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  1 / 79515 MEDLINE  
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[PMID]:29422671
[Au] Autor:Li C; Zhang B; Chen B; Ji L; Yu H
[Ad] Endereço:Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, 117543, Singapore.
[Ti] Título:Site-specific phosphorylation of TRANSPARENT TESTA GLABRA1 mediates carbon partitioning in Arabidopsis seeds.
[So] Source:Nat Commun;9(1):571, 2018 02 08.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Seed development is dependent on nutrients, such as a source of carbon, supplied by the parent plant. It remains largely unknown how these nutrients are distributed to zygotic and maternal tissues to coordinate storage of reserve compounds and development of protective tissues like seed coat. Here we show that phosphorylation of TRANSPARENT TESTA GLABRA1 (TTG1) is regulated by SHAGGY-like kinases 11/12 (SK11/12) and that this mediates carbon flow to fatty acid synthesis and seed coat traits in Arabidopsis seeds. SK11/12 phosphorylate TTG1 at serine 215, thus preventing TTG1 interaction with TRANSPARENT TESTA2. This compromises recruitment of TTG1 to the GLABRA2 locus and downregulates GLABRA2 expression, which enhances biosynthesis of fatty acids in the embryo, but reduces production of mucilage and flavonoid pigments in the seed coat. Therefore, site-specific phosphorylation of TTG1 by SK11/SK12 regulates carbon partitioning between zygotic and maternal sinks in seeds.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/genética
Arabidopsis/genética
Carbono/metabolismo
Regulação da Expressão Gênica de Plantas
Sementes/genética
[Mh] Termos MeSH secundário: Arabidopsis/crescimento & desenvolvimento
Arabidopsis/metabolismo
Proteínas de Arabidopsis/metabolismo
Ácidos Graxos/biossíntese
Flavonoides/biossíntese
Regulação da Expressão Gênica no Desenvolvimento
Quinase 3 da Glicogênio Sintase/genética
Quinase 3 da Glicogênio Sintase/metabolismo
Isoenzimas/genética
Isoenzimas/metabolismo
Mutação
Fenótipo
Fosforilação
Mucilagem Vegetal/biossíntese
Sementes/crescimento & desenvolvimento
Sementes/metabolismo
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Fatty Acids); 0 (Flavonoids); 0 (Isoenzymes); 0 (Plant Mucilage); 0 (TTG1 protein, Arabidopsis); 0 (TTG2 protein, Arabidopsis); 0 (Transcription Factors); 7440-44-0 (Carbon); EC 2.7.11.26 (ATSK11 protein, Arabidopsis); EC 2.7.11.26 (Glycogen Synthase Kinase 3)
[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:180210
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-018-03013-5


  2 / 79515 MEDLINE  
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[PMID]:29422501
[Au] Autor:Collopy LC; Ware TL; Goncalves T; Í Kongsstovu S; Yang Q; Amelina H; Pinder C; Alenazi A; Moiseeva V; Pearson SR; Armstrong CA; Tomita K
[Ad] Endereço:Chromosome Maintenance Group, UCL Cancer Institute, University College London, London, WC1E 6DD, UK.
[Ti] Título:LARP7 family proteins have conserved function in telomerase assembly.
[So] Source:Nat Commun;9(1):557, 2018 02 08.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Understanding the intricacies of telomerase regulation is crucial due to the potential health benefits of modifying its activity. Telomerase is composed of an RNA component and reverse transcriptase. However, additional factors required during biogenesis vary between species. Here we have identified fission yeast Lar7 as a member of the conserved LARP7 family, which includes the Tetrahymena telomerase-binding protein p65 and human LARP7. We show that Lar7 has conserved RNA-recognition motifs, which bind telomerase RNA to protect it from exosomal degradation. In addition, Lar7 is required to stabilise the association of telomerase RNA with the protective complex LSm2-8, and telomerase reverse transcriptase. Lar7 remains a component of the mature telomerase complex and is required for telomerase localisation to the telomere. Collectively, we demonstrate that Lar7 is a crucial player in fission yeast telomerase biogenesis, similarly to p65 in Tetrahymena, and highlight the LARP7 family as a conserved factor in telomere maintenance.
