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Pesquisa : G02.111.660.871 [Categoria DeCS]
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[PMID]:29414979
[Au] Autor:Takahashi H; Kozhuharova A; Sharma H; Hirose M; Ohyama T; Fasolo F; Yamazaki T; Cotella D; Santoro C; Zucchelli S; Gustincich S; Carninci P
[Ad] Endereço:RIKEN Center for Life Science Technologies, Division of Genomic Technologies, Yokohama, Kanagawa, Japan.
[Ti] Título:Identification of functional features of synthetic SINEUPs, antisense lncRNAs that specifically enhance protein translation.
[So] Source:PLoS One;13(2):e0183229, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:SINEUPs are antisense long noncoding RNAs, in which an embedded SINE B2 element UP-regulates translation of partially overlapping target sense mRNAs. SINEUPs contain two functional domains. First, the binding domain (BD) is located in the region antisense to the target, providing specific targeting to the overlapping mRNA. Second, the inverted SINE B2 represents the effector domain (ED) and enhances translation. To adapt SINEUP technology to a broader number of targets, we took advantage of a high-throughput, semi-automated imaging system to optimize synthetic SINEUP BD and ED design in HEK293T cell lines. Using SINEUP-GFP as a model SINEUP, we extensively screened variants of the BD to map features needed for optimal design. We found that most active SINEUPs overlap an AUG-Kozak sequence. Moreover, we report our screening of the inverted SINE B2 sequence to identify active sub-domains and map the length of the minimal active ED. Our synthetic SINEUP-GFP screening of both BDs and EDs constitutes a broad test with flexible applications to any target gene of interest.
[Mh] Termos MeSH primário: Biossíntese de Proteínas/genética
Proteínas/genética
RNA Longo não Codificante/genética
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Células HEK293
Seres Humanos
Camundongos
Fosforilação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Proteins); 0 (RNA, Long Noncoding)
[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:180208
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0183229


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[PMID]:29414693
[Au] Autor:Andreev DE; Dmitriev SE; Loughran G; Terenin IM; Baranov PV; Shatsky IN
[Ad] Endereço:Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Russia. Electronic address: cycloheximide@yandex.ru.
[Ti] Título:Translation control of mRNAs encoding mammalian translation initiation factors.
[So] Source:Gene;651:174-182, 2018 Apr 20.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Eukaryotic cells evolved highly complex and accurate protein synthesis machinery that is finely tuned by various signaling pathways. Dysregulation of translation is a hallmark of many diseases, including cancer, and thus pharmacological approaches to modulate translation become very promising. While there has been much progress in our understanding of mammalian mRNA-specific translation control, surprisingly, relatively little is known about whether and how the protein components of the translation machinery shape translation of their own mRNAs. Here we analyze mammalian mRNAs encoding components of the translation initiation machinery for potential regulatory features such as 5'TOP motifs, TISU motifs, poor start codon nucleotide context and upstream open reading frames.
[Mh] Termos MeSH primário: Fatores de Iniciação em Eucariotos/genética
Regulação da Expressão Gênica
RNA Mensageiro/metabolismo
[Mh] Termos MeSH secundário: Regiões 5' não Traduzidas
Animais
Seres Humanos
Mamíferos
Biossíntese de Proteínas
Sequência de Oligopirimidina na Região 5' Terminal do RNA
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (5' Untranslated Regions); 0 (Eukaryotic Initiation Factors); 0 (RNA, Messenger)
[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:180208
[St] Status:MEDLINE


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[PMID]:29410090
[Au] Autor:Brewer RA; Collins HE; Berry RD; Brahma MK; Tirado BA; Peliciari-Garcia RA; Stanley HL; Wende AR; Taegtmeyer H; Rajasekaran NS; Darley-Usmar V; Zhang J; Frank SJ; Chatham JC; Young ME
[Ad] Endereço:Division of Cardiovascular Disease, Department of Medicine, University of Alabama at Birmingham, Birmingham, AL, USA.
[Ti] Título:Temporal partitioning of adaptive responses of the murine heart to fasting.
[So] Source:Life Sci;197:30-39, 2018 Mar 15.
