Catalytic Acetylation
Mostrando 1-12 de 44 artigos, teses e dissertações.
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1. Desenvolvimento e avaliaÃÃo da tecnologia de produÃÃo de Ãsteres homogÃneos de sacarÃdeos por acetilaÃÃo catalÃtica
As part of the systematic study of the process of acetylation of saccharides aiming to obtain products of industrial interests, we did tests with monosaccharides (glucose and fructose), disaccharides (sucrose). The sucrose composing abundant raw material deserves special attention as reagent acetylation of departure for a homogeneous environment. In the pres
Publicado em: 2007
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2. Synthesis of AminoaÃÃcares and Compostos GlicoheterocÃclicos / SÃntese de AminoaÃÃcares e Compostos GlicoheterocÃclicos
In the present work, the synthesis of new 2,3-unsaturaed glycosides, amino and branchedchain amino sugars is reported. Reaction of tri-O-acetyl-D-glucal (20) with five alcohols 72a-e using Ferrierâs method provided 2,3-unsaturatd glycosides 73a-e. Deacetylation of compounds 73a-e followed by allylic oxidation furnished enones 75a-e, which are important prec
Publicado em: 1997
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3. Investigation of the catalytic triad of arylamine N-acetyltransferases: essential residues required for acetyl transfer to arylamines
The NATs (arylamine N-acetyltransferases) are a well documented family of enzymes found in both prokaryotes and eukaryotes. NATs are responsible for the acetylation of a range of arylamine, arylhydrazine and hydrazine compounds. We present here an investigation into the catalytic triad of residues (Cys-His-Asp) and other structural features of NATs using a v
Portland Press Ltd..
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4. Eaf3 Regulates the Global Pattern of Histone Acetylation in Saccharomyces cerevisiae
Saccharomyces cerevisiae has a global pattern of histone acetylation in which histone H3 and H4 acetylation levels are lower at protein-coding sequences than at promoter regions. The loss of Eaf3, a subunit of the NuA4 histone acetylase and Rpd3 histone deacetylase complexes, greatly alters the genomic profile of histone acetylation, with the effects on H4 a
American Society for Microbiology.
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5. Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation
Protein acetylation, especially histone acetylation, is the subject of both research and clinical investigation. At least four small-molecule histone deacetylase inhibitors are currently in clinical trials for the treatment of cancer. These and other inhibitors also affect microtubule acetylation. A multidimensional, chemical genetic screen of 7,392 small mo
The National Academy of Sciences.
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6. DNA-PK is activated by nucleosomes and phosphorylates H2AX within the nucleosomes in an acetylation-dependent manner
Eukaryotic DNA is organized into nucleosomes and higher order chromatin structure, which plays an important role in the regulation of many nuclear processes including DNA repair. Non-homologous end-joining, the major pathway for repairing DNA double-strand breaks (DSBs) in mammalian cells, is mediated by a set of proteins including DNA-dependent protein kina
Oxford University Press.
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7. Growth inhibition by the mammalian SWI–SNF subunit Brm is regulated by acetylation
In mammalian cells, the SWI–SNF chromatin-remodeling complex is a regulator of cell proliferation, and overexpression of the catalytic subunit Brm interferes with cell cycle progression. Here, we show that treatment with histone deacetylase (HDAC) inhibitors reduces the inhibitory effect of Brm on the growth of mouse fibroblasts. This observation led to th
Oxford University Press.
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8. Histone H3 specific acetyltransferases are essential for cell cycle progression
Longstanding observations suggest that acetylation and/or amino-terminal tail structure of histones H3 and H4 are critical for eukaryotic cells. For Saccharomyces cerevisiae, loss of a single H4-specific histone acetyltransferase (HAT), Esa1p, results in cell cycle defects and death. In contrast, although several yeast HAT complexes preferentially acetylate
Cold Spring Harbor Laboratory Press.
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9. Activation Domain-Specific and General Transcription Stimulation by Native Histone Acetyltransferase Complexes
Recent progress in identifying the catalytic subunits of histone acetyltransferase (HAT) complexes has implicated histone acetylation in the regulation of transcription. Here, we have analyzed the function of two native yeast HAT complexes, SAGA (Spt-Ada-Gcn5 Acetyltransferase) and NuA4 (nucleosome acetyltransferase of H4), in activating transcription from p
American Society for Microbiology.
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10. Yeast Enhancer of Polycomb defines global Esa1-dependent acetylation of chromatin
Drosophila Enhancer of Polycomb, E(Pc), is a suppressor of position-effect variegation and an enhancer of both Polycomb and trithorax mutations. A homologous yeast protein, Epl1, is a subunit of the NuA4 histone acetyltransferase complex. Epl1 depletion causes cells to accumulate in G2/M and global loss of acetylated histones H4 and H2A. In relation to t
Cold Spring Harbor Laboratory Press.
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11. A Novel Human Ada2 Homologue Functions with Gcn5 or Brg1 To Coactivate Transcription
In yeast, the transcriptional adaptor yeast Ada2 (yAda2) is a part of the multicomponent SAGA complex, which possesses histone acetyltransferase activity through action of the yGcn5 catalytic enzyme. yAda2, among several SAGA proteins, serves to recruit SAGA to genes via interactions with promoter-bound transcription factors. Here we report identification of
American Society for Microbiology.
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12. Histone acetyltransferase activity of yeast Gcn5p is required for the activation of target genes in vivo
Gcn5p is a transcriptional coactivator required for correct expression of various genes in yeast. Several transcriptional regulators, including Gcn5p, possess intrinsic histone acetyltransferase (HAT) activity in vitro. However, whether the HAT activity of any of these proteins is required for gene activation remains unclear. Here, we demonstrate that the HA
Cold Spring Harbor Laboratory Press.