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  1 / 8610 MEDLINE  
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[PMID]:29248751
[Au] Autor:Can NÖ; Osmaniye D; Levent S; Saglik BN; Korkut B; Atli Ö; Özkay Y; Kaplancikli ZA
[Ad] Endereço:Department of Analytical Chemistry, Faculty of Pharmacy, Anadolu University, 26470 Eskisehir, Turkey; Doping and Narcotic Compounds Analysis Laboratory, Faculty of Pharmacy, Anadolu University, 26470 Eskisehir, Turkey.
[Ti] Título:Design, synthesis and biological assessment of new thiazolylhydrazine derivatives as selective and reversible hMAO-A inhibitors.
[So] Source:Eur J Med Chem;144:68-81, 2018 Jan 20.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:In the recent works, it was shown that numerous thiazolylhydrazine derivatives display hMAO inhibitory activity in the range of micromolar concentration. Hence, in the present study a new series of new thiazole-hydrazines (3a-3n) were designed, synthesized, characterized and screened for their hMAO-A and hMAO-B inhibitory activity by an in vitro flurometric method. The enzyme inhibition assay revealed that most of the synthesized compounds have selective inhibition potency against hMAO-A. The compounds 3f and 3h showed promising hMAO-A inhibition with an IC values of 0.012 µM and 0.011 µM and significant selectivity indexes of 1214 and 1601 towards hMAO-A, respectively. The mechanism of hMAO-A inhibition of compounds 3f and 3h was investigated by Lineweaver-Burk graphics and reversible-competitive inhibition of hMAO-A was determined. Cytotoxicity and genotoxicity studies were carried out and the compound 3h was found as non-cytotoxic and non-genotoxic. Theoretical calculation of ADME properties suggested that synthesized compounds may have a good pharmacokinetic profile. The docking study of compound 3f and 3h revealed that there is a strong interaction between the active sites of hMAO-A and analyzed compound.
[Mh] Termos MeSH primário: Inibidores da Monoaminoxidase/química
Inibidores da Monoaminoxidase/farmacologia
Monoaminoxidase/metabolismo
Tiazóis/química
Tiazóis/farmacologia
[Mh] Termos MeSH secundário: Domínio Catalítico/efeitos dos fármacos
Desenho de Drogas
Seres Humanos
Hidrazinas/química
Hidrazinas/farmacologia
Simulação de Acoplamento Molecular
Monoaminoxidase/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hydrazines); 0 (Monoamine Oxidase Inhibitors); 0 (Thiazoles); EC 1.4.3.4 (Monoamine Oxidase)
[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:171218
[St] Status:MEDLINE


  2 / 8610 MEDLINE  
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[PMID]:29247860
[Au] Autor:Schulz-Fincke J; Hau M; Barth J; Robaa D; Willmann D; Kürner A; Haas J; Greve G; Haydn T; Fulda S; Lübbert M; Lüdeke S; Berg T; Sippl W; Schüle R; Jung M
[Ad] Endereço:Institute of Pharmaceutical Sciences, University of Freiburg, Germany; German Cancer Consortium (DKTK), Freiburg, Germany; German Cancer Research Center (DKFZ), Heidelberg, Germany.
[Ti] Título:Structure-activity studies on N-Substituted tranylcypromine derivatives lead to selective inhibitors of lysine specific demethylase 1 (LSD1) and potent inducers of leukemic cell differentiation.
