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[PMID]:28988145
[Au] Autor:Miranda BNM; Fotoran WL; Canduri F; Souza DHF; Wunderlich G; Carrilho E
[Ad] Endereço:Instituto de Química de São Carlos, Universidade de São Paulo, Av. Trabalhador São-carlense, 400, 13566-590 São Carlos, SP, Brazil; Instituto Nacional de Ciência e Tecnologia de Bioanalítica - INCTBio, 13083-970, Campinas, SP, Brazil.
[Ti] Título:Heterologous expression of Homo sapiens alpha-folate receptors in E. coli by fusion with a trigger factor for enhanced solubilization.
[So] Source:Protein Expr Purif;142:75-80, 2018 Feb.
[Is] ISSN:1096-0279
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The role of Alpha folate receptors (FRα) in folate metabolism and cancer development has been extensively studied. The reason for this is not only associated to its direct relation to disease development but also to its potential use as a highly sensitive and specific biomarker for cancers therapies. Over the recent years, the crystal structures of human FRα complexed with different ligands were described relying on an expensive and time-consuming production process. Here, we constructed an efficient system for the expression and purification of a human FRα in E. coli. Unlike a conventional expression method we used a specific protein fusion expressing the target protein together with a trigger factor (TF). This factor is a chaperone from E. coli that assists the correct folding of newly synthesized polypeptide chains. The activity of rTFFRα was comparable to glycosylphosphatidylinositol (GPI) anchored proteins extracted from HeLa tumor cells. Our work demonstrates a straightforward and versatile approach for the production of active human FRα by heterologous expression; this approach further enhances the development of inhibition studies and biotechnological applications. The purified product was then conjugated to liposomes, obtaining a 35% higher signal from densitometry measurement on the immunoblotting assay in the contruct containing the Ni-NTA tag, as a mimesis of an exosome, which is of vital importance to nanotherapeutic techniques associated to treatment and diagnosis of tumors.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/genética
Receptor 1 de Folato/genética
Peptidilprolil Isomerase/genética
Plasmídeos/química
Proteínas Recombinantes de Fusão/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Proteínas de Escherichia coli/metabolismo
Receptor 1 de Folato/metabolismo
Expressão Gênica
Células HeLa
Histidina/genética
Histidina/metabolismo
Seres Humanos
Cinética
Lipossomos/química
Lipossomos/metabolismo
Oligopeptídeos/genética
Oligopeptídeos/metabolismo
Peptidilprolil Isomerase/metabolismo
Plasmídeos/metabolismo
Proteólise
Proteínas Recombinantes de Fusão/metabolismo
Tetra-Hidrofolatos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (FOLR1 protein, human); 0 (Folate Receptor 1); 0 (His-His-His-His-His-His); 0 (Liposomes); 0 (Oligopeptides); 0 (Recombinant Fusion Proteins); 0 (Tetrahydrofolates); 43ZWB253H4 (5,6,7,8-tetrahydrofolic acid); 4QD397987E (Histidine); EC 5.2.1.- (trigger factor, E coli); EC 5.2.1.8 (Peptidylprolyl Isomerase)
[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:171009
[St] Status:MEDLINE


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[PMID]:28965803
[Au] Autor:Sui Y; Fu X; Wang Y; Hu W; Zhang T; Liu W; Jiang L; Xing S; Fu X; Xu X
[Ad] Endereço:Edmond H. Fischer Signal Transduction Laboratory, School of Life Sciences, Jilin University, Changchun 130012, PR China.
[Ti] Título:Expression, purification and characterization of a catalytic domain of human protein tyrosine phosphatase non-receptor 12 (PTPN12) in Escherichia coli with FKBP-type PPIase as a chaperon.
[So] Source:Protein Expr Purif;142:45-52, 2018 Feb.
