Base de dados : MEDLINE
Pesquisa : D08.811.277.040.025.142.500.500 [Categoria DeCS]
Referências encontradas : 5009 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 501 ir para página                         

  1 / 5009 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29300153
[Au] Autor:Modesto M; Michelini S; Oki K; Biavati B; Watanabe K; Mattarelli P
[Ad] Endereço:1​Department of Agricultural Sciences, University of Bologna, Italy.
[Ti] Título:Bifidobacterium catulorum sp. nov., a novel taxon from the faeces of the baby common marmoset (Callithrix jacchus).
[So] Source:Int J Syst Evol Microbiol;68(2):575-581, 2018 Feb.
[Is] ISSN:1466-5034
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In our previous study based on hsp60 PCR-restriction fragment length polymorphism and 16S rRNA gene sequencing, we stated that the bifidobacterial strains isolated from the individual faecal samples of five baby common marmosets constituted different phylogenetically isolated groups of the genus Bifidobacterium. In that study, we also proposed that these isolated groups potentially represented novel species of the genus Bifidobacterium. Out of them, Bifidobacterium aesculapii, Bifidobacterium myosotis, Bifidobacterium tissieri and Bifidobacterium hapali, have been described recently. Another strain, designated MRM 8.19 , has been classified as member of the genus Bifidobacterium on the basis of positive results for fructose-6-phosphate phosphoketolase activity and analysis of partial 16S rRNA, hsp60, clpC, dnaJ, dnaG and rpoB gene sequences. Analysis of 16S rRNA and hsp60 gene sequences revealed that strain MRM 8.19 was related to B. tissieri DSM 100201 (95.8 %) and to Bifidobacterium bifidum ATCC 29521 (93.7 %), respectively. The DNA G+C composition was 63.7 mol% and the peptidoglycan structure was l-Orn(Lys)-l-Ser. Based on the phylogenetic, genotypic and phenotypic data reported, strain MRM 8.19 represents a novel taxon within the genus Bifidobacterium for which the name Bifidobacterium catulorum sp. nov. (type strain MRM 8.19 =DSM 103154 =JCM 31794 ) is proposed.
[Mh] Termos MeSH primário: Bifidobacterium/classificação
Callithrix/microbiologia
Filogenia
[Mh] Termos MeSH secundário: Aldeído Liases/genética
Animais
Técnicas de Tipagem Bacteriana
Composição de Bases
Bifidobacterium/genética
Bifidobacterium/isolamento & purificação
Chaperonina 60/genética
DNA Bacteriano/genética
Fezes/microbiologia
Genes Bacterianos
Peptidoglicano/química
RNA Ribossômico 16S/genética
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chaperonin 60); 0 (DNA, Bacterial); 0 (Peptidoglycan); 0 (RNA, Ribosomal, 16S); EC 4.1.2.- (Aldehyde-Lyases); EC 4.1.2.22 (fructose-6-phosphate phosphoketolase)
[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:180105
[St] Status:MEDLINE
[do] DOI:10.1099/ijsem.0.002545


  2 / 5009 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29236386
[Au] Autor:Galkin OY; Besarab AB; Lutsenko TN
[Ti] Título:Characteristics of enzyme-linked immunosorbent assay for detection of IgG antibodies specific to Сhlamydia trachomatis heat shock protein (HSP-60)
[So] Source:Ukr Biochem J;89(1):22-30, 2017 Jan-Feb.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:The goal of this work was to study sensitivity and specificity of the developed ELISA set for the identification of IgG antibodies against Chlamydia trachomatis HSP-60 (using biotinylated tyramine-based signal amplification system). The study was conducted using a panel of characterized sera, as well as two reference ELISA sets of similar purpose. According to the results of ELISA informative value parameters, the ELISA we have developed showed the highest specificity and sensitivity parameters (no false negative or false positive results were registered). In 4 out of 15 intralaboratory panel serum samples initially identified as negative, anti-HSP-60 IgG-antibodies test result in reference ELISA sets upon dilution changed from negative to positive. The nature of titration curves of false negative sera and commercial monoclonal antibodies А57-В9 against C. trachomatis HSP-60 after incubation for 24 h was indicative of the presence of anti-idiotypic antibodies in these samples. Upon sera dilution, idiotypic-anti-idiotypic complexes dissociated, which caused the change of test result. High informative value of the developed ELISA set for identification of IgG antibodies against C. trachomatis HSP-60 has been proven. Anti-idiotypic antibodies possessing C. trachomatis anti-HSP-60 activity and being one of the causes of false negative results of the relevant ELISA-based tests have been identified in blood sera of individuals infected with chlamydial genitourinary infection agents.
