| Year |
Citation |
Score |
| 2023 |
Hale WD, Romero AM, Gonzalez CU, Jayaraman V, Lau AY, Huganir RL, Twomey EC. Allosteric Competition and Inhibition in AMPA Receptors. Biorxiv : the Preprint Server For Biology. PMID 38076818 DOI: 10.1101/2023.11.28.569057 |
0.398 |
|
| 2023 |
Paudyal N, Das A, Carrillo E, Berka V, Jayaraman V. Partial agonism in heteromeric GLUK2/GLUK5 kainate receptor. Proteins. PMID 37526035 DOI: 10.1002/prot.26565 |
0.551 |
|
| 2022 |
Gao X, Schmidpeter PAM, Berka V, Durham RJ, Fan C, Jayaraman V, Nimigean CM. Gating intermediates reveal inhibitory role of the voltage sensor in a cyclic nucleotide-modulated ion channel. Nature Communications. 13: 6919. PMID 36376326 DOI: 10.1038/s41467-022-34673-z |
0.31 |
|
| 2022 |
Chen J, Li L, Chen SR, Chen H, Xie JD, Sirrieh RE, MacLean DM, Zhang Y, Zhou MH, Jayaraman V, Pan HL. The α2δ-1-NMDA Receptor Complex Is Critically Involved in Neuropathic Pain Development and Gabapentin Therapeutic Actions. Cell Reports. 38: 110308. PMID 35081351 DOI: 10.1016/j.celrep.2022.110308 |
0.663 |
|
| 2021 |
Carrillo E, Gonzalez CU, Berka V, Jayaraman V. Delta glutamate receptors are functional glycine- and ᴅ-serine-gated cation channels in situ. Science Advances. 7: eabk2200. PMID 34936451 DOI: 10.1126/sciadv.abk2200 |
0.416 |
|
| 2021 |
Hansen KB, Wollmuth LP, Bowie D, Furukawa H, Menniti FS, Sobolevsky AI, Swanson GT, Swanger SA, Greger IH, Nakagawa T, McBain CJ, Jayaraman V, Low CM, Dell'Acqua ML, Diamond JS, et al. Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels. Pharmacological Reviews. 73: 298-487. PMID 34753794 DOI: 10.1124/pharmrev.120.000131 |
0.662 |
|
| 2021 |
Gonzalez CU, Carrillo E, Berka V, Jayaraman V. Structural Arrangement Produced by Concanavalin A Binding to Homomeric GluK2 Receptors. Membranes. 11. PMID 34436376 DOI: 10.3390/membranes11080613 |
0.578 |
|
| 2021 |
Zhang J, Tang W, Bhatia NK, Xu Y, Paudyal N, Liu D, Kim S, Song R, XiangWei W, Shaulsky G, Myers SJ, Dobyns W, Jayaraman V, Traynelis SF, Yuan H, et al. A Variant Associated With Myoclonus and Developmental Delay: From Molecular Mechanism to Rescue Pharmacology. Frontiers in Genetics. 12: 694312. PMID 34413877 DOI: 10.3389/fgene.2021.694312 |
0.443 |
|
| 2021 |
Paudyal N, Bhatia NK, Jayaraman V. Single molecule FRET methodology for investigating glutamate receptors. Methods in Enzymology. 652: 193-212. PMID 34059282 DOI: 10.1016/bs.mie.2021.02.005 |
0.345 |
|
| 2020 |
Bhatia NK, Carrillo E, Durham RJ, Berka V, Jayaraman V. Allosteric changes in the NMDA receptor associated with calcium-dependent inactivation. Biophysical Journal. PMID 33098865 DOI: 10.1016/j.bpj.2020.08.045 |
0.43 |
|
| 2020 |
Carrillo E, Bhatia NK, Akimzhanov AM, Jayaraman V. Activity Dependent Inhibition of AMPA Receptors by Zn. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. PMID 33046551 DOI: 10.1523/JNEUROSCI.1481-20.2020 |
0.394 |
|
| 2020 |
Durham RJ, Paudyal N, Carrillo E, Bhatia NK, Maclean DM, Berka V, Dolino DM, Gorfe AA, Jayaraman V. Conformational spread and dynamics in allostery of NMDA receptors. Proceedings of the National Academy of Sciences of the United States of America. PMID 32015122 DOI: 10.1073/Pnas.1910950117 |
0.784 |
|
| 2020 |
Durham RJ, Paudyal N, Carrillo E, MacLean DM, Berka V, Dolino DM, Kaur Bhatia N, Gorfe AA, Jayaraman V. Role of Conformational Dynamics in NMDA Receptor Negative Cooperativity Biophysical Journal. 118: 586a. DOI: 10.1016/J.Bpj.2019.11.3178 |
0.74 |
|
| 2020 |
