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Registro Completo |
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Biblioteca(s): |
Embrapa Florestas. |
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Data corrente: |
12/02/2007 |
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Data da última atualização: |
13/02/2015 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
SITA, R. C. M.; REISSMANN, C. B.; MARQUES, R.; OLIVEIRA, E. B. de; TAFFAREL, A. D. |
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Título: |
Effect of polymers associated with N and K fertilizer sources and Dendrathema grandiforum growth and K, Ca and Mg relations. |
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Ano de publicação: |
2005 |
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Fonte/Imprenta: |
Brazilian Archives of Biology and Technology, Curitiba, v. 48, n. 3, p. 335-342, 2005. |
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Idioma: |
Inglês |
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Conteúdo: |
This study was conducted to evaluate the effect of polymer used with different nitrogen and potassium sources on the growth and nutrition of chrysanthemum (Dendranthema grandiforum, var. "Virginal") and on chemical characteristics of substrate. Two substrates were evaluated: 1) composite with 50 % organic soil, 45 % sand, and 5 % composted tobacco; 2) plow layer soil (0-20 cm depth; red oxisol typical dystrophic). The experimental design was a factorial (4x2x2) and included four polymer rates (0, 1, 2, and 4 g kg-1of substrate), two nitrogen ((NH4)2SO4 and (H2N)2CO), and two potassium (KCl and K2SO4) sources. Dry biomass, flower number, and concentration of K, Ca, and Mg were evaluated. Inverse relationships between polymer rates and plant biomass, macronutrient uptake were noticed, regardless substrate or nutrient source. |
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Palavras-Chave: |
Crysanthemum; Hidrogel; Macronuutriente; Polyacrylamida. |
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Thesagro: |
Fertilizante. |
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Categoria do assunto: |
-- |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/27089/1/24754.pdf
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Marc: |
LEADER 01566naa a2200229 a 4500
001 1312519
005 2015-02-13
008 2005 bl uuuu u00u1 u #d
100 1 $aSITA, R. C. M.
245 $aEffect of polymers associated with N and K fertilizer sources and Dendrathema grandiforum growth and K, Ca and Mg relations.$h[electronic resource]
260 $c2005
520 $aThis study was conducted to evaluate the effect of polymer used with different nitrogen and potassium sources on the growth and nutrition of chrysanthemum (Dendranthema grandiforum, var. "Virginal") and on chemical characteristics of substrate. Two substrates were evaluated: 1) composite with 50 % organic soil, 45 % sand, and 5 % composted tobacco; 2) plow layer soil (0-20 cm depth; red oxisol typical dystrophic). The experimental design was a factorial (4x2x2) and included four polymer rates (0, 1, 2, and 4 g kg-1of substrate), two nitrogen ((NH4)2SO4 and (H2N)2CO), and two potassium (KCl and K2SO4) sources. Dry biomass, flower number, and concentration of K, Ca, and Mg were evaluated. Inverse relationships between polymer rates and plant biomass, macronutrient uptake were noticed, regardless substrate or nutrient source.
650 $aFertilizante
653 $aCrysanthemum
653 $aHidrogel
653 $aMacronuutriente
653 $aPolyacrylamida
700 1 $aREISSMANN, C. B.
700 1 $aMARQUES, R.
700 1 $aOLIVEIRA, E. B. de
700 1 $aTAFFAREL, A. D.
773 $tBrazilian Archives of Biology and Technology, Curitiba$gv. 48, n. 3, p. 335-342, 2005.
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Registro original: |
Embrapa Florestas (CNPF) |
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 | Acesso ao texto completo restrito à biblioteca da Embrapa Gado de Leite. Para informações adicionais entre em contato com cnpgl.biblioteca@embrapa.br. |
Registro Completo
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Biblioteca(s): |
Embrapa Gado de Leite. |
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Data corrente: |
20/05/2014 |
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Data da última atualização: |
05/02/2024 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
A - 1 |
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Autoria: |
CHRISTOPHOROU, M. A.; CASTELO-BRANCO, G.; HALLEY-STOTT, R. P.; OLIVEIRA, C. S.; LOOS, R.; RADZISHEUSKAYA, A.; MOWEN, K. A.; BERTONE, P.; SILVA, J. C. R.; ZERNICKA-GOETZ, M.; MICHAEL L. NIELSEN; GURDON, J. B.; KOUZARIDES, T. |
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Afiliação: |
MARIA A. CHRISTOPHOROU, University of Cambridge; GONÇALO CASTELO-BRANCO, University of Cambridge; Karolinska Institutet, Stockholm, Sweden; RICHARD P. HALLEY-STOTT, University of Cambridge; CLARA SLADE OLIVEIRA, CNPGL; REMCO LOOS, European Molecular Biology Laboratory, European Bioinformatics Institute, Wellcome Trust Genome Campus, Cambridge; ALIAKSANDRA RADZISHEUSKAYA, University of Cambridge; KERRI A. MOWEN, Department of Chemical Physiology, The Scripps Research Institute, La Jolla, California; PAUL BERTONE, European Molecular Biology Laboratory, European Bioinformatics Institute, Wellcome Trust Genome Campus, Cambridge; University of Cambridge; JOSÉ C. R. SILVA, European Molecular Biology Laboratory, European Bioinformatics Institute, Wellcome Trust Genome Campus, Cambridge , University of Cambridge.; MAGDALENA ZERNICKA-GOETZ, University of Cambridge; NIELSEN, M. L., University of Copenhagen,Copenhagen, Denmark; JOHN B. GURDON, University of Cambridge; TONY KOUZARIDES, University of Cambridge. |
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Título: |
Citrullination regulates pluripotency and histone H1 binding to chromatin |
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Ano de publicação: |
2014 |
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Fonte/Imprenta: |
Nature, v. 507, n. 7490, p. 104-108, 2014. |
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DOI: |
https://doi.org/10.1038/nature12942 |
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Idioma: |
Inglês |
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Conteúdo: |
