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[PMID]:29381770
[Au] Autor:Lin CY; Lin LY
[Ad] Endereço:Institute of Molecular and Cellular Biology and Department of Life Science, National Tsing Hua University, Hsinchu, Taiwan, ROC.
[Ti] Título:The conserved basic residues and the charged amino acid residues at the α-helix of the zinc finger motif regulate the nuclear transport activity of triple C2H2 zinc finger proteins.
[So] Source:PLoS One;13(1):e0191971, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Zinc finger (ZF) motifs on proteins are frequently recognized as a structure for DNA binding. Accumulated reports indicate that ZF motifs contain nuclear localization signal (NLS) to facilitate the transport of ZF proteins into nucleus. We investigated the critical factors that facilitate the nuclear transport of triple C2H2 ZF proteins. Three conserved basic residues (hot spots) were identified among the ZF sequences of triple C2H2 ZF proteins that reportedly have NLS function. Additional basic residues can be found on the α-helix of the ZFs. Using the ZF domain (ZFD) of Egr-1 as a template, various mutants were constructed and expressed in cells. The nuclear transport activity of various mutants was estimated by analyzing the proportion of protein localized in the nucleus. Mutation at any hot spot of the Egr-1 ZFs reduced the nuclear transport activity. Changes of the basic residues at the α-helical region of the second ZF (ZF2) of the Egr-1 ZFD abolished the NLS activity. However, this activity can be restored by substituting the acidic residues at the homologous positions of ZF1 or ZF3 with basic residues. The restored activity dropped again when the hot spots at ZF1 or the basic residues in the α-helix of ZF3 were mutated. The variations in nuclear transport activity are linked directly to the binding activity of the ZF proteins with importins. This study was extended to other triple C2H2 ZF proteins. SP1 and KLF families, similar to Egr-1, have charged amino acid residues at the second (α2) and the third (α3) positions of the α-helix. Replacing the amino acids at α2 and α3 with acidic residues reduced the NLS activity of the SP1 and KLF6 ZFD. The reduced activity can be restored by substituting the α3 with histidine at any SP1 and KLF6 ZFD. The results show again the interchangeable role of ZFs and charge residues in the α-helix in regulating the NLS activity of triple C2H2 ZF proteins.
[Mh] Termos MeSH primário: Aminoácidos/metabolismo
Núcleo Celular/metabolismo
Dedos de Zinco
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Transporte Proteico
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Acids)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180131
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191971


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[PMID]:29377959
[Au] Autor:Figura M; Kusmierska K; Bucior E; Szlufik S; Koziorowski D; Jamrozik Z; Janik P
[Ad] Endereço:Department of Neurology, Faculty of Heath Sciences, Medical University of Warsaw, Warsaw, Poland.
[Ti] Título:Serum amino acid profile in patients with Parkinson's disease.
[So] Source:PLoS One;13(1):e0191670, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Amino acids play numerous roles in the central nervous system, serving as neurotransmitters, neuromodulators and regulators of energy metabolism. The free amino acid profile in serum of Parkinson's disease (PD) patients may be influenced by neurodegeneration, mitochondrial dysfunction, malabsorption in the gastroenteric tract and received treatment. The aim of our study was the evaluation of the profile of amino acid concentrations against disease progression. We assessed the amino acid profile in the serum of 73 patients divided into groups with early PD, late PD with dyskinesia and late PD without dyskinesia. Serum amino acid analysis was performed by high-pressure liquid chromatography with fluorescence detection. We observed some significant differences amongst the groups with respect to concentrations of alanine, arginine, phenylalanine and threonine, although no significant differences were observed between patients with advanced PD with and without dyskinesia. We conclude that this specific amino acid profile could serve as biochemical marker of PD progression.