[Mh] Termos MeSH primário: Anticorpos Antibacterianos/análise
Antígenos de Bactérias/sangue
Chaperonina 60/sangue
Infecções por Chlamydia/diagnóstico
Chlamydia trachomatis/imunologia
Ensaio de Imunoadsorção Enzimática/métodos
Imunoglobulina G/análise
[Mh] Termos MeSH secundário: Anticorpos Anti-Idiotípicos/química
Anticorpos Antibacterianos/sangue
Anticorpos Antibacterianos/imunologia
Complexo Antígeno-Anticorpo/química
Antígenos de Bactérias/imunologia
Biotinilação
Chaperonina 60/imunologia
Infecções por Chlamydia/sangue
Infecções por Chlamydia/imunologia
Infecções por Chlamydia/microbiologia
Chlamydia trachomatis/química
Ensaio de Imunoadsorção Enzimática/normas
Reações Falso-Negativas
Seres Humanos
Soros Imunes/química
Imunoglobulina G/sangue
Imunoglobulina G/imunologia
Sensibilidade e Especificidade
Tiramina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Anti-Idiotypic); 0 (Antibodies, Bacterial); 0 (Antigen-Antibody Complex); 0 (Antigens, Bacterial); 0 (Chaperonin 60); 0 (Immune Sera); 0 (Immunoglobulin G); X8ZC7V0OX3 (Tyramine)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171214
[St] Status:MEDLINE
[do] DOI:10.15407/ubj89.01.022


  3 / 5009 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28467202
[Au] Autor:Shen L; Lu S; Huang D; Li G; Liu K; Cao R; Zong L; Jin L; Wu J
[Ad] Endereço:1 Minigene Pharmacy Laboratory, School of Life Science and Technology, China Pharmaceutical University, Nanjing, China.
[Ti] Título:A rationally designed peptide IA-2-P2 against type 1 diabetes in streptozotocin-induced diabetic mice.
[So] Source:Diab Vasc Dis Res;14(3):184-190, 2017 May.
[Is] ISSN:1752-8984
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Recent studies have investigated the potential of type 1 diabetes mellitus-related autoantigens, such as heat shock protein 60, to induce immunological tolerance or to suppress the immune response. A functional 24-residue peptide derived from heat shock protein 60 (P277) has shown anti-type 1 diabetes mellitus potential in experimental animals and in clinical studies, but it also carries a potential atherogenic effect. In this study, we have modified P277 to retain an anti-type 1 diabetes mellitus effect and minimize the atherogenic potential by replacing the P277 B epitope with another diabetes-associated autoantigen, insulinoma antigen-2 (IA-2), to create the fusion peptide IA-2-P2. In streptozotocin-induced diabetic C57BL/6J mice, the IA-2-P2 peptide displayed similar anti-diabetic effects to the control P277 peptide. Also, the IA-2-P2 peptide did not show atherogenic activity in a rabbit model. Our findings indicate the potential of IA-2-P2 as a promising vaccine against type 1 diabetes mellitus.
