| Year |
Citation |
Score |
| 2018 |
Hayama R, Sparks S, Hecht LM, Dutta K, Cabana CM, Karp JM, Rout MP, Cowburn D. Thermodynamic characterization of the multivalent interactions underlying rapid and selective translocation through the nuclear pore complex. The Journal of Biological Chemistry. PMID 29374059 DOI: 10.1074/Jbc.Ac117.001649 |
0.598 |
|
| 2017 |
Upla P, Kim SJ, Sampathkumar P, Dutta K, Cahill SM, Chemmama IE, Williams R, Bonanno JB, Rice WJ, Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J. Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure (London, England : 1993). PMID 28162953 DOI: 10.1016/J.Str.2017.01.006 |
0.562 |
|
| 2016 |
Raveh B, Karp JM, Sparks S, Dutta K, Rout MP, Sali A, Cowburn D. Slide-and-exchange mechanism for rapid and selective transport through the nuclear pore complex. Proceedings of the National Academy of Sciences of the United States of America. PMID 27091992 DOI: 10.1073/Pnas.1522663113 |
0.588 |
|
| 2016 |
Maguire LK, Wall K, Armstrong G, Dutta K, Sparks S, Temel DB, Kamal A, Tetenbaum-Novatt J, Rout MP, Cowburn D, Hough L. The Role of Intrinsic Disorder in the Molecular Mechanism of Nuclear Transport Biophysical Journal. 110: 558a. DOI: 10.1016/J.Bpj.2015.11.2983 |
0.58 |
|
| 2015 |
Ferrage F, Dutta K, Cowburn D. Identification of Hydrophobic Interfaces in Protein-Ligand Complexes by Selective Saturation Transfer NMR Spectroscopy. Molecules (Basel, Switzerland). 20: 21992-9. PMID 26690112 DOI: 10.3390/Molecules201219824 |
0.583 |
|
| 2015 |
Hough LE, Dutta K, Sparks S, Temel DB, Kamal A, Tetenbaum-Novatt J, Rout MP, Cowburn D. The molecular mechanism of nuclear transport revealed by atomic-scale measurements. Elife. 4. PMID 26371551 DOI: 10.7554/Elife.10027 |
0.599 |
|
| 2015 |
Dutta K, Varshney AK, Franklin MC, Goger M, Wang X, Fries BC. Mechanisms mediating enhanced neutralization efficacy of staphylococcal enterotoxin B by combinations of monoclonal antibodies. The Journal of Biological Chemistry. 290: 6715-30. PMID 25572397 DOI: 10.1074/Jbc.M114.630715 |
0.317 |
|
| 2015 |
Hough LE, Dutta K, Sparks S, Temel DB, Kamal A, Tetenbaum-Novatt J, Rout MP, Cowburn D. Author response: The molecular mechanism of nuclear transport revealed by atomic-scale measurements Elife. DOI: 10.7554/Elife.10027.019 |
0.512 |
|
| 2014 |
Chandrababu KB, Dutta K, Lokappa SB, Ndao M, Evans JS, Moradian-Oldak J. Structural adaptation of tooth enamel protein amelogenin in the presence of SDS micelles. Biopolymers. 101: 525-35. PMID 24114119 DOI: 10.1002/Bip.22415 |
0.421 |
|
| 2014 |
Temel DB, Dutta K, Ghose R. Sequence-specific backbone ¹H, ¹³C and ¹⁵N assignments of the catalytic domain of the Escherichia coli protein tyrosine kinase, Wzc. Biomolecular Nmr Assignments. 8: 37-41. PMID 23225198 DOI: 10.1007/S12104-012-9448-0 |
0.335 |
|
| 2013 |
Chen H, Huang Z, Dutta K, Blais S, Neubert TA, Li X, Cowburn D, Traaseth NJ, Mohammadi M. Cracking the molecular origin of intrinsic tyrosine kinase activity through analysis of pathogenic gain-of-function mutations. Cell Reports. 4: 376-84. PMID 23871672 DOI: 10.1016/J.Celrep.2013.06.025 |
0.505 |
|
| 2013 |
Temel DB, Dutta K, Alphonse S, Nourikyan J, Grangeasse C, Ghose R. Regulatory interactions between a bacterial tyrosine kinase and its cognate phosphatase. The Journal of Biological Chemistry. 288: 15212-28. PMID 23543749 DOI: 10.1074/Jbc.M113.457804 |
0.338 |
|
| 2013 |