[Is] ISSN:1096-0279
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Protein tyrosine phosphatase non-receptor type 12 (PTPN12), also known as PTP-PEST, was broadly expressed in hemopoietic cells. Recent research has shown that this enzyme is involved in tumorigenesis, as well as in tumor progression and transfer, as it can suppress multiple oncogenic tyrosine kinases. However, the difficulty of soluble expression of PTP-PEST in prokaryotic cells has resulted in great limitations in investigating its structure and functions. In this study, we successfully carried out soluble expression of the catalytic domain of PTP-PEST (ΔPTP-PEST) in Escherichia coli and performed an enzymatic characterization and kinetics. To confirm expression efficiency, we also induced the expression of the chaperon, FKBP_C. FKBP_C expression indicated efficacious prokaryotic expression of ΔPTP-PEST. In conclusion, our work yielded a practical expression system and two-step chromatography purification method that may serve as a valuable tool for the structural and functional analysis of proteins that are difficult to express in the soluble form in prokaryotic cells.
[Mh] Termos MeSH primário: Proteínas Arqueais/genética
Chaperonas Moleculares/genética
Peptidilprolil Isomerase/genética
Proteína Tirosina Fosfatase não Receptora Tipo 12/genética
Proteínas de Ligação a Tacrolimo/genética
Thermococcus/química
[Mh] Termos MeSH secundário: Proteínas Arqueais/metabolismo
Domínio Catalítico
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Seres Humanos
Cinética
Chaperonas Moleculares/metabolismo
Peptidilprolil Isomerase/metabolismo
Plasmídeos/química
Plasmídeos/metabolismo
Proteína Tirosina Fosfatase não Receptora Tipo 12/isolamento & purificação
Proteína Tirosina Fosfatase não Receptora Tipo 12/metabolismo
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/metabolismo
Proteínas de Ligação a Tacrolimo/metabolismo
Thermococcus/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Molecular Chaperones); 0 (Recombinant Fusion Proteins); EC 3.1.3.48 (PTPN12 protein, human); EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 12); EC 5.2.1.- (Tacrolimus Binding Proteins); EC 5.2.1.8 (Peptidylprolyl Isomerase)
[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:171003
[St] Status:MEDLINE


  3 / 2627 MEDLINE  
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[PMID]:28935721
[Au] Autor:Rajiv C; Jackson SR; Cocklin S; Eisenmesser EZ; Davis TL
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102, U.S.A.
[Ti] Título:The spliceosomal proteins PPIH and PRPF4 exhibit bi-partite binding.
[So] Source:Biochem J;474(21):3689-3704, 2017 Oct 25.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Pre-mRNA splicing is a dynamic, multistep process that is catalyzed by the RNA (ribonucleic acid)-protein complex called the spliceosome. The spliceosome contains a core set of RNAs and proteins that are conserved in all organisms that perform splicing. In higher organisms, peptidyl-prolyl isomerase H (PPIH) directly interacts with the core protein pre-mRNA processing factor 4 (PRPF4) and both integrate into the pre-catalytic spliceosome as part of the tri-snRNP (small nuclear RNA-protein complex) subcomplex. As a first step to understand the protein interactions that dictate PPIH and PRPF4 function, we expressed and purified soluble forms of each protein and formed a complex between them. We found two sites of interaction between PPIH and the N-terminus of PRPF4, an unexpected result. The N-terminus of PRPF4 is an intrinsically disordered region and does not adopt secondary structure in the presence of PPIH. In the absence of an atomic resolution structure, we used mutational analysis to identify point mutations that uncouple these two binding sites and find that mutations in both sites are necessary to break up the complex. A discussion of how this bipartite interaction between PPIH and PRPF4 may modulate spliceosomal function is included.
[Mh] Termos MeSH primário: Peptidilprolil Isomerase/metabolismo
Processamento de RNA
Ribonucleoproteína Nuclear Pequena U4-U6/metabolismo
Spliceossomos/metabolismo
[Mh] Termos MeSH secundário: Calorimetria
Dicroísmo Circular
Clonagem Molecular
Proteínas Intrinsicamente Desordenadas/metabolismo
Peptidilprolil Isomerase/genética
Ligação Proteica
Ribonucleoproteína Nuclear Pequena U4-U6/genética
Ressonância de Plasmônio de Superfície
Ultracentrifugação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Intrinsically Disordered Proteins); 0 (PRPF4 protein, human); 0 (Ribonucleoprotein, U4-U6 Small Nuclear); EC 5.2.1.8 (Peptidylprolyl Isomerase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171115
[Lr] Data última revisão:
171115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170923
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20170366


  4 / 2627 MEDLINE  
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[PMID]:28668496
[Au] Autor:Hu Y; Romão E; Vertommen D; Vincke C; Morales-Yánez F; Gutiérrez C; Liu C; Muyldermans S
[Ad] Endereço:Laboratory of Cellular and Molecular Immunology, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium; Department of Pharmaceutical Engineering, School of Chemical Engineering and Technology, Tianjin University, Tianjin, China; State Key Laboratory of Drug Delivery Technology and Pharmaco
[Ti] Título:Generation of Nanobodies against SlyD and development of tools to eliminate this bacterial contaminant from recombinant proteins.