[So] Source:Eur J Med Chem;144:52-67, 2018 Jan 20.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:FAD-dependent lysine-specific demethylase 1 (LSD1) is overexpressed or deregulated in many cancers such as AML and prostate cancer and hence is a promising anticancer target with first inhibitors in clinical trials. Clinical candidates are N-substituted derivatives of the dual LSD1-/monoamine oxidase-inhibitor tranylcypromine (2-PCPA) with a basic amine function in the N-substituent. These derivatives are selective over monoamine oxidases. So far, only very limited information on structure-activity studies about this important class of LSD1 inhibitors is published in peer reviewed journals. Here, we show that N-substituted 2-PCPA derivatives without a basic function or even a polar group are still potent inhibitors of LSD1 in vitro and effectively inhibit colony formation of leukemic cells in culture. Yet, these lipophilic inhibitors also block the structurally related monoamine oxidases (MAO-A and MAO-B), which may be of interest for the treatment of neurodegenerative disorders, but this property is undesired for applications in cancer treatment. The introduction of a polar, non-basic function led to optimized structures that retain potent LSD1 inhibitors but exhibit selectivity over MAOs and are highly potent in the suppression of colony formation of cultured leukemic cells. Cellular target engagement is shown via a Cellular Thermal Shift Assay (CETSA) for LSD1.
[Mh] Termos MeSH primário: Inibidores Enzimáticos/química
Inibidores Enzimáticos/farmacologia
Histona Desmetilases/antagonistas & inibidores
Tranilcipromina/análogos & derivados
Tranilcipromina/farmacologia
[Mh] Termos MeSH secundário: Animais
Antineoplásicos/química
Antineoplásicos/farmacologia
Diferenciação Celular/efeitos dos fármacos
Linhagem Celular Tumoral
Histona Desmetilases/metabolismo
Seres Humanos
Leucemia/tratamento farmacológico
Leucemia/metabolismo
Leucemia/patologia
Camundongos
Modelos Moleculares
Inibidores da Monoaminoxidase/química
Inibidores da Monoaminoxidase/farmacologia
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Enzyme Inhibitors); 0 (Monoamine Oxidase Inhibitors); 3E3V44J4Z9 (Tranylcypromine); EC 1.14.11.- (Histone Demethylases); EC 1.5.- (KDM1A protein, human)
[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:171217
[St] Status:MEDLINE


  3 / 8610 MEDLINE  
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[PMID]:29339253
[Au] Autor:Xiao X; Zhang XX; Zhan MM; Cheng K; Li S; Xie Z; Liao C
[Ad] Endereço:School of Biological and Medical Engineering, Hefei University of Technology, Hefei, Anhui 230009, PR China.
[Ti] Título:Design, synthesis and bioevalucation of novel 2,3-dihydro-1H-inden-1-amine derivatives as potent and selective human monoamine oxidase B inhibitors based on rasagiline.
[So] Source:Eur J Med Chem;145:588-593, 2018 Feb 10.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Parkinson's disease (PD) is associated with elevated levels of hMAO-B in the brain, and MAO-B has been recognized a successful target for developing anti-PD drugs. Herein we report rasagiline derivatives as novel potent and selective hMAO-B inhibitors. They were designed by employing fragment-based drug design strategy to link rasagiline and hydrophobic fragments, which may target a hydrophobic pocket in the entrance cavity of hMAO-B. Different linkers such as -OCH -, -SCH -, -OCH CH -, -OCH CH O-, -OCH CH CH O- were tried. A promising selective hMAO-B inhibitor D14 with similar inhibitory activity as rasagiline and improved isoform selectivity was yielded. The selectivity profile of compounds reported herein suggests that we can further develop more potent hMAO-B inhibitors with high isoform selectivity through this strategy.
[Mh] Termos MeSH primário: Aminas/farmacologia
Desenho de Drogas
Indanos/farmacologia
Indenos/farmacologia
Inibidores da Monoaminoxidase/farmacologia
Monoaminoxidase/metabolismo
[Mh] Termos MeSH secundário: Aminas/síntese química
Aminas/química
Cristalografia por Raios X
Relação Dose-Resposta a Droga
Seres Humanos
Indanos/química
Indenos/síntese química
Indenos/química
Modelos Moleculares
Estrutura Molecular
Inibidores da Monoaminoxidase/síntese química
Inibidores da Monoaminoxidase/química
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amines); 0 (Indans); 0 (Indenes); 0 (Monoamine Oxidase Inhibitors); 003N66TS6T (rasagiline); EC 1.4.3.4 (Monoamine Oxidase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180302
[Lr] Data última revisão:
180302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE


  4 / 8610 MEDLINE  
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[PMID]:29335210
[Au] Autor:Tripathi AC; Upadhyay S; Paliwal S; Saraf SK
[Ad] Endereço:Division of Pharmaceutical Chemistry, Faculty of Pharmacy, Babu Banarasi Das Northern India Institute of Technology, Lucknow 226028, UP, India.