[Is] ISSN:1879-0631
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Recent studies suggest that the time of day at which food is consumed dramatically influences clinically-relevant cardiometabolic parameters (e.g., adiposity, insulin sensitivity, and cardiac function). Meal feeding benefits may be the result of daily periods of feeding and/or fasting, highlighting the need for improved understanding of the temporal adaptation of cardiometabolic tissues (e.g., heart) to fasting. Such studies may provide mechanistic insight regarding how time-of-day-dependent feeding/fasting cycles influence cardiac function. We hypothesized that fasting during the sleep period elicits beneficial adaptation of the heart at transcriptional, translational, and metabolic levels. To test this hypothesis, temporal adaptation was investigated in wild-type mice fasted for 24-h, or for either the 12-h light/sleep phase or the 12-h dark/awake phase. Fasting maximally induced fatty acid responsive genes (e.g., Pdk4) during the dark/active phase; transcriptional changes were mirrored at translational (e.g., PDK4) and metabolic flux (e.g., glucose/oleate oxidation) levels. Similarly, maximal repression of myocardial p-mTOR and protein synthesis rates occurred during the dark phase; both parameters remained elevated in the heart of fasted mice during the light phase. In contrast, markers of autophagy (e.g., LC3II) exhibited peak responses to fasting during the light phase. Collectively, these data show that responsiveness of the heart to fasting is temporally partitioned. Autophagy peaks during the light/sleep phase, while repression of glucose utilization and protein synthesis is maximized during the dark/active phase. We speculate that sleep phase fasting may benefit cardiac function through augmentation of protein/cellular constituent turnover.
[Mh] Termos MeSH primário: Adaptação Fisiológica
Autofagia
Jejum/metabolismo
Miocárdio/metabolismo
Fases do Sono
[Mh] Termos MeSH secundário: Animais
Masculino
Camundongos
Proteínas Associadas aos Microtúbulos/metabolismo
Biossíntese de Proteínas/fisiologia
Proteínas Serina-Treonina Quinases/biossíntese
Serina-Treonina Quinases TOR/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MAP1LC3 protein, mouse); 0 (Microtubule-Associated Proteins); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.1.1 (mTOR protein, mouse); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.2 (pyruvate dehydrogenase (acetyl-transferring) kinase)
[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:180208
[St] Status:MEDLINE


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[PMID]:29200982
[Au] Autor:Hamarsland H; Nordengen AL; Nyvik Aas S; Holte K; Garthe I; Paulsen G; Cotter M; Børsheim E; Benestad HB; Raastad T
[Ad] Endereço:Department of Physical Performance, Norwegian School of Sport Sciences, P.O. Box 4014 Ullevål Stadion, 0806 Oslo, Norway.
[Ti] Título:Native whey protein with high levels of leucine results in similar post-exercise muscular anabolic responses as regular whey protein: a randomized controlled trial.
[So] Source:J Int Soc Sports Nutr;14:43, 2017.
[Is] ISSN:1550-2783
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Background: Protein intake is essential to maximally stimulate muscle protein synthesis, and the amino acid leucine seems to possess a superior effect on muscle protein synthesis compared to other amino acids. Native whey has higher leucine content and thus a potentially greater anabolic effect on muscle than regular whey (WPC-80). This study compared the acute anabolic effects of ingesting 2 × 20 g of native whey protein, WPC-80 or milk protein after a resistance exercise session. Methods: 24 young resistance trained men and women took part in this double blind, randomized, partial crossover, controlled study. Participants received either WPC-80 and native whey ( = 10), in a crossover design, or milk ( = 12). Supplements were ingested immediately (20 g) and two hours after (20 g) a bout of heavy-load lower body resistance exercise. Blood samples and muscle biopsies were collected to measure plasma concentrations of amino acids by gas-chromatography mass spectrometry, muscle phosphorylation of p70S6K, 4E-BP1 and eEF-2 by immunoblotting, and mixed muscle protein synthesis by use of [ H ]phenylalanine-infusion, gas-chromatography mass spectrometry and isotope-ratio mass spectrometry. Being the main comparison, differences between native whey and WPC-80 were analysed by a one-way ANOVA and comparisons between the whey supplements and milk were analysed by a two-way ANOVA. Results: Native whey increased blood leucine concentrations more than WPC-80 and milk ( < 0.05). Native whey ingestion induced a greater phosphorylation of p70S6K than milk 180 min after exercise ( = 0.03). Muscle protein synthesis rates increased 1-3 h hours after exercise with WPC-80 (0.119%), and 1-5 h after exercise with native whey (0.112%). Muscle protein synthesis rates were higher 1-5 h after exercise with native whey than with milk (0.112% vs. 0.064, = 0.023). Conclusions: Despite higher-magnitude increases in blood leucine concentrations with native whey, it was not superior to WPC-80 concerning effect on muscle protein synthesis and phosphorylation of p70S6K during a 5-h post-exercise period. Native whey increased phosphorylation of p70S6K and muscle protein synthesis rates to a greater extent than milk during the 5-h post exercise period. Trial registration: This study was retrospectively registered at clinicaltrials.gov as NCT02968888.