[So] Source:Protein Expr Purif;137:64-76, 2017 Sep.
[Is] ISSN:1096-0279
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The gene for a protein domain, derived from a tumor marker, fused to His tag codons and under control of a T7 promotor was expressed in E. coli strain BL21 (DE3). The recombinant protein was purified from cell lysates through immobilized metal affinity chromatography and size-exclusion chromatography. A contaminating bacterial protein was consistently co-purified, even using stringent washing solutions containing 50 or 100 mM imidazole. Immunization of a dromedary with this contaminated protein preparation, and the subsequent generation and panning of the immune Nanobody library yielded several Nanobodies of which 2/3 were directed against the bacterial contaminant, reflecting the immunodominance of this protein to steer the dromedary immune response. Affinity adsorption of this contaminant using one of our specific Nanobodies followed by mass spectrometry identified the bacterial contaminant as FKBP-type peptidyl-prolyl cis-trans isomerase (SlyD) from E. coli. This SlyD protein contains in its C-terminal region 14 histidines in a stretch of 31 amino acids, which explains its co-purification on Ni-NTA resin. This protein is most likely present to varying extents in all recombinant protein preparations after immobilized metal affinity chromatography. Using our SlyD-specific Nb 5 we generated an immune-complex that could be removed either by immunocapturing or by size exclusion chromatography. Both methods allow us to prepare a recombinant protein sample where the SlyD contaminant was quantitatively eliminated.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/química
Escherichia coli
Peptidilprolil Isomerase/química
Anticorpos de Domínio Único
[Mh] Termos MeSH secundário: Animais
Camelus
Escherichia coli/química
Escherichia coli/genética
Escherichia coli/metabolismo
Proteínas de Escherichia coli/antagonistas & inibidores
Peptidilprolil Isomerase/antagonistas & inibidores
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Anticorpos de Domínio Único/biossíntese
Anticorpos de Domínio Único/química
Anticorpos de Domínio Único/genética
Anticorpos de Domínio Único/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Recombinant Proteins); 0 (Single-Domain Antibodies); 0 (SlyD protein, E coli); EC 5.2.1.8 (Peptidylprolyl Isomerase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170703
[St] Status:MEDLINE


  5 / 2627 MEDLINE  
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[PMID]:28591185
[Au] Autor:Gholami K; Loh SY; Salleh N; Lam SK; Hoe SZ
[Ad] Endereço:Division of Human Biology, School of Medicine, International Medical University, Kuala Lumpur, Malaysia.
[Ti] Título:Selection of suitable endogenous reference genes for qPCR in kidney and hypothalamus of rats under testosterone influence.
[So] Source:PLoS One;12(6):e0176368, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Real-time quantitative PCR (qPCR) is the most reliable and accurate technique for analyses of gene expression. Endogenous reference genes are being used to normalize qPCR data even though their expression may vary under different conditions and in different tissues. Nonetheless, verification of expression of reference genes in selected studied tissue is essential in order to accurately assess the level of expression of target genes of interest. Therefore, in this study, we attempted to examine six commonly used reference genes in order to identify the gene being expressed most constantly under the influence of testosterone in the kidneys and hypothalamus. The reference genes include glyceraldehyde-3-phosphate dehydrogenase (GAPDH), actin beta (ACTB), beta-2 microglobulin (B2m), hypoxanthine phosphoribosyltransferase 1 (HPRT), peptidylprolylisomerase A (Ppia) and hydroxymethylbilane synthase (Hmbs). The cycle threshold (Ct) value for each gene was determined and data obtained were analyzed using the software programs NormFinder, geNorm, BestKeeper, and rank aggregation. Results showed that Hmbs and Ppia genes were the most stably expressed in the hypothalamus. Meanwhile, in kidneys, Hmbs and GAPDH appeared to be the most constant genes. In conclusion, variations in expression levels of reference genes occur in kidneys and hypothalamus under similar conditions; thus, it is important to verify reference gene levels in these tissues prior to commencing any studies.
