Year |
Citation |
Score |
2024 |
Sammons RM, Devkota AK, Kaoud TS, Warthaka M, Cho EJ, Dalby KN. Steady State and Time-Dependent Fluorescent Peptide Assays for Protein Kinases. Current Protocols. 4: e998. PMID 38439594 DOI: 10.1002/cpz1.998 |
0.834 |
|
2019 |
Kaoud TS, Johnson WH, Ebelt ND, Piserchio A, Zamora-Olivares D, Van Ravenstein SX, Pridgen JR, Edupuganti R, Sammons R, Cano M, Warthaka M, Harger M, Tavares CDJ, Park J, Radwan MF, et al. Modulating multi-functional ERK complexes by covalent targeting of a recruitment site in vivo. Nature Communications. 10: 5232. PMID 31745079 DOI: 10.1038/S41467-019-12996-8 |
0.76 |
|
2019 |
Kaoud TS, Johnson WH, Ebelt ND, Piserchio A, Zamora-Olivares D, Ravenstein SV, Pridgen JR, Edupuganti R, Sammons R, Cano M, Warthaka M, Ren P, Anslyn EV, Tsai KY, Ghose R, et al. Abstract 3872: Targeting multi-functional ERK-protein complexesin vivo Cancer Research. 79: 3872-3872. DOI: 10.1158/1538-7445.Am2019-3872 |
0.822 |
|
2017 |
Piserchio A, Warthaka M, Kaoud TS, Callaway K, Dalby KN, Ghose R. Local destabilization, rigid body, and fuzzy docking facilitate the phosphorylation of the transcription factor Ets-1 by the mitogen-activated protein kinase ERK2. Proceedings of the National Academy of Sciences of the United States of America. PMID 28716922 DOI: 10.1073/Pnas.1702973114 |
0.824 |
|
2016 |
Kaoud TS, Johnson WH, Ebelt ND, Piserchio A, Warthaka M, Cano M, Sammons R, Wang Q, Ren P, Ghose R, Dalby KN. Abstract 3771: Discovery of a covalent inhibitor of ERK docking-interactions that inhibits A375 melanoma cells proliferation Cancer Research. 76: 3771-3771. DOI: 10.1158/1538-7445.Am2016-3771 |
0.817 |
|
2015 |
Warthaka M, Adelmann CH, Kaoud TS, Edupuganti R, Yan C, Johnson WH, Ferguson S, Tavares CD, Pence LJ, Anslyn EV, Ren P, Tsai KY, Dalby KN. Quantification of a Pharmacodynamic ERK End Point in Melanoma Cell Lysates: Toward Personalized Precision Medicine. Acs Medicinal Chemistry Letters. 6: 47-52. PMID 25589929 DOI: 10.1021/Ml500198B |
0.779 |
|
2014 |
Tavares CD, Ferguson SB, Giles DH, Wang Q, Wellmann RM, O'Brien JP, Warthaka M, Brodbelt JS, Ren P, Dalby KN. The molecular mechanism of eukaryotic elongation factor 2 kinase activation. The Journal of Biological Chemistry. 289: 23901-16. PMID 25012662 DOI: 10.1074/Jbc.M114.577148 |
0.793 |
|
2014 |
Devkota AK, Warthaka M, Edupuganti R, Tavares CD, Johnson WH, Ozpolat B, Cho EJ, Dalby KN. High-throughput screens for eEF-2 kinase. Journal of Biomolecular Screening. 19: 445-52. PMID 24078616 DOI: 10.1177/1087057113505204 |
0.806 |
|
2012 |
Devkota AK, Tavares CD, Warthaka M, Abramczyk O, Marshall KD, Kaoud TS, Gorgulu K, Ozpolat B, Dalby KN. Investigating the kinetic mechanism of inhibition of elongation factor 2 kinase by NH125: evidence of a common in vitro artifact. Biochemistry. 51: 2100-12. PMID 22352903 DOI: 10.1021/Bi201787P |
0.79 |
|
2012 |
Tavares CD, O'Brien JP, Abramczyk O, Devkota AK, Shores KS, Ferguson SB, Kaoud TS, Warthaka M, Marshall KD, Keller KM, Zhang Y, Brodbelt JS, Ozpolat B, Dalby KN. Calcium/calmodulin stimulates the autophosphorylation of elongation factor 2 kinase on Thr-348 and Ser-500 to regulate its activity and calcium dependence. Biochemistry. 51: 2232-45. PMID 22329831 DOI: 10.1021/Bi201788E |
0.761 |
|
2011 |
Lee S, Warthaka M, Yan C, Kaoud TS, Ren P, Dalby KN. Examining docking interactions on ERK2 with modular peptide substrates. Biochemistry. 50: 9500-10. PMID 21955038 DOI: 10.1021/Bi201103B |
0.82 |
|
2011 |
Kaoud TS, Devkota AK, Harris R, Rana MS, Abramczyk O, Warthaka M, Lee S, Girvin ME, Riggs AF, Dalby KN. Activated ERK2 is a monomer in vitro with or without divalent cations and when complexed to the cytoplasmic scaffold PEA-15. Biochemistry. 50: 4568-78. PMID 21506533 DOI: 10.1021/Bi200202Y |
0.74 |
|
2011 |
Lee S, Warthaka M, Yan C, Kaoud TS, Piserchio A, Ghose R, Ren P, Dalby KN. A model of a MAPK•substrate complex in an active conformation: a computational and experimental approach. Plos One. 6: e18594. PMID 21494553 DOI: 10.1371/Journal.Pone.0018594 |
0.807 |
|
2011 |
Piserchio A, Warthaka M, Devkota AK, Kaoud TS, Lee S, Abramczyk O, Ren P, Dalby KN, Ghose R. Solution NMR insights into docking interactions involving inactive ERK2. Biochemistry. 50: 3660-72. PMID 21449613 DOI: 10.1021/Bi2000559 |
0.768 |
|
2010 |
Devkota AK, Kaoud TS, Warthaka M, Dalby KN. Fluorescent peptide assays for protein kinases. Current Protocols in Molecular Biology / Edited by Frederick M. Ausubel ... [Et Al.]. Unit 18.17. PMID 20583097 DOI: 10.1002/0471142727.Mb1817S91 |
0.828 |
|
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