[Mh] Termos MeSH primário: Suplementos Nutricionais
Leucina/análise
Músculo Esquelético/efeitos dos fármacos
Treinamento de Resistência
Fenômenos Fisiológicos da Nutrição Esportiva
Proteínas do Soro do Leite/química
Proteínas do Soro do Leite/farmacologia
[Mh] Termos MeSH secundário: Estudos Cross-Over
Método Duplo-Cego
Feminino
Voluntários Saudáveis
Seres Humanos
Leucina/farmacologia
Masculino
Proteínas Musculares/biossíntese
Músculo Esquelético/fisiologia
Biossíntese de Proteínas/efeitos dos fármacos
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RANDOMIZED CONTROLLED TRIAL
[Nm] Nome de substância:
0 (Muscle Proteins); 0 (Whey Proteins); GMW67QNF9C (Leucine)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[Cl] Clinical Trial:ClinicalTrial
[St] Status:MEDLINE
[do] DOI:10.1186/s12970-017-0202-y


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[PMID]:27770702
[Au] Autor:Mishra P; Dixit U; Pandey AK; Upadhyay A; Pandey VN
[Ad] Endereço:Department of Microbiology, Biochemistry, and Molecular Genetics, Rutgers New Jersey Medical School, Rutgers, The State University of New Jersey, Newark, NJ 07103, USA.
[Ti] Título:Modulation of HCV replication and translation by ErbB3 binding protein1 isoforms.
[So] Source:Virology;500:35-49, 2017 01.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We recently identified a cell-factor, ErbB3 binding protein 1 (Ebp-1), which specifically interacts with the viral RNA genome and modulates HCV replication and translation. Ebp1 has two isoforms, p48, and p42, that result from differential splicing. We found that both isoforms interact with HCV proteins NS5A and NS5B, as well as cell-factor PKR. The p48 isoform, which localizes in the cytoplasm and nuclei, promoted HCV replication, whereas the shorter p42 isoform, which resides exclusively in the cytoplasm, strongly inhibited HCV replication. Transient expression of individual isoforms in Ebp1-knockdown MH14 cells confirmed that the p48 isoform promotes HCV replication, while the p42 isoform inhibits it. We found that Ebp1-p42 significantly enhanced autophosphorylation of PKR, while Ebp1-p48 isoform strongly inhibited it. We propose that modulation of autophosphorylation of PKR by p48 isoform is an important mechanism whereby the HCV virus escapes innate antiviral immune responses by circumventing p42-mediated inhibition of its replication.
[Mh] Termos MeSH primário: Hepacivirus/fisiologia
Hepatite C/virologia
Replicação Viral
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Replicação do DNA
Hepacivirus/genética
Hepatite C/genética
Hepatite C/metabolismo
Seres Humanos
Queratina-20/genética
Queratina-20/metabolismo
Fosforilação
Biossíntese de Proteínas
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
eIF-2 Quinase/genética
eIF-2 Quinase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (KRT20 protein, human); 0 (Keratin-20); 0 (Protein Isoforms); EC 2.7.11.1 (EIF2AK2 protein, human); EC 2.7.11.1 (eIF-2 Kinase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:180303
[Lr] Data última revisão:
180303
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161023
[St] Status:MEDLINE


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[PMID]:28459443
[Au] Autor:Tavernier SJ; Osorio F; Vandersarren L; Vetters J; Vanlangenakker N; Van Isterdael G; Vergote K; De Rycke R; Parthoens E; van de Laar L; Iwawaki T; Del Valle JR; Hu CA; Lambrecht BN; Janssens S
[Ad] Endereço:Laboratory of Immunoregulation and Mucosal Immunology, VIB Center for Inflammation Research, 9052 Ghent, Belgium.
