| Year |
Citation |
Score |
| 2023 |
Kumar J, Popescu GK, Gantz SC. GluD receptors are functional ion channels. Biophysical Journal. PMID 37177782 DOI: 10.1016/j.bpj.2023.05.012 |
0.446 |
|
| 2022 |
Dhingra S, Yadav J, Kumar J. Structure, Function, and Regulation of the Kainate Receptor. Sub-Cellular Biochemistry. 99: 317-350. PMID 36151381 DOI: 10.1007/978-3-031-00793-4_10 |
0.512 |
|
| 2022 |
Kumar J. Ionotropic glutamate delta receptors: The enigma has finally begun to unravel. Neuropharmacology. 207: 108944. PMID 34999013 DOI: 10.1016/j.neuropharm.2022.108944 |
0.469 |
|
| 2021 |
Dutta P, Bharti P, Kumar J, Maiti S. Role of actin cytoskeleton in the organization and function of ionotropic glutamate receptors. Current Research in Structural Biology. 3: 277-289. PMID 34766008 DOI: 10.1016/j.crstbi.2021.10.001 |
0.329 |
|
| 2021 |
Vinnakota R, Dhingra S, Kumari J, Ansari MY, Shukla E, Nerkar MD, Kumar J. Role of Neto1 extracellular domain in modulation of kainate receptors. International Journal of Biological Macromolecules. 192: 525-536. PMID 34634333 DOI: 10.1016/j.ijbiomac.2021.10.001 |
0.518 |
|
| 2021 |
Burada AP, Vinnakota R, Lambolez B, Tricoire L, Kumar J. Structural biology of ionotropic glutamate delta receptors and their crosstalk with metabotropic glutamate receptors. Neuropharmacology. 108683. PMID 34181979 DOI: 10.1016/j.neuropharm.2021.108683 |
0.532 |
|
| 2020 |
Burada AP, Vinnakota R, Bharti P, Dutta P, Dubey N, Kumar J. Emerging Insights into the Structure and Function of Ionotropic GluD Receptors. British Journal of Pharmacology. PMID 33145757 DOI: 10.1111/bph.15313 |
0.438 |
|
| 2020 |
Burada AP, Vinnakota R, Kumar J. The Architecture of GluD2 Ionotropic Delta Glutamate Receptor Elucidated by cryo-EM. Journal of Structural Biology. 107546. PMID 32512155 DOI: 10.1016/J.Jsb.2020.107546 |
0.628 |
|
| 2020 |
Kumari J, Bendre AD, Bhosale S, Vinnakota R, Burada AP, Ravelli R, Peters PJ, Joshi M, Kumar J. Structural dynamics of the GluK3-kainate receptor neurotransmitter binding domains revealed by cryo-EM. International Journal of Biological Macromolecules. PMID 32006583 DOI: 10.1016/J.Ijbiomac.2020.01.282 |
0.609 |
|
| 2020 |
Burada AP, Vinnakota R, Kumar J. Cryo-EM structures of the ionotropic glutamate receptor GluD1 reveal a non-swapped architecture. Nature Structural & Molecular Biology. 27: 84-91. PMID 31925409 DOI: 10.1038/S41594-019-0359-Y |
0.633 |
|
| 2019 |
Kumari J, Vinnakota R, Kumar J. Structural and Functional Insights into GluK3-kainate Receptor Desensitization and Recovery. Scientific Reports. 9: 10254. PMID 31311973 DOI: 10.2210/Pdb6Jfy/Pdb |
0.613 |
|
| 2014 |
Meyerson JR, Rao P, Kumar J, Chittori S, Banerjee S, Pierson J, Mayer ML, Subramaniam S. Self-assembled monolayers improve protein distribution on holey carbon cryo-EM supports. Scientific Reports. 4: 7084. PMID 25403871 DOI: 10.1038/Srep07084 |
0.704 |
|
| 2014 |
Meyerson JR, Kumar J, Chittori S, Rao P, Pierson J, Bartesaghi A, Mayer ML, Subramaniam S. Structural mechanism of glutamate receptor activation and desensitization. Nature. 514: 328-34. PMID 25119039 DOI: 10.1038/Nature13603 |