Bhatia NK, Carrillo E, Durham RJ, Berka V, Jayaraman V. Structural Insights into the Calcium/Calmodulin Dependent Inactivation of N-Methyl-D-Aspartate (NMDA) Receptors Biophysical Journal. 118: 583a. DOI: 10.1016/J.Bpj.2019.11.3164 |
0.427 |
|
| 2019 |
Carrillo E, Shaikh SA, Berka V, Durham RJ, Litwin DB, Lee G, MacLean DM, Nowak LM, Jayaraman V. Mechanism of modulation of AMPA receptors by TARP-γ8. The Journal of General Physiology. PMID 31748249 DOI: 10.1016/J.Bpj.2019.11.1158 |
0.776 |
|
| 2019 |
Litwin DB, Paudyal N, Carrillo E, Berka V, Jayaraman V. The structural arrangement and dynamics of the heteromeric GluK2/GluK5 kainate receptor as determined by smFRET. Biochimica Et Biophysica Acta. Biomembranes. PMID 31194959 DOI: 10.1016/J.Bbamem.2019.05.023 |
0.597 |
|
| 2019 |
Litwin DB, Carrillo E, Shaikh SA, Berka V, Jayaraman V. The structural arrangement at intersubunit interfaces in homomeric kainate receptors. Scientific Reports. 9: 6969. PMID 31061516 DOI: 10.1038/S41598-019-43360-X |
0.518 |
|
| 2019 |
Litwin DB, Durham RJ, Jayaraman V. Single-Molecule FRET Methods to Study Glutamate Receptors. Methods in Molecular Biology (Clifton, N.J.). 1941: 3-16. PMID 30707423 DOI: 10.1007/978-1-4939-9077-1_1 |
0.453 |
|
| 2019 |
Chatterjee S, Ade C, Nurik CE, Carrejo NC, Dutta C, Jayaraman V, Landes CF. Correction to "Phosphorylation Induces Conformational Rigidity at the C-Terminal Domain of AMPA Receptors". The Journal of Physical Chemistry. B. PMID 30676747 DOI: 10.1021/Acs.Jpcb.9B00258 |
0.466 |
|
| 2019 |
Carrillo Flores E, Shaikh SA, Jayaraman V. Mechanism of AMPA Receptor Modulation by Gamma-8 Biophysical Journal. 116: 106a. DOI: 10.1016/J.Bpj.2018.11.606 |
0.478 |
|
| 2019 |
Paudyal N, Litwin DB, Berka V, Flores EC, Jayaraman V. Study of a Heteromeric Kainate Receptor Gluk2/K5 by Probing Single-Molecule FRET Biophysical Journal. 116. DOI: 10.1016/J.Bpj.2018.11.604 |
0.401 |
|
| 2019 |
Durham RJ, Paudyal N, Carrillo E, Berka V, Jayaraman V. Single-Molecule FRET Investigations of Negative Cooperativity in the NMDA Receptor Biophysical Journal. 116: 105a. DOI: 10.1016/J.Bpj.2018.11.603 |
0.48 |
|
| 2019 |
Litwin DB, Carrillo E, Shaikh S, Berka V, Jayaraman V. The Structural Arrangement and Dynamics of Homomeric Kainate Receptors Determined by smFRET Biophysical Journal. 116: 105a. DOI: 10.1016/J.Bpj.2018.11.602 |
0.467 |
|
| 2018 |
Prakash P, Litwin D, Liang H, Sarkar-Banerjee S, Dolino D, Zhou Y, Hancock JF, Jayaraman V, Gorfe AA. Dynamics of Membrane-Bound G12V-KRAS From Simulations and Single-Molecule FRET in Native Nanodiscs. Biophysical Journal. PMID 30616834 DOI: 10.1016/J.Bpj.2018.12.011 |
0.309 |
|
| 2018 |
Chatterjee S, Ade C, Nurik CE, Carrejo NC, Dutta C, Jayaraman V, Landes CF. Phosphorylation Induces Conformational Rigidity at the C-terminal Domain of AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) Receptors. The Journal of Physical Chemistry. B. PMID 30537817 DOI: 10.1021/Acs.Jpcb.8B10749 |
0.567 |
|
| 2018 |
MacLean DM, Durham RJ, Jayaraman V. Mapping the Conformational Landscape of Glutamate Receptors Using Single Molecule FRET. Trends in Neurosciences. PMID 30385052 DOI: 10.1016/J.Tins.2018.10.003 |
0.771 |
|
| 2018 |
Chen J, Li L, Chen SR, Chen H, Xie JD, Sirrieh RE, MacLean DM, Zhang Y, Zhou MH, Jayaraman V, Pan HL. The α2δ-1-NMDA Receptor Complex Is Critically Involved in Neuropathic Pain Development and Gabapentin Therapeutic Actions. Cell Reports. 22: 2307-2321. PMID 29490268 DOI: 10.1016/J.Celrep.2018.02.021 |
0.641 |
|
| 2018 |
Litwin D, Shaikh S, Berka V, Jayaraman V. Single Molecule FRET Studies into the Effects of Sodium on Kainate Receptor Dynamics Biophysical Journal. 114. DOI: 10.1016/J.Bpj.2017.11.711 |