[Mh] Termos MeSH primário: Perfilação da Expressão Gênica/métodos
Hipotálamo/metabolismo
Rim/metabolismo
Reação em Cadeia da Polimerase em Tempo Real/métodos
[Mh] Termos MeSH secundário: Actinas/biossíntese
Animais
Regulação da Expressão Gênica/genética
Gliceraldeído-3-Fosfato Desidrogenases/biossíntese
Hidroximetilbilano Sintase/biossíntese
Hipotálamo/efeitos dos fármacos
Hipoxantina Fosforribosiltransferase/biossíntese
Rim/efeitos dos fármacos
Peptidilprolil Isomerase/biossíntese
Ratos
Padrões de Referência
Testosterona/administração & dosagem
Microglobulina-2 beta/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (beta 2-Microglobulin); 3XMK78S47O (Testosterone); EC 1.2.1.- (Glyceraldehyde-3-Phosphate Dehydrogenases); EC 2.4.2.8 (Hypoxanthine Phosphoribosyltransferase); EC 2.5.1.61 (Hydroxymethylbilane Synthase); EC 5.2.1.8 (Peptidylprolyl Isomerase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170914
[Lr] Data última revisão:
170914
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170608
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0176368


  6 / 2627 MEDLINE  
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[PMID]:28434865
[Au] Autor:Cantillo JF; Puerta L; Lafosse-Marin S; Subiza JL; Caraballo L; Fernandez-Caldas E
[Ad] Endereço:Institute for Immunological Research, University of Cartagena, Cartagena, Colombia.
[Ti] Título:Allergens involved in the cross-reactivity of Aedes aegypti with other arthropods.
[So] Source:Ann Allergy Asthma Immunol;118(6):710-718, 2017 Jun.
[Is] ISSN:1534-4436
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Cross-reactivity between Aedes aegypti and mites, cockroaches, and shrimp has been previously suggested, but the involved molecular components have not been fully described. OBJECTIVE: To evaluate the cross-reactivity between A aegypti and other arthropods. METHODS: Thirty-four serum samples from patients with asthma and/or allergic rhinitis were selected, and specific IgE to A aegypti, Dermatophagoides pteronyssinus, Dermatophagoides farinae, Blomia tropicalis, Periplaneta americana. and Litopenaeus vannamei was measured by enzyme-linked immunosorbent assay. Cross-reactivity was investigated using pooled serum samples from allergic patients, allergenic extracts, and the recombinant tropomyosins (Aed a 10.0201, Der p 10, Blo t 10, Lit v 1, and Per a 7). Four IgE reactive bands were further characterized by matrix-assisted laser desorption/ionization tandem time of flight. RESULTS: Frequency of positive IgE reactivity was 82.35% to at least one mite species, 64.7% to A aegypti, 29.4% to P americana, and 23.5% to L vannamei. The highest IgE cross-reactivity was seen between A aegypti and D pteronyssinus (96.6%) followed by L vannamei (95.4%), B tropicalis (84.4%), and P americana (75.4%). Recombinant tropomyosins from mites, cockroach, or shrimp inhibited the IgE reactivity to the mosquito at a lower extent than the extracts from these arthropods. Several bands of A aegypti cross-reacted with arthropod extracts, and 4 of them were identified as odorant binding protein, mitochondrial cytochrome C, peptidyl-prolyl cis-trans isomerase, and protein with hypothetical magnesium ion binding function. CONCLUSION: We identified 4 novel cross-reactive allergens in A aegypti allergenic extract. These molecules could influence the manifestation of allergy to environmental allergens in the tropics.
