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  1 / 18 MEDLINE  
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[PMID]:26862473
[Au] Autor:Deniskin R; Frame IJ; Sosa Y; Akabas MH
[Ad] Endereço:Department of Physiology & Biophysics, Albert Einstein College of Medicine, Bronx, New York, USA.
[Ti] Título:Targeting the Plasmodium vivax equilibrative nucleoside transporter 1 (PvENT1) for antimalarial drug development.
[So] Source:Int J Parasitol Drugs Drug Resist;6(1):1-11, 2016 Apr.
[Is] ISSN:2211-3207
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Infection with Plasmodium falciparum and vivax cause most cases of malaria. Emerging resistance to current antimalarial medications makes new drug development imperative. Ideally a new antimalarial drug should treat both falciparum and vivax malaria. Because malaria parasites are purine auxotrophic, they rely on purines imported from the host erythrocyte via Equilibrative Nucleoside Transporters (ENTs). Thus, the purine import transporters represent a potential target for antimalarial drug development. For falciparum parasites the primary purine transporter is the P. falciparum Equilibrative Nucleoside Transporter Type 1 (PfENT1). Recently we identified potent PfENT1 inhibitors with nanomolar IC50 values using a robust, yeast-based high throughput screening assay. In the current work we characterized the Plasmodium vivax ENT1 (PvENT1) homologue and its sensitivity to the PfENT1 inhibitors. We expressed a yeast codon-optimized PvENT1 gene in Saccharomyces cerevisiae. PvENT1-expressing yeast imported both purines ([(3)H]adenosine) and pyrimidines ([(3)H]uridine), whereas wild type (fui1Δ) yeast did not. Based on radiolabel substrate uptake inhibition experiments, inosine had the lowest IC50 (3.8 µM), compared to guanosine (14.9 µM) and adenosine (142 µM). For pyrimidines, thymidine had an IC50 of 183 µM (vs. cytidine and uridine; mM range). IC50 values were higher for nucleobases compared to the corresponding nucleosides; hypoxanthine had a 25-fold higher IC50 than inosine. The archetypal human ENT1 inhibitor 4-nitrobenzylthioinosine (NBMPR) had no effect on PvENT1, whereas dipyridamole inhibited PvENT1, albeit with a 40 µM IC50, a 1000-fold less sensitive than human ENT1 (hENT1). The PfENT1 inhibitors blocked transport activity of PvENT1 and the five known naturally occurring non-synonymous single nucleotide polymorphisms (SNPs) with similar IC50 values. Thus, the PfENT1 inhibitors also target PvENT1. This implies that development of novel antimalarial drugs that target both falciparum and vivax ENT1 may be feasible.
[Mh] Termos MeSH primário: Antimaláricos/farmacologia
Descoberta de Drogas
Transportador Equilibrativo 1 de Nucleosídeo/antagonistas & inibidores
Proteínas de Transporte de Nucleobases, Nucleosídeos, Nucleotídeos e Ácidos Nucleicos/antagonistas & inibidores
Proteínas de Transporte de Nucleobases, Nucleosídeos, Nucleotídeos e Ácidos Nucleicos/metabolismo
Plasmodium falciparum/efeitos dos fármacos
Plasmodium vivax/efeitos dos fármacos
Proteínas de Protozoários/antagonistas & inibidores
Proteínas de Protozoários/metabolismo
[Mh] Termos MeSH secundário: Adenosina/farmacologia
Dipiridamol/farmacologia
Transportador Equilibrativo 1 de Nucleosídeo/genética
Guanosina/farmacologia
Seres Humanos
Concentração Inibidora 50
Inosina/farmacologia
