Base de dados : MEDLINE
Pesquisa : D08.811.682.732.165 [Categoria DeCS]
Referências encontradas : 1197 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 120 ir para página                         

  1 / 1197 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29253814
[Au] Autor:Faseela P; Puthur JT
[Ad] Endereço:Plant Physiology and Biochemistry Division, Department of Botany, University of Calicut, Malappuram, Kerala 673635, India.
[Ti] Título:The imprints of the high light and UV-B stresses in Oryza sativa L. 'Kanchana' seedlings are differentially modulated.
[So] Source:J Photochem Photobiol B;178:551-559, 2018 Jan.
[Is] ISSN:1873-2682
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:High light and ultraviolet-B radiation (UV-B) are generally considered to have negative impact on photosynthesis and plant growth. The present study evaluates the tolerance potential of three cultivars of Oryza sativa L. (Kanchana, Mattatriveni and Harsha) seedlings towards high light and UV-B stress on the basis of photosynthetic pigment degradation, chlorophyll a fluorescence parameters and rate of lipid peroxidation, expressed by malondialdehyde content. Surprisingly, it was revealed that Kanchana was the most sensitive cultivar towards high light and at the same time it was the most tolerant cultivar towards UV-B stress. This contrasting feature of Kanchana towards high light and UV-B tolerance was further studied by analyzing photosystem (PS) I and II activity, mitochondrial activity, chlorophyll a fluorescence transient, enzymatic and non-enzymatic antioxidant defense system. Due to the occurrence of more PS I and PSII damages, the inhibition of photochemical efficiency and emission of dissipated energy as heat or fluorescence per PSII reaction center was higher upon high light exposure than UV-B treatments in rice seedlings of Kanchana. The mitochondrial activity was also found to be drastically altered upon high light as compared to UV-B treatments. The UV-B induced accumulation of non-enzymatic antioxidants (proline, total phenolics, sugar and ascorbate) and enzymatic antioxidants (ascorbate peroxidase, guaiacol peroxidase, superoxide dismutase and glutathione reductase) in rice seedlings than those subjected to high light exposure afforded more efficient protection against UV-B radiation in rice seedlings. Our results proved that high tolerance of Kanchana towards UV-B than high light treatments, correlated linearly with the protected photosynthetic and mitochondrial machinery which was provided by upregulation of antioxidants particularly by total phenolics, ascorbate and ascorbate peroxidase in rice seedlings. Data presented in this study conclusively proved that rice cultivar Kanchana respond to different environmental signals independently and tolerance mechanisms to individual stress factors was also varied.
[Mh] Termos MeSH primário: Oryza/efeitos da radiação
Raios Ultravioleta
[Mh] Termos MeSH secundário: Antioxidantes/metabolismo
Ascorbato Peroxidases/metabolismo
Ácido Ascórbico/metabolismo
Clorofila/química
Clorofila/metabolismo
Malondialdeído/metabolismo
Mitocôndrias/metabolismo
Mitocôndrias/efeitos da radiação
Oryza/crescimento & desenvolvimento
Fenóis/metabolismo
Fotossíntese/efeitos da radiação
Complexo de Proteína do Fotossistema I/metabolismo
Complexo de Proteína do Fotossistema II/metabolismo
Prolina/metabolismo
Plântulas/metabolismo
Plântulas/efeitos da radiação
Espectrometria de Fluorescência
Regulação para Cima/efeitos da radiação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Phenols); 0 (Photosystem I Protein Complex); 0 (Photosystem II Protein Complex); 1406-65-1 (Chlorophyll); 4Y8F71G49Q (Malondialdehyde); 9DLQ4CIU6V (Proline); EC 1.11.1.11 (Ascorbate Peroxidases); PQ6CK8PD0R (Ascorbic Acid); YF5Q9EJC8Y (chlorophyll a)
[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:171219
[St] Status:MEDLINE


  2 / 1197 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29175605
[Au] Autor:Yadav S; Mishra A; Jha B
[Ad] Endereço:Marine Biotechnology and Ecology Division, CSIR-Central Salt and Marine Chemicals Research Institute, G. B. Marg, Bhavnagar, (Gujarat), India. Electronic address: sonamyadav@csmcri.org.
[Ti] Título:Elevated CO leads to carbon sequestration by modulating C photosynthesis pathway enzyme (PPDK) in Suaeda monoica and S. fruticosa.
