Base de dados : MEDLINE
Pesquisa : B01.650.940.800.575.912.250.401.096 [Categoria DeCS]
Referências encontradas : 215 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 22 ir para página                         

  1 / 215 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29183662
[Au] Autor:Taha M; Ullah H; Al Muqarrabun LMR; Khan MN; Rahim F; Ahmat N; Javid MT; Ali M; Khan KM
[Ad] Endereço:Department of Clinical Pharmacy, Institute for Research and Medical Consultations (IRMC), Imam Abdulrahman Bin Faisal University, P.O. Box 31441, Dammam, Saudi Arabia. Electronic address: taha_hej@yahoo.com.
[Ti] Título:Bisindolylmethane thiosemicarbazides as potential inhibitors of urease: Synthesis and molecular modeling studies.
[So] Source:Bioorg Med Chem;26(1):152-160, 2018 01 01.
[Is] ISSN:1464-3391
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Bisindolylmethane thiosemicarbazides 1-18 were synthesized, characterized by H NMR and ESI MS and evaluated for urease inhibitory potential. All analogs showed outstanding urease inhibitory potentials with IC values ranging between 0.14 ±â€¯0.01 to 18.50 ±â€¯0.90 µM when compared with the standard inhibitor thiourea having IC value 21.25 ±â€¯0.90 µM. Among the series, analog 9 (0.14 ±â€¯0.01 µM) with di-chloro substitution on phenyl ring was identified as the most potent inhibitor of urease. The structure activity relationship has been also established on the basis of binding interactions of the active analogs. These binding interactions were identified by molecular docking studies.
[Mh] Termos MeSH primário: Inibidores Enzimáticos/farmacologia
Indóis/farmacologia
Semicarbazidas/farmacologia
Urease/antagonistas & inibidores
[Mh] Termos MeSH secundário: Canavalia/enzimologia
Relação Dose-Resposta a Droga
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
Indóis/química
Modelos Moleculares
Estrutura Molecular
Semicarbazidas/química
Relação Estrutura-Atividade
Urease/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Indoles); 0 (Semicarbazides); 6056O8W6ET (thiosemicarbazide); EC 3.5.1.5 (Urease); SSZ9HQT61Z (3,3'-diindolylmethane)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180106
[Lr] Data última revisão:
180106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171130
[St] Status:MEDLINE


  2 / 215 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28753459
[Au] Autor:Iftikhar F; Ali Y; Ahmad Kiani F; Fahad Hassan S; Fatima T; Khan A; Niaz B; Hassan A; Latif Ansari F; Rashid U
[Ad] Endereço:Department of Chemistry, Hazara University, Mansehra 21120, Pakistan.
[Ti] Título:Design, synthesis, in vitro Evaluation and docking studies on dihydropyrimidine-based urease inhibitors.
[So] Source:Bioorg Chem;74:53-65, 2017 Oct.
[Is] ISSN:1090-2120
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In our previous report, we have identified 3,4-dihydropyrimidine scaffold as promising class of urease inhibitor in a structure based virtual screen (SBVS) experiment. In present study, we attempted to optimize the scaffold by varying C-5 substituent. The elongation of the C-5 chain was achieved by the reaction of C-5 ester with hydrazine leading to C-5 carbohydrazides which were further used as building blocks for the synthesis of fifteen new compounds having diverse moieties. A significantly higher in vitro urease inhibitory activity with IC values in submicromolar range was observed for semithiocarbazide derivatives (4a-c, 0.58-0.79µM) and isatin Schiff base derivative 5a (0.23µM). Docking analysis suggests that the synthesized compounds were anchored well in the catalytic site and extending to the entrance of binding pocket and thus restrict the mobility of the flap by interacting with its key amino acid residues. The overall results of urease inhibition have shown that these compounds can be further optimized and developed as lead urease inhibitors.
[Mh] Termos MeSH primário: Canavalia/enzimologia
Desenho de Drogas
Inibidores Enzimáticos/farmacologia
Simulação de Acoplamento Molecular
Pirimidinas/farmacologia
Urease/antagonistas & inibidores
[Mh] Termos MeSH secundário: Relação Dose-Resposta a Droga
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
Estrutura Molecular
Pirimidinas/síntese química
Pirimidinas/química
Teoria Quântica
Relação Estrutura-Atividade
Urease/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Pyrimidines); EC 3.5.1.5 (Urease)
[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:170729
[St] Status:MEDLINE