[Mh] Termos MeSH primário: Aminoácidos/sangue
Doença de Parkinson/sangue
[Mh] Termos MeSH secundário: Cromatografia Líquida de Alta Pressão
Seres Humanos
Espectrometria de Fluorescência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Acids)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180130
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191670


  3 / 118337 MEDLINE  
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[PMID]:28942275
[Au] Autor:Yadav P; Kaur R; Kanwar MK; Sharma A; Verma V; Sirhindi G; Bhardwaj R
[Ad] Endereço:Department of Botanical and Environmental Sciences, Guru Nanak Dev University, Amritsar 143005, Punjab, India.
[Ti] Título:Castasterone confers copper stress tolerance by regulating antioxidant enzyme responses, antioxidants, and amino acid balance in B. juncea seedlings.
[So] Source:Ecotoxicol Environ Saf;147:725-734, 2018 Jan.
[Is] ISSN:1090-2414
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The aim of the present study was to explore the effect of exogenous application of castasterone (CS) on physiologic and biochemical responses in Brassica juncea seedlings under copper (Cu) stress. Seeds were pre-soaked in different concentrations of CS and grown for 7 days under various levels of Cu. The exposure of B. juncea to higher levels of Cu led to decrease of morphologic parameters, with partial recovery of length and fresh weight in the CS pre-treated seedlings. Metal content was high in both roots and shoots under Cu exposure while the CS pre-treatment reduced the metal uptake. Accumulation of hydrogen peroxide (H O ) and superoxide anion radical (O ) were chosen as stress biomarker and higher levels of H O (88.89%) and O (62.11%) showed the oxidative stress in metal treated B. juncea seedlings, however, CS pre-treatment reduced ROS accumulation in Cu-exposed seedlings. The Cu exposures lead to enhance the plant's enzymatic and non-enzymatic antioxidant system. It was observed that enzymatic activities of ascorbate peroxidase (APOX), dehydroascorbate reductase (DHAR), and glutathione reductase (GR), glutathione perxoidase (GPOX) and gultrathione-s-transferase increased while activity of monodehydroascorbate reductase (MDHAR) decreased under Cu stress. The pre-treatment with CS positively affected the activities of enzymes. RT-PCR analysis showed that mRNA transcript levels were correlated with total enzymatic activity of DHAR, GR, GST and GSH. Increase in the gene expression of DHAR (1.85 folds), GR (3.24 folds), GST-1 (2.00 folds) and GSH-S (3.18 folds) was noticed with CS pre-treatment. Overall, the present study shows that Cu exposure induced severe oxidative stress in B. juncea plants and exogenous application of CS improved antioxidative defense system by modulating the ascorbate-glutathione cycle and amino acid metabolism.
[Mh] Termos MeSH primário: Antioxidantes/metabolismo
Colestanóis/farmacologia
Cobre/toxicidade
Mostardeira/efeitos dos fármacos
Estresse Oxidativo/efeitos dos fármacos
Poluentes do Solo/toxicidade
[Mh] Termos MeSH secundário: Aminoácidos/metabolismo
Cobre/metabolismo
Relação Dose-Resposta a Droga
Expressão Gênica/efeitos dos fármacos
Peróxido de Hidrogênio/metabolismo
Mostardeira/enzimologia
Mostardeira/genética
Poluentes do Solo/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Antioxidants); 0 (Cholestanols); 0 (Soil Pollutants); 789U1901C5 (Copper); 80736-41-0 (castasterone); BBX060AN9V (Hydrogen Peroxide)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170925
[St] Status:MEDLINE


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[PMID]:28452222
[Au] Autor:Zhu Y; Serra A; Guo T; Park JE; Zhong Q; Sze SK
[Ad] Endereço:School of Biological Sciences, Nanyang Technological University , 60 Nanyang Drive 637551, Singapore.
[Ti] Título:Application of Nanosecond Laser Photolysis Protein Footprinting to Study EGFR Activation by EGF in Cells.
[So] Source:J Proteome Res;16(6):2282-2293, 2017 Jun 02.