[So] Source:J Photochem Photobiol B;178:310-315, 2018 Jan.
[Is] ISSN:1873-2682
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The C halophytic species Suaeda monoica and S. fruticosa, possess the C photosynthesis pathway without Kranz anatomy were grown at ambient (470ppm CO ) and elevated (850ppm CO ) atmospheric CO under control containment facility to study the plant response under CO stress condition. The relative growth of both Suaeda species was enhanced with atmospheric CO enrichment compared to control (ambient) condition. The photosynthesis rate was found 2.5µmolCO m s in both species under stress condition compared to about 1.9µmolCO m s under control conditions. About 0.3molH Om s conductance was detected under an unstressed condition which decreased significantly to ~0.07molH Om s on the 6th day of stress treatment. Similarly, transpiration rate was also decreased significantly from 4.4-5.2mmolH Om s to 1.7-1.9 under stress condition. In contrast, VpdL increased significantly from 1.9kPa to 2.5kPa under stress condition. A higher total chlorophyll content observed in S. monoica (56.36mgg tissue) compared to S. fruticosa (33.12mgg tissue) under unstressed (control) condition. A significant increase was found in the total chlorophyll content of S. fruticosa (45.47mgg tissue) with stress treatment compared to control (33.12mgg tissue). In contrast, the total chlorophyll decreased in S. monoica (51.58mgg tissue) under similar stress condition compared to control plants (56.36mgg tissue). About 6-6.8mg total sugar per gram tissue found under control condition which enhanced further (7.5 to 11mgg tissue) under stress condition. Similarly, total reducing sugar (~2mgg tissue) and total starch content (6.5-11mgg tissue) increased under stress condition. About 6.5- and 3- fold higher expression of PPDK gene was observed for S. monoica and S. fruticosa, respectively under CO stress condition. PPDK (1.2- and 1.5- fold) and antioxidant enzymes; APX (12.7- and two-fold), CAT (2.2- and 6.4- fold) and SOD (4.6- and 94- fold) enhanced significantly in S. fruticosa and S. monoica, respectively under high CO stress condition compared to control plants. Overall, it was observed that PPDK enzyme plays a key role in C photosynthesis pathway and S. monoica is a potential candidate to be explored further for the saline agricultural and CO capture.
[Mh] Termos MeSH primário: Dióxido de Carbono/metabolismo
Chenopodiaceae/metabolismo
Proteínas de Plantas/metabolismo
Piruvato Ortofosfato Diquinase/metabolismo
[Mh] Termos MeSH secundário: Ascorbato Peroxidases/genética
Ascorbato Peroxidases/metabolismo
Sequestro de Carbono
Catalase/genética
Catalase/metabolismo
Chenopodiaceae/crescimento & desenvolvimento
Clorofila/metabolismo
Fotossíntese
Folhas de Planta/metabolismo
Proteínas de Plantas/genética
Piruvato Ortofosfato Diquinase/genética
Amido/metabolismo
Açúcares/metabolismo
Superóxido Dismutase/genética
Superóxido Dismutase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plant Proteins); 0 (Sugars); 1406-65-1 (Chlorophyll); 142M471B3J (Carbon Dioxide); 9005-25-8 (Starch); EC 1.11.1.11 (Ascorbate Peroxidases); EC 1.11.1.6 (Catalase); EC 1.15.1.1 (Superoxide Dismutase); EC 2.7.9.1 (Pyruvate, Orthophosphate Dikinase)
[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:171128
[St] Status:MEDLINE


  3 / 1197 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28963339
[Au] Autor:Lin Q; Liou YC
[Ad] Endereço:From the Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, 117543, Singapore dbslinqs@nus.edu.sg.
[Ti] Título:Fishing for key players in ER-mitochondrial contacts.
[So] Source:J Biol Chem;292(39):16393-16394, 2017 09 29.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Endoplasmic reticulum-mitochondrial contacts (EMCs) regulate multiple critical cellular activities, dysregulation of which correlates with various human maladies such as neurodegenerative diseases. A new study makes use of the ascorbate peroxidase proximity-labeling proteomics approach to scrutinize the components of EMCs in live cells, leading to the identification of reticulon 1A as a novel promoter of EMCs.