[Mh] Termos MeSH primário: Chaperonina 60/farmacologia
Diabetes Mellitus Experimental/tratamento farmacológico
Diabetes Mellitus Tipo 1/tratamento farmacológico
Desenho de Drogas
Hipoglicemiantes/farmacologia
Fragmentos de Peptídeos/farmacologia
Proteínas Tirosina Fosfatases Classe 8 Semelhantes a Receptores/farmacologia
Proteínas Recombinantes de Fusão/farmacologia
Vacinas/farmacologia
[Mh] Termos MeSH secundário: Animais
Aterosclerose/induzido quimicamente
Glicemia/efeitos dos fármacos
Glicemia/metabolismo
Proliferação Celular/efeitos dos fármacos
Células Cultivadas
Chaperonina 60/administração & dosagem
Chaperonina 60/toxicidade
Citocinas/metabolismo
Diabetes Mellitus Experimental/sangue
Diabetes Mellitus Experimental/induzido quimicamente
Diabetes Mellitus Experimental/imunologia
Diabetes Mellitus Tipo 1/sangue
Diabetes Mellitus Tipo 1/induzido quimicamente
Diabetes Mellitus Tipo 1/imunologia
Hipoglicemiantes/administração & dosagem
Hipoglicemiantes/toxicidade
Imunização
Ativação Linfocitária/efeitos dos fármacos
Masculino
Camundongos Endogâmicos C57BL
Fragmentos de Peptídeos/administração & dosagem
Fragmentos de Peptídeos/toxicidade
Coelhos
Proteínas Tirosina Fosfatases Classe 8 Semelhantes a Receptores/administração & dosagem
Proteínas Tirosina Fosfatases Classe 8 Semelhantes a Receptores/toxicidade
Proteínas Recombinantes de Fusão/administração & dosagem
Proteínas Recombinantes de Fusão/toxicidade
Estreptozocina
Linfócitos T/efeitos dos fármacos
Linfócitos T/imunologia
Linfócitos T/metabolismo
Fatores de Tempo
Vacinas/administração & dosagem
Vacinas/toxicidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Blood Glucose); 0 (Chaperonin 60); 0 (Cytokines); 0 (Hypoglycemic Agents); 0 (IA-2-P2 peptide); 0 (Peptide Fragments); 0 (Recombinant Fusion Proteins); 0 (Vaccines); 0 (peptide 277, heat shock protein 60); 5W494URQ81 (Streptozocin); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 8)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171219
[Lr] Data última revisão:
171219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1177/1479164116664189


  4 / 5009 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28951283
[Au] Autor:Wälti MA; Clore GM
[Ad] Endereço:Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, United States.
[Ti] Título:Disassembly/reassembly strategy for the production of highly pure GroEL, a tetradecameric supramolecular machine, suitable for quantitative NMR, EPR and mutational studies.
[So] Source:Protein Expr Purif;142:8-15, 2018 Feb.
[Is] ISSN:1096-0279
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:GroEL, a prototypical member of the chaperonin class of chaperones, is a large supramocular machine that assists protein folding and plays an important role in proteostasis. GroEL comprises two heptameric rings, each of which encloses a large cavity that provides a folding chamber for protein substrates. Many questions remain regarding the mechanistic details of GroEL facilitated protein folding. Thus, data at atomic resolution of the type provided by NMR and EPR are invaluable. Such studies often require complete deuteration of GroEL, uniform or residue specific C and N isotope labeling, and the introduction of selective cysteine mutations for site-specific spin labeling. In addition, high purity GroEL is essential for detailed studies of substrate-GroEL interactions as quantitative interpretation is impossible if the cavities are already occupied and blocked by other protein substrates present in the bacterial expression system. Here we present a new purification protocol designed to provide highly pure GroEL devoid of non-specific protein substrate contamination.
[Mh] Termos MeSH primário: Chaperonina 60/isolamento & purificação
Cromatografia em Gel/métodos
Cromatografia por Troca Iônica/métodos
Proteínas de Escherichia coli/isolamento & purificação
Mutação Puntual
[Mh] Termos MeSH secundário: Sulfato de Amônio/química
Chaperonina 60/química
Chaperonina 60/genética
Chaperonina 60/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Expressão Gênica
Isótopos de Nitrogênio/química
Ressonância Magnética Nuclear Biomolecular
Multimerização Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
Estreptomicina/química
Ureia/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chaperonin 60); 0 (Escherichia coli Proteins); 0 (Nitrogen Isotopes); 0 (Recombinant Proteins); 8W8T17847W (Urea); SU46BAM238 (Ammonium Sulfate); Y45QSO73OB (Streptomycin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170928
[St] Status:MEDLINE


  5 / 5009 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28922851
[Au] Autor:Mehta RI; Tsymbalyuk N; Ivanova S; Stokum JA; Woo K; Gerzanich V; Simard JM
[Ad] Endereço:Department of Pathology and Laboratory Medicine; Center for Neurotherapeutics Discovery, Department of Neuroscience; Center for Translational Neuromedicine, University of Rochester, Rochester, New York; Department of Pathology; Department of Neurosurgery; Department of Physiology, University of Mary
[Ti] Título:α-Endosulfine (ARPP-19e) Expression in a Rat Model of Stroke.
