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The Aspergillus flavus Histone Acetyltransferase AflGcnE Regulates Morphogenesis, Aflatoxin Biosynthesis, and Pathogenicity.

Frontiers in microbiology

Lan H, Sun R, Fan K, Yang K, Zhang F, Nie XY, Wang X, Zhuang Z, Wang S.
PMID: 27625637
Front Microbiol. 2016 Aug 30;7:1324. doi: 10.3389/fmicb.2016.01324. eCollection 2016.

Histone acetyltransferases (HATs) help regulate fungal development and the production of secondary metabolites. In this study, we determined that the HAT AflGcnE influenced morphogenesis and aflatoxin biosynthesis in Aspergillus flavus. We observed that AflGcnE localized to the nucleus and...

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Lan H, Sun R, Fan K, et al. The Aspergillus flavus Histone Acetyltransferase AflGcnE Regulates Morphogenesis, Aflatoxin Biosynthesis, and Pathogenicity. Front Microbiol. 2016;7:1324doi: 10.3389/fmicb.2016.01324.
Lan, H., Sun, R., Fan, K., Yang, K., Zhang, F., Nie, X. Y., Wang, X., Zhuang, Z., & Wang, S. (2016). The Aspergillus flavus Histone Acetyltransferase AflGcnE Regulates Morphogenesis, Aflatoxin Biosynthesis, and Pathogenicity. Frontiers in microbiology, 71324. https://doi.org/10.3389/fmicb.2016.01324
Lan, Huahui, et al. "The Aspergillus flavus Histone Acetyltransferase AflGcnE Regulates Morphogenesis, Aflatoxin Biosynthesis, and Pathogenicity." Frontiers in microbiology vol. 7 (2016): 1324. doi: https://doi.org/10.3389/fmicb.2016.01324
Lan H, Sun R, Fan K, Yang K, Zhang F, Nie XY, Wang X, Zhuang Z, Wang S. The Aspergillus flavus Histone Acetyltransferase AflGcnE Regulates Morphogenesis, Aflatoxin Biosynthesis, and Pathogenicity. Front Microbiol. 2016 Aug 30;7:1324. doi: 10.3389/fmicb.2016.01324. eCollection 2016. PMID: 27625637; PMCID: PMC5003836.
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Gut resistome development in healthy twin pairs in the first year of life.

Microbiome

Moore AM, Ahmadi S, Patel S, Gibson MK, Wang B, Ndao MI, Deych E, Shannon W, Tarr PI, Warner BB, Dantas G.
PMID: 26113976
Microbiome. 2015 Jun 25;3:27. doi: 10.1186/s40168-015-0090-9. eCollection 2015.

BACKGROUND: The early life of the human host marks a critically important time for establishment of the gut microbial community, yet the developmental trajectory of gut community-encoded resistance genes (resistome) is unknown. We present a longitudinal study of the...

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Moore AM, Ahmadi S, Patel S, et al. Gut resistome development in healthy twin pairs in the first year of life. Microbiome. 2015;3:27doi: 10.1186/s40168-015-0090-9.
Moore, A. M., Ahmadi, S., Patel, S., Gibson, M. K., Wang, B., Ndao, M. I., Deych, E., Shannon, W., Tarr, P. I., Warner, B. B., & Dantas, G. (2015). Gut resistome development in healthy twin pairs in the first year of life. Microbiome, 327. https://doi.org/10.1186/s40168-015-0090-9
Moore, Aimee M, et al. "Gut resistome development in healthy twin pairs in the first year of life." Microbiome vol. 3 (2015): 27. doi: https://doi.org/10.1186/s40168-015-0090-9
Moore AM, Ahmadi S, Patel S, Gibson MK, Wang B, Ndao MI, Deych E, Shannon W, Tarr PI, Warner BB, Dantas G. Gut resistome development in healthy twin pairs in the first year of life. Microbiome. 2015 Jun 25;3:27. doi: 10.1186/s40168-015-0090-9. eCollection 2015. PMID: 26113976; PMCID: PMC4480905.
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Biomarkers of exposure, effect, and susceptibility in workers exposed to chloronitrobenzenes.