[Mh] Termos MeSH primário: Retículo Endoplasmático
Mitocôndrias
[Mh] Termos MeSH secundário: Animais
Ascorbato Peroxidases
Seres Humanos
Proteômica
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
EC 1.11.1.11 (Ascorbate Peroxidases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171001
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.H117.795286


  4 / 1197 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28796234
[Au] Autor:Martell JD; Deerinck TJ; Lam SS; Ellisman MH; Ting AY
[Ad] Endereço:Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.
[Ti] Título:Electron microscopy using the genetically encoded APEX2 tag in cultured mammalian cells.
[So] Source:Nat Protoc;12(9):1792-1816, 2017 Sep.
[Is] ISSN:1750-2799
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Electron microscopy (EM) is the premiere technique for high-resolution imaging of cellular ultrastructure. Unambiguous identification of specific proteins or cellular compartments in electron micrographs, however, remains challenging because of difficulties in delivering electron-dense contrast agents to specific subcellular targets within intact cells. We recently reported enhanced ascorbate peroxidase 2 (APEX2) as a broadly applicable genetic tag that generates EM contrast on a specific protein or subcellular compartment of interest. This protocol provides guidelines for designing and validating APEX2 fusion constructs, along with detailed instructions for cell culture, transfection, fixation, heavy-metal staining, embedding in resin, and EM imaging. Although this protocol focuses on EM in cultured mammalian cells, APEX2 is applicable to many cell types and contexts, including intact tissues and organisms, and is useful for numerous applications beyond EM, including live-cell proteomic mapping. This protocol, which describes procedures for sample preparation from cell monolayers and cell pellets, can be completed in 10 d, including time for APEX2 fusion construct validation, cell growth, and solidification of embedding resins. Notably, the only additional steps required relative to a standard EM sample preparation are cell transfection and a 2- to 45-min staining period with 3,3-diaminobenzidine (DAB) and hydrogen peroxide (H O ).
[Mh] Termos MeSH primário: Ascorbato Peroxidases/genética
Técnicas Citológicas/métodos
Técnicas Genéticas
Microscopia Eletrônica/métodos
Imagem Molecular/métodos
[Mh] Termos MeSH secundário: Animais
Células COS
Células Cultivadas
Estruturas Celulares/ultraestrutura
Cercopithecus aethiops
Células HEK293
Hipocampo/citologia
Seres Humanos
Ratos
Proteínas Recombinantes de Fusão/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Recombinant Fusion Proteins); EC 1.11.1.11 (Ascorbate Peroxidases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170821
[Lr] Data última revisão:
170821
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170811
[St] Status:MEDLINE
[do] DOI:10.1038/nprot.2017.065


  5 / 1197 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28760823
[Au] Autor:Cho IT; Adelmant G; Lim Y; Marto JA; Cho G; Golden JA
[Ad] Endereço:From the Department of Pathology, Brigham and Women's Hospital, and.
[Ti] Título:Ascorbate peroxidase proximity labeling coupled with biochemical fractionation identifies promoters of endoplasmic reticulum-mitochondrial contacts.
[So] Source:J Biol Chem;292(39):16382-16392, 2017 Sep 29.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:To maintain cellular homeostasis, subcellular organelles communicate with each other and form physical and functional networks through membrane contact sites coupled by protein tethers. In particular, endoplasmic reticulum (ER)-mitochondrial contacts (EMC) regulate diverse cellular activities such as metabolite exchange (Ca and lipids), intracellular signaling, apoptosis, and autophagy. The significance of EMCs has been highlighted by reports indicating that EMC dysregulation is linked to neurodegenerative diseases. Therefore, obtaining a better understanding of the physical and functional components of EMCs should provide new insights into the pathogenesis of several neurodegenerative diseases. Here, we applied engineered ascorbate peroxidase (APEX) to map the proteome at EMCs in live HEK293 cells. APEX was targeted to the outer mitochondrial membrane, and proximity-labeled proteins were analyzed by stable isotope labeling with amino acids in culture (SILAC)-LC/MS-MS. We further refined the specificity of the proteins identified by combining biochemical subcellular fractionation to the protein isolation method. We identified 405 proteins with a 2.0-fold cutoff ratio (log base 2) in SILAC quantification from replicate experiments. We performed validation screening with a Split-Rluc8 complementation assay that identified reticulon 1A (RTN1A), an ER-shaping protein localized to EMCs as an EMC promoter. Proximity mapping augmented with biochemical fractionation and additional validation methods reported here could be useful to discover other components of EMCs, identify mitochondrial contacts with other organelles, and further unravel their communication.
