Ranajeet Ghose to Phosphorylation
This is a "connection" page, showing publications Ranajeet Ghose has written about Phosphorylation.
Connection Strength
2.342
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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. Proc Natl Acad Sci U S A. 2017 08 01; 114(31):E6287-E6296.
Score: 0.479
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Piserchio A, Dalby KN, Ghose R. Revealing eEF-2 kinase: recent structural insights into function. Trends Biochem Sci. 2024 02; 49(2):169-182.
Score: 0.187
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Piserchio A, Isiorho EA, Dalby KN, Ghose R. Structure of the complex between calmodulin and a functional construct of eukaryotic elongation factor 2 kinase bound to an ATP-competitive inhibitor. J Biol Chem. 2023 06; 299(6):104813.
Score: 0.179
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Piserchio A, Long KJ, Browning LS, Bohanon AL, Isiorho EA, Dalby KN, Ghose R. ADP enhances the allosteric activation of eukaryotic elongation factor 2 kinase by?calmodulin. Proc Natl Acad Sci U S A. 2023 04 25; 120(17):e2300902120.
Score: 0.178
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Hajredini F, Alphonse S, Ghose R. BY-kinases: Protein tyrosine kinases like no other. J Biol Chem. 2023 01; 299(1):102737.
Score: 0.173
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Alphonse S, Djemil I, Piserchio A, Ghose R. Structural basis for the recognition of the bacterial tyrosine kinase Wzc by its cognate tyrosine phosphatase Wzb. Proc Natl Acad Sci U S A. 2022 06 28; 119(26):e2201800119.
Score: 0.168
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Piserchio A, Long K, Lee K, Kumar EA, Abzalimov R, Dalby KN, Ghose R. Structural dynamics of the complex of calmodulin with a minimal functional construct of eukaryotic elongation factor 2 kinase and the role of Thr348 autophosphorylation. Protein Sci. 2021 06; 30(6):1221-1234.
Score: 0.156
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Piserchio A, Will N, Giles DH, Hajredini F, Dalby KN, Ghose R. Solution Structure of the Carboxy-Terminal Tandem Repeat Domain of Eukaryotic Elongation Factor 2 Kinase and Its Role in Substrate Recognition. J Mol Biol. 2019 07 12; 431(15):2700-2717.
Score: 0.136
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Ghose R. Nature of the Pre-Chemistry Ensemble in Mitogen-Activated Protein Kinases. J Mol Biol. 2019 01 18; 431(2):145-157.
Score: 0.132
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Will N, Lee K, Hajredini F, Giles DH, Abzalimov RR, Clarkson M, Dalby KN, Ghose R. Structural Dynamics of the Activation of Elongation Factor 2 Kinase by Ca2+-Calmodulin. J Mol Biol. 2018 08 17; 430(17):2802-2821.
Score: 0.127
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Will N, Piserchio A, Snyder I, Ferguson SB, Giles DH, Dalby KN, Ghose R. Structure of the C-Terminal Helical Repeat Domain of Eukaryotic Elongation Factor 2 Kinase. Biochemistry. 2016 09 27; 55(38):5377-86.
Score: 0.113
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Lee K, Alphonse S, Piserchio A, Tavares CD, Giles DH, Wellmann RM, Dalby KN, Ghose R. Structural Basis for the Recognition of Eukaryotic Elongation Factor 2 Kinase by Calmodulin. Structure. 2016 09 06; 24(9):1441-51.
Score: 0.112
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Piserchio A, Ramakrishan V, Wang H, Kaoud TS, Arshava B, Dutta K, Dalby KN, Ghose R. Structural and Dynamic Features of F-recruitment Site Driven Substrate Phosphorylation by ERK2. Sci Rep. 2015 Jun 08; 5:11127.
Score: 0.103
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Sammons RM, Perry NA, Li Y, Cho EJ, Piserchio A, Zamora-Olivares DP, Ghose R, Kaoud TS, Debevec G, Bartholomeusz C, Gurevich VV, Iverson TM, Giulianotti M, Houghten RA, Dalby KN. A Novel Class of Common Docking Domain Inhibitors That Prevent ERK2 Activation and Substrate Phosphorylation. ACS Chem Biol. 2019 06 21; 14(6):1183-1194.
Score: 0.034
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Tavares CDJ, Giles DH, Stancu G, Chitjian CA, Ferguson SB, Wellmann RM, Kaoud TS, Ghose R, Dalby KN. Signal Integration at Elongation Factor 2 Kinase: THE ROLES OF CALCIUM, CALMODULIN, AND SER-500 PHOSPHORYLATION. J Biol Chem. 2017 02 03; 292(5):2032-2045.
Score: 0.029
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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. 2011 Apr 11; 6(4):e18594.
Score: 0.019
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Piserchio A, Ghose R, Cowburn D. Optimized bacterial expression and purification of the c-Src catalytic domain for solution NMR studies. J Biomol NMR. 2009 Jun; 44(2):87-93.
Score: 0.017