| Year |
Citation |
Score |
| 2024 |
Stadnicki EJ, Ludewig H, Kumar RP, Wang X, Qiao Y, Kern D, Bradshaw N. Dual-Action Kinase Inhibitors Influence p38α MAP Kinase Dephosphorylation. Biorxiv : the Preprint Server For Biology. PMID 39149408 DOI: 10.1101/2024.05.15.594272 |
0.336 |
|
| 2022 |
Stiller JB, Otten R, Häussinger D, Rieder PS, Theobald DL, Kern D. Structure determination of high-energy states in a dynamic protein ensemble. Nature. 603: 528-535. PMID 35236984 DOI: 10.1038/s41586-022-04468-9 |
0.723 |
|
| 2020 |
Otten R, Pádua RAP, Bunzel HA, Nguyen V, Pitsawong W, Patterson M, Sui S, Perry SL, Cohen AE, Hilvert D, Kern D. How directed evolution reshapes the energy landscape in an enzyme to boost catalysis. Science (New York, N.Y.). PMID 33214289 DOI: 10.1126/science.abd3623 |
0.351 |
|
| 2020 |
Hoemberger M, Pitsawong W, Kern D. Cumulative mechanism of several major imatinib-resistant mutations in Abl kinase. Proceedings of the National Academy of Sciences of the United States of America. PMID 32719139 DOI: 10.1073/Pnas.1919221117 |
0.308 |
|
| 2020 |
Hadzipasic A, Wilson C, Nguyen V, Kern N, Kim C, Pitsawong W, Villali J, Zheng Y, Kern D. Ancient origins of allosteric activation in a Ser-Thr kinase. Science (New York, N.Y.). 367: 912-917. PMID 32079772 DOI: 10.1126/Science.Aay9959 |
0.419 |
|
| 2019 |
Stiller JB, Kerns SJ, Hoemberger M, Cho YJ, Otten R, Hagan MF, Kern D. Probing the Transition State in Enzyme Catalysis by High-Pressure NMR Dynamics. Nature Catalysis. 2: 726-734. PMID 32159076 DOI: 10.1038/s41929-019-0307-6 |
0.733 |
|
| 2019 |
Zorba A, Nguyen V, Koide A, Hoemberger M, Zheng Y, Kutter S, Kim C, Koide S, Kern D. Allosteric modulation of a human protein kinase with monobodies. Proceedings of the National Academy of Sciences of the United States of America. PMID 31239342 DOI: 10.1073/Pnas.1906024116 |
0.389 |
|
| 2018 |
Pádua RAP, Sun Y, Marko I, Pitsawong W, Stiller JB, Otten R, Kern D. Mechanism of activating mutations and allosteric drug inhibition of the phosphatase SHP2. Nature Communications. 9: 4507. PMID 30375376 DOI: 10.1038/S41467-018-06814-W |
0.41 |
|
| 2018 |
Pitsawong W, Buosi V, Otten R, Agafonov RV, Zorba A, Kern N, Kutter S, Kern G, Pádua RA, Meniche X, Kern D. Dynamics of human protein kinase Aurora A linked to drug selectivity. Elife. 7. PMID 29901437 DOI: 10.7554/Elife.36656 |
0.392 |
|
| 2018 |
Otten R, Liu L, Kenner LR, Clarkson MW, Mavor D, Tawfik DS, Kern D, Fraser JS. Rescue of conformational dynamics in enzyme catalysis by directed evolution. Nature Communications. 9: 1314. PMID 29615624 DOI: 10.1038/S41467-018-03562-9 |
0.467 |
|
| 2018 |
Pitsawong W, Buosi V, Otten R, Agafonov RV, Zorba A, Kern N, Kutter S, Kern G, Pádua RA, Meniche X, Kern D. Author response: Dynamics of human protein kinase Aurora A linked to drug selectivity Elife. DOI: 10.7554/Elife.36656.040 |
0.351 |
|
| 2017 |
Salafsky J, Agafonov R, Donohue Vo E, Connell K, Mercado G, George T, McCormick F, Kern D. Second Harmonic Generation as a Method to Identify and Screen for Allosteric Modulators of Protein Targets Biophysical Journal. 112: 201a. DOI: 10.1016/J.Bpj.2016.11.1113 |