Malária Falciparum/tratamento farmacológico
Malária Falciparum/parasitologia
Malária Vivax/tratamento farmacológico
Malária Vivax/parasitologia
Malária Vivax/prevenção & controle
Proteínas de Transporte de Nucleobases, Nucleosídeos, Nucleotídeos e Ácidos Nucleicos/genética
Plasmodium falciparum/metabolismo
Plasmodium vivax/genética
Polimorfismo de Nucleotídeo Único
Proteínas de Protozoários/genética
Purinas/metabolismo
Purinas/farmacologia
Pirimidinas/metabolismo
Saccharomyces cerevisiae/genética
Uridina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antimalarials); 0 (ENT1 protein, Plasmodium falciparum); 0 (Equilibrative Nucleoside Transporter 1); 0 (Nucleobase, Nucleoside, Nucleotide, and Nucleic Acid Transport Proteins); 0 (Protozoan Proteins); 0 (Purines); 0 (Pyrimidines); 12133JR80S (Guanosine); 5A614L51CT (Inosine); 64ALC7F90C (Dipyridamole); K72T3FS567 (Adenosine); WHI7HQ7H85 (Uridine)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160211
[St] Status:MEDLINE
[do] DOI:10.1016/j.ijpddr.2015.11.003


  2 / 18 MEDLINE  
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[PMID]:25602169
[Au] Autor:Frame IJ; Deniskin R; Rinderspacher A; Katz F; Deng SX; Moir RD; Adjalley SH; Coburn-Flynn O; Fidock DA; Willis IM; Landry DW; Akabas MH
[Ti] Título:Yeast-based high-throughput screen identifies Plasmodium falciparum equilibrative nucleoside transporter 1 inhibitors that kill malaria parasites.
[So] Source:ACS Chem Biol;10(3):775-83, 2015 Mar 20.
[Is] ISSN:1554-8937
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Equilibrative transporters are potential drug targets; however, most functional assays involve radioactive substrate uptake that is unsuitable for high-throughput screens (HTS). We developed a robust yeast-based growth assay that is potentially applicable to many equilibrative transporters. As proof of principle, we applied our approach to Equilibrative Nucleoside Transporter 1 of the malarial parasite Plasmodium falciparum (PfENT1). PfENT1 inhibitors might serve as novel antimalarial drugs since PfENT1-mediated purine import is essential for parasite proliferation. To identify PfENT1 inhibitors, we screened 64 560 compounds and identified 171 by their ability to rescue the growth of PfENT1-expressing fui1Δ yeast in the presence of a cytotoxic PfENT1 substrate, 5-fluorouridine (5-FUrd). In secondary assays, nine of the highest activity compounds inhibited PfENT1-dependent growth of a purine auxotrophic yeast strain with adenosine as the sole purine source (IC50 0.2-2 µM). These nine compounds completely blocked [(3)H]adenosine uptake into PfENT1-expressing yeast and erythrocyte-free trophozoite-stage parasites (IC50 5-50 nM), and inhibited chloroquine-sensitive and -resistant parasite proliferation (IC50 5-50 µM). Wild-type (WT) parasite IC50 values were up to 4-fold lower compared to PfENT1-knockout (pfent1Δ) parasites. pfent1Δ parasite killing showed a delayed-death phenotype not observed with WT. We infer that, in parasites, the compounds inhibit both PfENT1 and a secondary target with similar efficacy. The secondary target identity is unknown, but its existence may reduce the likelihood of parasites developing resistance to PfENT1 inhibitors. Our data support the hypothesis that blocking purine transport through PfENT1 may be a novel and compelling approach for antimalarial drug development.
