Primary Literature
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- Haile ST, et al. (2023) The SAGA HAT module is tethered by its SWIRM domain and modulates activity of the SAGA DUB module. Biochim Biophys Acta Gene Regul Mech 1866(2):194929 PMID: 36965704
- Culbertson SJ and Shogren-Knaak MA (2021) Mechanisms of stimulation of SAGA-mediated nucleosome acetylation by a transcriptional activator. Biochem Biophys Rep 25:100884 PMID: 33437882
- Kollenstart L, et al. (2021) Epigenetics Identifier screens reveal regulators of chromatin acylation and limited specificity of acylation antibodies. Sci Rep 11(1):12795 PMID: 34140538
- Rössl A, et al. (2019) A synthetic non-histone substrate to study substrate targeting by the Gcn5 HAT and sirtuin HDACs. J Biol Chem 294(16):6227-6239 PMID: 30804216
- Helmlinger D and Tora L (2017) Sharing the SAGA. Trends Biochem Sci 42(11):850-861 PMID: 28964624
- Kamata K, et al. (2013) C-terminus of the Sgf73 subunit of SAGA and SLIK is important for retention in the larger complex and for heterochromatin boundary function. Genes Cells 18(9):823-37 PMID: 23819448
- Zamostna B, et al. (2012) N-terminal domain of nuclear IL-1α shows structural similarity to the C-terminal domain of Snf1 and binds to the HAT/core module of the SAGA complex. PLoS One 7(8):e41801 PMID: 22879895
- Lee KK, et al. (2011) Combinatorial depletion analysis to assemble the network architecture of the SAGA and ADA chromatin remodeling complexes. Mol Syst Biol 7:503 PMID: 21734642
- Vernarecci S, et al. (2008) Gcn5p plays an important role in centromere kinetochore function in budding yeast. Mol Cell Biol 28(3):988-96 PMID: 18039853
- Wang YL, et al. (2008) Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel NC2-like histone fold module that interacts with the TATA-binding protein. J Biol Chem 283(49):33808-15 PMID: 18838386
- Wyce A, et al. (2004) H2B ubiquitylation and de-ubiquitylation in gene activation. Novartis Found Symp 259:63-73; discussion 73-7, 163-9 PMID: 15171247
- Shuen M, et al. (2002) The adenovirus E1A protein targets the SAGA but not the ADA transcriptional regulatory complex through multiple independent domains. J Biol Chem 277(34):30844-51 PMID: 12070146
- Chen BS, et al. (2001) A Gal4-sigma 54 hybrid protein that functions as a potent activator of RNA polymerase II transcription in yeast. J Biol Chem 276(26):23881-7 PMID: 11313364
- Sterner DE and Berger SL (2000) Acetylation of histones and transcription-related factors. Microbiol Mol Biol Rev 64(2):435-59 PMID: 10839822
- Eberharter A, et al. (1999) The ADA complex is a distinct histone acetyltransferase complex in Saccharomyces cerevisiae. Mol Cell Biol 19(10):6621-31 PMID: 10490601
- Martens JA, et al. (1996) Transcriptional activation by yeast PDR1p is inhibited by its association with NGG1p/ADA3p. J Biol Chem 271(27):15884-90 PMID: 8663102
- Horiuchi J, et al. (1995) ADA3, a putative transcriptional adaptor, consists of two separable domains and interacts with ADA2 and GCN5 in a trimeric complex. Mol Cell Biol 15(3):1203-9 PMID: 7862114