[Ti] Título:Regulated IRE1-dependent mRNA decay sets the threshold for dendritic cell survival.
[So] Source:Nat Cell Biol;19(6):698-710, 2017 Jun.
[Is] ISSN:1476-4679
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The IRE1-XBP1 signalling pathway is part of a cellular programme that protects against endoplasmic reticulum (ER) stress, but also controls development and survival of immune cells. Loss of XBP1 in splenic type 1 conventional dendritic cells (cDC1s) results in functional alterations without affecting cell survival. However, in mucosal cDC1s, loss of XBP1 impaired survival in a tissue-specific manner-while lung cDC1s die, intestinal cDC1s survive. This was not caused by differential activation of ER stress cell-death regulators CHOP or JNK. Rather, survival of intestinal cDC1s was associated with their ability to shut down protein synthesis through a protective integrated stress response and their marked increase in regulated IRE1-dependent messenger RNA decay. Furthermore, loss of IRE1 endonuclease on top of XBP1 led to cDC1 loss in the intestine. Thus, mucosal DCs differentially mount ATF4- and IRE1-dependent adaptive mechanisms to survive in the face of ER stress.
[Mh] Termos MeSH primário: Células Dendríticas/enzimologia
Mucosa Intestinal/enzimologia
Proteínas de Membrana/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
Estabilidade de RNA
RNA Mensageiro/metabolismo
Mucosa Respiratória/enzimologia
[Mh] Termos MeSH secundário: Fator 4 Ativador da Transcrição/genética
Fator 4 Ativador da Transcrição/metabolismo
Animais
Apoptose
Sobrevivência Celular
Células Dendríticas/patologia
Estresse do Retículo Endoplasmático
Genótipo
Mucosa Intestinal/patologia
Proteínas Quinases JNK Ativadas por Mitógeno/metabolismo
Proteínas de Membrana/genética
Camundongos Transgênicos
Fenótipo
Biossíntese de Proteínas
Proteínas Serina-Treonina Quinases/genética
RNA Mensageiro/genética
Mucosa Respiratória/patologia
Transdução de Sinais
Fatores de Tempo
Fator de Transcrição CHOP/genética
Fator de Transcrição CHOP/metabolismo
Resposta a Proteínas não Dobradas
Proteína 1 de Ligação a X-Box/genética
Proteína 1 de Ligação a X-Box/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Atf4 protein, mouse); 0 (Ddit3 protein, mouse); 0 (Membrane Proteins); 0 (RNA, Messenger); 0 (X-Box Binding Protein 1); 0 (Xbp1 protein, mouse); 145891-90-3 (Activating Transcription Factor 4); 147336-12-7 (Transcription Factor CHOP); EC 2.7.1.- (Ern2 protein, mouse); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.24 (JNK Mitogen-Activated Protein Kinases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180302
[Lr] Data última revisão:
180302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE
[do] DOI:10.1038/ncb3518


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[PMID]:29342219
[Au] Autor:Hassan MK; Kumar D; Naik M; Dixit M
[Ad] Endereço:School of Biological Sciences, National Institute of Science Education and Research, HBNI, Bhimpur- Padanpur, Jatni, Khurda, Odisha, India.
[Ti] Título:The expression profile and prognostic significance of eukaryotic translation elongation factors in different cancers.
