| Year |
Citation |
Score |
| 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 |
0.735 |
|
| 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 |
0.707 |
|
| 2012 |
Abramczyk O, Tavares CDJ, Devkota AK, Ryazanov AG, Turk BE, Riggs AF, Ozpolat B, Dalby KN. Corrigendum to "Purification and characterization of tagless recombinant human elongation factor 2 kinase (eEF-2K) expressed in Escherichia coli" [Protein Expression and Purification 79 (2011) 237-244] (DOI:10.1016/j.pep.2011.05.005) Protein Expression and Purification. DOI: 10.1016/J.Pep.2012.07.010 |
0.771 |
|
| 2011 |
McCaig C, Potter L, Abramczyk O, Murray JT. Phosphorylation of NDRG1 is temporally and spatially controlled during the cell cycle Biochemical and Biophysical Research Communications. 411: 227-234. PMID 21708134 DOI: 10.1016/J.Bbrc.2011.06.092 |
0.38 |
|
| 2011 |
Abramczyk O, Tavares CD, Devkota AK, Ryazanov AG, Turk BE, Riggs AF, Ozpolat B, Dalby KN. Purification and characterization of tagless recombinant human elongation factor 2 kinase (eEF-2K) expressed in Escherichia coli. Protein Expression and Purification. 79: 237-44. PMID 21605678 DOI: 10.1016/J.Pep.2011.05.005 |
0.802 |
|
| 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 |
0.696 |
|
| 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 |
0.714 |
|
| 2007 |
Callaway K, Abramczyk O, Martin L, Dalby KN. The anti-apoptotic protein PEA-15 is a tight binding inhibitor of ERK1 and ERK2, which blocks docking interactions at the D-recruitment site. Biochemistry. 46: 9187-98. PMID 17658892 DOI: 10.1021/Bi700206U |
0.823 |
|
| 2007 |
Abramczyk O, Rainey MA, Barnes R, Martin L, Dalby KN. Expanding the repertoire of an ERK2 recruitment site: cysteine footprinting identifies the D-recruitment site as a mediator of Ets-1 binding. Biochemistry. 46: 9174-86. PMID 17658891 DOI: 10.1021/Bi7002058 |
0.779 |
|
| 2006 |
Callaway KA, Rainey MA, Riggs AF, Abramczyk O, Dalby KN. Properties and regulation of a transiently assembled ERK2.Ets-1 signaling complex. Biochemistry. 45: 13719-33. PMID 17105191 DOI: 10.1021/Bi0610451 |
0.78 |
|
| 2003 |
Zień P, Abramczyk O, Domańska K, Bretner M, Szyszka R. TBBz but not TBBt discriminates between two molecular forms of CK2 in vivo and its implications. Biochemical and Biophysical Research Communications. 312: 623-8. PMID 14680810 DOI: 10.1016/j.bbrc.2003.10.165 |
0.454 |
|
| 2003 |
Abramczyk O, Zień P, Zieliński R, Pilecki M, Hellman U, Szyszka R. The protein kinase 60S is a free catalytic CK2alpha' subunit and forms an inactive complex with superoxide dismutase SOD1. Biochemical and Biophysical Research Communications. 307: 31-40. PMID 12849977 DOI: 10.1016/s0006-291x(03)01126-4 |
0.459 |
|
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