Hough L, Dutta K, Kamal A, Temel D, Sparks S, Tetenbaum-Novatt J, Cowburn D, Cowburn D, Rout M. The Behavior of the Intrinsically Disordered FG Nups Determined by in Cell NMR Biophysical Journal. 104: 120a. DOI: 10.1016/J.Bpj.2012.11.692 |
0.596 |
|
| 2012 |
Ferrage F, Dutta K, Nistal-Villán E, Patel JR, Sánchez-Aparicio MT, De Ioannes P, Buku A, Aseguinolaza GG, García-Sastre A, Aggarwal AK. Structure and dynamics of the second CARD of human RIG-I provide mechanistic insights into regulation of RIG-I activation. Structure (London, England : 1993). 20: 2048-61. PMID 23063562 DOI: 10.1016/J.Str.2012.09.003 |
0.374 |
|
| 2012 |
Kalinina J, Dutta K, Ilghari D, Beenken A, Goetz R, Eliseenkova AV, Cowburn D, Mohammadi M. The alternatively spliced acid box region plays a key role in FGF receptor autoinhibition. Structure (London, England : 1993). 20: 77-88. PMID 22244757 DOI: 10.1016/J.Str.2011.10.022 |
0.563 |
|
| 2011 |
Ndao M, Dutta K, Bromley KM, Lakshminarayanan R, Sun Z, Rewari G, Moradian-Oldak J, Evans JS. Probing the self-association, intermolecular contacts, and folding propensity of amelogenin. Protein Science : a Publication of the Protein Society. 20: 724-34. PMID 21351181 DOI: 10.1002/Pro.603 |
0.373 |
|
| 2011 |
Dutta K, Natarajan A, Nair PA, Shuman S, Ghose R. Sequence-specific 1H, 13C and 15N assignments of the phosphoesterase (PE) domain of Pseudomonas aeruginosa DNA ligase D (LigD). Biomolecular Nmr Assignments. 5: 151-5. PMID 21213076 DOI: 10.1007/S12104-010-9289-7 |
0.305 |
|
| 2011 |
Hough L, Dutta K, Tetenbaum-Novatt J, Cowburn D, Rout M. The Solution and Binding Behavior of the Intrinsically Disordered FG Nups Determined by STINT-NMR Biophysical Journal. 100: 185a. DOI: 10.1016/J.Bpj.2010.12.1229 |
0.608 |
|
| 2010 |
Tait S, Dutta K, Cowburn D, Warwicker J, Doig AJ, McCarthy JE. Local control of a disorder-order transition in 4E-BP1 underpins regulation of translation via eIF4E. Proceedings of the National Academy of Sciences of the United States of America. 107: 17627-32. PMID 20880835 DOI: 10.1073/Pnas.1008242107 |
0.573 |
|
| 2010 |
Schwalbe M, Dutta K, Libich DS, Venugopal H, Claridge JK, Gell DA, Mackay JP, Edwards PJ, Pascal SM. Two-state conformational equilibrium in the Par-4 leucine zipper domain. Proteins. 78: 2433-49. PMID 20602362 DOI: 10.1002/Prot.22752 |
0.421 |
|
| 2010 |
Ferrage F, Dutta K, Shekhtman A, Cowburn D. Structural determination of biomolecular interfaces by nuclear magnetic resonance of proteins with reduced proton density. Journal of Biomolecular Nmr. 47: 41-54. PMID 20372977 DOI: 10.1007/S10858-010-9409-9 |
0.585 |
|
| 2009 |
Libich DS, Schwalbe M, Kate S, Venugopal H, Claridge JK, Edwards PJ, Dutta K, Pascal SM. Intrinsic disorder and coiled-coil formation in prostate apoptosis response factor 4. The Febs Journal. 276: 3710-28. PMID 19490121 DOI: 10.1111/J.1742-4658.2009.07087.X |
0.407 |
|
| 2008 |
Schwartz EC, Shekhtman A, Dutta K, Pratt MR, Cowburn D, Darst S, Muir TW. A full-length group 1 bacterial sigma factor adopts a compact structure incompatible with DNA binding. Chemistry & Biology. 15: 1091-103. PMID 18940669 DOI: 10.1016/J.Chembiol.2008.09.008 |
0.541 |
|
| 2008 |
Eryilmaz E, Benach J, Su M, Seetharaman J, Dutta K, Wei H, Gottlieb P, Hunt JF, Ghose R. Structure and dynamics of the P7 protein from the bacteriophage phi 12. Journal of Molecular Biology. 382: 402-22. PMID 18647606 DOI: 10.1016/J.Jmb.2008.07.006 |
0.401 |
|
| 2008 |