[Is] ISSN:1535-3907
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mass spectrometry-based protein footprinting emerged as a useful technology to understand protein ligand interactions in vitro. We have previously demonstrated the application of footprinting in live E. coli cells. Here, we further optimized an ultrafast laser photolysis hydroxyl radical footprinting method and applied it to study the interaction of EGF and EGFR in live mammalian cells. This method used a nanosecond laser to photochemically generate a burst of hydroxyl radicals in situ in-cell suspension to oxidize the amino acids on the protein surface. Mass spectrometric analysis of the thus modified peptides was interpreted to probe the solvent-accessible surface areas of the protein in its native biological state with and without EGF activation. Our footprinting data agreed with the two relevant EGFR crystal structures, indicating that this in-cell laser photolysis footprinting technique is a valid approach to study the structural properties of integral membrane proteins directly in the native environment.
[Mh] Termos MeSH primário: Fator de Crescimento Epidérmico/metabolismo
Pegadas de Proteínas/métodos
Receptor do Fator de Crescimento Epidérmico/metabolismo
[Mh] Termos MeSH secundário: Aminoácidos/química
Ativação Enzimática
Células HEK293
Seres Humanos
Radical Hidroxila
Lasers
Proteínas de Membrana/metabolismo
Estrutura Molecular
Oxirredução
Fotólise
Receptor do Fator de Crescimento Epidérmico/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; VALIDATION STUDIES
[Nm] Nome de substância:
0 (Amino Acids); 0 (Membrane Proteins); 3352-57-6 (Hydroxyl Radical); 62229-50-9 (Epidermal Growth Factor); EC 2.7.10.1 (EGFR protein, human); EC 2.7.10.1 (Receptor, Epidermal Growth Factor)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jproteome.7b00154


  5 / 118337 MEDLINE  
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[PMID]:29244012
[Au] Autor:Jelínek J; Skoda P; Hoksza D
[Ad] Endereço:Department of Software Engineering, Faculty of Mathematics and Physics, Charles University, Ke Karlovu 3, Prague 2, Czech Republic. jelinek@ksi.mff.cuni.cz.
[Ti] Título:Utilizing knowledge base of amino acids structural neighborhoods to predict protein-protein interaction sites.
[So] Source:BMC Bioinformatics;18(Suppl 15):492, 2017 Dec 06.
[Is] ISSN:1471-2105
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Protein-protein interactions (PPI) play a key role in an investigation of various biochemical processes, and their identification is thus of great importance. Although computational prediction of which amino acids take part in a PPI has been an active field of research for some time, the quality of in-silico methods is still far from perfect. RESULTS: We have developed a novel prediction method called INSPiRE which benefits from a knowledge base built from data available in Protein Data Bank. All proteins involved in PPIs were converted into labeled graphs with nodes corresponding to amino acids and edges to pairs of neighboring amino acids. A structural neighborhood of each node was then encoded into a bit string and stored in the knowledge base. When predicting PPIs, INSPiRE labels amino acids of unknown proteins as interface or non-interface based on how often their structural neighborhood appears as interface or non-interface in the knowledge base. We evaluated INSPiRE's behavior with respect to different types and sizes of the structural neighborhood. Furthermore, we examined the suitability of several different features for labeling the nodes. Our evaluations showed that INSPiRE clearly outperforms existing methods with respect to Matthews correlation coefficient. CONCLUSION: In this paper we introduce a new knowledge-based method for identification of protein-protein interaction sites called INSPiRE. Its knowledge base utilizes structural patterns of known interaction sites in the Protein Data Bank which are then used for PPI prediction. Extensive experiments on several well-established datasets show that INSPiRE significantly surpasses existing PPI approaches.