[Mh] Termos MeSH primário: Proteínas Nucleares/genética
Fosfoproteínas/genética
Proteínas de Protozoários/genética
RNA Fúngico/genética
DNA Polimerase Dirigida por RNA/genética
RNA/genética
Ribonucleoproteínas/genética
Schizosaccharomyces/genética
Telomerase/genética
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Sequência Conservada
Expressão Gênica
Seres Humanos
Isoenzimas/genética
Isoenzimas/metabolismo
Proteínas Nucleares/metabolismo
Fosfoproteínas/metabolismo
Ligação Proteica
Proteínas de Protozoários/metabolismo
RNA/metabolismo
Estabilidade de RNA
RNA Fúngico/metabolismo
DNA Polimerase Dirigida por RNA/metabolismo
Ribonucleoproteínas/metabolismo
Schizosaccharomyces/metabolismo
Telomerase/metabolismo
Telômero/química
Telômero/ultraestrutura
Tetrahymena thermophila/genética
Tetrahymena thermophila/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Isoenzymes); 0 (Larp7 protein, human); 0 (Nuclear Proteins); 0 (Pdd1 protein, Tetrahymena); 0 (Phosphoproteins); 0 (Protozoan Proteins); 0 (RNA, Fungal); 0 (Ribonucleoproteins); 0 (Ter1 telomerase subunit, S pombe); 63231-63-0 (RNA); EC 2.7.7.49 (RNA-Directed DNA Polymerase); EC 2.7.7.49 (Telomerase)
[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:180210
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02296-4


  3 / 79515 MEDLINE  
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[PMID]:29381398
[Au] Autor:Orywal K; Jelski W; Werel T; Szmitkowski M
[Ad] Endereço:a Department of Biochemical Diagnostics , Medical University , Bialystok , Podlaskie , Poland.
[Ti] Título:The Activity of Class I-IV Alcohol Dehydrogenase Isoenzymes and Aldehyde Dehydrogenase in Bladder Cancer Cells.
[So] Source:Cancer Invest;36(1):66-72, 2018 Jan 02.
[Is] ISSN:1532-4192
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:OBJECTIVES: The aim of this study was to determine the differences in the activity of Alcohol Dehydrogenase (ADH) isoenzymes and Aldehyde Dehydrogenase (ALDH) in normal and cancerous bladder cells. METHODS: Class III, IV of ADH and total ADH activity were measured by the photometric method and class I, II ADH and ALDH activity by the fluorometric method. RESULTS: Significantly higher total activity of ADH was found in both, low-grade and high-grade bladder cancer, in comparison to healthy tissues. CONCLUSION: The increased activity of total ADH in bladder cancer cells may be the cause of metabolic disorders in cancer cells, which may intensify carcinogenesis.
[Mh] Termos MeSH primário: Álcool Desidrogenase/metabolismo
Aldeído Desidrogenase/metabolismo
Isoenzimas/metabolismo
Neoplasias da Bexiga Urinária/metabolismo
[Mh] Termos MeSH secundário: Adulto
Idoso
Idoso de 80 Anos ou mais
Carcinogênese/metabolismo
Feminino
Seres Humanos
Masculino
Meia-Idade
Bexiga Urinária/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Isoenzymes); EC 1.1.1.1 (Alcohol Dehydrogenase); EC 1.2.1.3 (Aldehyde Dehydrogenase)
[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:180131
[St] Status:MEDLINE
[do] DOI:10.1080/07357907.2017.1422511


  4 / 79515 MEDLINE  
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[PMID]:29386454
[Au] Autor:Matsumoto A
[Ad] Endereço:Department of Social Medicine, Saga University School of Medicine.
[Ti] Título:[Importance of an Aldehyde Dehydrogenase 2 Polymorphism in Preventive Medicine].
[So] Source:Nihon Eiseigaku Zasshi;73(1):9-20, 2018.