[Mh] Termos MeSH primário: Alérgenos/imunologia
Proteínas de Artrópodes/imunologia
Artrópodes/imunologia
[Mh] Termos MeSH secundário: Adolescente
Adulto
Animais
Proteínas de Artrópodes/genética
Asma/sangue
Asma/imunologia
Criança
Pré-Escolar
Reações Cruzadas/imunologia
Feminino
Seres Humanos
Imunoglobulina E/imunologia
Lactente
Masculino
Meia-Idade
Peptidilprolil Isomerase/química
Peptidilprolil Isomerase/imunologia
Proteínas Recombinantes/imunologia
Rinite Alérgica/sangue
Rinite Alérgica/imunologia
Tropomiosina/genética
Tropomiosina/imunologia
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Allergens); 0 (Arthropod Proteins); 0 (Recombinant Proteins); 0 (Tropomyosin); 37341-29-0 (Immunoglobulin E); EC 5.2.1.8 (Peptidylprolyl Isomerase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170719
[Lr] Data última revisão:
170719
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170425
[St] Status:MEDLINE


  7 / 2627 MEDLINE  
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[PMID]:28425861
[Au] Autor:Kaur G; Singh H; Kaur K; Roy S; Pareek A; Singh P
[Ad] Endereço:Department of Biotechnology, Guru Nanak Dev University, Amritsar-143005, Punjab. India.
[Ti] Título:Role of Cysteine Residues in Regulation of Peptidyl-prolyl cis-trans Isomerase Activity of Wheat Cyclophilin TaCYPA-1.
[So] Source:Protein Pept Lett;24(6):551-560, 2017.
[Is] ISSN:1875-5305
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The wheat cyclophilin, TaCYPA-1, shows peptidyl-prolyl cis-trans isomerase (PPIase) activity. However, the significance of different cysteine residues in regulation of PPIase activity of this protein has not been investigated. OBJECTIVES: The main objective of this study was to analyze the role of different disulphide linkages in redox mechanisms that modulate the PPIase activity of TaCYPA-1. METHOD: Site-directed mutants of TaCYPA-1 were generated by substituting cysteine residues at positions -40 and -122 with serine and -126 with proline. The recombinant proteins were expressed in Escherichia coli and purified. The effect of Cu2+ and N-ethylmaleimide was studied on PPIase activity of the purified recombinant cyclophilins for analyzing the role of different cysteine residues in the modulation of enzyme activity. The changes in secondary structure of TaCYPA-1 and its mutants were analysed by recording far UV CD spectra. The effect of different cysteine substitutions on thermotolerance of E. coli was studied by monitoring the cell growth at 47 °C after 2 h, 3 h and 5 h of heat stress. RESULTS: The catalytic efficiencies (Kcat/Km) of TaCYPA-1C40S (0.37 X 106 M-1 s-1) and TaCYPA- 1C122S (0.31 X 106 M-1 s-1) were significantly lower as compared to the native TaCYPA-1 (1.33 X 106 M-1 s-1), whereas Kcat/Km of the double mutant TaCYPA-1C40S/C122S was significantly higher (2.36 X 106 M-1 s-1). Compared to the wild-type TaCYPA-1, the different mutants also showed differential sensitivity to Cu2+. Furthermore, the results of this study also revealed that despite lacking PPIase activity, the mutant TaCYPA-1C126P was able to confer partial protection against heat stress. CONCLUSION: This study revealed that mutation of different cysteine residues in TaCYPA-1 results in differential effect on PPIase activity. It was also observed that of the two pairs of cysteine residues i.e. Cys40/Cys168 and Cys122/Cys126, the latter appears to play major role in redox regulation of TaCYPA-1. The mutant TaCYPA-1C126P, though lacking PPIase activity, was able to impart partial tolerance to heat stress in E. coli, suggesting other functions besides cis to trans isomerisation. This study, therefore, provides new insights into the regulation of plant cyclophilins.