[So] Source:PLoS One;13(1):e0191377, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Eukaryotic translation factors, especially initiation factors have garnered much attention with regards to their role in the onset and progression of different cancers. However, the expression levels and prognostic significance of translation elongation factors remain poorly explored in different cancers. In this study, we have investigated the mRNA transcript levels of seven translation elongation factors in different cancer types using Oncomine and TCGA databases. Furthermore, we have identified the prognostic significance of these factors using Kaplan-Meier Plotter and SurvExpress databases. We observed altered expression levels of all the elongation factors in different cancers. Higher expression of EEF1A2, EEF1B2, EEF1G, EEF1D, EEF1E1 and EEF2 was observed in most of the cancer types, whereas reverse trend was observed for EEF1A1. Overexpression of many factors predicted poor prognosis in breast (EEF1D, EEF1E1, EEF2) and lung cancer (EEF1A2, EEF1B2, EEF1G, EEF1E1). However, we didn't see any common correlation of expression levels of elongation factors with survival outcomes across cancer types. Cancer subtype stratification showed association of survival outcomes and expression levels of elongation factors in specific sub-types of breast, lung and gastric cancer. Most interestingly, we observed a reciprocal relationship between the expression levels of the two EEF1A isoforms viz. EEF1A1 and EEF1A2, in most of the cancer types. Our results suggest that translation elongation factors can have a role in tumorigenesis and affect survival in cancer specific manner. Elongation factors have potential to serve as biomarkers and therapeutic drug targets, yet further study is required. Reciprocal relationship of differential expression between EEF1A isoforms observed in multiple cancer types indicates opposing roles in cancer and needs further investigation.
[Mh] Termos MeSH primário: Neoplasias/genética
Elongação Traducional da Cadeia Peptídica/genética
Transcriptoma/genética
[Mh] Termos MeSH secundário: Transformação Celular Neoplásica
Bases de Dados de Ácidos Nucleicos
Seres Humanos
Estimativa de Kaplan-Meier
Elongação Traducional da Cadeia Peptídica/fisiologia
Fator 1 de Elongação de Peptídeos/genética
Fator 1 de Elongação de Peptídeos/metabolismo
Prognóstico
Biossíntese de Proteínas
Isoformas de Proteínas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (EEF1A1 protein, human); 0 (EEF1A2 protein, human); 0 (EEF1D protein, human); 0 (Peptide Elongation Factor 1); 0 (Protein Isoforms)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191377


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[PMID]:29329354
[Au] Autor:Perry BD; Rahnert JA; Xie Y; Zheng B; Woodworth-Hobbs ME; Price SR
[Ad] Endereço:Department of Medicine, Renal Division, Emory University, Atlanta, GA, United States of America.
[Ti] Título:Palmitate-induced ER stress and inhibition of protein synthesis in cultured myotubes does not require Toll-like receptor 4.
[So] Source:PLoS One;13(1):e0191313, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Saturated fatty acids, such as palmitate, are elevated in metabolically dysfunctional conditions like type 2 diabetes mellitus. Palmitate has been shown to impair insulin sensitivity and suppress protein synthesis while upregulating proteolytic systems in skeletal muscle. Increased sarco/endoplasmic reticulum (ER) stress and subsequent activation of the unfolded protein response may contribute to the palmitate-induced impairment of muscle protein synthesis. In some cell types, ER stress occurs through activation of the Toll-like receptor 4 (TLR4). Given the link between ER stress and suppression of protein synthesis, we investigated whether palmitate induces markers of ER stress and protein synthesis by activating TLR4 in cultured mouse C2C12 myotubes. Myotubes were treated with vehicle, a TLR4-specific ligand (lipopolysaccharides), palmitate, or a combination of palmitate plus a TLR4-specific inhibitor (TAK-242). Inflammatory indicators of TLR4 activation (IL-6 and TNFα) and markers of ER stress were measured, and protein synthesis was assessed using puromycin incorporation. Palmitate substantially increased the levels of IL-6, TNF-α, CHOP, XBP1s, and ATF 4 mRNAs and augmented the levels of CHOP, XBP1s, phospho-PERK and phospho-eIF2α proteins. The TLR4 antagonist attenuated both acute palmitate and LPS-induced increases in IL-6 and TNFα, but did not reduce ER stress signaling with either 6 h or 24 h palmitate treatment. Similarly, treating myotubes with palmitate for 6 h caused a 43% decline in protein synthesis consistent with an increase in phospho-eIF2α, and the TLR4 antagonist did not alter these responses. These results suggest that palmitate does not induce ER stress through TLR4 in muscle, and that palmitate impairs protein synthesis in skeletal muscle in part by induction of ER stress.