[Mh] Termos MeSH primário: Retículo Endoplasmático/metabolismo
Mitocôndrias/metabolismo
Proteínas do Tecido Nervoso/metabolismo
Mapeamento de Interação de Proteínas/métodos
[Mh] Termos MeSH secundário: Ascorbato Peroxidases/metabolismo
Teste de Complementação Genética
Células HEK293
Seres Humanos
Indicadores e Reagentes/metabolismo
Marcação por Isótopo
Luciferases de Renilla/genética
Luciferases de Renilla/metabolismo
Proteínas do Tecido Nervoso/química
Proteínas do Tecido Nervoso/genética
Proteínas do Tecido Nervoso/isolamento & purificação
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Projetos Piloto
Engenharia de Proteínas
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; VALIDATION STUDIES
[Nm] Nome de substância:
0 (Indicators and Reagents); 0 (Nerve Tissue Proteins); 0 (Peptide Fragments); 0 (RTN1 protein, human); 0 (Recombinant Proteins); EC 1.11.1.11 (Ascorbate Peroxidases); EC 1.13.12.5 (Luciferases, Renilla)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170802
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.795286


  6 / 1197 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28651180
[Au] Autor:Esperanza M; Houde M; Seoane M; Cid Á; Rioboo C
[Ad] Endereço:Laboratorio de Microbiología, Facultad de Ciencias, Universidade da Coruña, Campus de A Zapateira s/n 15071. A Coruña, Spain.
[Ti] Título:Does a short-term exposure to atrazine provoke cellular senescence in Chlamydomonas reinhardtii?
[So] Source:Aquat Toxicol;189:184-193, 2017 Aug.
[Is] ISSN:1879-1514
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The aim of this study was to investigate the impacts and modes of action of a chemical and nutrient deprivation on the cellular senescence process of Chlamydomonas reinhardtii. Several molecular and cellular parameters related to senescence phenomena were monitored in C. reinhardtii cells exposed for 24h to a sublethal concentration (0.25µM) of the herbicide atrazine and in unexposed 96h cells in an early stationary phase of growth. All endpoints showed the same pattern of response between treatments, except for the intracellular level of calcium, where a significant increase was observed in 24h-exposed cultures compared to 24h-log controls. Results also indicated that cell viability remained above 98% for all conditions. Reactive oxygen species (ROS) levels and caspase activity increased in all experimental cultures with respect to 24h-log controls and alterations in the nuclear morphology and cells with auto-phagosomes were observed in all treatments. However, a decrease in lipid peroxidation was detected which could be related to the observed increment of autophagic vacuoles that recycle damaged material, such as altered lipids in microalgal membranes. Furthermore, responses at the molecular level were also investigated. Gene transcription analyses, carried out by RT-qPCR technique, indicated an increase in transcripts for genes encoding glutathione S-transferase (GST) and ascorbate peroxidase (APX I) and a decrease for those encoding catalase (CAT), glutathione peroxidase (GPX) and Mn-superoxide dismutase (SOD-1) in both experimental treatments. Overall molecular and cellular results suggest that a short-term exposure to a sublethal concentration of atrazine may induce senescence features in microalgal cells which are the base of aquatic food webs.
[Mh] Termos MeSH primário: Atrazina/toxicidade
Senescência Celular/efeitos dos fármacos
Chlamydomonas reinhardtii/efeitos dos fármacos
Herbicidas/toxicidade
Poluentes Químicos da Água/toxicidade
[Mh] Termos MeSH secundário: Ascorbato Peroxidases/genética
Ascorbato Peroxidases/metabolismo
Catalase/genética
Catalase/metabolismo
Senescência Celular/genética
Chlamydomonas reinhardtii/citologia
Chlamydomonas reinhardtii/genética
Chlamydomonas reinhardtii/metabolismo
Glutationa Peroxidase/genética
Glutationa Peroxidase/metabolismo
Glutationa Transferase/genética
Glutationa Transferase/metabolismo
Peroxidação de Lipídeos/efeitos dos fármacos
Estresse Oxidativo/efeitos dos fármacos
Estresse Oxidativo/genética
Espécies Reativas de Oxigênio/metabolismo
Superóxido Dismutase/genética
Superóxido Dismutase/metabolismo
Fatores de Tempo
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Herbicides); 0 (Reactive Oxygen Species); 0 (Water Pollutants, Chemical); EC 1.11.1.11 (Ascorbate Peroxidases); EC 1.11.1.6 (Catalase); EC 1.11.1.9 (Glutathione Peroxidase); EC 1.15.1.1 (Superoxide Dismutase); EC 2.5.1.18 (Glutathione Transferase); QJA9M5H4IM (Atrazine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170627
[St] Status:MEDLINE


  7 / 1197 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28634178
[Au] Autor:Ma Z; Davidson VL
[Ad] Endereço:Burnett School of Biomedical Sciences, College of Medicine, University of Central Florida, 6900 Lake Nona Blvd, Orlando, FL 32827, U.S.A.