  3 / 215 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28623137
[Au] Autor:Ahmed M; Qadir MA; Hameed A; Arshad MN; Asiri AM; Muddassar M
[Ad] Endereço:Institute of Chemistry, University of the Punjab, Lahore, 54590, Pakistan. Electronic address: mahmoodresearchscholar@gmail.com.
[Ti] Título:Azomethines, isoxazole, N-substituted pyrazoles and pyrimidine containing curcumin derivatives: Urease inhibition and molecular modeling studies.
[So] Source:Biochem Biophys Res Commun;490(2):434-440, 2017 Aug 19.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Curcumin has shown large number of pharmacological properties against different phenotypes of various disease models. Different synthetic routes have been employed to develop its various derivatives for diverse biological functions. In this study, curcumin derived azomethine, isoxazole, pyrimidines and N-substituted pyrazoles were synthesized to investigate their urease enzyme inhibition. The structures of newly synthesized compounds were described by IR, MS, H NMR and C NMR spectral data. Urease enzyme inhibition was evaluated through in vitro assays in which compound 8b was found to be the most potent (IC = 2.44 ± 0.07 µM) among the tested compounds. The compounds with diazine ring system except the 4d showed better urease inhibition (IC = 11.43 ± 0.21-19.63 ± 0.28 µM) than the standard urease inhibitor thiourea (IC = 22.61 ± 0.23 µM). Similarly enzyme kinetics data revealed that compounds 3c-3e and 8b were competitive inhibitors with Ki values of 20.0, 19.87, 20.23 and 19.11 µM respectively while the compounds 4b, 4c and 4e were mixed type of inhibitors with Ki values 6.72, 19.69 and 6.72 µM respectively. Molecular docking studies were also performed to identify the plausible binding modes of the most active compounds.
[Mh] Termos MeSH primário: Canavalia/enzimologia
Curcumina/análogos & derivados
Curcumina/farmacologia
Inibidores Enzimáticos/química
Inibidores Enzimáticos/farmacologia
Urease/antagonistas & inibidores
[Mh] Termos MeSH secundário: Compostos Azo/química
Compostos Azo/farmacologia
Concentração Inibidora 50
Isoxazóis/química
Isoxazóis/farmacologia
Pirazóis/química
Pirazóis/farmacologia
Pirimidinas/química
Pirimidinas/farmacologia
Relação Estrutura-Atividade
Tiossemicarbazonas/química
Tiossemicarbazonas/farmacologia
Tioureia/análogos & derivados
Tioureia/farmacologia
Urease/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Azo Compounds); 0 (Enzyme Inhibitors); 0 (Isoxazoles); 0 (Pyrazoles); 0 (Pyrimidines); 0 (Thiosemicarbazones); 0 (azomethine); EC 3.5.1.5 (Urease); GYV9AM2QAG (Thiourea); IT942ZTH98 (Curcumin)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170731
[Lr] Data última revisão:
170731
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170618
[St] Status:MEDLINE


  4 / 215 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28526368
[Au] Autor:Mentese E; Bektas H; Sokmen BB; Emirik M; Çakir D; Kahveci B
[Ad] Endereço:Department of Chemistry, Art and Science Faculty, Recep Tayyip Erdogan University, Rize, Turkey. Electronic address: emre.mentese@erdogan.edu.tr.
[Ti] Título:Synthesis and molecular docking study of some 5,6-dichloro-2-cyclopropyl-1H-benzimidazole derivatives bearing triazole, oxadiazole, and imine functionalities as potent inhibitors of urease.
[So] Source:Bioorg Med Chem Lett;27(13):3014-3018, 2017 07 01.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A new series of benzimidazole compounds including hydrazinecarbothioamide, 1,2,4-triazole, 1,3,4-oxadiazole and imine function were synthesized starting from 5,6-dichloro-2-cyclopropyl-1H-benzimidazole. All of the benzimidazole derivatives exhibited good urease inhibitor activity. Compound 6a proved to be the most potent showing an enzyme inhibitory activity with an IC =0.06µM. Molecular docking studies were also conducted on enzyme extracted from Jack bean urease to identify the binding mode of the newly synthesized compounds.
[Mh] Termos MeSH primário: Benzimidazóis/farmacologia
Inibidores Enzimáticos/farmacologia
Simulação de Acoplamento Molecular
Urease/antagonistas & inibidores
[Mh] Termos MeSH secundário: Benzimidazóis/síntese química
Benzimidazóis/química
Canavalia/enzimologia
Relação Dose-Resposta a Droga
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
Iminas/química
Iminas/farmacologia
Estrutura Molecular
Oxidiazóis/química
Oxidiazóis/farmacologia
Relação Estrutura-Atividade
Triazóis/química
Triazóis/farmacologia
Urease/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzimidazoles); 0 (Enzyme Inhibitors); 0 (Imines); 0 (Oxadiazoles); 0 (Triazoles); EC 3.5.1.5 (Urease)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171124
[Lr] Data última revisão:
171124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170521
[St] Status:MEDLINE