[Ti] Título:Privileged scaffolds as MAO inhibitors: Retrospect and prospects.
[So] Source:Eur J Med Chem;145:445-497, 2018 Feb 10.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:This review aims to be a comprehensive, authoritative, critical, and readable review of general interest to the medicinal chemistry community because it focuses on the pharmacological, chemical, structural and computational aspects of diverse chemical categories as monoamine oxidase inhibitors (MAOIs). Monoamine oxidases (MAOs), namely MAO-A and MAO-B represent an enormously valuable class of neuronal enzymes embodying neurobiological origin and functions, serving as potential therapeutic target in neuronal pharmacotherapy, and hence we have coined the term "Neurozymes" which is being introduced for the first time ever. Nowadays, therapeutic attention on MAOIs engrosses two imperative categories; MAO-A inhibitors, in certain mental disorders such as depression and anxiety, and MAO-B inhibitors, in neurodegenerative disorders like Alzheimer's disease (AD) and Parkinson's disease (PD). The use of MAOIs declined due to some potential side effects, food and drug interactions, and introduction of other classes of drugs. However, curiosity in MAOIs is reviving and the recent developments of new generation of highly selective and reversible MAOIs, have renewed the therapeutic prospective of these compounds. The initial section of the review emphasizes on the detailed classification, structural and binding characteristics, therapeutic potential, current status and future challenges of the privileged pharmacophores. However, the chemical prospective of privileged scaffolds such as; aliphatic and aromatic amines, amides, hydrazines, azoles, diazoles, tetrazoles, indoles, azines, diazines, xanthenes, tricyclics, benzopyrones, and more interestingly natural products, along with their conclusive SARs have been discussed in the later segment of review. The last segment of the article encompasses some patents granted in the field of MAOIs, in a simplistic way.
[Mh] Termos MeSH primário: Inibidores da Monoaminoxidase/farmacologia
Monoaminoxidase/metabolismo
[Mh] Termos MeSH secundário: Animais
Sítios de Ligação/efeitos dos fármacos
Relação Dose-Resposta a Droga
Seres Humanos
Estrutura Molecular
Inibidores da Monoaminoxidase/química
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Monoamine Oxidase Inhibitors); EC 1.4.3.4 (Monoamine Oxidase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180302
[Lr] Data última revisão:
180302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180117
[St] Status:MEDLINE


  5 / 8610 MEDLINE  
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[PMID]:29268246
[Au] Autor:Herraiz T; Flores A; Fernández L
[Ad] Endereço:Instituto de Ciencia y Tecnología de Alimentos y Nutrición (ICTAN), Spanish National Research Council (CSIC), Juan de la Cierva 3, 28006, Madrid, Spain. Electronic address: tomas.herraiz@csic.es.
[Ti] Título:Analysis of monoamine oxidase (MAO) enzymatic activity by high-performance liquid chromatography-diode array detection combined with an assay of oxidation with a peroxidase and its application to MAO inhibitors from foods and plants.
[So] Source:J Chromatogr B Analyt Technol Biomed Life Sci;1073:136-144, 2018 Jan 15.