[Ti] Título:Ascorbate protects the diheme enzyme, MauG, against self-inflicted oxidative damage by an unusual antioxidant mechanism.
[So] Source:Biochem J;474(15):2563-2572, 2017 Jul 17.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ascorbate protects MauG from self-inactivation that occurs during the autoreduction of the reactive -Fe state of its diheme cofactor. The mechanism of protection does not involve direct reaction with reactive oxygen species in solution. Instead, it binds to MauG and mitigates oxidative damage that occurs via internal transfer of electrons from amino acid residues within the protein to the high-valent hemes. The presence of ascorbate does not inhibit the natural catalytic reaction of MauG, which catalyzes oxidative post-translational modifications of a substrate protein that binds to the surface of MauG and is oxidized by the high-valent hemes via long-range electron transfer. Ascorbate was also shown to prolong the activity of a P107V MauG variant that is more prone to inactivation. A previously unknown ascorbate peroxidase activity of MauG was characterized with a of 0.24 s and a of 2.2 µM for ascorbate. A putative binding site for ascorbate was inferred from inspection of the crystal structure of MauG and comparison with the structure of soybean ascorbate peroxidase with bound ascorbate. The ascorbate bound to MauG was shown to accelerate the rates of both electron transfers to the hemes and proton transfers to hemes which occur during the multistep autoreduction to the diferric state which is accompanied by oxidative damage. A structural basis for these effects is inferred from the putative ascorbate-binding site. This could be a previously unrecognized mechanism by which ascorbate mitigates oxidative damage to heme-dependent enzymes and redox proteins in nature.
[Mh] Termos MeSH primário: Antioxidantes/farmacologia
Ácido Ascórbico/farmacologia
Proteínas de Bactérias/metabolismo
Heme/metabolismo
Estresse Oxidativo/efeitos dos fármacos
Paracoccus denitrificans/enzimologia
[Mh] Termos MeSH secundário: Ascorbato Peroxidases/química
Ascorbato Peroxidases/metabolismo
Proteínas de Bactérias/química
Cristalografia por Raios X
Peróxido de Hidrogênio/metabolismo
Hidroxiureia/farmacologia
Indolquinonas/química
Indolquinonas/metabolismo
Ferro/metabolismo
Cinética
Proteínas Mutantes/metabolismo
Oxirredução/efeitos dos fármacos
Análise Espectral
Fatores de Tempo
Triptofano/análogos & derivados
Triptofano/química
Triptofano/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Bacterial Proteins); 0 (Indolequinones); 0 (Mutant Proteins); 134645-25-3 (tryptophan tryptophylquinone); 42VZT0U6YR (Heme); 8DUH1N11BX (Tryptophan); BBX060AN9V (Hydrogen Peroxide); E1UOL152H7 (Iron); EC 1.11.1.11 (Ascorbate Peroxidases); PQ6CK8PD0R (Ascorbic Acid); X6Q56QN5QC (Hydroxyurea)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170731
[Lr] Data última revisão:
170731
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170622
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20170349


  8 / 1197 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28589727
[Au] Autor:Chu Q; Rathore A; Diedrich JK; Donaldson CJ; Yates JR; Saghatelian A
[Ad] Endereço:Clayton Foundation Laboratories for Peptide Biology, The Salk Institute for Biological Studies , 10010 North Torrey Pines Road, La Jolla, California 92037, United States.
[Ti] Título:Identification of Microprotein-Protein Interactions via APEX Tagging.