[So] Source:J Neuropathol Exp Neurol;76(10):898-907, 2017 10 01.
[Is] ISSN:1554-6578
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In nutrient restricted environments, the yeast endosulfines Igo1/2 are activated via TORC1 inhibition and function critically to initiate and coordinate the cellular stress response that promotes survival. We examined expression of αEnsa, the mammalian homolog of yeast endosulfines, in rat stroke. Prominent neuronal upregulation of αEnsa was identified in 3 patterns within the ischemic gradient: (1) neurons in GFAP-/HSF1+ cortex showed upregulation and near-complete nuclear translocation of αEnsa protein within hours of ischemic onset; (2) neurons in GFAP+/HSF1+ cortex showed upregulation in cytoplasm and nuclei that persisted for days; (3) neurons in GFAP+/HSF1- cortex showed delayed cytosolic-only upregulation that persisted for days. Findings were corroborated using in situ hybridization for ENSA mRNA. Rapamycin treatment was found to reduce infarct size and behavioral deficits and, in GFAP+/HSF1+ zones, enhance αEnsa neuronal nuclear translocation and mitigate cell death, relative to controls. Based on the conservation of TOR signaling across species, and on the finding that the Rim15-Igo1/2-PP2A module is triggered by substrate deprivation in eukaryotic yeast, we speculate that αEnsa is activated by substrate deprivation, functioning through the homologous MASTL-αEnsa/ARPP19-PP2A module to promote neuronal survival. In conjunction with recent studies suggesting a neuroprotective role, our data highlight a potential function for αEnsa within ischemic brain.
[Mh] Termos MeSH primário: Encéfalo/patologia
Regulação da Expressão Gênica/fisiologia
Neurônios/metabolismo
Peptídeos/metabolismo
Acidente Vascular Cerebral/patologia
[Mh] Termos MeSH secundário: Animais
Encéfalo/metabolismo
Infarto Encefálico/tratamento farmacológico
Infarto Encefálico/patologia
Moléculas de Adesão Celular/metabolismo
Chaperonina 60/metabolismo
Modelos Animais de Doenças
Regulação da Expressão Gênica/efeitos dos fármacos
Seres Humanos
Imunossupressores/farmacologia
Masculino
Proteínas Mitocondriais/metabolismo
Proteínas do Tecido Nervoso/metabolismo
Neurônios/efeitos dos fármacos
Peptídeos/genética
Molécula-1 de Adesão Celular Endotelial de Plaquetas/metabolismo
Ratos
Ratos Wistar
Sirolimo/farmacologia
Somatostatina/metabolismo
Acidente Vascular Cerebral/tratamento farmacológico
Acidente Vascular Cerebral/fisiopatologia
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Adhesion Molecules); 0 (Chaperonin 60); 0 (Esam protein, rat); 0 (Hspd1 protein, rat); 0 (Immunosuppressive Agents); 0 (Mitochondrial Proteins); 0 (Nerve Tissue Proteins); 0 (Peptides); 0 (Platelet Endothelial Cell Adhesion Molecule-1); 0 (endosulfine); 51110-01-1 (Somatostatin); W36ZG6FT64 (Sirolimus)
[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:170920
[St] Status:MEDLINE
[do] DOI:10.1093/jnen/nlx074


  6 / 5009 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28792419
[Au] Autor:Ning MX; Xiu YJ; Bi JX; Liu YH; Hou LB; Ding ZF; Gu W; Wang W; Meng QG
[Ad] Endereço:Jiangsu Key Laboratory for Biodiversity & Biotechnology and Jiangsu Key Laboratory for Aquatic Crustacean Diseases, College of Life Sciences, Nanjing Normal University, Nanjing 210023, PR China.
[Ti] Título:Interaction of heat shock protein 60 (HSP60) with microRNA in Chinese mitten crab during Spiroplasma eriocheiris infection.
[So] Source:Dis Aquat Organ;125(3):207-215, 2017 08 09.