[Is] ISSN:1882-6482
[Cp] País de publicação:Japan
[La] Idioma:jpn
[Ab] Resumo:Unlike genetic alterations in other aldehyde dehydrogenase (ALDH) isozymes, a defective ALDH2 polymorphism (rs671), which is carried by almost half of East Asians, does not show a clear phenotype such as a shortened life span. However, impacts of a defective ALDH2 allele, ALDH2*2, on various disease risks have been reported. As ALDH2 is responsible for the detoxification of endogenous aldehydes, a negative effect of this polymorphism is predicted, but bidirectional effects have been actually observed and the mechanisms underlying such influences are often complex. One reason for this complexity may be the existence of compensatory aldehyde detoxification systems and the secondary effects of these systems. There are many issues to be addressed with regard to the ALDH2 polymorphism in the field of preventive medicine, including the following concerns. First, ALDH2 in the fetal stage plays a role in aldehyde detoxification; therefore, prenatal health effects of environmental aldehyde exposure are of concern for ALDH2*2-carrying fetuses. Second, ALDH2*2 carriers are at high risk of drinking-related cancers. However, their drinking habits result in less worsening of physiological findings, such as energy metabolism index and liver functions, compared with non-ALDH2*2 carriers, and therefore opportunities to detect excessive drinking can be lost. Third, personalized medicine such as personalized prescriptions for ALDH2*2 carriers will be required in the clinical setting, and accumulation of evidence is awaited. Lastly, since the ALDH2 polymorphism is not considered in workers' limits of exposure to aldehydes and their precursors, efforts to lower exposure levels beyond legal standards are required.
[Mh] Termos MeSH primário: Aldeído-Desidrogenase Mitocondrial/genética
Aldeído-Desidrogenase Mitocondrial/fisiologia
Aldeídos/efeitos adversos
Aldeídos/metabolismo
Estudos de Associação Genética
Inativação Metabólica/genética
Saúde do Trabalhador
Polimorfismo Genético
Medicina Preventiva
[Mh] Termos MeSH secundário: Consumo de Bebidas Alcoólicas/genética
Feminino
Heterozigoto
Seres Humanos
Isoenzimas/genética
Isoenzimas/fisiologia
Estilo de Vida
Exposição Materna/efeitos adversos
Troca Materno-Fetal
Exposição Ocupacional/efeitos adversos
Exposição Ocupacional/prevenção & controle
Gravidez
Risco
Estresse Fisiológico
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Aldehydes); 0 (Isoenzymes); EC 1.2.1.3 (ALDH2 protein, human); EC 1.2.1.3 (Aldehyde Dehydrogenase, Mitochondrial)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180228
[Lr] Data última revisão:
180228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180202
[St] Status:MEDLINE
[do] DOI:10.1265/jjh.73.9


  5 / 79515 MEDLINE  
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[PMID]:29441928
[Au] Autor:Wang Y; Nie W; Yao K; Wang Z; He H
[Ti] Título:Interleukin 6 induces expression of NADPH oxidase 2 in human aortic endothelial cells via long noncoding RNA MALAT1.
[So] Source:Pharmazie;71(10):592-597, 2016 Oct 01.
[Is] ISSN:0031-7144
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Human abdominal aortic aneurysm (AAA) is characterized by the induction of intracellular and extracellular inflammatory cytokines and the production of reactive oxygen species (ROS) associated with localized inflammatory responses in the vascular wall. Recent studies have shown that greater circulating levels of the proinflammatory cytokine interleukin-6 (IL-6) are closely associated with AAA presence, suggesting that IL-6 plays an important role in the development of AAA. Previous in vivo studies have indicated that excess activities of NADPH oxidase (NOX), a major oxidase system for ROS production, promote AAA development. Furthermore, long noncoding RNAs (lncRNAs) are involved in the development of AAA. LncRNA MALAT1 has been found closely involved in endothelial cell functions and dysfunctions. In the present study, we explored the effects and the underlying mechanisms of IL-6 and MALAT1 on the expression/activity of NOXs in human aortic endothelial cells (HAOECs). Primary HAOECs with or without overexpression or knockdown of MALTA1 were cultured in the presence of IL-6. We found that IL-6 concentration- and time-dependently elevated the NOX activity as well as the MALAT1 level in HAOECs. Among different NOXs, only NOX2 was induced by IL-6. Overexpression and knockdown of MALAT1 respectively augmented and abolished IL6-induced expression of NOX2, NOX activity/cellular ROS production, and activation of the human NOX2 gene promoter, whereas MALAT1 alone in the absence of IL-6 treatment showed no significant effect. Knockdown of extracellular signal-regulated kinase (ERK) abolished IL6-induced expression of MALAT1. In conclusion, this study provides the first evidence that IL-6 induces expression/activity of NOX2 in HAOECs via inducing MALAT1 by an ERK-dependent mechanism. It adds new insights into the molecular mechanisms underlying AAA development.