[So] Source:Biochemistry;56(26):3299-3306, 2017 Jul 05.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Microproteins are peptides and small proteins encoded by small open reading frames (smORFs). Newer technologies have led to the recent discovery of hundreds to thousands of new microproteins. The biological functions of a few microproteins have been elucidated, and these microproteins have fundamental roles in biology ranging from limb development to muscle function, highlighting the value of characterizing these molecules. The identification of microprotein-protein interactions (MPIs) has proven to be a successful approach to the functional characterization of these genes; however, traditional immunoprecipitation methods result in the enrichment of nonspecific interactions for microproteins. Here, we test and apply an in situ proximity tagging method that relies on an engineered ascorbate peroxidase 2 (APEX) to elucidate MPIs. The results demonstrate that APEX tagging is superior to traditional immunoprecipitation methods for microproteins. Furthermore, the application of APEX tagging to an uncharacterized microprotein called C11orf98 revealed that this microprotein interacts with nucleolar proteins nucleophosmin and nucleolin, demonstrating the ability of this approach to identify novel hypothesis-generating MPIs.
[Mh] Termos MeSH primário: Ascorbato Peroxidases/metabolismo
Nucléolo Celular/metabolismo
Proteínas Nucleares/metabolismo
Fosfoproteínas/metabolismo
Engenharia de Proteínas
Proteômica/métodos
Proteínas de Ligação a RNA/metabolismo
[Mh] Termos MeSH secundário: Transporte Ativo do Núcleo Celular
Sequência de Aminoácidos
Animais
Ascorbato Peroxidases/química
Ascorbato Peroxidases/genética
Sequência Conservada
Células HEK293
Células HeLa
Hemaglutininas/química
Hemaglutininas/genética
Hemaglutininas/metabolismo
Seres Humanos
Microscopia Confocal
Microscopia de Fluorescência
Proteínas Nucleares/química
Proteínas Nucleares/genética
Oligopeptídeos/química
Oligopeptídeos/genética
Oligopeptídeos/metabolismo
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Fosfoproteínas/química
Fosfoproteínas/genética
Domínios e Motivos de Interação entre Proteínas
Proteínas de Ligação a RNA/química
Proteínas de Ligação a RNA/genética
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Alinhamento de Sequência
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; VALIDATION STUDIES
[Nm] Nome de substância:
0 (C11orf98 protein, human); 0 (Hemagglutinins); 0 (Nuclear Proteins); 0 (Oligopeptides); 0 (Peptide Fragments); 0 (Phosphoproteins); 0 (RNA-Binding Proteins); 0 (Recombinant Fusion Proteins); 0 (nucleolin); 117896-08-9 (nucleophosmin); 98849-88-8 (FLAG peptide); EC 1.11.1.11 (Ascorbate Peroxidases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170608
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00265


  9 / 1197 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28570900
[Au] Autor:Cahyanurani AB; Chiu KH; Wu TM
[Ad] Endereço:Department of Aquaculture, Fisheries and Marine Science Faculty, University of Brawijaya, Malang 65145, Indonesia; Department of Aquaculture, National Pingtung University of Science and Technology, Pingtung 91201, Taiwan.
[Ti] Título:Glutathione biosynthesis plays an important role against 4-tert-octylphenol-induced oxidative stress in Ceratophyllum demersum.
[So] Source:Chemosphere;183:565-573, 2017 Sep.
[Is] ISSN:1879-1298
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:4-tert-octylphenol (OP) is a persistent environmental pollutant with an endocrine-disrupting property. In the present study, we examined the effect of various concentrations of OP (0, 0.5, 1, 1.5, 2 and 3 mg L ) applied to an aquatic plant, the submersed macrophyte Ceratophyllum demersum. The toxic effect caused by OP inhibited the plant's growth rate, reduced total chlorophyll content and increased levels of the reactive oxygen species (ROS) O and H O . OP treatment significantly increased the activities of antioxidant enzymes including superoxide dismutase, guaiacol peroxidase, glutathione reductase and ascorbate peroxidase. The contents of the non-enzymatic antioxidant glutathione (GSH) and ratio of GSH to glutathione disulfide were markedly increased with OP treatment. Pretreatment with buthionine sulfoximine, a specific and potent inhibitor of GSH biosynthesis, significantly reduced total GSH content and conferred a more severe toxic phenotype on OP exposure. Thus, with OP-induced oxidative stress, C. demersum might actively regulate the antioxidant machinery, especially the biosynthesis and redox state of GSH.