[Is] ISSN:0177-5103
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Heat shock protein 60 from the Chinese mitten crab Eriocheir sinensis (EsHSP60) was previously identified in relation to Spiroplasma eriocheiris infection by isobaric tags for relative and absolute quantitation labelling followed by liquid chromatography-tandem mass spectrometry. In the present study, to validate the immune function of this protein, the cDNA of the EsHSP60 gene was cloned. Various crab tissues were assessed using real-time PCR, which showed that EsHSP60 transcription occurred in all tissues examined. The expression profiles of EsHSP60 in haemolymph at transcription and protein levels when infected with S. eriocheiris were investigated by real-time PCR and Western blot analysis, respectively. A significant increase of EsHSP60 transcription and protein expression appeared post-injection in response to S. eriocheiris infection when compared to the control group. The double-luciferase reporter gene assay showed that the microRNA PC-533-3p interacted with the 3'-untranslated region of EsHSP60 and inhibited the translation of EsHSP60. The expression profiles of PC-533-3p during S. eriocheiris infection were also investigated by real-time PCR. However, the change tendency of PC-533-3p was opposite to that of the EsHSP60 after S. eriocheiris challenge. These data indicate that the EsHSP60 proteins may play an important role in mediating the immune responses of E. sinensis to an S. eriocheiris challenge.
[Mh] Termos MeSH primário: Braquiúros/microbiologia
Chaperonina 60/metabolismo
Regulação da Expressão Gênica/fisiologia
MicroRNAs/metabolismo
Spiroplasma/fisiologia
[Mh] Termos MeSH secundário: Animais
Braquiúros/genética
Braquiúros/metabolismo
Chaperonina 60/genética
Brânquias/metabolismo
Hemócitos/metabolismo
Hemolinfa
Hepatopâncreas/metabolismo
Interações Hospedeiro-Patógeno
Intestinos/metabolismo
MicroRNAs/genética
Músculos/metabolismo
Miocárdio/metabolismo
Neurônios/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chaperonin 60); 0 (MicroRNAs); 0 (RNA, Messenger)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170810
[St] Status:MEDLINE
[do] DOI:10.3354/dao03144


  7 / 5009 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28774748
[Au] Autor:Ricci C; Carrotta R; Rappa GC; Mangione MR; Librizzi F; San Biagio PL; Amenitsch H; Ortore MG; Vilasi S
[Ad] Endereço:Dept. Life and Environmental Sciences, Marche Polytechnic University, Ancona 60131, Italy. Electronic address: c.ricci@univpm.it.
[Ti] Título:Investigation on different chemical stability of mitochondrial Hsp60 and its precursor.
[So] Source:Biophys Chem;229:31-38, 2017 Oct.
[Is] ISSN:1873-4200
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:In the large class of molecules that maintain protein homeostasis, called molecular chaperones, chaperonins constitute a subclass that specifically assist the correct folding of newly synthesized proteins. Among them, Hsp60 is composed of a double heptameric ring structure with a large central cavity where the unfolded protein binds via hydrophobic interactions and is supported, in this function, by the co-chaperonin Hsp10. Hsp60 is typically located in the mitochondria, but in some pathological situations, such as cancers and chronic inflammatory diseases, Hsp60 accumulates in the cytoplasm. In these cases, cytoplasmatic Hsp60 is a mixture of mitochondrial Hsp60 secreted from mitochondria upon stress, and its precursor, called naïve Hsp60, never entered into the organella. The difference between the naïve and mitochondrial Hsp60s resides in the absence of the mitochondrial import signal (MIS) in the mitochondrial form, but information on their different structure and stability is still lacking. We present here a study on the stability against a chemical denaturant, of the different cytoplasmic Hsp60 species. By combining Circular Dichroism and Small Angle X-ray Scattering as experimental biophysical techniques to investigate Hsp60, we find that naïve and mitochondrial Hsp60 (mtHsp60) forms differ in their stability. Furthermore, specific responses from the two forms are discussed in terms of the biological environment they are working in, thus opening new questions on their biological function.