0.373 |
|
| 2016 |
Nguyen V, Wilson C, Hoemberger M, Stiller JB, Agafonov RV, Kutter S, English J, Theobald DL, Kern D. Evolutionary drivers of thermoadaptation in enzyme catalysis. Science (New York, N.Y.). PMID 28008087 DOI: 10.1126/Science.Aah3717 |
0.73 |
|
| 2016 |
Eichner T, Kutter S, Labeikovsky W, Buosi V, Kern D. Molecular mechanism of Pin1-tau recognition and catalysis. Journal of Molecular Biology. PMID 26996941 DOI: 10.1016/J.Jmb.2016.03.009 |
0.789 |
|
| 2016 |
Kutter S, Eichner T, Deaconescu AM, Kern D. Regulation of microtubule assembly by tau and not by Pin1. Journal of Molecular Biology. PMID 26996940 DOI: 10.1016/J.Jmb.2016.03.010 |
0.324 |
|
| 2015 |
Chakrabarti KS, Agafonov RV, Pontiggia F, Otten R, Higgins MK, Schertler GF, Oprian DD, Kern D. Conformational Selection in a Protein-Protein Interaction Revealed by Dynamic Pathway Analysis. Cell Reports. PMID 26725117 DOI: 10.1016/J.Celrep.2015.12.010 |
0.439 |
|
| 2015 |
Pontiggia F, Pachov DV, Clarkson MW, Villali J, Hagan MF, Pande VS, Kern D. Free energy landscape of activation in a signalling protein at atomic resolution. Nature Communications. 6: 7284. PMID 26073309 DOI: 10.1038/Ncomms8284 |
0.818 |
|
| 2015 |
Wilson C, Agafonov RV, Hoemberger M, Kutter S, Zorba A, Halpin J, Buosi V, Otten R, Waterman D, Theobald DL, Kern D. Kinase dynamics. Using ancient protein kinases to unravel a modern cancer drug's mechanism. Science (New York, N.Y.). 347: 882-6. PMID 25700521 DOI: 10.1126/Science.Aaa1823 |
0.731 |
|
| 2015 |
Kerns SJ, Agafonov RV, Cho YJ, Pontiggia F, Otten R, Pachov DV, Kutter S, Phung LA, Murphy PN, Thai V, Alber T, Hagan MF, Kern D. The energy landscape of adenylate kinase during catalysis. Nature Structural & Molecular Biology. 22: 124-31. PMID 25580578 DOI: 10.1038/Nsmb.2941 |
0.78 |
|
| 2015 |
Hass MA, Liu WM, Agafonov RV, Otten R, Phung LA, Schilder JT, Kern D, Ubbink M. A minor conformation of a lanthanide tag on adenylate kinase characterized by paramagnetic relaxation dispersion NMR spectroscopy. Journal of Biomolecular Nmr. 61: 123-36. PMID 25563704 DOI: 10.1007/S10858-014-9894-3 |
0.482 |
|
| 2015 |
Pontiggia F, Pachov DV, Clarkson MW, Villali J, Hagan MF, Pande VS, Kern D. Free energy landscape of activation in a signalling protein at atomic resolution Nature Communications. 6. DOI: 10.1038/ncomms8284 |
0.783 |
|
| 2015 |
Agafonov RV, Wilson C, Buosi V, Otten R, Kern D. Kinase Structural Dynamics Enables Tight and Selective Binding of Inhibitors Biophysical Journal. 108: 55a. DOI: 10.1016/J.Bpj.2014.11.336 |
0.374 |
|
| 2015 |
Agafonov R, Wilson C, Biswas S, Kern D. Regulation of Kinases: 1 Billion Years of Evolution Biophysical Journal. 108: 381a. DOI: 10.1016/J.Bpj.2014.11.2088 |
0.368 |
|
| 2015 |
Pontiggia F, Pachov DV, Clarkson MW, Villali J, Hagan MF, Pande VS, Kern D. Activation Mechanism of a Signaling Protein at Atomic Resolution Biophysical Journal. 108: 376a. DOI: 10.1016/J.Bpj.2014.11.2064 |
0.815 |
|
| 2014 |