Biomarkers : biochemical indicators of exposure, response, and susceptibility to chemicals

Sabbioni G, Norppa H, Hirvonen A, Järventaus H, Jones CR, Yan H, Sepai O.
PMID: 27121198
Biomarkers. 2016 Dec;21(8):721-730. doi: 10.3109/1354750X.2016.1172116. Epub 2016 Apr 27.

Biomonitoring methods were applied to workers exposed to high levels of chloronitrobenzenes. The external dose, internal dose, biologically effective dose, and biological effects were determined. Individual susceptibility was assessed by analyzing genetic polymorphisms of glutathione S-transferases M1, P1 and...

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Sabbioni G, Norppa H, Hirvonen A, et al. Biomarkers of exposure, effect, and susceptibility in workers exposed to chloronitrobenzenes. Biomarkers. 2016;21(8):721-730doi: 10.3109/1354750X.2016.1172116.
Sabbioni, G., Norppa, H., Hirvonen, A., Järventaus, H., Jones, C. R., Yan, H., & Sepai, O. (2016). Biomarkers of exposure, effect, and susceptibility in workers exposed to chloronitrobenzenes. Biomarkers : biochemical indicators of exposure, response, and susceptibility to chemicals, 21(8), 721-730. https://doi.org/10.3109/1354750X.2016.1172116
Sabbioni, Gabriele, et al. "Biomarkers of exposure, effect, and susceptibility in workers exposed to chloronitrobenzenes." Biomarkers : biochemical indicators of exposure, response, and susceptibility to chemicals vol. 21,8 (2016): 721-730. doi: https://doi.org/10.3109/1354750X.2016.1172116
Sabbioni G, Norppa H, Hirvonen A, Järventaus H, Jones CR, Yan H, Sepai O. Biomarkers of exposure, effect, and susceptibility in workers exposed to chloronitrobenzenes. Biomarkers. 2016 Dec;21(8):721-730. doi: 10.3109/1354750X.2016.1172116. Epub 2016 Apr 27. PMID: 27121198.
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p53 Acetylation: Regulation and Consequences.

Cancers

Reed SM, Quelle DE.
PMID: 25545885
Cancers (Basel). 2014 Dec 23;7(1):30-69. doi: 10.3390/cancers7010030.

Post-translational modifications of p53 are critical in modulating its tumor suppressive functions. Ubiquitylation, for example, plays a major role in dictating p53 stability, subcellular localization and transcriptional vs. non-transcriptional activities. Less is known about p53 acetylation. It has been...

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Reed SM, Quelle DE. p53 Acetylation: Regulation and Consequences. Cancers (Basel). 2014;7(1):30-69doi: 10.3390/cancers7010030.
Reed, S. M., & Quelle, D. E. (2014). p53 Acetylation: Regulation and Consequences. Cancers, 7(1), 30-69. https://doi.org/10.3390/cancers7010030
Reed, Sara M, and Quelle, Dawn E. "p53 Acetylation: Regulation and Consequences." Cancers vol. 7,1 (2014): 30-69. doi: https://doi.org/10.3390/cancers7010030
Reed SM, Quelle DE. p53 Acetylation: Regulation and Consequences. Cancers (Basel). 2014 Dec 23;7(1):30-69. doi: 10.3390/cancers7010030. PMID: 25545885; PMCID: PMC4381250.
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Emerging roles for histone deacetylases in pulmonary hypertension and right ventricular remodeling (2013 Grover Conference series).

Pulmonary circulation

Cavasin MA, Stenmark KR, McKinsey TA.
PMID: 25992271
Pulm Circ. 2015 Mar;5(1):63-72. doi: 10.1086/679700.

