistry. 48: 8594-602. PMID 19673491 DOI: 10.1021/Bi901127S |
0.435 |
|
| 2009 |
Ahmed AH, Thompson MD, Fenwick MK, Romero B, Loh AP, Jane DE, Sondermann H, Oswald RE. Mechanisms of antagonism of the GluR2 AMPA receptor: structure and dynamics of the complex of two willardiine antagonists with the glutamate binding domain. Biochemistry. 48: 3894-903. PMID 19284741 DOI: 10.1021/Bi900107M |
0.685 |
|
| 2009 |
Ahmed AH, Wang Q, Sondermann H, Oswald RE. Structure of the S1S2 glutamate binding domain of GLuR3. Proteins. 75: 628-37. PMID 19003990 DOI: 10.1002/Prot.22274 |
0.465 |
|
| 2009 |
Poon K, Nowak LM, Oswald RE. Functional Characteristics of iGluR3 AMPA Receptor-Channels in Cell Attached Recordings Biophysical Journal. 96: 490a-491a. DOI: 10.1016/J.Bpj.2008.12.2533 |
0.639 |
|
| 2009 |
Poon K, Nowak LM, Oswald RE. Functional Characteristics of iGluR3 AMPA Receptor-Channels in Cell Attached Recordings Biophysical Journal. 96: 490a-491a. DOI: 10.1016/J.Bpj.2008.12.2533 |
0.639 |
|
| 2009 |
Poon K, Nowak LM, Oswald RE. Functional Characteristics of iGluR3 AMPA Receptor-Channels in Cell Attached Recordings Biophysical Journal. 96: 490a-491a. DOI: 10.1016/j.bpj.2008.12.2533 |
0.33 |
|
| 2009 |
Fenwick MK, Oswald RE. Microsecond-to-second Timescale Motions In The Ligand Binding Domain Of Glutamate Receptor 2 Biophysical Journal. 96: 490a. DOI: 10.1016/J.Bpj.2008.12.2532 |
0.428 |
|
| 2009 |
Maltsev AS, Oswald RE. Partial Agonism And Lobe Orientation In The Glutamate Receptor, Glur2 Biophysical Journal. 96: 490a. DOI: 10.1016/j.bpj.2008.12.2531 |
0.346 |
|
| 2009 |
Maltsev AS, Oswald RE. Partial Agonism And Lobe Orientation In The Glutamate Receptor, Glur2 Biophysical Journal. 96: 490a. DOI: 10.1016/j.bpj.2008.12.2531 |
0.696 |
|
| 2009 |
Maltsev AS, Oswald RE. Partial Agonism And Lobe Orientation In The Glutamate Receptor, Glur2 Biophysical Journal. 96: 490a. DOI: 10.1016/j.bpj.2008.12.2531 |
0.346 |
|
| 2008 |
Maltsev AS, Ahmed AH, Fenwick MK, Jane DE, Oswald RE. Mechanism of partial agonism at the GluR2 AMPA receptor: Measurements of lobe orientation in solution. Biochemistry. 47: 10600-10. PMID 18795801 DOI: 10.1021/Bi800843C |
0.749 |
|
| 2008 |
Fenwick MK, Oswald RE. NMR spectroscopy of the ligand-binding core of ionotropic glutamate receptor 2 bound to 5-substituted willardiine partial agonists. Journal of Molecular Biology. 378: 673-85. PMID 18387631 DOI: 10.1016/J.Jmb.2008.03.012 |
0.447 |
|
| 2007 |
Fenwick MK, Oswald RE. Backbone chemical shift assignment of a glutamate receptor ligand binding domain in complexes with five partial agonists. Biomolecular Nmr Assignments. 1: 241-3. PMID 19636875 DOI: 10.1007/S12104-007-9067-3 |
0.446 |
|
| 2007 |
Oswald RE. Flexibility of a glutamate-binding domain. Structure (London, England : 1993). 15: 1157-8. PMID 17937903 DOI: 10.1016/j.str.2007.09.005 |
0.353 |
|
| 2007 |
Oswald RE, Ahmed A, Fenwick MK, Loh AP. Structure of glutamate receptors. Current Drug Targets. 8: 573-82. PMID 17504102 DOI: 10.2174/138945007780618526 |
0.448 |
|
| 2007 |
Kornreich BG, Niu L, Roberson MS, Oswald RE. Identification of C-terminal domain residues involved in protein kinase A-mediated potentiation of kainate receptor subtype 6. Neuroscience. 146: 1158-68. PMID 17379418 DOI: 10.1016/J.Neuroscience.2007.02.012 |
0.721 |
|
| 2007 |
Ahmed AH, Loh AP, Jane DE, Oswald RE. Dynamics of the S1S2 glutamate binding domain of GluR2 measured using 19F NMR spectroscopy. The Journal of Biological Chemistry. 282: 12773-84. PMID 17337449 DOI: 10.1074/Jbc.M610077200 |
0.356 |
|
| 2006 |
Gizachew D, Oswald R. NMR structural studies of the myristoylated N-terminus of ADP ribosylation factor 6 (Arf6). Febs Letters. 580: 4296-301. PMID 16839550 DOI: 10.1016/J.Febslet.2006.06.086 |