  5 / 215 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28388008
[Au] Autor:Saeed A; Larik FA; Channar PA; Mehfooz H; Ashraf MH; Abbas Q; Hassan M; Seo SY
[Ad] Endereço:Department of Chemistry, Quaid-I-Azam University, Islamabad, Pakistan.
[Ti] Título:An expedient synthesis of N-(1-(5-mercapto-4-((substituted benzylidene)amino)-4H-1,2,4-triazol-3-yl)-2-phenylethyl)benzamides as jack bean urease inhibitors and free radical scavengers: Kinetic mechanism and molecular docking studies.
[So] Source:Chem Biol Drug Des;90(5):764-777, 2017 Nov.
[Is] ISSN:1747-0285
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In this study, some new azomethine-triazole hybrids 5a-5l derived from N-benzoyl-L-phenylalanine were synthesized and characterized. The synthesized compounds showed first-rate, urease inhibition, and compounds 5c and 5e were found to be most effective inhibitors with 0.0137 ± 0.00082 µm and 0.0183 ± 0.00068 µm, respectively (thiourea 15.151 ± 1.27 µm). The kinetic mechanism of urease inhibition revealed the compounds 5c and 5e to be non-competitive inhibitors, whereas compounds 5d and 5j were found to be of mixed-type inhibitors. Docking studies also indicated better interaction patterns with urease enzyme. The results of enzyme inhibition, kinetic mechanism and molecular docking suggest that these compounds can serve as lead compounds in the design of more effective urease inhibitors.
[Mh] Termos MeSH primário: Benzamidas/química
Benzamidas/farmacologia
Canavalia/enzimologia
Inibidores Enzimáticos/química
Inibidores Enzimáticos/farmacologia
Depuradores de Radicais Livres/química
Depuradores de Radicais Livres/farmacologia
Urease/antagonistas & inibidores
[Mh] Termos MeSH secundário: Benzamidas/síntese química
Canavalia/efeitos dos fármacos
Inibidores Enzimáticos/síntese química
Depuradores de Radicais Livres/síntese química
Simulação de Acoplamento Molecular
Triazóis/síntese química
Triazóis/química
Triazóis/farmacologia
Urease/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzamides); 0 (Enzyme Inhibitors); 0 (Free Radical Scavengers); 0 (Triazoles); EC 3.5.1.5 (Urease)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170408
[St] Status:MEDLINE
[do] DOI:10.1111/cbdd.12998