Reversible lysine acetylation has emerged as a critical mechanism for controlling the function of nucleosomal histones as well as diverse nonhistone proteins. Acetyl groups are conjugated to lysine residues in proteins by histone acetyltransferases and removed by histone deacetylases...

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Cavasin MA, Stenmark KR, McKinsey TA. Emerging roles for histone deacetylases in pulmonary hypertension and right ventricular remodeling (2013 Grover Conference series). Pulm Circ. 2015;5(1):63-72doi: 10.1086/679700.
Cavasin, M. A., Stenmark, K. R., & McKinsey, T. A. (2015). Emerging roles for histone deacetylases in pulmonary hypertension and right ventricular remodeling (2013 Grover Conference series). Pulmonary circulation, 5(1), 63-72. https://doi.org/10.1086/679700
Cavasin, Maria A, et al. "Emerging roles for histone deacetylases in pulmonary hypertension and right ventricular remodeling (2013 Grover Conference series)." Pulmonary circulation vol. 5,1 (2015): 63-72. doi: https://doi.org/10.1086/679700
Cavasin MA, Stenmark KR, McKinsey TA. Emerging roles for histone deacetylases in pulmonary hypertension and right ventricular remodeling (2013 Grover Conference series). Pulm Circ. 2015 Mar;5(1):63-72. doi: 10.1086/679700. PMID: 25992271; PMCID: PMC4405717.
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Restitution of gene expression and histone acetylation signatures altered by hepatitis B virus through antiviral microRNA-like molecules in nontransformed murine hepatocytes.

Clinical epigenetics

Jenke AC, Hensel KO, Klein A, Willuhn L, Prax S, Weil PP, Winkler T, Deba T, Orth V, Baiker A, Wirth S, Postberg J.
PMID: 25859285
Clin Epigenetics. 2014 Nov 14;6(1):26. doi: 10.1186/1868-7083-6-26. eCollection 2014.

BACKGROUND: Virus-host interactions result in altered gene expression profiles in host cell nuclei and enable virus particle production, thus obligatorily involving changes in their epigenomes. Neither such epigenome changes nor their response to antiviral treatment have been extensively studied...

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Jenke AC, Hensel KO, Klein A, et al. Restitution of gene expression and histone acetylation signatures altered by hepatitis B virus through antiviral microRNA-like molecules in nontransformed murine hepatocytes. Clin Epigenetics. 2014;6(1):26doi: 10.1186/1868-7083-6-26.
Jenke, A. C., Hensel, K. O., Klein, A., Willuhn, L., Prax, S., Weil, P. P., Winkler, T., Deba, T., Orth, V., Baiker, A., Wirth, S., & Postberg, J. (2014). Restitution of gene expression and histone acetylation signatures altered by hepatitis B virus through antiviral microRNA-like molecules in nontransformed murine hepatocytes. Clinical epigenetics, 6(1), 26. https://doi.org/10.1186/1868-7083-6-26
Jenke, Andreas Cw, et al. "Restitution of gene expression and histone acetylation signatures altered by hepatitis B virus through antiviral microRNA-like molecules in nontransformed murine hepatocytes." Clinical epigenetics vol. 6,1 (2014): 26. doi: https://doi.org/10.1186/1868-7083-6-26
Jenke AC, Hensel KO, Klein A, Willuhn L, Prax S, Weil PP, Winkler T, Deba T, Orth V, Baiker A, Wirth S, Postberg J. Restitution of gene expression and histone acetylation signatures altered by hepatitis B virus through antiviral microRNA-like molecules in nontransformed murine hepatocytes. Clin Epigenetics. 2014 Nov 14;6(1):26. doi: 10.1186/1868-7083-6-26. eCollection 2014. PMID: 25859285; PMCID: PMC4391130.
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Microbial communication leading to the activation of silent fungal secondary metabolite gene clusters.