[Mh] Termos MeSH primário: Aminoácidos
Bases de Conhecimento
Mapeamento de Interação de Proteínas/métodos
Proteínas
Software
[Mh] Termos MeSH secundário: Aminoácidos/química
Aminoácidos/metabolismo
Biologia Computacional
Bases de Dados de Proteínas
Modelos Estatísticos
Proteínas/química
Proteínas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Proteins)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180307
[Lr] Data última revisão:
180307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171216
[St] Status:MEDLINE
[do] DOI:10.1186/s12859-017-1921-4


  6 / 118337 MEDLINE  
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[PMID]:29486760
[Au] Autor:Ji Y; Rong X; Lu Y
[Ad] Endereço:Department of Ophthalmology and Eye Institute, Eye and ENT Hospital of Fudan University, Key Laboratory of Myopia of State Health Ministry, and Key Laboratory of Visual Impairment and Restoration of Shanghai, No. 83 Fenyang Road, Shanghai, 200031, China.
[Ti] Título:Metabolic characterization of human aqueous humor in the cataract progression after pars plana vitrectomy.
[So] Source:BMC Ophthalmol;18(1):63, 2018 Feb 27.
[Is] ISSN:1471-2415
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: While pars plana vitrectomy (PPV) has become the third most commonly performed surgery in the world, it can also induce multiple post complications easily. Among them, cataract progression is the most frequent one that can lead to blindness eventually. METHODS: To understand the underlying mechanisms of post PPV cataract progression, we performed comprehensive metabolic characterization of aqueous humor (AH) samples from 20 cataract patients (10 post PPV complication and 10 none PPV cataract) by a non-targeted metabolomic analysis using gas chromatography combined with time-of-flight mass spectrometer (GC/TOF MS). RESULTS: A total of 263 metabolites were identified and eight of them are determined to be significantly different (VIP ≥ 1 and p ≤ 0.05) between post PPV group and none PPV control group. The significantly changed metabolites included glutaric acid and pelargonic acid that play key roles in the regulation of oxidative stress and inflammatory responses. Furthermore, we constructed a metabolic regulatory network in each group based on metabolite-metabolite correlations, which reveals key metabolic pathways and regulatory elements including amino acids and lipids metabolisms that are related to cataract progression. CONCLUSIONS: Altogether, this work discovered some potential metabolite biomarkers for post PPV cataract diagnostics, as well as casted some novel insights into the underlying mechanisms of cataract progression after PPV.
[Mh] Termos MeSH primário: Humor Aquoso/metabolismo
Catarata/metabolismo
Vitrectomia/efeitos adversos
[Mh] Termos MeSH secundário: Idoso
Aminoácidos/metabolismo
Metabolismo dos Carboidratos/fisiologia
Carboidratos
Estudos de Casos e Controles
Catarata/etiologia
Progressão da Doença
Feminino
Seres Humanos
Metabolismo dos Lipídeos/fisiologia
Masculino
Meia-Idade
Análise de Regressão
Acuidade Visual
Vitrectomia/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Carbohydrates)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180307
[Lr] Data última revisão:
180307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180301
[St] Status:MEDLINE
[do] DOI:10.1186/s12886-018-0729-y


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[PMID]:29187139
[Au] Autor:Calyseva J; Vihinen M
[Ad] Endereço:Protein Structure and Bioinformatics, Department of Experimental Medical Science, Lund University, BMC B13, SE-22 184, Lund, Sweden.
[Ti] Título:PON-SC - program for identifying steric clashes caused by amino acid substitutions.
[So] Source:BMC Bioinformatics;18(1):531, 2017 Nov 29.
[Is] ISSN:1471-2105
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Amino acid substitutions due to DNA nucleotide replacements are frequently disease-causing because of affecting functionally important sites. If the substituting amino acid does not fit into the protein, it causes structural alterations that are often harmful. Clashes of amino acids cause local or global structural changes. Testing structural compatibility of variations has been difficult due to the lack of a dedicated method that could handle vast amounts of variation data produced by next generation sequencing technologies. RESULTS: We developed a method, PON-SC, for detecting protein structural clashes due to amino acid substitutions. The method utilizes side chain rotamer library and tests whether any of the common rotamers can be fitted into the protein structure. The tool was tested both with variants that cause and do not cause clashes and found to have accuracy of 0.71 over five test datasets. CONCLUSIONS: We developed a fast method for residue side chain clash detection. The method provides in addition to the prediction also visualization of the variant in three dimensional structure.