[Mh] Termos MeSH primário: Chaperonina 60/química
Mitocôndrias/metabolismo
[Mh] Termos MeSH secundário: Chaperonina 60/genética
Chaperonina 60/metabolismo
Dicroísmo Circular
Escherichia coli/metabolismo
Guanidina/química
Desnaturação Proteica
Precursores de Proteínas/química
Precursores de Proteínas/metabolismo
Estabilidade Proteica
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/química
Proteínas Recombinantes/isolamento & purificação
Espalhamento a Baixo Ângulo
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chaperonin 60); 0 (Protein Precursors); 0 (Recombinant Proteins); JU58VJ6Y3B (Guanidine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170805
[St] Status:MEDLINE


  8 / 5009 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28719870
[Au] Autor:Cocci P; Capriotti M; Mosconi G; Palermo FA
[Ad] Endereço:School of Biosciences and Veterinary Medicine, University of Camerino, Via Gentile III Da Varano, I-62032 Camerino, MC, Italy. Electronic address: paolo.cocci@unicam.it.
[Ti] Título:Effects of endocrine disrupting chemicals on estrogen receptor alpha and heat shock protein 60 gene expression in primary cultures of loggerhead sea turtle (Caretta caretta) erythrocytes.
[So] Source:Environ Res;158:616-624, 2017 10.
[Is] ISSN:1096-0953
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The loggerhead turtle (Caretta caretta) can be considered a good indicator species for studying the ecological impact of endocrine disrupting chemicals (EDCs) on wildlife. However, the effect of these environmental pollutants on nuclear steroid hormone signaling has not yet been addressed in sea turtles mainly due to the legal constraints of their endangered status. Here we describe the use of primary erythrocyte cell cultures as in vitro models for evaluating the effects of different EDCs on the expression of estrogen receptor α (ERα). In addition, we evaluated erythrocyte toxicity caused by EDCs using Alamar Blue assay and heat shock proteins 60 (HSP60) expression. Primary cultures of erythrocytes were exposed to increasing concentrations of 4-nonylphenol (4NP), Diisodecyl phthalate (DiDP), Tri-m-cresyl phosphate (TMCP) and Tributyltin (TBT) for 48h. Alamar Blue demonstrated that exposure of erythrocytes to each contaminant for up to 48h led to a significant impairment of cellular metabolic activity at 100µM, with the exception of TBT. Moreover, our data indicate that loggerhead erythrocytes constitutively express ERα and HSP60 at the transcript level and respond to EDCs by up-regulating their expression. In this regard, ERα was up-regulated in a dose-dependent manner after 48h exposure to both 4NP and TMCP. Interestingly, the dosage-dependent effects of DiDP on ERα expression were opposite in comparison to that obtained following exposure to the other tested compounds. This work provides the first indication regarding the potential of primary erythrocytes as study models for evaluating the effects of EDCs on sea turtles.
[Mh] Termos MeSH primário: Chaperonina 60/genética
Disruptores Endócrinos/toxicidade
Eritrócitos/efeitos dos fármacos
Receptor alfa de Estrogênio/genética
Regulação da Expressão Gênica/efeitos dos fármacos
Proteínas de Répteis/genética
Tartarugas/genética
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Chaperonina 60/metabolismo
Receptor alfa de Estrogênio/metabolismo
Proteínas de Répteis/metabolismo
Tartarugas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chaperonin 60); 0 (Endocrine Disruptors); 0 (Estrogen Receptor alpha); 0 (Reptilian Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171120
[Lr] Data última revisão:
171120
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170719
[St] Status:MEDLINE


  9 / 5009 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28678004
[Au] Autor:Ochirkhuu N; Konnai S; Odbileg R; Murata S; Ohashi K
[Ad] Endereço:1 Department of Disease Control, Graduate School of Veterinary Medicine, Hokkaido University , Sapporo, Japan .
[Ti] Título:Molecular Epidemiological Survey and Genetic Characterization of Anaplasma Species in Mongolian Livestock.
[So] Source:Vector Borne Zoonotic Dis;17(8):539-549, 2017 Aug.