Agafonov RV, Wilson C, Otten R, Buosi V, Kern D. Energetic dissection of Gleevec's selectivity toward human tyrosine kinases. Nature Structural & Molecular Biology. 21: 848-53. PMID 25218445 DOI: 10.1038/Nsmb.2891 |
0.385 |
|
| 2014 |
Zorba A, Buosi V, Kutter S, Kern N, Pontiggia F, Cho YJ, Kern D. Molecular mechanism of Aurora A kinase autophosphorylation and its allosteric activation by TPX2. Elife. 3: e02667. PMID 24867643 DOI: 10.7554/Elife.02667 |
0.444 |
|
| 2014 |
Villali J, Pontiggia F, Clarkson MW, Hagan MF, Kern D. Evidence against the "Y-T coupling" mechanism of activation in the response regulator NtrC. Journal of Molecular Biology. 426: 1554-67. PMID 24406745 DOI: 10.1016/J.Jmb.2013.12.027 |
0.461 |
|
| 2014 |
Zorba A, Buosi V, Kutter S, Kern N, Pontiggia F, Cho Y, Kern D. Author response: Molecular mechanism of Aurora A kinase autophosphorylation and its allosteric activation by TPX2 Elife. DOI: 10.7554/Elife.02667.022 |
0.36 |
|
| 2014 |
Hoemberger MS, Wilson CG, Kern D. Probing an Ancient Protein's Dynamics with NMR Biophysical Journal. 106: 657a. DOI: 10.1016/J.Bpj.2013.11.3637 |
0.429 |
|
| 2014 |
Agafonov RV, Wilson C, Otten R, Buosi V, Kern D. Molecular Mechanisms Underlying the Clinical Success of the Cancer Drug Gleevec Biophysical Journal. 106: 647a. DOI: 10.1016/J.Bpj.2013.11.3580 |
0.365 |
|
| 2013 |
Ranaghan MJ, Kumar RP, Chakrabarti KS, Buosi V, Kern D, Oprian DD. A highly conserved cysteine of neuronal calcium-sensing proteins controls cooperative binding of Ca2+ to recoverin. The Journal of Biological Chemistry. 288: 36160-7. PMID 24189072 DOI: 10.1074/Jbc.M113.524355 |
0.322 |
|
| 2013 |
Park JM, Hu JH, Milshteyn A, Zhang PW, Moore CG, Park S, Datko MC, Domingo RD, Reyes CM, Wang XJ, Etzkorn FA, Xiao B, Szumlinski KK, Kern D, Linden DJ, et al. A prolyl-isomerase mediates dopamine-dependent plasticity and cocaine motor sensitization. Cell. 154: 637-50. PMID 23911326 DOI: 10.1016/J.Cell.2013.07.001 |
0.722 |
|
| 2013 |
Kern D. Proteins in Flagrante: Excursions in Silico and in Proteo Biophysical Journal. 104: 375a-376a. DOI: 10.1016/J.Bpj.2012.11.2088 |
0.509 |
|
| 2012 |
Morrison EA, DeKoster GT, Dutta S, Vafabakhsh R, Clarkson MW, Bahl A, Kern D, Ha T, Henzler-Wildman KA. Antiparallel EmrE exports drugs by exchanging between asymmetric structures. Nature. 481: 45-50. PMID 22178925 DOI: 10.1038/Nature10703 |
0.801 |
|
| 2012 |
Morrison E, Dekoster G, Dutta S, Clarkson M, Vafabakhsh R, Kern D, Ha T, Henzler-Wildman K. Direct Observation of Conformational Exchange in the Small Multidrug Resistance Transporter EmrE Biophysical Journal. 102: 215a. DOI: 10.1016/J.Bpj.2011.11.1179 |
0.658 |
|
| 2011 |
Agafonov R, Kerns J, Phung L, Kern D. Energy Landscape of Adenylate Kinase: Phosphoryl Transfer and Conformational Transitions Biophysical Journal. 100: 17a-18a. DOI: 10.1016/J.Bpj.2010.12.306 |
0.513 |
|
| 2011 |
Cho Y, Kern D. Visualizing Adenylate Kinase Catalysis Through the X-ray Lens Biophysical Journal. 100. DOI: 10.1016/J.Bpj.2010.12.1453 |
0.447 |
|
| 2010 |