0.347 |
|
| 2004 |
Oswald RE. Ionotropic glutamate receptor recognition and activation. Advances in Protein Chemistry. 68: 313-49. PMID 15500865 DOI: 10.1016/S0065-3233(04)68009-0 |
0.436 |
|
| 2004 |
McFeeters RL, Oswald RE. Emerging structural explanations of ionotropic glutamate receptor function. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 18: 428-38. PMID 15003989 DOI: 10.1096/Fj.03-0873Rev |
0.729 |
|
| 2003 |
Li G, Oswald RE, Niu L. Channel-opening kinetics of GluR6 kainate receptor. Biochemistry. 42: 12367-75. PMID 14567698 DOI: 10.1021/Bi034797T |
0.362 |
|
| 2002 |
McFeeters RL, Oswald RE. Structural mobility of the extracellular ligand-binding core of an ionotropic glutamate receptor. Analysis of NMR relaxation dynamics. Biochemistry. 41: 10472-81. PMID 12173934 DOI: 10.1021/Bi026010P |
0.719 |
|
| 2002 |
Oswald RE, Suchyna TM, McFeeters R, Gottlieb P, Sachs F. Solution structure of peptide toxins that block mechanosensitive ion channels. The Journal of Biological Chemistry. 277: 34443-50. PMID 12082099 DOI: 10.1074/Jbc.M202715200 |
0.642 |
|
| 2002 |
McFeeters RL, Swapna GV, Montelione GT, Oswald RE. Semi-automated backbone resonance assignments of the extracellular ligand-binding domain of an ionotropic glutamate receptor. Journal of Biomolecular Nmr. 22: 297-8. PMID 11991359 DOI: 10.1023/A:1014954931635 |
0.728 |
|
| 2000 |
Straub SG, Kornreich B, Oswald RE, Nemeth EF, Sharp GW. The calcimimetic R-467 potentiates insulin secretion in pancreatic beta cells by activation of a nonspecific cation channel. The Journal of Biological Chemistry. 275: 18777-84. PMID 10751384 DOI: 10.1074/Jbc.M000090200 |
0.667 |
|
| 2000 |
Chohan KK, Wo ZG, Oswald RE, Sutcliffe MJ. Structural insights into NMDA ionotropic glutamate receptors via molecular modelling Journal of Molecular Modeling. 6: 16-25. |
0.319 |
|
| 1999 |
Wo ZG, Chohan KK, Chen H, Sutcliffe MJ, Oswald RE. Cysteine mutagenesis and homology modeling of the ligand-binding site of a kainate-binding protein. The Journal of Biological Chemistry. 274: 37210-8. PMID 10601284 DOI: 10.1074/jbc.274.52.37210 |
0.409 |
|
| 1998 |
Sutcliffe MJ, Smeeton AH, Wo ZG, Oswald RE. Three-dimensional models of glutamate receptors. Faraday Discussions. 259-72; discussion 3. PMID 10822613 |
0.436 |
|
| 1998 |
Sutcliffe MJ, Smeeton AH, Wo ZG, Oswald RE. Three-dimensional models of glutamate receptors. Biochemical Society Transactions. 26: 450-8. PMID 9765895 |
0.317 |
|
| 1996 |
Niu L, Vazquez RW, Nagel G, Friedrich T, Bamberg E, Oswald RE, Hess GP. Rapid chemical kinetic techniques for investigations of neurotransmitter receptors expressed in Xenopus oocytes. Proceedings of the National Academy of Sciences of the United States of America. 93: 12964-8. PMID 8917527 DOI: 10.1073/Pnas.93.23.12964 |
0.569 |
|
| 1996 |
Wo ZG, Oswald RE. Ligand-binding characteristics and related structural features of the expressed goldfish kainate receptors: Identification of a conserved disulfide bond and three residues important for ligand binding Molecular Pharmacology. 50: 770-780. PMID 8863821 |
0.454 |
|
| 1996 |
Sutcliffe MJ, Wo ZG, Oswald RE. Three-dimensional models of non-NMDA glutamate receptors Biophysical Journal. 70: 1575-1589. PMID 8785317 |
0.429 |
|
| 1995 |
Wo ZG, Oswald RE. A topological analysis of goldfish kainate receptors predicts three transmembrane segments Journal of Biological Chemistry. 270: 2000-2009. PMID 7836426 DOI: 10.1074/jbc.270.5.2000 |
0.318 |
|
| 1995 |
Galen Wo Z, Christine Bian Z, Oswald RE. Asn-265 of frog kainate binding protein is a functional glycosylation site: implications for the transmembrane topology of glutamate receptors Febs Letters. 368: 230-234. PMID 7628611 DOI: 10.1016/0014-5793(95)00655-S |