[Mh] Termos MeSH primário: Ciclofilinas/química
Peptidilprolil Isomerase/química
Proteínas Recombinantes/química
[Mh] Termos MeSH secundário: Ciclofilinas/genética
Cisteína/genética
Escherichia coli/genética
Peptidilprolil Isomerase/genética
Prolina/química
Estrutura Secundária de Proteína
Proteínas Recombinantes/genética
Triticum/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Recombinant Proteins); 9DLQ4CIU6V (Proline); EC 5.2.1.- (Cyclophilins); EC 5.2.1.8 (Peptidylprolyl Isomerase); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170421
[St] Status:MEDLINE
[do] DOI:10.2174/0929866524666170417165823


  8 / 2627 MEDLINE  
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[PMID]:28413971
[Au] Autor:Gao Y; Zhang HM; Wang PW; Li M
[Ad] Endereço:College of Agronomy, Jilin Agricultural University, No.2888 Xincheng Street, Changchun, Jilin, China.
[Ti] Título:Structure of C-terminal Domain of Peptidyl-prolyl cis-trans Isomerase from Pseudomonas syringae pv. Tomato str. DC3000 at 1.6Å Resolution.
[So] Source:Protein Pept Lett;24(6):528-533, 2017.
[Is] ISSN:1875-5305
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Peptidyl-prolyl cis-trans isomerase (PPIase) accelerates the intrinsically slow conversion between cis- and trans- configurations of proline, thus affecting backbone conformation and altering the direction of peptide chains. PPIase from Pseudomonas syringae pv. Tomato (PSPTO) DC3000 (PSPTO-PPIase) is considered to belong to the FKBP subfamily of PPIase. OBJECTIVE: To solve the high resolution structure of the PSPTO-PPIase, and to explore its potential function in plants pathogen PSPTO DC3000. METHOD: The PSPTO-PPIase was expressed in E.coli and purified through ion exchange and size exclusion chromatography. While only the C-terminal domain of PSPTO-PPIase was successfully crystalized, and its structure was solved to 1.6 Å resolution by molecular replacement method. RESULTS: Structural comparison showed that PSPTO-PPIase adopts a similar overall fold with microphage infectivity potentiators (MIPs), which also belong to the FKBP subfamily of PPIase. In addition, the BIAcore result confirmed that PSPTO-PPIase can bind an immunosuppressive drug FK506 as some other FKBP subfamily members do. CONCLUSION: Our results suggested that PSPTO-PPIase may function in a similar manner to virulent factor MIPs during pathogenesis. And the immunosuppressive drugs FK506 and rapamycin binding to PSPTO-PPIase potentially interferes and inhibits the plant pathogen PSPTO DC3000. In addition, the amino acids with short side chains in the fourth loop (L4) of PSPTO-PPIase may account for its variable roles in the respective pathogen.
[Mh] Termos MeSH primário: Sequência de Aminoácidos/genética
Peptidilprolil Isomerase/química
Pseudomonas syringae/enzimologia
[Mh] Termos MeSH secundário: Sítios de Ligação
Cristalografia por Raios X
Escherichia coli/genética
Peptidilprolil Isomerase/genética
Conformação Proteica
Dobramento de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 5.2.1.8 (Peptidylprolyl Isomerase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170418
[St] Status:MEDLINE
[do] DOI:10.2174/0929866524666170414093308


  9 / 2627 MEDLINE  
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[PMID]:28396241
[Au] Autor:Gong X; Li J; Zhang Y; Hou S; Qu P; Yang Z; Chen S
[Ad] Endereço:Guangzhou Center for Disease Control and Prevention, Guangzhou 510440, China; Ocean University of China, Qingdao 266100, China.
[Ti] Título:Molecular typing of Legionella pneumophila from air-conditioning cooling waters using mip gene, SBT, and FAFLP methods.
[So] Source:J Microbiol Methods;139:1-7, 2017 Aug.