0.434 |
|
| 2018 |
Durham R, Dolino D, Jayaraman V. Allostery in NMDA Receptors Biophysical Journal. 114: 422a. DOI: 10.1016/J.Bpj.2017.11.2340 |
0.507 |
|
| 2017 |
Dolino DM, Chatterjee S, MacLean DM, Flatebo C, Bishop LDC, Shaikh SA, Landes CF, Jayaraman V. The structure-energy landscape of NMDA receptor gating. Nature Chemical Biology. PMID 28991238 DOI: 10.1038/Nchembio.2487 |
0.786 |
|
| 2017 |
Coombs ID, MacLean DM, Jayaraman V, Farrant M, Cull-Candy SG. Dual Effects of TARP γ-2 on Glutamate Efficacy Can Account for AMPA Receptor Autoinactivation. Cell Reports. 20: 1123-1135. PMID 28768197 DOI: 10.1016/J.Celrep.2017.07.014 |
0.736 |
|
| 2017 |
Ma J, Yanez-Orozco IS, Rezaei Adariani S, Dolino D, Jayaraman V, Sanabria H. High Precision FRET at Single-molecule Level for Biomolecule Structure Determination. Journal of Visualized Experiments : Jove. PMID 28570518 DOI: 10.3791/55623 |
0.506 |
|
| 2017 |
MacLean DM, Jayaraman V. Deactivation kinetics of acid-sensing ion channel 1a are strongly pH-sensitive. Proceedings of the National Academy of Sciences of the United States of America. PMID 28265090 DOI: 10.1073/Pnas.1620508114 |
0.672 |
|
| 2017 |
MacLean DM, Jayaraman V. Acid Sensing Ion Channels have Agonist-Dependent Deactivation Biophysical Journal. 112: 420a. DOI: 10.1016/J.Bpj.2016.11.2246 |
0.657 |
|
| 2017 |
Musgaard M, MacLean DM, Litwin DB, Jayaraman V, Biggin PC. Investigating Coupling between Proton Sensors and Channel Motions in Acid-Sensing Ion Channels Biophysical Journal. 112: 420a. DOI: 10.1016/J.Bpj.2016.11.2245 |
0.635 |
|
| 2017 |
Litwin DB, MacLean DM, Jayaraman V. Reduced Structural Dynamics in Kainate Receptors through Auxiliary Protein Modulation Biophysical Journal. 112: 419a. DOI: 10.1016/J.Bpj.2016.11.2242 |
0.719 |
|
| 2017 |
Shaikh SA, Dolino DM, Lee G, Chatterjee S, MacLean DM, Flatebo C, Landes CF, Jayaraman V. AMPA Receptor Modulation by Stargazin Biophysical Journal. 112: 418a. DOI: 10.1016/J.Bpj.2016.11.2239 |
0.741 |
|
| 2017 |
Nurik CE, Devi S, Shaikh S, Dolino D, Boehning D, Jayaraman V, Howe J. Phosphorylation in AMPA Receptor Carboxy-Terminus: Structure, Function, and Lipid Regulation Biophysical Journal. 112: 418a. DOI: 10.1016/J.Bpj.2016.11.2237 |
0.434 |
|
| 2017 |
Purwar N, Shaikh SA, Jayaraman V, Czajkowski C. Structural Rearrangements in GABA Biophysical Journal. 112: 321a. DOI: 10.1016/J.Bpj.2016.11.1741 |
0.535 |
|
| 2017 |
Jayaraman V. Dynamics of Glutamate Receptor Studied with Single Molecule FRET Biophysical Journal. 112. DOI: 10.1016/J.Bpj.2016.11.104 |
0.631 |
|
| 2016 |
Vitrac H, MacLean DM, Karlstaedt A, Taegtmeyer H, Jayaraman V, Bogdanov M, Dowhan W. Dynamic lipid-dependent modulation of protein topology by post-translational phosphorylation. The Journal of Biological Chemistry. PMID 27974465 DOI: 10.1074/Jbc.M116.765719 |
0.629 |
|
| 2016 |
Shaikh SA, Dolino DM, Lee G, Chatterjee S, MacLean DM, Flatebo C, Landes CF, Jayaraman V. Stargazin Modulation of AMPA Receptors. Cell Reports. 17: 328-335. PMID 27705782 DOI: 10.1016/J.Celrep.2016.09.014 |
0.787 |
|
| 2016 |
Dolino DM, Rezaei Adariani S, Shaikh SA, Jayaraman V, Sanabria H. Conformational selection and submillisecond dynamics of the ligand-binding domain of the N-methyl-D-Aspartate receptor. The Journal of Biological Chemistry. PMID 27226581 DOI: 10.1074/Jbc.M116.721274 |
0.534 |
|
| 2016 |
MacLean DM, Jayaraman V. Acid sensing ion channels are tuned to follow high frequency stimuli. The Journal of Physiology. PMID 26931316 DOI: 10.1113/Jp271915 |
0.649 |
|
| 2016 |