Frontiers in microbiology

Netzker T, Fischer J, Weber J, Mattern DJ, König CC, Valiante V, Schroeckh V, Brakhage AA.
PMID: 25941517
Front Microbiol. 2015 Apr 20;6:299. doi: 10.3389/fmicb.2015.00299. eCollection 2015.

Microorganisms form diverse multispecies communities in various ecosystems. The high abundance of fungal and bacterial species in these consortia results in specific communication between the microorganisms. A key role in this communication is played by secondary metabolites (SMs), which...

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Netzker T, Fischer J, Weber J, et al. Microbial communication leading to the activation of silent fungal secondary metabolite gene clusters. Front Microbiol. 2015;6:299doi: 10.3389/fmicb.2015.00299.
Netzker, T., Fischer, J., Weber, J., Mattern, D. J., König, C. C., Valiante, V., Schroeckh, V., & Brakhage, A. A. (2015). Microbial communication leading to the activation of silent fungal secondary metabolite gene clusters. Frontiers in microbiology, 6299. https://doi.org/10.3389/fmicb.2015.00299
Netzker, Tina, et al. "Microbial communication leading to the activation of silent fungal secondary metabolite gene clusters." Frontiers in microbiology vol. 6 (2015): 299. doi: https://doi.org/10.3389/fmicb.2015.00299
Netzker T, Fischer J, Weber J, Mattern DJ, König CC, Valiante V, Schroeckh V, Brakhage AA. Microbial communication leading to the activation of silent fungal secondary metabolite gene clusters. Front Microbiol. 2015 Apr 20;6:299. doi: 10.3389/fmicb.2015.00299. eCollection 2015. PMID: 25941517; PMCID: PMC4403501.
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Structure of Thermoplasma volcanium Ard1 belongs to N-acetyltransferase family member suggesting multiple ligand binding modes with acetyl coenzyme A and coenzyme A.

Biochimica et biophysica acta

Ma C, Pathak C, Jang S, Lee SJ, Nam M, Kim SJ, Im H, Lee BJ.
PMID: 25062911
Biochim Biophys Acta. 2014 Oct;1844(10):1790-7. doi: 10.1016/j.bbapap.2014.07.011. Epub 2014 Jul 22.

Acetylation and deacetylation reactions result in biologically important modifications that are involved in normal cell function and cancer development. These reactions, carried out by protein acetyltransferase enzymes, act by transferring an acetyl group from acetyl-coenzymeA (Ac-CoA) to various substrate...

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Ma C, Pathak C, Jang S, et al. Structure of Thermoplasma volcanium Ard1 belongs to N-acetyltransferase family member suggesting multiple ligand binding modes with acetyl coenzyme A and coenzyme A. Biochim Biophys Acta. 2014;1844(10):1790-7doi: 10.1016/j.bbapap.2014.07.011.
Ma, C., Pathak, C., Jang, S., Lee, S. J., Nam, M., Kim, S. J., Im, H., & Lee, B. J. (2014). Structure of Thermoplasma volcanium Ard1 belongs to N-acetyltransferase family member suggesting multiple ligand binding modes with acetyl coenzyme A and coenzyme A. Biochimica et biophysica acta, 1844(10), 1790-7. https://doi.org/10.1016/j.bbapap.2014.07.011
Ma, Chao, et al. "Structure of Thermoplasma volcanium Ard1 belongs to N-acetyltransferase family member suggesting multiple ligand binding modes with acetyl coenzyme A and coenzyme A." Biochimica et biophysica acta vol. 1844,10 (2014): 1790-7. doi: https://doi.org/10.1016/j.bbapap.2014.07.011
Ma C, Pathak C, Jang S, Lee SJ, Nam M, Kim SJ, Im H, Lee BJ. Structure of Thermoplasma volcanium Ard1 belongs to N-acetyltransferase family member suggesting multiple ligand binding modes with acetyl coenzyme A and coenzyme A. Biochim Biophys Acta. 2014 Oct;1844(10):1790-7. doi: 10.1016/j.bbapap.2014.07.011. Epub 2014 Jul 22. PMID: 25062911.
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An activator for pyruvoyl-dependent l-aspartate α-decarboxylase is conserved in a small group of the γ-proteobacteria including Escherichia coli.