  6 / 215 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28190471
[Au] Autor:Batista J; Ralph MT; Vaz RV; Souza P; Silva AB; Nascimento D; Souza LT; Ramos MV; Mastroeni P; Lima-Filho JV
[Ad] Endereço:Department of Biology, Federal Rural University of Pernambuco, Recife-PE, CEP 52171-900 Brazil.
[Ti] Título:Plant lectins ConBr and CFL modulate expression toll-like receptors, pro-inflammatory cytokines and reduce the bacterial burden in macrophages infected with Salmonella enterica serovar Typhimurium.
[So] Source:Phytomedicine;25:52-60, 2017 Feb 15.
[Is] ISSN:1618-095X
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Plant lectins have long been used in biomedical research as immunomodulators against tumor cells and microbial infections. PURPOSE: To test the ability of plant lectins ConBr (Canavalia brasiliensis) and CFL (Cratylia argentea) to activate antimicrobial and immunomodulatory activities of murine peritoneal macrophages (pMØ) infected with a virulent strain of Salmonella enterica serovar Typhimurium (STm). METHODS: We incubated pMØ with non-toxic amounts of ConBr and CFL either before (preventive schedule) or after (curative schedule) exposure to STm. RESULTS: In uninfected pMØ, ConBr and CFL greatly increased levels of mRNA transcripts for IL-1ß, TNF-α and IL-6 and the inducible nitric oxide synthase (iNOs), but not IL-10 and IL-12. Exposure to naïve splenocytes of culture supernatants of pMØ previously stimulated with CFL resulted in expression of IL-12 and IFN-γ. Both preventive and curative treatment schedules significantly reduced the intracellular load of Salmonella. Experiments in infected macrophages exposed to lectins in the preventive schedule showed that mRNA transcripts for IL-6 and TNF-α were increased by CFL, whereas ConBr enhanced IL-12 (subunit p40). In the curative schedule, CFL induced significant expression of IL-12 (p40) whereas ConBr enhanced expression IL-1ß and TNF-α genes. The lectin treatments did not influence on iNOs expression in pMØ infected with STm C5 regardless of the treatment schedule. Curative treatments with CFL increased approximately 130-fold expression of TLR-4 whist expression of TLR-9 was increased by treatments with ConBr. CONCLUSION: We conclude that lectins ConBr and CFL have immunomodulatory properties that are beneficial on control of cells infected by Salmonella.
[Mh] Termos MeSH primário: Citocinas/metabolismo
Fabaceae/química
Macrófagos Peritoneais/efeitos dos fármacos
Lectinas de Plantas/farmacologia
Salmonella typhimurium/efeitos dos fármacos
Receptores Toll-Like/metabolismo
[Mh] Termos MeSH secundário: Animais
Antibacterianos/farmacologia
Antibacterianos/uso terapêutico
Canavalia/química
Fatores Imunológicos/farmacologia
Fatores Imunológicos/uso terapêutico
Inflamação/metabolismo
Interleucina-12/metabolismo
Interleucina-1beta/metabolismo
Interleucina-6/metabolismo
Macrófagos Peritoneais/metabolismo
Macrófagos Peritoneais/microbiologia
Camundongos
Óxido Nítrico Sintase Tipo II/metabolismo
Fitoterapia
Lectinas de Plantas/uso terapêutico
Infecções por Salmonella/tratamento farmacológico
Infecções por Salmonella/metabolismo
Infecções por Salmonella/microbiologia
Sorogrupo
Transdução de Sinais/efeitos dos fármacos
Fator de Necrose Tumoral alfa
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Cytokines); 0 (Immunologic Factors); 0 (Interleukin-1beta); 0 (Interleukin-6); 0 (Plant Lectins); 0 (Toll-Like Receptors); 0 (Tumor Necrosis Factor-alpha); 0 (lectin, Canavalia); 187348-17-0 (Interleukin-12); EC 1.14.13.39 (Nitric Oxide Synthase Type II)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170517
[Lr] Data última revisão:
170517
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170214
[St] Status:MEDLINE


  7 / 215 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28087670
[Au] Autor:Gong T; Wang X; Yang Y; Yan Y; Yu C; Zhou R; Jiang W
[Ad] Endereço:Institute of Immunology and the Chinese Academy of Sciences Key Laboratory of Innate Immunity and Chronic Disease, Chinese Academy of Sciences Center for Excellence in Molecular Cell Sciences, School of Life Sciences and Medical Center, University of Science and Technology of China, Hefei 230027, Ch
[Ti] Título:Plant Lectins Activate the NLRP3 Inflammasome To Promote Inflammatory Disorders.
[So] Source:J Immunol;198(5):2082-2092, 2017 Mar 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Plant-derived dietary lectins have been reported to be involved in the pathogenesis of several inflammatory diseases, including inflammatory bowel disease, diabetes, rheumatoid arthritis, and celiac disease, but little is known about the molecular mechanisms underlying lectin-induced inflammation. In this study, we showed that plant lectins can induce caspase-1 activation and IL-1ß secretion via the NLRP3 inflammasome. Lectins were internalized and subsequently escaped from the lysosome and then translocated to the endoplasmic reticulum. Endoplasmic reticulum-loaded plant lectins then triggered Ca release and mitochondrial damage, and inhibition of Ca release and mitochondrial reactive oxygen species by chemical inhibitors significantly suppressed NLRP3 inflammasome activation. In vivo, plant lectin-induced inflammation and tissue damage also depended on the NLRP3 inflammasome. Our findings indicate that plant lectins can act as an exogenous "danger signal" that can activate the NLRP3 inflammasome and suggest that dietary lectins might promote inflammatory diseases via the NLRP3 inflammasome.
[Mh] Termos MeSH primário: Doenças Autoimunes/imunologia
Canavalia/imunologia
Inflamassomos/metabolismo
Inflamação/imunologia
Mitocôndrias/metabolismo
Proteína 3 que Contém Domínio de Pirina da Família NLR/metabolismo
Lectinas de Plantas/metabolismo
[Mh] Termos MeSH secundário: Animais
Sinalização do Cálcio
Caspase 1/metabolismo
Dieta
Retículo Endoplasmático/metabolismo
Seres Humanos
Interleucina-1beta/metabolismo
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Lectinas de Plantas/imunologia
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Inflammasomes); 0 (Interleukin-1beta); 0 (NLR Family, Pyrin Domain-Containing 3 Protein); 0 (Nlrp3 protein, mouse); 0 (Plant Lectins); 0 (Reactive Oxygen Species); EC 3.4.22.36 (Caspase 1)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170919
[Lr] Data última revisão:
170919
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170115
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1600145