Nurik CE, Chattergee S, Devi S, Cooper DR, Ramaswamy SS, Landes C, Howe J, Jayaraman V. Structural Effects of Phosphorylation on C-Terminal Segment of AMPA Receptor Biophysical Journal. 110: 290a. DOI: 10.1016/J.Bpj.2015.11.1570 |
0.446 |
|
| 2016 |
Litwin DB, Lee G, Maclean D, Jayaraman V. Modulation of Glutamate Receptors by Auxiliary Proteins a Structural Investigation Biophysical Journal. 110: 289a. DOI: 10.1016/J.Bpj.2015.11.1564 |
0.798 |
|
| 2016 |
Dolino D, Chatterjee S, Cooper D, Jaurich H, Ramaswamy S, Rezaei Adariani S, Sanabria H, Landes C, Jayaraman V. Intra and Interdomain Motions of the NMDA Receptor using Single Molecule FRET Biophysical Journal. 110: 288a. DOI: 10.1016/J.Bpj.2015.11.1560 |
0.627 |
|
| 2016 |
MacLean DM, Jayaraman V. Acid Sensing Ion Channels are Uniquely Tuned to Follow High Frequency ‘Synaptic’ Stimuli Biophysical Journal. 110: 201a. DOI: 10.1016/J.Bpj.2015.11.1123 |
0.639 |
|
| 2016 |
Sirrieh RE, Jayaraman V. LRET methods for investigating conformational changes in functional ionotropic glutamate receptors Neuromethods. 106: 133-144. DOI: 10.1007/978-1-4939-2812-5_10 |
0.427 |
|
| 2015 |
Vitrac H, MacLean DM, Jayaraman V, Bogdanov M, Dowhan W. Dynamic membrane protein topological switching upon changes in phospholipid environment. Proceedings of the National Academy of Sciences of the United States of America. PMID 26512118 DOI: 10.1073/Pnas.1512994112 |
0.623 |
|
| 2015 |
Sirrieh RE, MacLean DM, Jayaraman V. A conserved structural mechanism of NMDA receptor inhibition: A comparison of ifenprodil and zinc. The Journal of General Physiology. PMID 26170175 DOI: 10.1085/Jgp.201511422 |
0.791 |
|
| 2015 |
Cooper DR, Dolino DM, Jaurich H, Shuang B, Ramaswamy S, Nurik CE, Chen J, Jayaraman V, Landes CF. Conformational Transitions in the Glycine-Bound GluN1 NMDA Receptor LBD via Single-Molecule FRET. Biophysical Journal. 109: 66-75. PMID 26153703 DOI: 10.1016/J.Bpj.2015.05.025 |
0.551 |
|
| 2015 |
Sirrieh RE, MacLean DM, Jayaraman V. Subtype-dependent N-methyl-D-aspartate receptor amino-terminal domain conformations and modulation by spermine. The Journal of Biological Chemistry. 290: 12812-20. PMID 25829490 DOI: 10.1074/Jbc.M115.649723 |
0.773 |
|
| 2015 |
Dolino DM, Cooper D, Ramaswamy S, Jaurich H, Landes CF, Jayaraman V. Structural dynamics of the glycine-binding domain of the N-methyl-D-aspartate receptor. The Journal of Biological Chemistry. 290: 797-804. PMID 25404733 DOI: 10.1074/Jbc.M114.605436 |
0.617 |
|
| 2015 |
Cooper DR, Dolino DM, Jaurich H, Shuang B, Ramaswamy S, Nurik CE, Chen J, Jayaraman V, Landes CF. Conformational Transitions in the Glycine-Bound GluN1 NMDA Receptor LBD via Single-Molecule FRET Biophysical Journal. 109: 66-75. DOI: 10.1016/j.bpj.2015.05.025 |
0.409 |
|
| 2015 |
Ramaswamy SS, MacLean D, Sanabria H, Jayaraman V. Gating Mechanism and Movements in Acid Sensing Ion Channel 1A Biophysical Journal. 108: 288a. DOI: 10.1016/J.Bpj.2014.11.1573 |
0.68 |
|
| 2015 |
Nurik CE, Cooper DR, Ramaswamy SS, Jayaraman V. Effect of Phosphorylation on Structure of C-Terminal Segment of AMPA Receptor Biophysical Journal. 108. DOI: 10.1016/J.Bpj.2014.11.1564 |
0.48 |
|
| 2015 |
MacLean DM, Jayaraman V. The Structural Basis of Negative Cooperativity between Subunits of the NMDA Receptor Biophysical Journal. 108: 286a. DOI: 10.1016/J.Bpj.2014.11.1562 |
0.783 |
|
| 2015 |
Dolino DM, Cooper DR, Ramaswamy SS, Jaurich H, Landes CF, Jayaraman V. NMDA Receptor smFRET Studies Reveal Role of Dynamics of the Agonist-Binding Domain in Mediating Agonist Efficacy Biophysical Journal. 108: 285a-286a. DOI: 10.1016/J.Bpj.2014.11.1559 |
0.644 |