Citrullination is the post-translational conversion of an arginine residue within a protein to the non-coded amino acid citrulline. This modification leads to the loss of a positive charge and reduction in hydrogen-bonding ability. It is carried out by a small family of tissue-specific vertebrate enzymes called peptidylarginine deiminases (PADIs) and is associated with the development of diverse pathological states such as autoimmunity, cancer, neurodegenerative disorders, prion diseases and thrombosis. Nevertheless, the physiological functions of citrullination remain ill-defined, although citrullination of core histones has been linked to transcriptional regulation and the DNA damage response. PADI4 (also called PAD4 or PADV), the only PADI with a nuclear localization signal, was previously shown to act in myeloid cells where it mediates profound chromatin decondensation during the innate immune response to infection. Here we show that the expression and enzymatic activity of Padi4 are also induced under conditions of ground-state pluripotency and during reprogramming in mouse. Padi4 is part of the pluripotency transcriptional network, binding to regulatory elements of key stem-cell genes and activating their expression. Its inhibition lowers the percentage of pluripotent cells in the early mouse embryo and significantly reduces reprogramming efficiency. Using an unbiased proteomic approach we identify linker histone H1 variants, which are involved in the generation of compact chromatin, as novel PADI4 substrates. Citrullination of a single arginine residue within the DNA-binding site of H1 results in its displacement from chromatin and global chromatin decondensation. Together, these results uncover a role for citrullination in the regulation of pluripotency and provide new mechanistic insights into how citrullination regulates chromatin compaction. MenosCitrullination is the post-translational conversion of an arginine residue within a protein to the non-coded amino acid citrulline. This modification leads to the loss of a positive charge and reduction in hydrogen-bonding ability. It is carried out by a small family of tissue-specific vertebrate enzymes called peptidylarginine deiminases (PADIs) and is associated with the development of diverse pathological states such as autoimmunity, cancer, neurodegenerative disorders, prion diseases and thrombosis. Nevertheless, the physiological functions of citrullination remain ill-defined, although citrullination of core histones has been linked to transcriptional regulation and the DNA damage response. PADI4 (also called PAD4 or PADV), the only PADI with a nuclear localization signal, was previously shown to act in myeloid cells where it mediates profound chromatin decondensation during the innate immune response to infection. Here we show that the expression and enzymatic activity of Padi4 are also induced under conditions of ground-state pluripotency and during reprogramming in mouse. Padi4 is part of the pluripotency transcriptional network, binding to regulatory elements of key stem-cell genes and activating their expression. Its inhibition lowers the percentage of pluripotent cells in the early mouse embryo and significantly reduces reprogramming efficiency. Using an unbiased proteomic approach we identify linker histone H1 variants, which are involved in the generation of com... Mostrar Tudo |
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Palavras-Chave: |
Histone post-translational modifications; Reprogramming. |
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Categoria do assunto: |
W Química e Física |
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Marc: |
LEADER 02780naa a2200301 a 4500
001 1986615
005 2024-02-05
008 2014 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.1038/nature12942$2DOI
100 1 $aCHRISTOPHOROU, M. A.
245 $aCitrullination regulates pluripotency and histone H1 binding to chromatin$h[electronic resource]
260 $c2014
520 $aCitrullination is the post-translational conversion of an arginine residue within a protein to the non-coded amino acid citrulline. This modification leads to the loss of a positive charge and reduction in hydrogen-bonding ability. It is carried out by a small family of tissue-specific vertebrate enzymes called peptidylarginine deiminases (PADIs) and is associated with the development of diverse pathological states such as autoimmunity, cancer, neurodegenerative disorders, prion diseases and thrombosis. Nevertheless, the physiological functions of citrullination remain ill-defined, although citrullination of core histones has been linked to transcriptional regulation and the DNA damage response. PADI4 (also called PAD4 or PADV), the only PADI with a nuclear localization signal, was previously shown to act in myeloid cells where it mediates profound chromatin decondensation during the innate immune response to infection. Here we show that the expression and enzymatic activity of Padi4 are also induced under conditions of ground-state pluripotency and during reprogramming in mouse. Padi4 is part of the pluripotency transcriptional network, binding to regulatory elements of key stem-cell genes and activating their expression. Its inhibition lowers the percentage of pluripotent cells in the early mouse embryo and significantly reduces reprogramming efficiency. Using an unbiased proteomic approach we identify linker histone H1 variants, which are involved in the generation of compact chromatin, as novel PADI4 substrates. Citrullination of a single arginine residue within the DNA-binding site of H1 results in its displacement from chromatin and global chromatin decondensation. Together, these results uncover a role for citrullination in the regulation of pluripotency and provide new mechanistic insights into how citrullination regulates chromatin compaction.
653 $aHistone post-translational modifications
653 $aReprogramming
700 1 $aCASTELO-BRANCO, G.
700 1 $aHALLEY-STOTT, R. P.
700 1 $aOLIVEIRA, C. S.
700 1 $aLOOS, R.
700 1 $aRADZISHEUSKAYA, A.
700 1 $aMOWEN, K. A.
700 1 $aBERTONE, P.
700 1 $aSILVA, J. C. R.
700 1 $aZERNICKA-GOETZ, M.
700 1 $aMICHAEL L. NIELSEN
700 1 $aGURDON, J. B.
700 1 $aKOUZARIDES, T.
773 $tNature$gv. 507, n. 7490, p. 104-108, 2014.
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