[Is] ISSN:1873-376X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Monoamine oxidase (MAO) enzymes catalyze the oxidative deamination of biogenic amines and neurotransmitters and produce ammonia, aldehydes, and hydrogen peroxide which is involved in oxidative processes. Inhibitors of MAO-A and -B isozymes are useful as antidepressants and neuroprotectants. The assays of MAO usually measure amine oxidation products or hydrogen peroxide by spectrophotometric techniques. Those assays are often compromised by interfering compounds resulting in poor results. This research describes a new method that combines in the same assay the oxidative deamination of kynuramine to 4-hydroxyquinoline analyzed by HPLC-DAD with the oxidation of tetramethylbenzidine (TMB) (or Amplex Rex) by horseradish peroxidase (HRP) in presence of hydrogen peroxide. The new method was applied to study the inhibition of human MAO-A and -B by bioactive compounds including ß-carboline alkaloids and flavonoids occurring in foods and plants. As determined by HPLC-DAD, ß-carbolines, methylene blue, kaempferol and clorgyline inhibited MAO-A and methylene blue, 5-nitroindazole, norharman and deprenyl inhibited MAO-B, and all of them inhibited the oxidation of TMB in the same extent. The flavonoids catechin and cyanidin were not inhibitors of MAO by HPLC-DAD but highly inhibited the oxidation of TMB (or Amplex Red) by peroxidase whereas quercetin and resveratrol were moderate inhibitors of MAO-A by HPLC-DAD, but inhibited the peroxidase assay in a higher level. For some phenolic compounds, using the peroxidase-coupled assay to measure MAO activity led to mistaken results. The new method permits to discern between true inhibitors of MAO from those that are antioxidants and which interfere with peroxidase assays but do not inhibit MAO. For true inhibitors of MAO, inhibition as determined by HPLC-DAD correlated well with inhibition of the oxidation of TMB and this approach can be used to assess the in vitro antioxidant activity (less hydrogen peroxide production) resulting from MAO inhibition.
[Mh] Termos MeSH primário: Cromatografia Líquida de Alta Pressão/métodos
Inibidores da Monoaminoxidase/metabolismo
Monoaminoxidase/análise
Monoaminoxidase/metabolismo
Peroxidase/metabolismo
[Mh] Termos MeSH secundário: Antioxidantes/metabolismo
Carbolinas
Flavonoides
Seres Humanos
Cinuramina/análise
Cinuramina/metabolismo
Oxirredução
Extratos Vegetais/análise
Extratos Vegetais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Carbolines); 0 (Flavonoids); 0 (Monoamine Oxidase Inhibitors); 0 (Plant Extracts); 363-36-0 (Kynuramine); EC 1.11.1.7 (Peroxidase); EC 1.4.3.4 (Monoamine Oxidase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180302
[Lr] Data última revisão:
180302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171222
[St] Status:MEDLINE


  6 / 8610 MEDLINE  
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[PMID]:29324067
[Au] Autor:Carradori S; Secci D; Petzer JP
[Ad] Endereço:a Department of Pharmacy , "G. d'Annunzio" University of Chieti-Pescara , Chieti , Italy.
[Ti] Título:MAO inhibitors and their wider applications: a patent review.
[So] Source:Expert Opin Ther Pat;28(3):211-226, 2018 Mar.
[Is] ISSN:1744-7674
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: Monoamine oxidase (MAO) inhibitors, after the initial 'golden age', are currently used as third-line antidepressants (selective MAO-A inhibitors) or clinically enrolled as co-adjuvants for neurodegenerative diseases (selective MAO-B inhibitors). However, the research within this field is always increasing due to their pivotal role in modulating synaptic functions and monoamines metabolism. Areas covered: In this paper, MAO inhibitors (2015-2017) are disclosed ordering all the patents according to their chemical scaffold. Structure-activity relationships (SARs) are extrapolated for the most investigated chemotypes (coumarins, pyrazole/oxazepinones, (hetero)arylamides). 108 Compounds are divided into two main groups: newly synthesized molecules and naturally-occurring metabolites. Finally, new therapeutic options are outlined to ensure a more complete view on the potential of these inhibitors. Expert opinion: New proposed MAO inhibitors are endowed with a marked isoform selectivity, with innovative therapeutic potential toward other targets (gliomas, inflammation, muscle dystrophies, migraine, chronic pain, pseudobulbar affect), and with a promising ability to address multi-faceted pathologies such as Alzheimer's disease. The increasing number of patents is analyzed collecting data from 2002 to 2017.