|
| 2015 |
Sirrieh RE, MacLean DM, Jayaraman V. Investigations of the Structural Mechanism of Modulation of the NMDA Receptor Biophysical Journal. 108: 285a. DOI: 10.1016/J.Bpj.2014.11.1557 |
0.804 |
|
| 2014 |
MacLean DM, Ramaswamy SS, Du M, Howe JR, Jayaraman V. Stargazin promotes closure of the AMPA receptor ligand-binding domain. The Journal of General Physiology. 144: 503-12. PMID 25422502 DOI: 10.1085/Jgp.201411287 |
0.781 |
|
| 2014 |
Dolino DM, Ramaswamy SS, Jayaraman V. Luminescence resonance energy transfer to study conformational changes in membrane proteins expressed in mammalian cells. Journal of Visualized Experiments : Jove. 51895. PMID 25285993 DOI: 10.3791/51895 |
0.301 |
|
| 2014 |
Lee G, MacLean DM, Ulrich H, Zhao X, Aronowski J, Jayaraman V. RNA based antagonist of NMDA receptors. Acs Chemical Neuroscience. 5: 559-67. PMID 24708087 DOI: 10.1021/Cn500041K |
0.77 |
|
| 2014 |
Oak N, Jayaraman VK. Identification of ligand binding pockets on nuclear receptors by machine learning methods. Protein and Peptide Letters. 21: 808-14. PMID 23855664 |
0.314 |
|
| 2014 |
Sirrieh RE, MacLean DM, Jayaraman V. Inter-Subunit Interactions of NMDA Receptor Amino-Terminal Domains Associated with Allosteric Modulation Biophysical Journal. 106: 152a. DOI: 10.1016/J.Bpj.2013.11.875 |
0.805 |
|
| 2014 |
Dolino D, Cooper D, Ramaswamy S, Landes C, Jayaraman V. Single Molecule FRET Studies of the NMDA Receptor using Unnatural Amino Acids Biophysical Journal. 106: 659a. DOI: 10.1016/J.Bpj.2013.11.3652 |
0.645 |
|
| 2013 |
Ramaswamy SS, MacLean DM, Gorfe AA, Jayaraman V. Proton-mediated conformational changes in an acid-sensing ion channel. The Journal of Biological Chemistry. 288: 35896-903. PMID 24196950 DOI: 10.1074/Jbc.M113.478982 |
0.699 |
|
| 2013 |
Sirrieh RE, MacLean DM, Jayaraman V. Amino-terminal domain tetramer organization and structural effects of zinc binding in the N-methyl-D-aspartate (NMDA) receptor. The Journal of Biological Chemistry. 288: 22555-64. PMID 23792960 DOI: 10.1074/Jbc.M113.482356 |
0.794 |
|
| 2013 |
MacLean DM, Ramaswamy S, Howe JR, Jayaraman V. Towards a Mechanism of TARP Action at AMPA Receptors Biophysical Journal. 104: 543a. DOI: 10.1016/J.Bpj.2012.11.3007 |
0.778 |
|
| 2013 |
Sirrieh RE, MacLean DM, Jayaraman V. Arrangement of the N-Terminal Domains in NMDA Receptors Biophysical Journal. 104: 272a-273a. DOI: 10.1016/J.Bpj.2012.11.1529 |
0.799 |
|
| 2013 |
Ramaswamy SS, MacLean DM, Jayaraman V. Cleft Closure Mechanism in Gating of Acid Sensing Ion Channel 1A Biophysical Journal. 104: 270a. DOI: 10.1016/J.Bpj.2012.11.1516 |
0.691 |
|
| 2012 |
Ramaswamy S, Cooper D, Poddar N, MacLean DM, Rambhadran A, Taylor JN, Uhm H, Landes CF, Jayaraman V. Role of conformational dynamics in α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) receptor partial agonism. The Journal of Biological Chemistry. 287: 43557-64. PMID 23115239 DOI: 10.1074/Jbc.M112.371815 |
0.847 |
|
| 2012 |
Sirrieh RE, Jayaraman V. N-Terminal Domain of NMDA Receptors as Studied by LRET Biophysical Journal. 102: 115a-116a. DOI: 10.1016/J.Bpj.2011.11.649 |
0.531 |
|
| 2012 |
Jayaraman V, Rambhadran A. Mechanism of Activation in NMDA Receptors Biophysical Journal. 102: 418a. DOI: 10.1016/J.Bpj.2011.11.2288 |
0.862 |
|
| 2012 |
Ramaswamy SS, Suppiramaniam V, Jayaraman V. Conformational Change Involved in Gating of Acid Sensing Ion Channel (ASIC1a) Biophysical Journal. 102: 336. DOI: 10.1016/J.Bpj.2011.11.1842 |
0.4 |
|
| 2011 |
Rambhadran A, Gonzalez J, Jayaraman V. Conformational changes at the agonist binding domain of the N-methyl-D-aspartic acid receptor. The Journal of Biological Chemistry. 286: 16953-7. PMID 21454656 DOI: 10.1074/Jbc.M111.224576 |