Otten R, Villali J, Kern D, Mulder FA. Probing microsecond time scale dynamics in proteins by methyl (1)H Carr-Purcell-Meiboom-Gill relaxation dispersion NMR measurements. Application to activation of the signaling protein NtrC(r). Journal of the American Chemical Society. 132: 17004-14. PMID 21058670 DOI: 10.1021/Ja107410X |
0.406 |
|
| 2010 |
Villali J, Kern D. Choreographing an enzyme's dance. Current Opinion in Chemical Biology. 14: 636-43. PMID 20822946 DOI: 10.1016/J.Cbpa.2010.08.007 |
0.459 |
|
| 2010 |
Bosco DA, Eisenmesser EZ, Clarkson MW, Wolf-Watz M, Labeikovsky W, Millet O, Kern D. Dissecting the microscopic steps of the cyclophilin A enzymatic cycle on the biological HIV-1 capsid substrate by NMR. Journal of Molecular Biology. 403: 723-38. PMID 20708627 DOI: 10.1016/J.Jmb.2010.08.001 |
0.798 |
|
| 2009 |
Gardino AK, Villali J, Kivenson A, Lei M, Liu CF, Steindel P, Eisenmesser EZ, Labeikovsky W, Wolf-Watz M, Clarkson MW, Kern D. Transient non-native hydrogen bonds promote activation of a signaling protein. Cell. 139: 1109-18. PMID 20005804 DOI: 10.1016/J.Cell.2009.11.022 |
0.819 |
|
| 2009 |
Fraser JS, Clarkson MW, Degnan SC, Erion R, Kern D, Alber T. Hidden alternative structures of proline isomerase essential for catalysis Nature. 462: 669-673. PMID 19956261 DOI: 10.1038/Nature08615 |
0.486 |
|
| 2009 |
Shim S, Yuan JP, Kim JY, Zeng W, Huang G, Milshteyn A, Kern D, Muallem S, Ming GL, Worley PF. Peptidyl-prolyl isomerase FKBP52 controls chemotropic guidance of neuronal growth cones via regulation of TRPC1 channel opening. Neuron. 64: 471-83. PMID 19945390 DOI: 10.1016/J.Neuron.2009.09.025 |
0.733 |
|
| 2009 |
Clarkson MW, Lei M, Eisenmesser EZ, Labeikovsky W, Redfield A, Kern D. Mesodynamics in the SARS nucleocapsid measured by NMR field cycling. Journal of Biomolecular Nmr. 45: 217-25. PMID 19641854 DOI: 10.1007/S10858-009-9347-6 |
0.776 |
|
| 2009 |
Lei M, Velos J, Gardino A, Kivenson A, Karplus M, Kern D. Segmented transition pathway of the signaling protein nitrogen regulatory protein C. Journal of Molecular Biology. 392: 823-36. PMID 19576227 DOI: 10.1016/J.Jmb.2009.06.065 |
0.805 |
|
| 2009 |
Clarkson MW, Fraser J, Alber T, Kern D. Cyclophilin Dynamics and Catalysis are Mechanistically Linked Biophysical Journal. 96: 555a. DOI: 10.1016/J.Bpj.2008.12.3644 |
0.434 |
|
| 2009 |
Lei M, Velos J, Gardino A, Karplus M, Kern D. Segmented Transition Pathway Of The Receiver Domain Of Nitrogen Regulatory Protein C Biophysical Journal. 96: 586a. DOI: 10.1016/J.Bpj.2008.12.3069 |
0.781 |
|
| 2009 |
Velos J, Lei M, Liu CF, Steindel P, Kern D. Experimental Confirmation of an NtrC Transition Pathway Predicted by Targeted MD Biophysical Journal. 96: 377a. DOI: 10.1016/J.Bpj.2008.12.2831 |
0.805 |
|
| 2009 |
Pachov D, Kerns SJ, Kern D. Conformational pathways of Adenylate Kinase characterized by computations, pressure and experiments Biophysical Journal. 96: 321a-322a. DOI: 10.1016/J.Bpj.2008.12.1613 |
0.814 |
|
| 2008 |
Thai V, Renesto P, Fowler CA, Brown DJ, Davis T, Gu W, Pollock DD, Kern D, Raoult D, Eisenmesser EZ. Structural, biochemical, and in vivo characterization of the first virally encoded cyclophilin from the Mimivirus. Journal of Molecular Biology. 378: 71-86. PMID 18342330 DOI: 10.1016/J.Jmb.2007.08.051 |