[Mh] Termos MeSH primário: Aminoácidos/química
Proteínas/química
Software
[Mh] Termos MeSH secundário: Algoritmos
Substituição de Aminoácidos
Aminoácidos/metabolismo
Bases de Dados de Proteínas
Conformação Proteica
Engenharia de Proteínas/métodos
Proteínas/genética
Proteínas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Proteins)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE
[do] DOI:10.1186/s12859-017-1947-7


  8 / 118337 MEDLINE  
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[PMID]:29339755
[Au] Autor:Rout SK; Friedmann MP; Riek R; Greenwald J
[Ad] Endereço:Laboratory of Physical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 2, 8093, Zürich, Switzerland.
[Ti] Título:A prebiotic template-directed peptide synthesis based on amyloids.
[So] Source:Nat Commun;9(1):234, 2018 01 16.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The prebiotic replication of information-coding molecules is a central problem concerning life's origins. Here, we report that amyloids composed of short peptides can direct the sequence-selective, regioselective and stereoselective condensation of amino acids. The addition of activated DL-arginine and DL-phenylalanine to the peptide RFRFR-NH in the presence of the complementary template peptide Ac-FEFEFEFE-NH yields the isotactic product FRFRFRFR-NH , 1 of 64 possible triple addition products, under conditions in which the absence of template yields only single and double additions of mixed stereochemistry. The templating mechanism appears to be general in that a different amyloid formed by (Orn)V(Orn)V(Orn)V(Orn)V-NH and Ac-VDVDVDVDV-NH is regioselective and stereoselective for N-terminal, L-amino-acid addition while the ornithine-valine peptide alone yields predominantly sidechain condensation products with little stereoselectivity. Furthermore, the templating reaction is stable over a wide range of pH (5.6-8.6), salt concentration (0-4 M NaCl), and temperature (25-90 °C), making the amyloid an attractive model for a prebiotic peptide replicating system.
[Mh] Termos MeSH primário: Aminoácidos/química
Amiloide/química
Técnicas de Química Sintética/métodos
Peptídeos/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Aminoácidos/genética
Aminoácidos/metabolismo
Amiloide/metabolismo
Amiloide/ultraestrutura
Arginina/química
Arginina/genética
Arginina/metabolismo
Concentração de Íons de Hidrogênio
Microscopia Eletrônica
Origem da Vida
Biossíntese Peptídica/genética
Peptídeos/genética
Peptídeos/metabolismo
Fenilalanina/química
Fenilalanina/genética
Fenilalanina/metabolismo
Cloreto de Sódio/química
Estereoisomerismo
Temperatura Ambiente
Moldes Genéticos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Acids); 0 (Amyloid); 0 (Peptides); 451W47IQ8X (Sodium Chloride); 47E5O17Y3R (Phenylalanine); 94ZLA3W45F (Arginine)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02742-3


  9 / 118337 MEDLINE  
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[PMID]:28460466
[Au] Autor:Mesclon F; Lambert-Langlais S; Carraro V; Parry L; Hainault I; Jousse C; Maurin AC; Bruhat A; Fafournoux P; Averous J
[Ad] Endereço:Université Clermont Auvergne, INRA, UNH, Unité de Nutrition Humaine, CRNH Auvergne, F-63000 Clermont-Ferrand, France.
[Ti] Título:Decreased ATF4 expression as a mechanism of acquired resistance to long-term amino acid limitation in cancer cells.