MicrobiologyOpen

Nozaki S, Webb ME, Niki H.
PMID: 23170229
Microbiologyopen. 2012 Sep;1(3):298-310. doi: 10.1002/mbo3.34. Epub 2012 Aug 14.

In bacteria, β-alanine is formed via the action of l-aspartate α-decarboxylase (PanD) which is one of the small class of pyruvoyl-dependent enzymes. The pyruvoyl cofactor in these enzymes is formed via the intramolecular rearrangement of a serine residue in...

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Nozaki S, Webb ME, Niki H. An activator for pyruvoyl-dependent l-aspartate α-decarboxylase is conserved in a small group of the γ-proteobacteria including Escherichia coli. Microbiologyopen. 2012;1(3):298-310doi: 10.1002/mbo3.34.
Nozaki, S., Webb, M. E., & Niki, H. (2012). An activator for pyruvoyl-dependent l-aspartate α-decarboxylase is conserved in a small group of the γ-proteobacteria including Escherichia coli. MicrobiologyOpen, 1(3), 298-310. https://doi.org/10.1002/mbo3.34
Nozaki, Shingo, et al. "An activator for pyruvoyl-dependent l-aspartate α-decarboxylase is conserved in a small group of the γ-proteobacteria including Escherichia coli." MicrobiologyOpen vol. 1,3 (2012): 298-310. doi: https://doi.org/10.1002/mbo3.34
Nozaki S, Webb ME, Niki H. An activator for pyruvoyl-dependent l-aspartate α-decarboxylase is conserved in a small group of the γ-proteobacteria including Escherichia coli. Microbiologyopen. 2012 Sep;1(3):298-310. doi: 10.1002/mbo3.34. Epub 2012 Aug 14. PMID: 23170229; PMCID: PMC3496974.
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Dietary, metabolic, and potentially environmental modulation of the lysine acetylation machinery.

International journal of cell biology

Kim GW, Gocevski G, Wu CJ, Yang XJ.
PMID: 20976254
Int J Cell Biol. 2010;2010:632739. doi: 10.1155/2010/632739. Epub 2010 Oct 05.

Healthy lifestyles and environment produce a good state of health. A number of scientific studies support the notion that external stimuli regulate an individual's epigenomic profile. Epigenetic changes play a key role in defining gene expression patterns under both...

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Kim GW, Gocevski G, Wu CJ, et al. Dietary, metabolic, and potentially environmental modulation of the lysine acetylation machinery. Int J Cell Biol. 2010;2010:632739doi: 10.1155/2010/632739.
Kim, G. W., Gocevski, G., Wu, C. J., & Yang, X. J. (2010). Dietary, metabolic, and potentially environmental modulation of the lysine acetylation machinery. International journal of cell biology, 2010632739. https://doi.org/10.1155/2010/632739
Kim, Go-Woon, et al. "Dietary, metabolic, and potentially environmental modulation of the lysine acetylation machinery." International journal of cell biology vol. 2010 (2010): 632739. doi: https://doi.org/10.1155/2010/632739
Kim GW, Gocevski G, Wu CJ, Yang XJ. Dietary, metabolic, and potentially environmental modulation of the lysine acetylation machinery. Int J Cell Biol. 2010;2010:632739. doi: 10.1155/2010/632739. Epub 2010 Oct 05. PMID: 20976254; PMCID: PMC2952894.
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Mutations in HISTONE ACETYLTRANSFERASE1 affect sugar response and gene expression in Arabidopsis.

Frontiers in plant science

Heisel TJ, Li CY, Grey KM, Gibson SI.
PMID: 23882272
Front Plant Sci. 2013 Jul 17;4:245. doi: 10.3389/fpls.2013.00245. eCollection 2013.