  8 / 215 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28063388
[Au] Autor:Chen L; Tse WH; Chen Y; McDonald MW; Melling J; Zhang J
[Ad] Endereço:Department of Chemical & Biochemical Engineering, University of Western Ontario, London, Ontario, Canada N6A 5B9.
[Ti] Título:Nanostructured biosensor for detecting glucose in tear by applying fluorescence resonance energy transfer quenching mechanism.
[So] Source:Biosens Bioelectron;91:393-399, 2017 May 15.
[Is] ISSN:1873-4235
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In this paper, a nanostructured biosensor is developed to detect glucose in tear by using fluorescence resonance energy transfer (FRET) quenching mechanism. The designed FRET pair, including the donor, CdSe/ZnS quantum dots (QDs), and the acceptor, dextran-binding malachite green (MG-dextran), was conjugated to concanavalin A (Con A), an enzyme with specific affinity to glucose. In the presence of glucose, the quenched emission of QDs through the FRET mechanism is restored by displacing the dextran from Con A. To have a dual-modulation sensor for convenient and accurate detection, the nanostructured FRET sensors were assembled onto a patterned ZnO nanorod array deposited on the synthetic silicone hydrogel. Consequently, the concentration of glucose detected by the patterned sensor can be converted to fluorescence spectra with high signal-to-noise ratio and calibrated image pixel value. The photoluminescence intensity of the patterned FRET sensor increases linearly with increasing concentration of glucose from 0.03mmol/L to 3mmol/L, which covers the range of tear glucose levels for both diabetics and healthy subjects. Meanwhile, the calibrated values of pixel intensities of the fluorescence images captured by a handhold fluorescence microscope increases with increasing glucose. Four male Sprague-Dawley rats with different blood glucose concentrations were utilized to demonstrate the quick response of the patterned FRET sensor to 2µL of tear samples.
[Mh] Termos MeSH primário: Técnicas Biossensoriais/métodos
Glicemia/análise
Transferência Ressonante de Energia de Fluorescência/métodos
Glucose/análise
Pontos Quânticos/química
Lágrimas/química
[Mh] Termos MeSH secundário: Animais
Compostos de Cádmio/química
Canavalia/química
Corantes/química
Concanavalina A/química
Dextranos/química
Hidrogel de Polietilenoglicol-Dimetacrilato/química
Masculino
Modelos Moleculares
Nanotubos/química
Nanotubos/ultraestrutura
Pontos Quânticos/ultraestrutura
Ratos Sprague-Dawley
Corantes de Rosanilina/química
Compostos de Selênio/química
Razão Sinal-Ruído
Silício/química
Sulfetos/química
Compostos de Zinco/química
Óxido de Zinco/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Blood Glucose); 0 (Cadmium Compounds); 0 (Coloring Agents); 0 (Dextrans); 0 (Rosaniline Dyes); 0 (Selenium Compounds); 0 (Sulfides); 0 (Zinc Compounds); 11028-71-0 (Concanavalin A); 12058M7ORO (malachite green); 25852-47-5 (Hydrogel, Polyethylene Glycol Dimethacrylate); A7F646JC5C (cadmium selenide); IY9XDZ35W2 (Glucose); KPS085631O (zinc sulfide); SOI2LOH54Z (Zinc Oxide); Z4152N8IUI (Silicon)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170108
[St] Status:MEDLINE