[Is] ISSN:1872-8359
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Legionella spp. are important waterborne pathogens. Molecular typing has become an important method for outbreaks investigations and source tracking of Legionnaires. In a survey program conducted by the Guangzhou Center for Disease Control and Prevention, multiple serotypes Legionella pneumophila (L. pneumophila) were isolated from waters in air-conditioning cooling towers in urban Guangzhou region, China between 2008 and 2011. Three genotyping methods, mip (macrophage infectivity potentiator) genotyping, SBT (sequence-based typing), and FAFLP (fluorescent amplified fragment length polymorphism analysis) were used to type these waterborne L. pneumophila isolates. The three methods were capable of typing all the 134 isolates and a reference strain of L. pneumophila (ATCC33153), with discriminatory indices of 0.7034, 0.9218, and 0.9376, for the mip, SBT, and FAFLP methods respectively. Among the 9 serotypes of the 134 isolates, 10, 50, and 34 molecular types were detected by the mip, SBT, and FAFLP methods respectively. The mip genotyping and SBT typing are more feasible for inter-laboratory results sharing and comparison of different types of L. pneumophila. The SBT and FAFLP typing methods were rapid with higher discriminatory abilities. Combinations of two or more of the typing methods enables more accurate typing of Legionella isolates for outbreak investigations and source tracking of Legionnaires.
[Mh] Termos MeSH primário: Ar Condicionado
Análise do Polimorfismo de Comprimento de Fragmentos Amplificados/métodos
Proteínas de Bactérias/genética
Legionella pneumophila/genética
Tipagem Molecular/métodos
Peptidilprolil Isomerase/genética
Análise de Sequência de DNA
Microbiologia da Água
[Mh] Termos MeSH secundário: China
Temperatura Baixa
DNA Bacteriano/genética
Fluorescência
Técnicas de Genotipagem
Seres Humanos
Legionella pneumophila/classificação
Legionella pneumophila/isolamento & purificação
Doença dos Legionários/diagnóstico
Doença dos Legionários/microbiologia
Sorogrupo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (DNA, Bacterial); EC 5.2.1.8 (Mip protein, Legionella pneumophila); EC 5.2.1.8 (Peptidylprolyl Isomerase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170412
[St] Status:MEDLINE


  10 / 2627 MEDLINE  
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[PMID]:28385637
[Au] Autor:Koubek J; Chang YC; Yang SY; Huang JJ
[Ad] Endereço:Institute of Chemistry, Academia Sinica, Taipei, Taiwan, 11529, R.O.C.
[Ti] Título:Trigger Factor-Induced Nascent Chain Dynamics Changes Suggest Two Different Chaperone-Nascent Chain Interactions during Translation.
[So] Source:J Mol Biol;429(11):1733-1745, 2017 Jun 02.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Protein biogenesis is poorly understood due to the ribosome that perturbs measurement attempted on the ribosome-bound nascent chain (RNC). Investigating nascent chain dynamics may provide invaluable insight into the co-translational processes such as structure formation or interaction with a chaperone [e.g., the bacterial trigger factor (TF)]. In this study, we aim to establish a platform for studying nascent chain dynamics by exploring the local environment near the fluorescent dye on site-specifically labeled RNCs with time-resolved fluorescence anisotropy. To prepare a quantitative model of fluorescence depolarization, we utilized intrinsically disordered protein bound to ribosome, which helped us couple the sub-nanosecond depolarization with the motion of the nascent chain backbone. This was consistent with zinc-finger-domain-containing RNCs, where the extent of sub-nanosecond motion decreased upon the addition of zinc when the fluorophore was in close proximity of the domain. After the characterization of disordered nascent chain dynamics, we investigated the synthesis of a model cytosolic protein, Entner-Doudoroff aldolase, labeled at different sites during various stages of translation. Depending on the stage of translation, the addition of the TF to the nascent chain led to two different responses in the nascent chain dynamics serendipitously, suggesting steric hindrance between the nascent chain and the chaperone as a mechanism for TF dissociation from the ribosome during translation. Overall, our study demonstrates the possible use of site-specific labeling and time-resolved anisotropy to gain insight on chaperone binding event at various stages of translation and hints on TF co-translational mechanism.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/metabolismo
Frutose-Bifosfato Aldolase/química
Frutose-Bifosfato Aldolase/metabolismo
Peptidilprolil Isomerase/metabolismo
Biossíntese de Proteínas
Dobramento de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); EC 4.1.2.13 (Fructose-Bisphosphate Aldolase); EC 5.2.1.- (trigger factor, E coli); EC 5.2.1.8 (Peptidylprolyl Isomerase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170408
[St] Status:MEDLINE



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