[Mh] Termos MeSH primário: Estresse do Retículo Endoplasmático/efeitos dos fármacos
Fibras Musculares Esqueléticas/citologia
Fibras Musculares Esqueléticas/metabolismo
Palmitatos/farmacologia
Biossíntese de Proteínas/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Camundongos
Fibras Musculares Esqueléticas/efeitos dos fármacos
Fosforilação/efeitos dos fármacos
Proteínas Serina-Treonina Quinases/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Transdução de Sinais/efeitos dos fármacos
Receptor 4 Toll-Like/antagonistas & inibidores
Receptor 4 Toll-Like/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Palmitates); 0 (RNA, Messenger); 0 (Toll-Like Receptor 4); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.1 (eIF2alpha kinase, mouse)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180113
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191313


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[PMID]:29311466
[Au] Autor:Goto Y
[Ad] Endereço:Department of Chemistry, Graduate School of Science, The University of Tokyo.
[Ti] Título:[Elaboration of Pseudo-natural Products Using Artificial In Vitro Biosynthesis Systems].
[So] Source:Yakugaku Zasshi;138(1):55-61, 2018.
[Is] ISSN:1347-5231
[Cp] País de publicação:Japan
[La] Idioma:jpn
[Ab] Resumo:Peptidic natural products often consist of not only proteinogenic building blocks but also unique non-proteinogenic structures such as macrocyclic scaffolds and N-methylated backbones. Since such non-proteinogenic structures are important structural motifs that contribute to diverse bioactivity, we have proposed that peptides with non-proteinogenic structures should be attractive candidates as artificial bioactive peptides mimicking natural products, or so-called pseudo-natural products. We previously devised an engineered translation system for pseudo-natural peptides, referred to as the flexible in vitro translation (FIT) system. This system enabled "one-pot" synthesis of highly diverse pseudo-natural peptide libraries, which can be rapidly screened by mRNA display technology for the discovery of pseudo-natural peptides with diverse bioactivities.
[Mh] Termos MeSH primário: Produtos Biológicos/química
Reatores Biológicos
Biossíntese de Proteínas
[Mh] Termos MeSH secundário: Perfilação da Expressão Gênica
Compostos Macrocíclicos
Biblioteca de Peptídeos
Peptídeos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Biological Products); 0 (Macrocyclic Compounds); 0 (Peptide Library); 0 (Peptides)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180110
[St] Status:MEDLINE
[do] DOI:10.1248/yakushi.17-00186-3


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[PMID]:29352242
[Au] Autor:Cottrell KA; Chaudhari HG; Cohen BA; Djuranovic S
[Ad] Endereço:Department of Cell Biology and Physiology, School of Medicine, Washington University, St. Louis, MO, 63110, USA.
[Ti] Título:PTRE-seq reveals mechanism and interactions of RNA binding proteins and miRNAs.
[So] Source:Nat Commun;9(1):301, 2018 01 19.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:RNA binding proteins (RBP) and microRNAs (miRNAs) often bind sequences in 3' untranslated regions (UTRs) of mRNAs, and regulate stability and translation efficiency. With the identification of numerous RBPs and miRNAs, there is an urgent need for new technologies to dissect the function of the cis-acting elements of RBPs and miRNAs. We describe post-transcriptional regulatory element sequencing (PTRE-seq), a massively parallel method for assaying the target sequences of miRNAs and RBPs. We use PTRE-seq to dissect sequence preferences and interactions between miRNAs and RBPs. The binding sites for these effector molecules influenced different aspects of the RNA lifecycle: RNA stability, translation efficiency, and translation initiation. In some cases, post-transcriptional control is modular, with different factors acting independently of each other, while in other cases factors show specific epistatic interactions. The throughput, flexibility, and reproducibility of PTRE-seq make it a valuable tool to study post-transcriptional regulation by 3'UTR elements.
[Mh] Termos MeSH primário: MicroRNAs/genética
Biossíntese de Proteínas
Processamento Pós-Transcricional do RNA
Proteínas de Ligação a RNA/genética
Elementos Reguladores de Transcrição
Fatores de Transcrição/genética
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Sequência de Bases
Sítios de Ligação
Linhagem Celular
Biblioteca Gênica
Células HEK293
Células HeLa
Seres Humanos
MicroRNAs/metabolismo
Ligação Proteica
Estabilidade de RNA
Proteínas de Ligação a RNA/metabolismo
Análise de Sequência de RNA
Termodinâmica
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (MicroRNAs); 0 (RNA-Binding Proteins); 0 (Transcription Factors); 0 (mirnlet7 microRNA, human); 0 (pumilio protein, human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180121
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02745-0



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