  9 / 215 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28011200
[Au] Autor:Pervez H; Khan N; Zaib S; Yaqub M; Naseer MM; Tahir MN; Iqbal J
[Ad] Endereço:Institute of Chemical Sciences, Organic Chemistry Division, Bahauddin Zakariya University, Multan 60800, Pakistan. Electronic address: pdhpervez@hotmail.com.
[Ti] Título:Synthesis, X-ray molecular structure, biological evaluation and molecular docking studies of some N -benzyl substituted 5-nitroisatin-3-thiosemicarbazones.
[So] Source:Bioorg Med Chem;25(3):1022-1029, 2017 Feb 01.
[Is] ISSN:1464-3391
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A series of fifteen N -benzyl substituted 5-nitroisatin-3-thiosemicarbazones 5a-o was synthesized and evaluated for urease inhibitory, phytotoxic and cytotoxic influences. All the compounds proved to be highly potent inhibitors of the enzyme, showing inhibitory activity (IC =0.87±0.25-8.09±0.23µM) much better than the reference inhibitor, thiourea (IC =22.3±1.12µM) and may thus act as persuasive leads for further studies. In phytotoxicity assay, twelve out of fifteen thiosemicarbazones tested i.e. 5a-e, 5g, 5i and 5k-o appeared to be active, exhibiting weak or non-significant (5-35%) growth inhibition at the highest tested concentrations (1000 or 500µg/mL). In contrast, only one compound i.e. 5i was active in the brine shrimp (Artemia salina) lethality bioassay, demonstrating cytotoxic activity with LD value 2.55×10 M. Molecular docking studies of compounds 5a-o were also performed to identify their probable binding modes in the active site of the enzyme.
[Mh] Termos MeSH primário: Artemia/efeitos dos fármacos
Canavalia/enzimologia
Inibidores Enzimáticos/farmacologia
Isatina/farmacologia
Tiossemicarbazonas/farmacologia
Urease/antagonistas & inibidores
[Mh] Termos MeSH secundário: Animais
Artemia/citologia
Cristalografia por Raios X
Relação Dose-Resposta a Droga
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
Isatina/síntese química
Isatina/química
Modelos Moleculares
Estrutura Molecular
Relação Estrutura-Atividade
Tiossemicarbazonas/síntese química
Tiossemicarbazonas/química
Urease/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Thiosemicarbazones); 82X95S7M06 (Isatin); EC 3.5.1.5 (Urease)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170803
[Lr] Data última revisão:
170803
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161225
[St] Status:MEDLINE


  10 / 215 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27914345
[Au] Autor:Saxena A; Bhattacharya A; Kumar S; Epstein IR; Sahney R
[Ad] Endereço:Amity Institute of Biotechnology, AUUP, Noida 201301, India.
[Ti] Título:Biopolymer matrix for nano-encapsulation of urease - A model protein and its application in urea detection.
[So] Source:J Colloid Interface Sci;490:452-461, 2017 Mar 15.
[Is] ISSN:1095-7103
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Alginate microparticles and nanoparticles crosslinked with Ca ions are frequently employed in biomedical applications. Here we use microemulsion polymerization to prepare alginate nanoparticles (nanogels) using different crosslinking ions (Ca , Sr , Ba ) to encapsulate a model protein, urease enzyme (jackbeans). With alginate concentrations of 0.2wt% in the aqueous phase, emulsion droplets showed good stability and narrow, monomodal distributions with radii ∼65±10nm. The size of the nanogel varies with the crosslinking cation and its affinity for the mannuronate and guluronate units in the linear alginate chain. The nanogels were further characterized using dynamic light scattering, scanning electron microscopy, energy dispersive X-ray spectrometry and zeta potential. This work demonstrates the potential application of Ba-alginate as an alternative matrix for nano-encapsulation of proteins and its use for biomedical applications.
[Mh] Termos MeSH primário: Alginatos/química
Canavalia/enzimologia
Enzimas Imobilizadas/química
Géis/química
Nanopartículas/química
Ureia/sangue
Urease/química
[Mh] Termos MeSH secundário: Cátions/química
Reagentes para Ligações Cruzadas/química
Emulsões/química
Enzimas Imobilizadas/metabolismo
Ácido Glucurônico/química
Ácidos Hexurônicos/química
Seres Humanos
Ureia/metabolismo
Urease/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Alginates); 0 (Cations); 0 (Cross-Linking Reagents); 0 (Emulsions); 0 (Enzymes, Immobilized); 0 (Gels); 0 (Hexuronic Acids); 8A5D83Q4RW (Glucuronic Acid); 8C3Z4148WZ (alginic acid); 8W8T17847W (Urea); EC 3.5.1.5 (Urease)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170418
[Lr] Data última revisão:
170418
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161204
[St] Status:MEDLINE



página 1 de 22 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