[Mh] Termos MeSH primário: Desenho de Drogas
Inibidores da Monoaminoxidase/farmacologia
Doenças Neurodegenerativas/tratamento farmacológico
[Mh] Termos MeSH secundário: Animais
Antidepressivos/química
Antidepressivos/farmacologia
Seres Humanos
Monoaminoxidase/efeitos dos fármacos
Monoaminoxidase/metabolismo
Inibidores da Monoaminoxidase/química
Doenças Neurodegenerativas/fisiopatologia
Patentes como Assunto
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antidepressive Agents); 0 (Monoamine Oxidase Inhibitors); EC 1.4.3.4 (Monoamine Oxidase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE
[do] DOI:10.1080/13543776.2018.1427735


  7 / 8610 MEDLINE  
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[PMID]:29250969
[Au] Autor:Szász JA; Constantin V; Fazakas PA; Blényesi E; Grieb LG; Balla A; Sárig M; Szegedi K; Bartha EN; Szatmári S
[Ad] Endereço:Neurológiai Tanszék (Department of Neurology), Marosvásárhelyi Orvosi és Gyógyszerészeti Egyetem (University of Medicine and Pharmacy of Tirgu Mures) 540081 Marosvásárhely (Tirgu Mures), Gral Ion Dumitrache u. 20/2, Románia.
[Ti] Título:[The role of selective monoamine oxidase B inhibitors in the therapeutic strategy of Parkinson's disease in the neurology clinics of Tirgu Mures County Emergency Clinical Hospital].
[Ti] Título:A szelektív monoaminoxidáz-B-gátlók helye a Parkinson-kór kezelési stratégiájában a marosvásárhelyi ideggyógyászati klinikák gyakorlatában..
[So] Source:Orv Hetil;158(51):2023-2028, 2017 Dec.
[Is] ISSN:0030-6002
[Cp] País de publicação:Hungary
[La] Idioma:hun
[Ab] Resumo:INTRODUCTION: Selective monoamine oxidase B inhibitors have an accurate place in therapeutical strategy of Parkinsons's disease. In the early stages of the disease, especially in younger patients with milder symptoms, the introduction of levodopa substitution could be efficacious in delaying; in advanced stages they are mainly used to treat motor complications, as an adjunct to levodopa. AIM: The evaluation of therapeutical strategies used in the neurology clinics of Tirgu Mures County Emergency Clinical Hospital in order to define the role of monoamine oxidase B inhibitors. METHOD: This retrospective study includes all records of patients with Parkinson's disease hospitalized between 1 January 2003 and 31 December 2016. From the 2194 reports we used data focusing on the therapeutic recommendations. Regarding disease duration, we divided the patients in two groups: less than or equal to 5 years and more than 5 years. RESULTS: From the 1183 patients in first group, 243 received monoamine oxidase inhibitors: 12 as monotherapy, 52 together with dopamine agonists, in 61 cases combined with levodopa. In 118 cases monoamine oxidase inhibitors were combined with levodopa and dopamine agonists. From 582 cases whith Parkinson's disease for more than 5 years, 195 received monoamine oxidase B inhibitors (selegiline: 10 cases, rasagiline: 185 cases). In 429 cases we did not find accurate data regarding disease duration (selegiline: 5 cases, rasagiline: 93 cases). CONCLUSION: The use of monoamine oxidase B inhibitors was similar to those found in literature. The treating physicians should utilise more confidently the available therapeutical combinations. Orv Hetil. 2017; 158(51): 2023-2028.