[Mh] Termos MeSH primário: Células Endoteliais/metabolismo
Interleucina-6/farmacologia
NADPH Oxidase 2/biossíntese
RNA Longo não Codificante/genética
[Mh] Termos MeSH secundário: Aorta Torácica/citologia
Aorta Torácica/efeitos dos fármacos
Células Endoteliais/efeitos dos fármacos
Técnicas de Silenciamento de Genes
Seres Humanos
Isoenzimas/genética
Isoenzimas/metabolismo
Sistema de Sinalização das MAP Quinases/efeitos dos fármacos
NADPH Oxidase 2/genética
Cultura Primária de Células
Processamento de Proteína Pós-Traducional
RNA Longo não Codificante/farmacologia
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (IL6 protein, human); 0 (Interleukin-6); 0 (Isoenzymes); 0 (MALAT1 long non-coding RNA, human); 0 (RNA, Long Noncoding); 0 (Reactive Oxygen Species); EC 1.6.3.- (CYBB protein, human); EC 1.6.3.- (NADPH Oxidase 2)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180215
[St] Status:MEDLINE
[do] DOI:10.1691/ph.2016.6598


  6 / 79515 MEDLINE  
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[PMID]:29441922
[Au] Autor:Sienkiewicz B; Hurkacz M; Kuriata-Kordek M; Augustyniak-Bartosik H; Wiela-Hojenska A; Klinger M
[Ti] Título:The impact of CYP3A5 on the metabolism of cyclosporine A and tacrolimus in the evaluation of efficiency and safety of immunosuppressive treatment in patients after kidney transplantation.
[So] Source:Pharmazie;71(10):562-565, 2016 Oct 01.
[Is] ISSN:0031-7144
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The aim of the study was to determine the impact of CYP3A5 mutation on the serum levels of immunosuppressive drugs (tacrolimus and cyclosporine A), and on the occurrence of acute rejection episodes among patients after kidney transplantation. A limited number of such research in Polish patients was also an important factor encouraging to perform the study. Fifty-two persons were recruited. The tested patients underwent kidney transplantation and were treated either with cyclosporine A (17 persons) or with tacrolimus (35 persons). The group included 21 women and 31 men. DNA was isolated from whole blood and a modified Van Schaik et al. (2002) PCR-RFLP method was used for genotyping. The serum levels were controlled at the 7th, 14th, 30th, 90th, 180th and 360th day after transplantation. The CYP3A5 genotype had no impact on the concentrations of cyclosporine A and tacrolimus at any investigated time point. No correlation between the rate of acute rejection episodes and different genotypes of the CYP3A5 isoenzyme could be proven.