[So] Source:Oncotarget;8(16):27440-27453, 2017 Apr 18.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The uncontrolled growth of tumor can lead to the formation of area deprived in nutrients. Due to their high genetic instability, tumor cells can adapt and develop resistance to this pro-apoptotic environment. Among the resistance mechanisms, those involved in the resistance to long-term amino acid restriction are not elucidated. A long-term amino acid restriction is particularly deleterious since nine of them cannot be synthetized by the cells. In order to determine how cancer cells face a long-term amino acid deprivation, we developed a cell model selected for its capacity to resist a long-term amino acid limitation. We exerted a selection pressure on mouse embryonic fibroblast to isolate clones able to survive with low amino acid concentration. The study of several clones revealed an alteration of the eiF2α/ATF4 pathway. Compared to the parental cells, the clones exhibited a decreased expression of the transcription factor ATF4 and its target genes. Likewise, the knock-down of ATF4 in parental cells renders them resistant to amino acid deprivation. Moreover, this association between a low level of ATF4 protein and the resistance to amino acid deprivation was also observed in the cancer cell line BxPC-3. This resistance was abolished when ATF4 was overexpressed. Therefore, decreasing ATF4 expression may be one important mechanism for cancer cells to survive under prolonged amino acid deprivation.
[Mh] Termos MeSH primário: Fator 4 Ativador da Transcrição/genética
Aminoácidos/metabolismo
Regulação Neoplásica da Expressão Gênica
[Mh] Termos MeSH secundário: Fator 4 Ativador da Transcrição/metabolismo
Animais
Apoptose/genética
Linhagem Celular
Proliferação Celular/efeitos dos fármacos
Perfilação da Expressão Gênica
Seres Humanos
Alvo Mecanístico do Complexo 1 de Rapamicina/metabolismo
Camundongos
Modelos Biológicos
Neoplasias/genética
Neoplasias/metabolismo
Ligação Proteica
Proteínas Serina-Treonina Quinases/metabolismo
Interferência de RNA
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 145891-90-3 (Activating Transcription Factor 4); EC 2.7.11.1 (EIF2AK4 protein, human); EC 2.7.11.1 (Mechanistic Target of Rapamycin Complex 1); EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.15828


  10 / 118337 MEDLINE  
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[PMID]:28521524
[Au] Autor:Roggatz CC; González-Wangüemert M; Pereira H; Vizetto-Duarte C; Rodrigues MJ; Barreira L; da Silva MM; Varela J; Custódio L
[Ad] Endereço:a Faculty of Sciences and Technology, Center of Marine Sciences (CCMAR) , University of Algarve , Faro , Portugal.
[Ti] Título:A first glance into the nutritional properties of the sea cucumber Parastichopus regalis from the Mediterranean Sea (SE Spain).
[So] Source:Nat Prod Res;32(1):116-120, 2018 Jan.
[Is] ISSN:1478-6427
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:This work reports for the first time the nutritional profile, including proximate chemical composition, amino acids, fatty acids and minerals of Parastichopus regalis from the Mediterranean Sea (SE Spain). The studied species had a high moisture content, moderate protein and low lipid levels. The most abundant amino acids were glutamic acid, arginine and tyrosine. Polyunsaturated fatty acids, especially arachidonic acid, dominated the fatty acid profile. Iron, sodium, calcium and zinc were the most abundant mine rals. In general, P. regalis has a balanced nutritional quality suitable for human consumption.
[Mh] Termos MeSH primário: Aminoácidos/análise
Ácidos Graxos/análise
Minerais/análise
Valor Nutritivo
Pepinos-do-Mar/química
[Mh] Termos MeSH secundário: Animais
Ácidos Graxos Insaturados/análise
Mar Mediterrâneo
Espanha
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Fatty Acids); 0 (Fatty Acids, Unsaturated); 0 (Minerals)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180301
[Lr] Data última revisão:
180301
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170520
[St] Status:MEDLINE
[do] DOI:10.1080/14786419.2017.1331224



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