0.782 |
|
| 2014 |
Chittori S, Kumar J, Lomash S, Zhao H, Schuck P, Mayer ML. Role of Amino-Terminal Domain in the Assembly Mechanism of Kainate-Subtype Glutamate Receptor Ion Channels Biophysical Journal. 106: 151a. DOI: 10.1016/J.Bpj.2013.11.869 |
0.787 |
|
| 2013 |
Zhao H, Berger AJ, Brown PH, Kumar J, Balbo A, May CA, Casillas E, Laue TM, Patterson GH, Mayer ML, Schuck P. Analysis of high-affinity assembly for AMPA receptor amino-terminal domains. The Journal of General Physiology. 141: 747-9. PMID 23855058 DOI: 10.1085/Jgp.20121077004292013C |
0.587 |
|
| 2013 |
Kumar J, Mayer ML. Functional insights from glutamate receptor ion channel structures. Annual Review of Physiology. 75: 313-37. PMID 22974439 DOI: 10.1146/Annurev-Physiol-030212-183711 |
0.739 |
|
| 2013 |
Kumar J, Veran J, Pinheiro PS, Athane A, Perrais D, Mulle C, Mayer ML. The GluK3 Ligand Binding Domain has a Zinc Binding Site at the Dimer Interface Biophysical Journal. 104: 272a. DOI: 10.1016/J.Bpj.2012.11.1526 |
0.713 |
|
| 2012 |
Veran J, Kumar J, Pinheiro PS, Athané A, Mayer ML, Perrais D, Mulle C. Zinc potentiates GluK3 glutamate receptor function by stabilizing the ligand binding domain dimer interface. Neuron. 76: 565-78. PMID 23141068 DOI: 10.1016/J.Neuron.2012.08.027 |
0.684 |
|
| 2012 |
Zhao H, Berger AJ, Brown PH, Kumar J, Balbo A, May CA, Casillas E, Laue TM, Patterson GH, Mayer ML, Schuck P. Analysis of high-affinity assembly for AMPA receptor amino-terminal domains. The Journal of General Physiology. 139: 371-88. PMID 22508847 DOI: 10.1085/Jgp.201210770 |
0.594 |
|
| 2012 |
Kumar J, Zhang J, Mayer ML. Optimization of Constructs for Expression, Purification and Crystallization of Glutamate Receptor Ion Channels Biophysical Journal. 102: 116a. DOI: 10.1016/J.Bpj.2011.11.650 |
0.707 |
|
| 2011 |
Chaudhry C, Scimemi A, Kumar J. Building and breaking interfaces: how a receptor takes shape. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 31: 10749-51. PMID 21795526 DOI: 10.1523/JNEUROSCI.2312-11.2011 |
0.539 |
|
| 2011 |
Kumar J, Schuck P, Mayer ML. Structure and assembly mechanism for heteromeric kainate receptors. Neuron. 71: 319-31. PMID 21791290 DOI: 10.1016/J.Neuron.2011.05.038 |
0.756 |
|
| 2011 |
Pandey SP, Minesinger BK, Kumar J, Walker GC. A highly conserved protein of unknown function in Sinorhizobium meliloti affects sRNA regulation similar to Hfq. Nucleic Acids Research. 39: 4691-708. PMID 21325267 DOI: 10.1093/Nar/Gkr060 |
0.305 |
|
| 2011 |
Kumar J, Schuck P, Mayer ML. Structure & Mechanisms Underlying Heteromeric Glutamate Receptor Assembly Biophysical Journal. 100: 24a. DOI: 10.1016/J.Bpj.2010.12.337 |
0.742 |
|
| 2010 |
Kumar J, Mayer ML. Crystal structures of the glutamate receptor ion channel GluK3 and GluK5 amino-terminal domains. Journal of Molecular Biology. 404: 680-96. PMID 20951142 DOI: 10.1016/J.Jmb.2010.10.006 |
0.725 |
|
| 2010 |
Das U, Kumar J, Mayer ML, Plested AJ. Domain organization and function in GluK2 subtype kainate receptors. Proceedings of the National Academy of Sciences of the United States of America. 107: 8463-8. PMID 20404149 DOI: 10.1073/Pnas.1000838107 |