Nutrient response networks are likely to have been among the first response networks to evolve, as the ability to sense and respond to the levels of available nutrients is critical for all organisms. Although several forward genetic screens have...

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Heisel TJ, Li CY, Grey KM, et al. Mutations in HISTONE ACETYLTRANSFERASE1 affect sugar response and gene expression in Arabidopsis. Front Plant Sci. 2013;4:245doi: 10.3389/fpls.2013.00245.
Heisel, T. J., Li, C. Y., Grey, K. M., & Gibson, S. I. (2013). Mutations in HISTONE ACETYLTRANSFERASE1 affect sugar response and gene expression in Arabidopsis. Frontiers in plant science, 4245. https://doi.org/10.3389/fpls.2013.00245
Heisel, Timothy J, et al. "Mutations in HISTONE ACETYLTRANSFERASE1 affect sugar response and gene expression in Arabidopsis." Frontiers in plant science vol. 4 (2013): 245. doi: https://doi.org/10.3389/fpls.2013.00245
Heisel TJ, Li CY, Grey KM, Gibson SI. Mutations in HISTONE ACETYLTRANSFERASE1 affect sugar response and gene expression in Arabidopsis. Front Plant Sci. 2013 Jul 17;4:245. doi: 10.3389/fpls.2013.00245. eCollection 2013. PMID: 23882272; PMCID: PMC3713338.
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Xenobiotic metabolizing gene variants and renal cell cancer: a multicenter study.

Frontiers in oncology

Heck JE, Moore LE, Lee YC, McKay JD, Hung RJ, Karami S, Gaborieau V, Szeszenia-Dabrowska N, Zaridze DG, Mukeriya A, Mates D, Foretova L, Janout V, Kollárová H, Bencko V, Rothman N, Brennan P, Chow WH, Boffetta P.
PMID: 22645715
Front Oncol. 2012 Feb 20;2:16. doi: 10.3389/fonc.2012.00016. eCollection 2012.

BACKGROUND: The countries of Central and Eastern Europe have among the highest worldwide rates of renal cell cancer (RCC). Few studies have examined whether genetic variation in xenobiotic metabolic pathway genes may modify risk for this cancer.METHODS: The Central...

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Heck JE, Moore LE, Lee YC, et al. Xenobiotic metabolizing gene variants and renal cell cancer: a multicenter study. Front Oncol. 2012;2:16doi: 10.3389/fonc.2012.00016.
Heck, J. E., Moore, L. E., Lee, Y. C., McKay, J. D., Hung, R. J., Karami, S., Gaborieau, V., Szeszenia-Dabrowska, N., Zaridze, D. G., Mukeriya, A., Mates, D., Foretova, L., Janout, V., Kollárová, H., Bencko, V., Rothman, N., Brennan, P., Chow, W. H., & Boffetta, P. (2012). Xenobiotic metabolizing gene variants and renal cell cancer: a multicenter study. Frontiers in oncology, 216. https://doi.org/10.3389/fonc.2012.00016
Heck, Julia E, et al. "Xenobiotic metabolizing gene variants and renal cell cancer: a multicenter study." Frontiers in oncology vol. 2 (2012): 16. doi: https://doi.org/10.3389/fonc.2012.00016
Heck JE, Moore LE, Lee YC, McKay JD, Hung RJ, Karami S, Gaborieau V, Szeszenia-Dabrowska N, Zaridze DG, Mukeriya A, Mates D, Foretova L, Janout V, Kollárová H, Bencko V, Rothman N, Brennan P, Chow WH, Boffetta P. Xenobiotic metabolizing gene variants and renal cell cancer: a multicenter study. Front Oncol. 2012 Feb 20;2:16. doi: 10.3389/fonc.2012.00016. eCollection 2012. PMID: 22645715; PMCID: PMC3355831.
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Showing 1 to 12 of 289 entries