[Mh] Termos MeSH primário: Ciclosporina/metabolismo
Ciclosporina/uso terapêutico
Citocromo P-450 CYP3A/metabolismo
Imunossupressores/metabolismo
Imunossupressores/uso terapêutico
Transplante de Rim/métodos
Tacrolimo/metabolismo
Tacrolimo/uso terapêutico
[Mh] Termos MeSH secundário: Ciclosporina/efeitos adversos
Citocromo P-450 CYP3A/genética
DNA/genética
Feminino
Genótipo
Rejeição de Enxerto/genética
Rejeição de Enxerto/prevenção & controle
Seres Humanos
Imunossupressores/efeitos adversos
Isoenzimas/genética
Isoenzimas/metabolismo
Masculino
Mutação
Polônia
Reação em Cadeia da Polimerase
Polimorfismo de Fragmento de Restrição/genética
Tacrolimo/efeitos adversos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Immunosuppressive Agents); 0 (Isoenzymes); 83HN0GTJ6D (Cyclosporine); 9007-49-2 (DNA); EC 1.14.14.1 (CYP3A5 protein, human); EC 1.14.14.1 (Cytochrome P-450 CYP3A); WM0HAQ4WNM (Tacrolimus)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180215
[St] Status:MEDLINE
[do] DOI:10.1691/ph.2016.6717


  7 / 79515 MEDLINE  
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[PMID]:29338035
[Au] Autor:Bradai M; Mahjoubi H; Chini A; Chabouté ME; Hanin M; Ebel C
[Ad] Endereço:Laboratory of Biotechnology and Plant Improvement, Center of Biotechnology of Sfax, Sfax, Tunisia.
[Ti] Título:Genome wide identification of wheat and Brachypodium type one protein phosphatases and functional characterization of durum wheat TdPP1a.
[So] Source:PLoS One;13(1):e0191272, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Reversible phosphorylation is an essential mechanism regulating signal transduction during development and environmental stress responses. An important number of dephosphorylation events in the cell are catalyzed by type one protein phosphatases (PP1), which catalytic activity is driven by the binding of regulatory proteins that control their substrate specificity or subcellular localization. Plants harbor several PP1 isoforms accounting for large functional redundancies. While animal PP1s were reported to play relevant roles in controlling multiple cellular processes, plant orthologs remain poorly studied. To decipher the role of plant PP1s, we compared PP1 genes from three monocot species, Brachypodium, common wheat and rice at the genomic and transcriptomic levels. To gain more insight into the wheat PP1 proteins, we identified and characterized TdPP1a, the first wheat type one protein phosphatase from a Tunisian durum wheat variety Oum Rabiaa3. TdPP1a is highly conserved in sequence and structure when compared to mammalian, yeast and other plant PP1s. We demonstrate that TdPP1a is an active, metallo-dependent phosphatase in vitro and is able to interact with AtI2, a typical regulator of PP1 functions. Also, TdPP1a is capable to complement the heat stress sensitivity of the yeast mutant indicating that TdPP1a is functional also in vivo. Moreover, transient expression of TdPP1a::GFP in tobacco leaves revealed that it is ubiquitously distributed within the cell, with a strong accumulation in the nucleus. Finally, transcriptional analyses showed similar expression levels in roots and leaves of durum wheat seedlings. Interestingly, the expression in leaves is significantly induced following salinity stress, suggesting a potential role of TdPP1a in wheat salt stress response.
[Mh] Termos MeSH primário: Brachypodium/enzimologia
Brachypodium/genética
Fosfoproteínas Fosfatases/genética
Proteínas de Plantas/genética
Triticum/enzimologia
Triticum/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sequência Conservada
Evolução Molecular
Regulação Enzimológica da Expressão Gênica
Regulação da Expressão Gênica de Plantas
Isoenzimas/genética
Isoenzimas/metabolismo
Oryza/enzimologia
Oryza/genética
Fosfoproteínas Fosfatases/metabolismo
Filogenia
Proteínas de Plantas/metabolismo
Proteína Fosfatase 1/genética
Proteína Fosfatase 1/metabolismo
Homologia de Sequência de Aminoácidos
Especificidade da Espécie
Estresse Fisiológico
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Isoenzymes); 0 (Plant Proteins); EC 3.1.3.16 (Phosphoprotein Phosphatases); EC 3.1.3.16 (Protein Phosphatase 1)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180117
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191272


  8 / 79515 MEDLINE  
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[PMID]:29198706
[Au] Autor:Kim S; Kim KJ
[Ad] Endereço:School of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University, Daehak-ro 80, Buk-ku, Daegu, 41566, Republic of Korea; KNU Institute for Microorganisms, Kyungpook National University, Daehak-ro 80, Buk-ku, Daegu, 41566, Republic of Korea.