Dutta K, Cox CJ, Basavappa R, Pascal SM. 15N relaxation studies of Apo-Mts1: A dynamic S100 protein Biochemistry. 47: 7637-7647. PMID 18627127 DOI: 10.1021/Bi8005048 |
0.393 |
|
| 2008 |
Liu D, Xu R, Dutta K, Cowburn D. N-terminal cysteinyl proteins can be prepared using thrombin cleavage. Febs Letters. 582: 1163-7. PMID 18331839 DOI: 10.1016/J.Febslet.2008.02.078 |
0.558 |
|
| 2007 |
Headey SJ, Huang H, Claridge JK, Soares GA, Dutta K, Schwalbe M, Yang D, Pascal SM. NMR structure of stem-loop D from human rhinovirus-14 Rna. 13: 351-360. PMID 17194719 DOI: 10.1261/Rna.313707 |
0.373 |
|
| 2007 |
Del Rio A, Dutta K, Chavez J, Ubarretxena-Belandia I, Ghose R. Solution structure and dynamics of the N-terminal cytosolic domain of rhomboid intramembrane protease from Pseudomonas aeruginosa: insights into a functional role in intramembrane proteolysis. Journal of Molecular Biology. 365: 109-22. PMID 17059825 DOI: 10.1016/J.Jmb.2006.09.047 |
0.34 |
|
| 2006 |
Burz DS, Dutta K, Cowburn D, Shekhtman A. In-cell NMR for protein-protein interactions (STINT-NMR). Nature Protocols. 1: 146-52. PMID 17406226 DOI: 10.1038/Nprot.2006.23 |
0.602 |
|
| 2006 |
Muralidharan V, Dutta K, Cho J, Vila-Perello M, Raleigh DP, Cowburn D, Muir TW. Solution structure and folding characteristics of the C-terminal SH3 domain of c-Crk-II. Biochemistry. 45: 8874-84. PMID 16846230 DOI: 10.1021/Bi060590Z |
0.57 |
|
| 2006 |
Mukherjee M, Dutta K, White MA, Cowburn D, Fox RO. NMR solution structure and backbone dynamics of domain III of the E protein of tick-borne Langat flavivirus suggests a potential site for molecular recognition. Protein Science : a Publication of the Protein Society. 15: 1342-55. PMID 16731969 DOI: 10.1110/Ps.051844006 |
0.555 |
|
| 2006 |
Burz DS, Dutta K, Cowburn D, Shekhtman A. Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR). Nature Methods. 3: 91-3. PMID 16432517 DOI: 10.1038/Nmeth851 |
0.594 |
|
| 2004 |
Dutta K, Shi H, Cruz-Chu ER, Kami K, Ghose R. Dynamic influences on a high-affinity, high-specificity interaction involving the C-terminal SH3 domain of p67phox. Biochemistry. 43: 8094-106. PMID 15209505 DOI: 10.1021/Bi030268D |
0.387 |
|
| 2003 |
Dutta K, Engler FA, Cotton L, Alexandrov A, Bedi GS, Colquhoun J, Pascal SM. Stabilization of a pH-sensitive apoptosis-linked coiled coil through single point mutations. Protein Science : a Publication of the Protein Society. 12: 257-65. PMID 12538889 DOI: 10.1110/Ps.0223903 |
0.328 |
|
| 2002 |
Cox CJ, Dutta K, Petri ET, Hwang WC, Lin Y, Pascal SM, Basavappa R. The regions of securin and cyclin B proteins recognized by the ubiquitination machinery are natively unfolded. Febs Letters. 527: 303-8. PMID 12220679 DOI: 10.1016/S0014-5793(02)03246-5 |
0.367 |
|
| 2002 |
Dutta K, Cox CJ, Huang H, Basavappa R, Pascal SM. Calcium coordination studies of the metastatic Mts1 protein. Biochemistry. 41: 4239-45. PMID 11914069 DOI: 10.1021/Bi012061V |
0.303 |
|
| 2001 |
Dutta K, Alexandrov A, Huang H, Pascal SM. pH-induced folding of an apoptotic coiled coil. Protein Science : a Publication of the Protein Society. 10: 2531-40. PMID 11714921 DOI: 10.1110/Ps.28801 |
0.34 |
|
| 2001 |
Alexandrov A, Dutta K, Pascal SM. MBP fusion protein with a viral protease cleavage site: one-step cleavage/purification of insoluble proteins. Biotechniques. 30: 1194-8. PMID 11414203 DOI: 10.2144/01306Bm01 |
0.312 |
|
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