0.751 |
|
| 2007 |
Henzler-Wildman K, Kern D. Dynamic personalities of proteins Nature. 450: 964-972. PMID 18075575 DOI: 10.1038/Nature06522 |
0.698 |
|
| 2007 |
Henzler-Wildman KA, Lei M, Thai V, Kerns SJ, Karplus M, Kern D. A hierarchy of timescales in protein dynamics is linked to enzyme catalysis. Nature. 450: 913-6. PMID 18026087 DOI: 10.1038/Nature06407 |
0.804 |
|
| 2007 |
Henzler-Wildman KA, Thai V, Lei M, Ott M, Wolf-Watz M, Fenn T, Pozharski E, Wilson MA, Petsko GA, Karplus M, Hübner CG, Kern D. Intrinsic motions along an enzymatic reaction trajectory. Nature. 450: 838-44. PMID 18026086 DOI: 10.1038/Nature06410 |
0.811 |
|
| 2007 |
Gardino AK, Kern D. Functional dynamics of response regulators using NMR relaxation techniques. Methods in Enzymology. 423: 149-65. PMID 17609130 DOI: 10.1016/S0076-6879(07)23006-X |
0.803 |
|
| 2007 |
Labeikovsky W, Eisenmesser EZ, Bosco DA, Kern D. Structure and dynamics of pin1 during catalysis by NMR. Journal of Molecular Biology. 367: 1370-81. PMID 17316687 DOI: 10.1016/J.Jmb.2007.01.049 |
0.818 |
|
| 2005 |
Wemmer DE, Kern D. Beryllofluoride binding mimics phosphorylation of aspartate in response regulators. Journal of Bacteriology. 187: 8229-30. PMID 16321925 DOI: 10.1128/Jb.187.24.8229-8230.2005 |
0.635 |
|
| 2005 |
Wemmer DE, Kern D. Rebuttal: conformational changes of Spo0F along the phosphotransfer pathway. Journal of Bacteriology. 187: 8228. PMID 16321924 DOI: 10.1128/Jb.187.24.8228.2005 |
0.622 |
|
| 2005 |
Eisenmesser EZ, Millet O, Labeikovsky W, Korzhnev DM, Wolf-Watz M, Bosco DA, Skalicky JJ, Kay LE, Kern D. Intrinsic dynamics of an enzyme underlies catalysis. Nature. 438: 117-21. PMID 16267559 DOI: 10.1038/Nature04105 |
0.814 |
|
| 2005 |
Tittmann K, Neef H, Golbik R, Hübner G, Kern D. Kinetic control of thiamin diphosphate activation in enzymes studied by proton-nitrogen correlated NMR spectroscopy. Biochemistry. 44: 8697-700. PMID 15952776 DOI: 10.1021/Bi050522X |
0.392 |
|
| 2005 |
Kern D, Eisenmesser EZ, Wolf-Watz M. Enzyme dynamics during catalysis measured by NMR spectroscopy. Methods in Enzymology. 394: 507-24. PMID 15808235 DOI: 10.1016/S0076-6879(05)94021-4 |
0.437 |
|
| 2004 |
Wolf-Watz M, Thai V, Henzler-Wildman K, Hadjipavlou G, Eisenmesser EZ, Kern D. Linkage between dynamics and catalysis in a thermophilic-mesophilic enzyme pair Nature Structural and Molecular Biology. 11: 945-949. PMID 15334070 DOI: 10.1038/Nsmb821 |
0.813 |
|
| 2004 |
Bosco DA, Kern D. Catalysis and binding of cyclophilin A with different HIV-1 capsid constructs. Biochemistry. 43: 6110-9. PMID 15147195 DOI: 10.1021/Bi049841Z |
0.67 |
|
| 2003 |
Kern D, Zuiderweg ER. The role of dynamics in allosteric regulation. Current Opinion in Structural Biology. 13: 748-57. PMID 14675554 DOI: 10.1016/J.Sbi.2003.10.008 |
0.411 |
|
| 2003 |
Gardino AK, Volkman BF, Cho HS, Lee SY, Wemmer DE, Kern D. The NMR solution structure of BeF(3)(-)-activated Spo0F reveals the conformational switch in a phosphorelay system. Journal of Molecular Biology. 331: 245-54. PMID 12875849 DOI: 10.1016/S0022-2836(03)00733-2 |