[Ti] Título:Structural insight into the substrate specificity of acyl-CoA oxidase1 from Yarrowia lipolytica for short-chain dicarboxylyl-CoAs.
[So] Source:Biochem Biophys Res Commun;495(2):1628-1634, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acyl-CoA oxidase (ACOX) plays an important role in fatty acid degradation. The enzyme catalyzes the first reaction in peroxisomal fatty acid ß-oxidation by reducing acyl-CoA to 2-trans-enoyl-CoA. The yeast Yarrowia lipolytica is able to utilize fatty acids, fats, and oil as carbon sources to produce valuable bioproducts. We determined the crystal structure of ACOX1 from Y. lipolytica (YlACOX1) at a resolution of 2.5 Å. YlACOX1 forms a homodimer, and the monomeric structure is composed of four domains, the Nα, Nß, Cα1, and Cα2. The FAD cofactor is bound at the dimerization interface between the Nß- and Cα1-domains. The substrate-binding tunnel formed by the interface between the Nα-, Nß-, and Cα1-domains is located proximal to FAD. Amino acid and structural comparisons of YlACOX1 with other ACOXs show that the substrate-binding pocket of YlACOX1 is much smaller than that of the medium- or long-chain ACOXs but is rather similar to that of the short-chain ACOXs. Moreover, the hydrophilicity of residues constituting the end region of the substrate-binding pocket in YlACOX1 is quite similar to those in the short-chain ACOXs but different from those of the medium- or long-chain ACOXs. These observations provide structural insights how YlACOX1 prefers short-chain dicarboxylyl-CoAs as a substrate.
[Mh] Termos MeSH primário: Acil-CoA Oxidase/química
Acil-CoA Oxidase/metabolismo
Proteínas Fúngicas/química
Proteínas Fúngicas/metabolismo
Yarrowia/enzimologia
[Mh] Termos MeSH secundário: Acil Coenzima A/química
Acil Coenzima A/metabolismo
Acil-CoA Oxidase/genética
Sequência de Aminoácidos
Domínio Catalítico
Cristalografia por Raios X
Flavina-Adenina Dinucleotídeo/metabolismo
Proteínas Fúngicas/genética
Interações Hidrofóbicas e Hidrofílicas
Isoenzimas/química
Isoenzimas/genética
Isoenzimas/metabolismo
Modelos Moleculares
Estrutura Quaternária de Proteína
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
Yarrowia/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Fungal Proteins); 0 (Isoenzymes); 146-14-5 (Flavin-Adenine Dinucleotide); EC 1.3.3.6 (Acyl-CoA Oxidase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE


  9 / 79515 MEDLINE  
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[PMID]:29307824
[Au] Autor:Yan J; He H; Fang L; Zhang A
[Ad] Endereço:National Key Laboratory of Crop Genetics and Germplasm Enhancement, Nanjing Agricultural University, Nanjing, Jiangsu, 210095, China; College of Life Sciences, Nanjing Agricultural University, Nanjing, Jiangsu, 210095, China.
[Ti] Título:Pectin methylesterase31 positively regulates salt stress tolerance in Arabidopsis.
[So] Source:Biochem Biophys Res Commun;496(2):497-501, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The alteration of cell wall component and structure is an important adaption to saline environment. Pectins, a major cell wall component, are often present in a highly methylesterified form. The level of methyl esterification determined by pectin methylesterases (PMEs) influences many important wall properties that are believed to relate to the adaption to saline stress. However, little is known about the function of PMEs in response to salt stress. Here, we established a link between pectin methylesterase31 (PME31) and salt stress tolerance. Salt stress significantly increases PME31 expression. PME31 is located in the plasma membrane and the expression level of PME31 was high in dry seeds. Knock-down mutants in PME31 conferred hypersensitive phenotypes to salt stress in seed germination and post-germination growth. Real-time PCR analysis revealed that the transcript levels of several stress genes (DREB2A, RD29A and RD29B) are lower in pme31-2 mutant than that in the wild type in response to salt stress. These results suggested that PME31 could positively modulate salt stress tolerance.