[Mh] Termos MeSH primário: Antiparkinsonianos/uso terapêutico
Agonistas de Dopamina/uso terapêutico
Inibidores da Monoaminoxidase/uso terapêutico
Doença de Parkinson/tratamento farmacológico
[Mh] Termos MeSH secundário: Idoso
Instituições de Assistência Ambulatorial
Relação Dose-Resposta a Droga
Seres Humanos
Hungria
Levodopa/uso terapêutico
Masculino
Meia-Idade
Estudos Retrospectivos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antiparkinson Agents); 0 (Dopamine Agonists); 0 (Monoamine Oxidase Inhibitors); 46627O600J (Levodopa)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171219
[St] Status:MEDLINE
[do] DOI:10.1556/650.2017.30914


  8 / 8610 MEDLINE  
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[PMID]:29221756
[Au] Autor:Lesniak A; Aarnio M; Diwakarla S; Norberg T; Nyberg F; Gordh T
[Ad] Endereço:Uppsala University, Department of Pharmaceutical Biosciences, SE 751 24 Uppsala, Sweden; Medical University of Warsaw, Department of Pharmacodynamics, Centre for Preclinical Research and Technology, 02-097 Warsaw, Poland. Electronic address: anna.lesniak@wum.edu.pl.
[Ti] Título:Characterization of the binding site for d-deprenyl in human inflamed synovial membrane.
[So] Source:Life Sci;194:26-33, 2018 Feb 01.
[Is] ISSN:1879-0631
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:AIMS: d-Deprenyl when used as a positron emission tomography tracer visualizes peripheral inflammation. The major aim of the current study was to identify and investigate the properties of the binding target for d-deprenyl in synovial membrane explants from arthritic patients. MAIN METHODS: Thirty patients diagnosed with arthritis or osteoarthritis were enrolled into the study. Homologous and competitive radioligand binding assays utilizing [ H]d-deprenyl were performed to investigate the biochemical characteristics of the binding site and assess differences in the binding profile in synovial membranes exhibiting varying levels of inflammation. KEY FINDINGS: The [ H]d-deprenyl binding assay confirmed the existence of a single, saturable population of membrane-bound protein binding sites in synovial membrane homogenates. The macroscopically determined level of inflammation correlated with an increase in [ H]d-deprenyl binding affinity, without significant alterations in binding site density. Selective monoamine oxidase B inhibitor, selegiline competed for the same site as [ H]d-deprenyl, but failed to differentiate the samples with regard to their inflammation grade. A monoamine oxidase A inhibitor, pirlindole mesylate showed only weak displacement of [ H]d-deprenyl binding. No significant alterations in monoamine oxidase B expression was detected, thus it was not confirmed whether it could serve as a marker for ongoing inflammation. SIGNIFICANCE: Our study was the first to show the biochemical characteristics of the [ H]d-deprenyl binding site in inflamed human synovium. We confirmed that d-deprenyl could differentiate between patients with varying severity of synovitis in the knee joint by binding to a protein target distinct from monoamine oxidase B.
[Mh] Termos MeSH primário: Artrite/diagnóstico
Inibidores da Monoaminoxidase/metabolismo
Monoaminoxidase/análise
Selegilina/metabolismo
Membrana Sinovial/patologia
Sinovite/diagnóstico
[Mh] Termos MeSH secundário: Idoso
Artrite/metabolismo
Sítios de Ligação
Feminino
Seres Humanos
Masculino
Meia-Idade
Monoaminoxidase/metabolismo
Tomografia por Emissão de Pósitrons
Ensaio Radioligante
Membrana Sinovial/metabolismo
Sinovite/metabolismo
Trítio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Monoamine Oxidase Inhibitors); 10028-17-8 (Tritium); 2K1V7GP655 (Selegiline); EC 1.4.3.4 (Monoamine Oxidase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171210
[St] Status:MEDLINE


  9 / 8610 MEDLINE  
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[PMID]:29198609
[Au] Autor:Yeon SK; Choi JW; Park JH; Lee YR; Kim HJ; Shin SJ; Jang BK; Kim S; Bahn YS; Han G; Lee YS; Pae AN; Park KD
[Ad] Endereço:Convergence Research Center for Diagnosis, Treatment and Care System of Dementia, Korea Institute of Science and Technology, Seoul, Republic of Korea; Department of Biotechnology, Yonsei University, Seoul, Republic of Korea.