0.808 |
|
| 2002 |
Kern G, Pelton J, Marqusee S, Kern D. Structural properties of the histidine-containing loop in HIV-1 RNase H. Biophysical Chemistry. 96: 285-91. PMID 12034447 DOI: 10.1016/S0301-4622(02)00019-4 |
0.36 |
|
| 2002 |
Bosco DA, Eisenmesser EZ, Pochapsky S, Sundquist WI, Kern D. Catalysis of cis/trans isomerization in native HIV-1 capsid by human cyclophilin A. Proceedings of the National Academy of Sciences of the United States of America. 99: 5247-52. PMID 11929983 DOI: 10.1073/Pnas.082100499 |
0.668 |
|
| 2002 |
Eisenmesser EZ, Bosco DA, Akke M, Kern D. Enzyme dynamics during catalysis. Science (New York, N.Y.). 295: 1520-3. PMID 11859194 DOI: 10.1126/Science.1066176 |
0.735 |
|
| 2001 |
Volkman BF, Lipson D, Wemmer DE, Kern D. Two-state allosteric behavior in a single-domain signaling protein. Science (New York, N.Y.). 291: 2429-33. PMID 11264542 DOI: 10.1126/Science.291.5512.2429 |
0.744 |
|
| 1999 |
Kern D, Volkman BF, Luginbühl P, Nohaile MJ, Kustu S, Wemmer DE. Structure of a transiently phosphorylated switch in bacterial signal transduction. Nature. 402: 894-8. PMID 10622255 DOI: 10.1038/47273 |
0.714 |
|
| 1998 |
Hübner G, Tittmann K, Killenberg-Jabs M, Schäffner J, Spinka M, Neef H, Kern D, Kern G, Schneider G, Wikner C, Ghisla S. Activation of thiamin diphosphate in enzymes Biochimica Et Biophysica Acta - Protein Structure and Molecular Enzymology. 1385: 221-228. PMID 9655909 DOI: 10.1016/S0167-4838(98)00070-3 |
0.386 |
|
| 1997 |
Nohaile M, Kern D, Wemmer D, Stedman K, Kustu S. Structural and functional analyses of activating amino acid substitutions in the receiver domain of NtrC: Evidence for an activating surface Journal of Molecular Biology. 273: 299-316. PMID 9367763 DOI: 10.1006/Jmbi.1997.1296 |
0.538 |
|
| 1995 |
Kern G, Kern D, Schmid FX, Fischer G. A kinetic analysis of the folding of human carbonic anhydrase II and its catalysis by cyclophilin Journal of Biological Chemistry. 270: 740-745. PMID 7822304 DOI: 10.1074/Jbc.270.2.740 |
0.546 |
|
| 1995 |
Kern D, Kern G, Scherer G, Fischer G, Drakenberg T. Kinetic analysis of cyclophilin-catalyzed prolyl cis/trans isomerization by dynamic NMR spectroscopy Biochemistry. 34: 13594-13602. PMID 7577948 DOI: 10.1021/Bi00041A039 |
0.531 |
|
| 1994 |
Kern G, Kern D, Schmid FX, Fischer G. Reassessment of the putative chaperone function of prolyl-cis/trans-isomerases Febs Letters. 348: 145-148. PMID 7913447 DOI: 10.1016/0014-5793(94)00591-5 |
0.533 |
|
| 1993 |
Kern D, Drakenberg T, Wikström M, Forsén S, Bang H, Fischer G. The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin Febs Letters. 323: 198-202. PMID 8500610 DOI: 10.1016/0014-5793(93)81338-Z |
0.461 |
|
| 1993 |
Kern G, Kern D, Jaenicke R, Seckler R. Kinetics of folding and association of differently glycosylated variants of invertase from Saccharomyces cerevisiae Protein Science. 2: 1862-1868. PMID 8268797 DOI: 10.1002/Pro.5560021108 |
0.381 |
|
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