0.857 |
|
| 2011 |
Landes CF, Rambhadran A, Taylor JN, Salatan F, Jayaraman V. Structural landscape of isolated agonist-binding domains from single AMPA receptors. Nature Chemical Biology. 7: 168-73. PMID 21297640 DOI: 10.1038/Nchembio.523 |
0.845 |
|
| 2011 |
Jayaraman V, Rambhadran A. Erratum: (Biophysical Journal) Biophysical Journal. 100. DOI: 10.1016/J.Bpj.2011.03.038 |
0.726 |
|
| 2011 |
Landes CF, Taylor JN, Rambhadran A, Jayaraman V. Wavelet Shrinkage to Resolve Single Molecule FRET Structural Landscape of the Isolated Ligand Binding Domain of the AMPA Receptor Biophysical Journal. 100: 478a. DOI: 10.1016/J.Bpj.2010.12.2800 |
0.822 |
|
| 2010 |
Gonzalez J, Du M, Parameshwaran K, Suppiramaniam V, Jayaraman V. Role of dimer interface in activation and desensitization in AMPA receptors. Proceedings of the National Academy of Sciences of the United States of America. 107: 9891-6. PMID 20457909 DOI: 10.1073/Pnas.0911854107 |
0.615 |
|
| 2010 |
Rambhadran A, Gonzalez J, Jayaraman V. Subunit arrangement in N-methyl-D-aspartate (NMDA) receptors. The Journal of Biological Chemistry. 285: 15296-301. PMID 20304927 DOI: 10.1074/Jbc.M109.085035 |
0.858 |
|
| 2009 |
Du M, Rambhadran A, Jayaraman V. Vibrational spectroscopic investigation of the ligand binding domain of kainate receptors. Protein Science : a Publication of the Protein Society. 18: 1585-91. PMID 19544581 DOI: 10.1002/Pro.174 |
0.834 |
|
| 2009 |
Gonzalez J, Jayaraman V. A LRET Based Method To Studying Intersubunit Conformational Changes In The Ligand Binding Domain Of A Functional AMPA Receptor Biophysical Journal. 96. DOI: 10.1016/J.Bpj.2008.12.2530 |
0.621 |
|
| 2009 |
Rambhadran A, Jayaraman V. NMDA Receptor Subunit Arrangement Probed By LRET Biophysical Journal. 96: 489a. DOI: 10.1016/J.Bpj.2008.12.2525 |
0.847 |
|
| 2008 |
Gonzalez J, Rambhadran A, Du M, Jayaraman V. LRET investigations of conformational changes in the ligand binding domain of a functional AMPA receptor. Biochemistry. 47: 10027-32. PMID 18759455 DOI: 10.1021/Bi800690B |
0.847 |
|
| 2008 |
Liu Z, Ramanoudjame G, Liu D, Fox RO, Jayaraman V, Kurnikova M, Cascio M. Overexpression and functional characterization of the extracellular domain of the human alpha1 glycine receptor. Biochemistry. 47: 9803-10. PMID 18710260 DOI: 10.1021/Bi800659X |
0.488 |
|
| 2008 |
Du M, Rambhadran A, Jayaraman V. Luminescence resonance energy transfer investigation of conformational changes in the ligand binding domain of a kainate receptor. The Journal of Biological Chemistry. 283: 27074-8. PMID 18658129 DOI: 10.1074/Jbc.M805040200 |
0.851 |
|
| 2008 |
Mankiewicz KA, Rambhadran A, Wathen L, Jayaraman V. Chemical interplay in the mechanism of partial agonist activation in alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors. Biochemistry. 47: 398-404. PMID 18081322 DOI: 10.1021/Bi702004B |
0.844 |
|
| 2007 |
Mankiewicz KA, Jayaraman V. Glutamate receptors as seen by light: spectroscopic studies of structure-function relationships. Brazilian Journal of Medical and Biological Research = Revista Brasileira De Pesquisas MéDicas E BiolóGicas / Sociedade Brasileira De BiofíSica ... [Et Al.]. 40: 1419-27. PMID 17934637 DOI: 10.1590/S0100-879X2007001100001 |
0.855 |
|
| 2007 |
Du M, Ulrich H, Zhao X, Aronowski J, Jayaraman V. Water soluble RNA based antagonist of AMPA receptors. Neuropharmacology. 53: 242-51. PMID 17588619 DOI: 10.1016/J.Neuropharm.2007.05.007 |
0.68 |
|
| 2007 |