[Ti] Título:Synthesis and evaluation of biaryl derivatives for structural characterization of selective monoamine oxidase B inhibitors toward Parkinson's disease therapy.
[So] Source:Bioorg Med Chem;26(1):232-244, 2018 01 01.
[Is] ISSN:1464-3391
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Benzyloxyphenyl moiety is a common structure of highly potent, selective and reversible inhibitors of monoamine oxidase B (MAO-B), safinamide and sembragiline. We synthesized 4-(benzyloxy)phenyl and biphenyl-4-yl derivatives including halogen substituents on the terminal aryl unit. In addition, we modified the carbon linker between amine group and the biaryl linked unit. Among synthesized compounds, 12c exhibited the most potent and selective MAO-B inhibitory effect (hMAO-B IC : 8.9 nM; >10,000-fold selectivity over MAO-A) as a competitive inhibitor. In addition, 12c showed greater MAO-B inhibitory activity and selectivity compared to well-known MAO-B inhibitors such as selegiline, safinamide and sembragiline. In the MPTP-induced mouse model of Parkinson's disease (PD), 12c significantly protected the tyrosine hydroxylase (TH)-immunopositive DAergic neurons and attenuated the PD-associated behavioral deficits. This study suggests characteristic structures as a MAO-B inhibitor that may provide a good insight for the development of therapeutic agents for PD.
[Mh] Termos MeSH primário: Derivados de Benzeno/farmacologia
Inibidores da Monoaminoxidase/farmacologia
Monoaminoxidase/metabolismo
Doença de Parkinson/tratamento farmacológico
[Mh] Termos MeSH secundário: 1-Metil-4-Fenil-1,2,3,6-Tetra-Hidropiridina/administração & dosagem
Animais
Derivados de Benzeno/síntese química
Derivados de Benzeno/química
Modelos Animais de Doenças
Relação Dose-Resposta a Droga
Seres Humanos
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Estrutura Molecular
Inibidores da Monoaminoxidase/síntese química
Inibidores da Monoaminoxidase/química
Doença de Parkinson/metabolismo
Doença de Parkinson/patologia
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Benzene Derivatives); 0 (Monoamine Oxidase Inhibitors); 9P21XSP91P (1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine); EC 1.4.3.4 (Monoamine Oxidase); EC 1.4.3.4. (monoamine oxidase A, human)
[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:171205
[St] Status:MEDLINE


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[PMID]:28828469
[Au] Autor:Okun MS
[Ad] Endereço:Departments of Neurology and Neurosurgery, University of Florida Center for Movement Disorders and Neurorestoration, Gainesville.
[Ti] Título:Management of Parkinson Disease in 2017: Personalized Approaches for Patient-Specific Needs.
[So] Source:JAMA;318(9):791-792, 2017 Sep 05.
[Is] ISSN:1538-3598
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Antiparkinsonianos/uso terapêutico
Estimulação Encefálica Profunda
Levodopa/uso terapêutico
Doença de Parkinson/terapia
Medicina de Precisão
[Mh] Termos MeSH secundário: Seres Humanos
Bombas de Infusão
Inibidores da Monoaminoxidase/uso terapêutico
Doença de Parkinson/tratamento farmacológico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antiparkinson Agents); 0 (Monoamine Oxidase Inhibitors); 46627O600J (Levodopa)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170823
[St] Status:MEDLINE
[do] DOI:10.1001/jama.2017.7914



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