0.78 |
|
| 2010 |
Kumar J, Mayer ML. Crystal Structure of KA2-Subtype Ionotropic Glutamate Receptor Amino Terminal Domain Biophysical Journal. 98: 524a. DOI: 10.1016/J.Bpj.2009.12.2846 |
0.731 |
|
| 2009 |
Kumar J, Schuck P, Jin R, Mayer ML. The N-terminal domain of GluR6-subtype glutamate receptor ion channels. Nature Structural & Molecular Biology. 16: 631-8. PMID 19465914 DOI: 10.1038/Nsmb.1613 |
0.759 |
|
| 2009 |
Kumar J, Mayer M. Purification and crystallization of iGluR Amino Terminal Domains Biophysical Journal. 96: 491a. DOI: 10.1016/J.Bpj.2008.12.2536 |
0.735 |
|
| 2007 |
Ethayathulla AS, Srivastava DB, Kumar J, Saravanan K, Bilgrami S, Sharma S, Kaur P, Srinivasan A, Singh TP. Structure of the buffalo secretory signalling glycoprotein at 2.8 A resolution. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 63: 258-65. PMID 17401190 DOI: 10.1107/S1744309107010445 |
0.369 |
|
| 2007 |
Kumar J, Ethayathulla AS, Srivastava DB, Singh N, Sharma S, Kaur P, Srinivasan A, Singh TP. Carbohydrate-binding properties of goat secretory glycoprotein (SPG-40) and its functional implications: structures of the native glycoprotein and its four complexes with chitin-like oligosaccharides. Acta Crystallographica. Section D, Biological Crystallography. 63: 437-46. PMID 17372347 DOI: 10.1107/S0907444907001631 |
0.369 |
|
| 2006 |
Srivastava DB, Ethayathulla AS, Kumar J, Somvanshi RK, Sharma S, Dey S, Singh TP. Carbohydrate binding properties and carbohydrate induced conformational switch in sheep secretory glycoprotein (SPS-40): crystal structures of four complexes of SPS-40 with chitin-like oligosaccharides. Journal of Structural Biology. 158: 255-66. PMID 17188513 DOI: 10.1016/J.Jsb.2006.11.002 |
0.399 |
|
| 2006 |
Kumar J, Ethayathulla AS, Srivastava DB, Sharma S, Singh SB, Srinivasan A, Yadav MP, Singh TP. Structure of a bovine secretory signalling glycoprotein (SPC-40) at 2.1 Angstrom resolution. Acta Crystallographica. Section D, Biological Crystallography. 62: 953-63. PMID 16929095 DOI: 10.1107/S0907444906020427 |
0.396 |
|
| 2006 |
Srivastava DB, Ethayathulla AS, Kumar J, Singh N, Sharma S, Das U, Srinivasan A, Singh TP. Crystal structure of a secretory signalling glycoprotein from sheep at 2.0A resolution. Journal of Structural Biology. 156: 505-16. PMID 16859926 DOI: 10.1016/J.Jsb.2006.05.008 |
0.343 |
|
| 2004 |
Bilgrami S, Tomar S, Yadav S, Kaur P, Kumar J, Jabeen T, Sharma S, Singh TP. Crystal structure of schistatin, a disintegrin homodimer from saw-scaled viper (Echis carinatus) at 2.5 A resolution. Journal of Molecular Biology. 341: 829-37. PMID 15317139 DOI: 10.1016/J.Jmb.2004.06.048 |
0.412 |
|
| 2003 |
Sharma S, Jasti J, Kumar J, Mohanty AK, Singh TP. Crystal structure of a proteolytically generated functional monoferric C-lobe of bovine lactoferrin at 1.9A resolution. Journal of Molecular Biology. 331: 485-96. PMID 12888354 DOI: 10.1016/S0022-2836(03)00717-4 |
0.413 |
|
| Show low-probability matches. |