Mankiewicz KA, Rambhadran A, Du M, Ramanoudjame G, Jayaraman V. Role of the chemical interactions of the agonist in controlling alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor activation. Biochemistry. 46: 1343-9. PMID 17260963 DOI: 10.1021/Bi062270L |
0.847 |
|
| 2006 |
Ramanoudjame G, Du M, Mankiewicz KA, Jayaraman V. Allosteric mechanism in AMPA receptors: a FRET-based investigation of conformational changes. Proceedings of the National Academy of Sciences of the United States of America. 103: 10473-8. PMID 16793923 DOI: 10.1073/Pnas.0603225103 |
0.853 |
|
| 2006 |
Madden DR, Cheng Q, Thiran S, Rajan S, Rigo F, Keinänen K, Reinelt S, Zimmermann H, Jayaraman V. Erratum: Stereochemistry of glutamate receptor agonist efficacy: Engineering a dual-specificity AMPA/kainate receptor (Biochemistry (December 21, 2004) 43, 50 (15838-15844)) Biochemistry. 45. DOI: 10.1021/Bi0680025 |
0.831 |
|
| 2005 |
Cheng Q, Du M, Ramanoudjame G, Jayaraman V. Evolution of glutamate interactions during binding to a glutamate receptor. Nature Chemical Biology. 1: 329-32. PMID 16408071 DOI: 10.1038/Nchembio738 |
0.618 |
|
| 2005 |
Du M, Reid SA, Jayaraman V. Conformational changes in the ligand-binding domain of a functional ionotropic glutamate receptor. The Journal of Biological Chemistry. 280: 8633-6. PMID 15632199 DOI: 10.1074/Jbc.C400590200 |
0.604 |
|
| 2004 |
Madden DR, Cheng Q, Thiran S, Rajan S, Rigo F, Keinänen K, Reinelt S, Zimmermann H, Jayaraman V. Stereochemistry of glutamate receptor agonist efficacy: engineering a dual-specificity AMPA/kainate receptor. Biochemistry. 43: 15838-44. PMID 15595838 DOI: 10.1021/Bi048447Y |
0.864 |
|
| 2004 |
Cheng Q, Jayaraman V. Chemistry and conformation of the ligand-binding domain of GluR2 subtype of glutamate receptors. The Journal of Biological Chemistry. 279: 26346-50. PMID 15100219 DOI: 10.1074/Jbc.M403111200 |
0.558 |
|
| 2004 |
Jayaraman V. Spectroscopic and kinetic methods for ligand-protein interactions of glutamate receptor. Methods in Enzymology. 380: 170-87. PMID 15051337 DOI: 10.1016/S0076-6879(04)80008-9 |
0.528 |
|
| 2003 |
Deming D, Cheng Q, Jayaraman V. Is the isolated ligand binding domain a good model of the domain in the native receptor? The Journal of Biological Chemistry. 278: 17589-92. PMID 12657650 DOI: 10.1074/Jbc.C300105200 |
0.568 |
|
| 2002 |
Ramachandran H, Jayaraman V, Banerjee B, Greenberger PA, Kelly KJ, Fink JN, Kurup VP. IgE binding conformational epitopes of Asp f 3, a major allergen of Aspergillus fumigatus. Clinical Immunology (Orlando, Fla.). 103: 324-33. PMID 12173308 DOI: 10.1006/Clim.2002.5219 |
0.329 |
|
| 2002 |
Cheng Q, Steinmetz MG, Jayaraman V. Photolysis of gamma-(alpha-carboxy-2-nitrobenzyl)-L-glutamic acid investigated in the mcrosecond time scale by time-resolved FTIR. Journal of the American Chemical Society. 124: 7676-7. PMID 12083919 DOI: 10.1021/Ja0259988 |
0.351 |
|
| 2002 |
Cheng Q, Thiran S, Yernool D, Gouaux E, Jayaraman V. A vibrational spectroscopic investigation of interactions of agonists with GluR0, a prokaryotic glutamate receptor. Biochemistry. 41: 1602-8. PMID 11814354 DOI: 10.1021/Bi015729E |
0.84 |
|
| 2001 |
Madden DR, Thiran S, Zimmermann H, Romm J, Jayaraman V. Stereochemistry of quinoxaline antagonist binding to a glutamate receptor investigated by Fourier transform infrared spectroscopy. The Journal of Biological Chemistry. 276: 37821-6. PMID 11481334 DOI: 10.1074/Jbc.M106171200 |
0.842 |
|
| 2000 |