[Is] ISSN:1557-7759
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Anaplasma species are obligate intracellular rickettsial pathogens that cause great economic loss to the animal industry. Few studies on Anaplasma infections in Mongolian livestock have been conducted. This study examined the prevalence of Anaplasma marginale, Anaplasma ovis, Anaplasma phagocytophilum, and Anaplasma bovis by polymerase chain reaction assay in 928 blood samples collected from native cattle and dairy cattle (Bos taurus), yaks (Bos grunniens), sheep (Ovis aries), and goats (Capra aegagrus hircus) in four provinces of Ulaanbaatar city in Mongolia. We genetically characterized positive samples through sequencing analysis based on the heat-shock protein groEL, major surface protein 4 (msp4), and 16S rRNA genes. Only A. ovis was detected in Mongolian livestock (cattle, yaks, sheep, and goats), with 413 animals (44.5%) positive for groEL and 308 animals (33.2%) positive for msp4 genes. In the phylogenetic tree, we separated A. ovis sequences into two distinct clusters based on the groEL gene. One cluster comprised sequences derived mainly from sheep and goats, which was similar to that in A. ovis isolates from other countries. The other divergent cluster comprised sequences derived from cattle and yaks and appeared to be newly branched from that in previously published single isolates in Mongolian cattle. In addition, the msp4 gene of A. ovis using same and different samples with groEL gene of the pathogen demonstrated that all sequences derived from all animal species, except for three sequences derived from cattle and yak, were clustered together, and were identical or similar to those in isolates from other countries. We used 16S rRNA gene sequences to investigate the genetically divergent A. ovis and identified high homology of 99.3-100%. However, the sequences derived from cattle did not match those derived from sheep and goats. The results of this study on the prevalence and molecular characterization of A. ovis in Mongolian livestock can facilitate the control of infectious diseases in livestock.
[Mh] Termos MeSH primário: Anaplasma/isolamento & purificação
Anaplasmose/microbiologia
Gado/microbiologia
Epidemiologia Molecular
[Mh] Termos MeSH secundário: Anaplasma/genética
Anaplasmose/epidemiologia
Animais
Chaperonina 60/genética
Chaperonina 60/metabolismo
DNA Bacteriano/genética
Regulação Bacteriana da Expressão Gênica
Mongólia/epidemiologia
Filogenia
Zoonoses
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chaperonin 60); 0 (DNA, Bacterial)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170706
[St] Status:MEDLINE
[do] DOI:10.1089/vbz.2017.2111


  10 / 5009 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28651912
[Au] Autor:Jacobsen MT; Erickson PW; Kay MS
[Ad] Endereço:Department of Biochemistry, University of Utah School of Medicine, 15 North Medical Drive East, Room 4100, Salt Lake City, UT 84112-5650, United States.
[Ti] Título:Aligator: A computational tool for optimizing total chemical synthesis of large proteins.
[So] Source:Bioorg Med Chem;25(18):4946-4952, 2017 Sep 15.
[Is] ISSN:1464-3391
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The scope of chemical protein synthesis (CPS) continues to expand, driven primarily by advances in chemical ligation tools (e.g., reversible solubilizing groups and novel ligation chemistries). However, the design of an optimal synthesis route can be an arduous and fickle task due to the large number of theoretically possible, and in many cases problematic, synthetic strategies. In this perspective, we highlight recent CPS tool advances and then introduce a new and easy-to-use program, Aligator (Automated Ligator), for analyzing and designing the most efficient strategies for constructing large targets using CPS. As a model set, we selected the E. coli ribosomal proteins and associated factors for computational analysis. Aligator systematically scores and ranks all feasible synthetic strategies for a particular CPS target. The Aligator script methodically evaluates potential peptide segments for a target using a scoring function that includes solubility, ligation site quality, segment lengths, and number of ligations to provide a ranked list of potential synthetic strategies. We demonstrate the utility of Aligator by analyzing three recent CPS projects from our lab: TNFα (157 aa), GroES (97 aa), and DapA (312 aa). As the limits of CPS are extended, we expect that computational tools will play an increasingly important role in the efficient execution of ambitious CPS projects such as production of a mirror-image ribosome.
[Mh] Termos MeSH primário: Biologia Computacional/métodos
Proteínas/síntese química
Software
[Mh] Termos MeSH secundário: Chaperonina 10/síntese química
Chaperonina 10/química
Chaperonina 60/síntese química
Chaperonina 60/química
Escherichia coli/metabolismo
Proteínas/química
Proteínas Ribossômicas/síntese química
Proteínas Ribossômicas/química
Fator de Necrose Tumoral alfa/síntese química
Fator de Necrose Tumoral alfa/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Chaperonin 10); 0 (Chaperonin 60); 0 (Proteins); 0 (Ribosomal Proteins); 0 (Tumor Necrosis Factor-alpha)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170628
[St] Status:MEDLINE



página 1 de 501 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