[Mh] Termos MeSH primário: Arabidopsis/efeitos dos fármacos
Hidrolases de Éster Carboxílico/genética
Regulação da Expressão Gênica de Plantas
Células Vegetais/efeitos dos fármacos
Cloreto de Sódio/farmacologia
[Mh] Termos MeSH secundário: Arabidopsis/genética
Arabidopsis/metabolismo
Proteínas de Arabidopsis/genética
Proteínas de Arabidopsis/metabolismo
Hidrolases de Éster Carboxílico/metabolismo
Membrana Celular/efeitos dos fármacos
Membrana Celular/metabolismo
Parede Celular/efeitos dos fármacos
Parede Celular/metabolismo
Proteínas e Peptídeos de Choque Frio/genética
Proteínas e Peptídeos de Choque Frio/metabolismo
Germinação/efeitos dos fármacos
Isoenzimas/genética
Isoenzimas/metabolismo
Mutação
Células Vegetais/metabolismo
Salinidade
Tolerância a Sal
Sementes/efeitos dos fármacos
Sementes/genética
Sementes/metabolismo
Estresse Fisiológico
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Cold Shock Proteins and Peptides); 0 (DREB2A protein, Arabidopsis); 0 (Isoenzymes); 0 (RD29B protein, Arabidopsis); 0 (RD29a protein, Arabidopsis); 0 (Transcription Factors); 451W47IQ8X (Sodium Chloride); EC 3.1.1.- (Carboxylic Ester Hydrolases); EC 3.1.1.11 (pectinesterase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180109
[St] Status:MEDLINE


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[PMID]:28456989
[Au] Autor:Sozmen EY; Sezer ED
[Ad] Endereço:Department of Medical Biochemistry and Metabolism Laboratory, Ege University Faculty of Medicine, Izmir, Turkey. eser.sozmen@ege.edu.tr.
[Ti] Título:Methods for Determination of α-Glycosidase, ß-Glycosidase, and α-Galactosidase Activities in Dried Blood Spot Samples.
[So] Source:Methods Mol Biol;1594:255-264, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The lysosomal storage diseases (LDSs) are a heterogeneous group of inherited genetic disorders caused by defects of lysosomal proteins. The accumulation of undigested substrates from different catabolic pathways leads to cellular dysfunction. LSDs generally presents during early childhood and have a devastating impact on the families and on public health. Over the years, approaches for treatment of some LSDs have been developed with different strategies. Increasing availability of treatments of these diseases has accelerated the development of new methods and techniques for rapid diagnosis in patients with clinical indication.The use of dried blood spot (DBS) test has been proposed as a first tier test to identify patients with Gaucher, Pompe, and Fabry diseases. DBS usage is advantageous for the purpose of screening as it is non-invasive, sensitive, has low-cost and fast turnaround time compared to measurements in leucocyte and/or fibroblast culture. This chapter focuses on the activity measurement of three lysosomal enzymes (α-glucosidase, ß-glucosidase, and α galactosidase) in DBS samples by using fluorescent substrates and by the LC-MS/MS (liquid chromatography-mass spectrometry) method. All steps of the methods, from preparation of the solutions to calculation of the enzyme activity, will be explained in detail.
[Mh] Termos MeSH primário: Teste em Amostras de Sangue Seco/métodos
Doenças por Armazenamento dos Lisossomos/enzimologia
alfa-Galactosidase/sangue
alfa-Glucosidases/sangue
[Mh] Termos MeSH secundário: Seres Humanos
Recém-Nascido
Isoenzimas/sangue
Doenças por Armazenamento dos Lisossomos/sangue
Doenças por Armazenamento dos Lisossomos/diagnóstico
Triagem Neonatal
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Isoenzymes); 2HLC17MX9G (agalsidase alfa); EC 3.2.1.20 (alpha-Glucosidases); EC 3.2.1.22 (alpha-Galactosidase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170501
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-6934-0_17



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