[Mh] Termos MeSH primário: Antioxidantes/metabolismo
Glutationa/biossíntese
Magnoliopsida/efeitos dos fármacos
Estresse Oxidativo/efeitos dos fármacos
Fenóis/toxicidade
Poluentes Químicos da Água/toxicidade
[Mh] Termos MeSH secundário: Ascorbato Peroxidases/metabolismo
Clorofila/metabolismo
Relação Dose-Resposta a Droga
Glutationa/metabolismo
Glutationa Redutase/metabolismo
Glutationa Transferase/metabolismo
Peróxido de Hidrogênio/metabolismo
Magnoliopsida/crescimento & desenvolvimento
Magnoliopsida/metabolismo
Peroxidase/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Superóxido Dismutase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Phenols); 0 (Reactive Oxygen Species); 0 (Water Pollutants, Chemical); 1406-65-1 (Chlorophyll); BBX060AN9V (Hydrogen Peroxide); EC 1.11.1.- (guaiacol peroxidase); EC 1.11.1.11 (Ascorbate Peroxidases); EC 1.11.1.7 (Peroxidase); EC 1.15.1.1 (Superoxide Dismutase); EC 1.8.1.7 (Glutathione Reductase); EC 2.5.1.18 (Glutathione Transferase); GAN16C9B8O (Glutathione); IOY9FVU3J3 (4-tert-octylphenol)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170602
[St] Status:MEDLINE


  10 / 1197 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28534307
[Au] Autor:Shackira AM; Puthur JT; Nabeesa Salim E
[Ad] Endereço:Plant Physiology and Biochemistry Division, Department of Botany, University of Calicut, C.U. Campus P.O, Kerala, 673635, India.
[Ti] Título:Acanthus ilicifolius L. a promising candidate for phytostabilization of zinc.
[So] Source:Environ Monit Assess;189(6):282, 2017 Jun.
[Is] ISSN:1573-2959
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The potential of a halophyte species-Acanthus ilicifolius L.-to phytostabilize zinc (Zn) grown under hydroponics culture conditions was critically evaluated in this study. The propagules after treating with ZnSO (4 mM) were analysed for the bioaccumulation pattern, translocation rate of Zn to the shoot, effects of Zn accumulation on organic solutes and the antioxidant defence system. It was found that most of the Zn absorbed by the plant was retained in the root (47%) and only a small portion was transported to stem (12%) and leaves (11%). This is further confirmed by the high BCF (bioconcentration factor) value (1.99) and low TF (translocation factor) value (0.5), which indicates the increased retention of Zn in the root itself. Moreover, treatment with Zn resulted in an increased accumulation of organic solutes (proline, free amino acids and soluble sugars) and non-enzymatic antioxidants (ascorbate, glutathione and phenol) in the leaf and root tissue. Likewise, the activity of antioxidant enzymes namely superoxide dismutase (SOD), catalase (CAT), guaiacol peroxidase (GPX) and ascorbate peroxidase (APX) recorded an enhanced activity upon exposure to Zn as compared to the control plants. Thus, the increased tolerance for Zn in A. ilicifolius may be attributed to the efficient free radical scavenging mechanisms operating under excess Zn. In addition, being a high accumulator (53.7 mg of Zn) and at the same time a poor translocator of Zn to the aerial parts of the plant, A. ilicifolius can be recommended as a potential candidate for the phytostabilization of Zn in the contaminated wetlands.
[Mh] Termos MeSH primário: Biodegradação Ambiental
Poluentes do Solo/metabolismo
Zinco/metabolismo
[Mh] Termos MeSH secundário: Acanthaceae
Antioxidantes/metabolismo
Ascorbato Peroxidases/metabolismo
Catalase/metabolismo
Monitoramento Ambiental
Glutationa/metabolismo
Hidroponia
Peroxidase
Folhas de Planta/química
Raízes de Plantas/química
Plantas Tolerantes a Sal
Poluentes do Solo/análise
Poluentes do Solo/toxicidade
Superóxido Dismutase/metabolismo
Zinco/análise
Zinco/toxicidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Soil Pollutants); EC 1.11.1.- (guaiacol peroxidase); EC 1.11.1.11 (Ascorbate Peroxidases); EC 1.11.1.6 (Catalase); EC 1.11.1.7 (Peroxidase); EC 1.15.1.1 (Superoxide Dismutase); GAN16C9B8O (Glutathione); J41CSQ7QDS (Zinc)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171020
[Lr] Data última revisão:
171020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170524
[St] Status:MEDLINE
[do] DOI:10.1007/s10661-017-6001-8



página 1 de 120 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde