Citation: Mr. Langer et al., Mutational analysis of conserved residues in the GCN5 family of histone acetyltransferases, J BIOL CHEM, 276(33), 2001, pp. 31321-31331
Citation: M. Kumano et al., Calcium-mediated inactivation of the MAP kinase pathway in sea urchin eggsat fertilization, DEVELOP BIO, 236(1), 2001, pp. 244-257
Citation: Md. Jackson et Jm. Denu, Molecular reactions of protein phosphatases - Insights from structure and chemistry, CHEM REV, 101(8), 2001, pp. 2313-2340
Authors:
Rigas, JD
Hoff, RH
Rice, AE
Hengge, AC
Denu, JM
Citation: Jd. Rigas et al., Transition state analysis and requirement of Asp-262 general acid/base catalyst for full activation of dual-specificity phosphatase MKP3 by extracellular regulated kinase, BIOCHEM, 40(14), 2001, pp. 4398-4406
Authors:
Cheung, P
Tanner, KG
Cheung, WL
Sassone-Corsi, P
Denu, JM
Allis, CD
Citation: P. Cheung et al., Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation, MOL CELL, 5(6), 2000, pp. 905-915
Authors:
Tanner, KG
Landry, J
Sternglanz, R
Denu, JM
Citation: Kg. Tanner et al., Silent information regulator 2 family of NAD-dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose, P NAS US, 97(26), 2000, pp. 14178-14182
Authors:
Fjeld, CC
Rice, AE
Kim, Y
Gee, KR
Denu, JM
Citation: Cc. Fjeld et al., Mechanistic basis for catalytic activation of mitogen-activated protein kinase phosphatase 3 by extracellular signal-regulated kinase, J BIOL CHEM, 275(10), 2000, pp. 6749-6757
Citation: Kg. Tanner et al., Kinetic mechanism of human histone acetyltransferase P/CAF (vol 39, pg 11961, 2000), BIOCHEM, 39(50), 2000, pp. 15652-15652
Authors:
Tanner, KG
Trievel, RC
Kuo, MH
Howard, RM
Berger, SL
Allis, CD
Marmorstein, R
Denu, JM
Citation: Kg. Tanner et al., Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator, J BIOL CHEM, 274(26), 1999, pp. 18157-18160
Citation: Jl. Todd et al., Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR - A novel role indown-regulating the ERK pathway, J BIOL CHEM, 274(19), 1999, pp. 13271-13280