Hess GP, Ulrich H, Breitinger HG, Niu L, Gameiro AM, Grewer C, Srivastava S, Ippolito JE, Lee SM, Jayaraman V, Coombs SE. Mechanism-based discovery of ligands that counteract inhibition of the nicotinic acetylcholine receptor by cocaine and MK-801. Proceedings of the National Academy of Sciences of the United States of America. 97: 13895-900. PMID 11095713 DOI: 10.1073/Pnas.240459497 |
0.816 |
|
| 2000 |
Jayaraman V, Keesey R, Madden DR. Ligand--protein interactions in the glutamate receptor. Biochemistry. 39: 8693-7. PMID 10913279 DOI: 10.1021/Bi000892F |
0.778 |
|
| 2000 |
Jayaraman V, Thiran S, Madden DR. Fourier transform infrared spectroscopic characterization of a photolabile precursor of glutamate. Febs Letters. 475: 278-82. PMID 10869571 DOI: 10.1016/S0014-5793(00)01690-2 |
0.828 |
|
| 2000 |
Jayaraman V, Keesey R, Madden DR. Ligand-protein interactions in the glutamate receptor Biochemistry. 39: X-8697. |
0.721 |
|
| 1999 |
Jayaraman V, Usherwood PN, Hess GP. Inhibition of nicotinic acetylcholine receptor by philanthotoxin-343: kinetic investigations in the microsecond time region using a laser-pulse photolysis technique. Biochemistry. 38: 11406-14. PMID 10471291 DOI: 10.1021/Bi991219X |
0.637 |
|
| 1999 |
Jayaraman V, Thiran S, Hess GP. How fast does the gamma-aminobutyric acid receptor channel open? Kinetic investigations in the microsecond time region using a laser-pulse photolysis technique. Biochemistry. 38: 11372-8. PMID 10471287 DOI: 10.1021/Bi990454C |
0.806 |
|
| 1999 |
Gee KR, Niu L, Schaper K, Jayaraman V, Hess GP. Synthesis and photochemistry of a photolabile precursor of N-methyl-D-aspartate (NMDA) that is photolyzed in the microsecond time region and is suitable for chemical kinetic investigations of the NMDA receptor. Biochemistry. 38: 3140-7. PMID 10074369 DOI: 10.1021/Bi9826557 |
0.811 |
|
| 1998 |
Jayaraman V. Channel-opening mechanism of a kainate-activated glutamate receptor: kinetic investigations using a laser-pulse photolysis technique. Biochemistry. 37: 16735-40. PMID 9843443 DOI: 10.1021/Bi9813328 |
0.489 |
|
| 1997 |
Jayaraman V, Hess GP. Channel-opening kinetics of the y-amino butyric acid (GABA) receptor investigated by rapid chemical kinetic methods Faseb Journal. 11: A969. |
0.576 |
|
| 1996 |
Jayaraman V, Spiro TG. Structural evolution of the heme group during the allosteric transition in hemoglobin: Insights from resonance Raman spectra of isotopically labeled heme Biospectroscopy. 2: 311-316. DOI: 10.1002/(Sici)1520-6343(1996)2:5<311::Aid-Bspy4>3.0.Co;2-7 |
0.452 |
|
| 1995 |
Gregoriou VG, Jayaraman V, Hu X, Spiro TG. FT-IR difference spectroscopy of hemoglobins A and Kempsey: evidence that a key quaternary interaction induces protonation of Asp beta 99. Biochemistry. 34: 6876-82. PMID 7756319 DOI: 10.1021/Bi00020A035 |
0.45 |
|
| 1995 |
Jayaraman V, Spiro TG. Structure of a third cooperativity state of hemoglobin: ultraviolet resonance Raman spectroscopy of cyanomethemoglobin ligation microstates. Biochemistry. 34: 4511-5. PMID 7718552 DOI: 10.1021/Bi00014A002 |
0.47 |
|
| 1995 |
Jayaraman V, Rodgers KR, Mukerji I, Spiro TG. Hemoglobin allostery: resonance Raman spectroscopy of kinetic intermediates. Science (New York, N.Y.). 269: 1843-8. PMID 7569921 DOI: 10.1126/Science.7569921 |
0.683 |
|
| 1993 |
Jayaraman V, Rodgers KR, Mukerji I, Spiro TG. R and T states of fluoromethemoglobin probed by ultraviolet resonance Raman spectroscopy. Biochemistry. 32: 4547-51. PMID 8485131 DOI: 10.1021/Bi00068A009 |
0.665 |
|
| 1993 |
Rodgers K, Mukerji I, Jayaraman V, Spiro T. Hemoglobin dynamics from transient raman spectroscopy Journal of Inorganic Biochemistry. 51: 215. DOI: 10.1016/0162-0134(93)85249-8 |
0.606 |
|
| Show low-probability matches. |