0.386 |
|
| 1995 |
Galen Wo Z, Oswald RE. Unraveling the modular design of glutamate-gated ion channels Trends in Neurosciences. 18: 161-168. PMID 7539962 DOI: 10.1016/0166-2236(95)93895-5 |
0.389 |
|
| 1994 |
Wo ZG, Oswald RE. Transmembrane topology of two kainate receptor subunits revealed by N- glycosylation Proceedings of the National Academy of Sciences of the United States of America. 91: 7154-7158. PMID 8041762 DOI: 10.1073/pnas.91.15.7154 |
0.435 |
|
| 1992 |
Willard JM, Oswald RE. Interaction of the frog brain kainate receptor expressed in Chinese hamster ovary cells with a GTP-binding protein Journal of Biological Chemistry. 267: 19112-19116. PMID 1326545 |
0.318 |
|
| 1992 |
Willard JM, Ziegra CJ, Oswald RE. The interaction of a kainate receptor from goldfish brain with a pertussis toxin-sensitive GTP binding protein Annals of the New York Academy of Sciences. 648: 351-352. PMID 1322086 |
0.313 |
|
| 1992 |
Ziegra CJ, Willard JM, Oswald RE. Coupling of a purified goldfish brain kainate receptor with a pertussis toxin-sensitive G protein Proceedings of the National Academy of Sciences of the United States of America. 89: 4134-4138. PMID 1315052 |
0.321 |
|
| 1991 |
Willard JM, Ziegra CJ, Oswald RE. The interaction of a kainate receptor from goldfish brain with a pertussis toxin-sensitive GTP-binding protein Journal of Biological Chemistry. 266: 10196-10200. PMID 1674742 |
0.342 |
|
| 1989 |
Papke RL, Oswald RE. Mechanisms of noncompetitive inhibition of acetylcholine-induced single-channel currents. The Journal of General Physiology. 93: 785-811. PMID 2472461 DOI: 10.1085/Jgp.93.5.785 |
0.333 |
|
| 1988 |
Henley JM, Oswald RE. Characterization and regional distribution of glutamatergic and cholinergic ligand binding sites in goldfish brain. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 8: 2101-7. PMID 2898516 DOI: 10.1523/Jneurosci.08-06-02101.1988 |
0.384 |
|
| 1986 |
Horne WA, Weiland GA, Oswald RE, Cerione RA. Rapid incorporation of the solubilized dihydropyridine receptor into phospholipid vesicles. Biochimica Et Biophysica Acta. 863: 205-12. PMID 3024719 DOI: 10.1016/0005-2736(86)90260-9 |
0.371 |
|
| 1983 |
Oswald RE, Heidmann T, Changeux JP. Multiple affinity states for noncompetitive blockers revealed by [3H]phencyclidine binding to acetylcholine receptor rich membrane fragments from Torpedo marmorata. Biochemistry. 22: 3128-36. PMID 6882741 DOI: 10.1021/bi00282a015 |
0.301 |
|
| 1983 |
Oswald RE. Binding of phencyclidine to the detergent solubilized acetylcholine receptor from Torpedo marmorata Life Sciences. 32: 1143-1149. PMID 6827894 DOI: 10.1016/0024-3205(83)90120-0 |
0.374 |
|
| 1982 |
Cartaud J, Oswald R, Clément G, Changeux J. Evidence for a skeleton in acetylcholine receptor-rich membranes from Torpedo marmorata
electric organ Febs Letters. 145: 250-257. DOI: 10.1016/0014-5793(82)80177-4 |
0.335 |
|
| 1981 |
Oswald RE, Freeman JA. Analysis of alpha-bungarotoxin binding in the goldfish central nervous system. Journal of Neurochemistry. 37: 1586-93. PMID 7334377 DOI: 10.1111/j.1471-4159.1981.tb06331.x |
0.308 |
|
| 1981 |
Wennogle LP, Oswald R, Saitoh T, Changeux JP. Dissection of the 66 000-dalton subunit of the acetylcholine receptor. Biochemistry. 20: 2492-2497. PMID 7236616 DOI: 10.1021/Bi00512A020 |
0.412 |
|
| 1981 |
Oswald R, Changeux JP. Ultraviolet light-induced labeling by noncompetitive blockers of the acetylcholine receptor from Torpedo marmorata Proceedings of the National Academy of Sciences of the United States of America. 78: 3925-3929. PMID 6943590 DOI: 10.1073/Pnas.78.6.3925 |
0.407 |
|
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