[Mh] Termos MeSH primário: Antimaláricos/farmacologia
Ensaios de Triagem em Larga Escala
Proteínas de Transporte de Nucleobases, Nucleosídeos, Nucleotídeos e Ácidos Nucleicos/antagonistas & inibidores
Plasmodium falciparum/efeitos dos fármacos
Proteínas de Protozoários/antagonistas & inibidores
Bibliotecas de Moléculas Pequenas/farmacologia
Trofozoítos/efeitos dos fármacos
[Mh] Termos MeSH secundário: Adenosina/metabolismo
Antimaláricos/química
Cultura Axênica
Transporte Biológico/efeitos dos fármacos
Deleção de Genes
Expressão Gênica
Teste de Complementação Genética
Proteínas de Transporte de Nucleobases, Nucleosídeos, Nucleotídeos e Ácidos Nucleicos/genética
Proteínas de Transporte de Nucleobases, Nucleosídeos, Nucleotídeos e Ácidos Nucleicos/metabolismo
Proteínas de Transporte de Nucleosídeos/genética
Proteínas de Transporte de Nucleosídeos/metabolismo
Plasmodium falciparum/crescimento & desenvolvimento
Plasmodium falciparum/metabolismo
Proteínas de Protozoários/genética
Proteínas de Protozoários/metabolismo
Saccharomyces cerevisiae/efeitos dos fármacos
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Bibliotecas de Moléculas Pequenas/química
Relação Estrutura-Atividade
Trofozoítos/crescimento & desenvolvimento
Trofozoítos/metabolismo
Uridina/análogos & derivados
Uridina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antimalarials); 0 (ENT1 protein, Plasmodium falciparum); 0 (FUI1 protein, S cerevisiae); 0 (Nucleobase, Nucleoside, Nucleotide, and Nucleic Acid Transport Proteins); 0 (Nucleoside Transport Proteins); 0 (Protozoan Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (Small Molecule Libraries); 4K0M952561 (5-fluorouridine); K72T3FS567 (Adenosine); WHI7HQ7H85 (Uridine)
[Em] Mês de entrada:1512
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150121
[St] Status:MEDLINE
[do] DOI:10.1021/cb500981y


  3 / 18 MEDLINE  
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[PMID]:25424653
[Au] Autor:Frame IJ; Deniskin R; Arora A; Akabas MH
[Ad] Endereço:Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York.
[Ti] Título:Purine import into malaria parasites as a target for antimalarial drug development.
[So] Source:Ann N Y Acad Sci;1342:19-28, 2015 Apr.
[Is] ISSN:1749-6632
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Infection with Plasmodium species parasites causes malaria. Plasmodium parasites are purine auxotrophs. In all life cycle stages, they require purines for RNA and DNA synthesis and other cellular metabolic processes. Purines are imported from the host erythrocyte by equilibrative nucleoside transporters (ENTs). They are processed via purine salvage pathway enzymes to form the required purine nucleotides. The Plasmodium falciparum genome encodes four putative ENTs (PfENT1-4). Genetic, biochemical, and physiologic evidence suggest that PfENT1 is the primary purine transporter supplying the purine salvage pathway. Protein mass spectrometry shows that PfENT1 is expressed in all parasite stages. PfENT1 knockout parasites are not viable in culture at purine concentrations found in human blood (<10 µM). Thus, PfENT1 is a potential target for novel antimalarial drugs, but no PfENT1 inhibitors have been identified to test the hypothesis. Identifying inhibitors of PfENT1 is an essential step to validate PfENT1 as a potential antimalarial drug target.
[Mh] Termos MeSH primário: Antimaláricos/metabolismo
Sistemas de Liberação de Medicamentos/tendências
Descoberta de Drogas/tendências
Proteínas de Transporte de Nucleobases, Nucleosídeos, Nucleotídeos e Ácidos Nucleicos/metabolismo
Plasmodium falciparum/metabolismo
Proteínas de Protozoários/metabolismo
Purinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Antimaláricos/administração & dosagem
Seres Humanos
Malária/tratamento farmacológico
Malária/metabolismo
Proteínas de Transporte de Nucleobases, Nucleosídeos, Nucleotídeos e Ácidos Nucleicos/antagonistas & inibidores
Parasitos/efeitos dos fármacos
Parasitos/metabolismo
Plasmodium falciparum/efeitos dos fármacos
Proteínas de Protozoários/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Antimalarials); 0 (ENT1 protein, Plasmodium falciparum); 0 (Nucleobase, Nucleoside, Nucleotide, and Nucleic Acid Transport Proteins); 0 (Protozoan Proteins); 0 (Purines); W60KTZ3IZY (purine)
[Em] Mês de entrada:1506
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141127
[St] Status:MEDLINE
[do] DOI:10.1111/nyas.12568


  4 / 18 MEDLINE  
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[PMID]:24878340
[Au] Autor:O'Shea VL; Berger JM
[Ad] Endereço:Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, 725 N. Wolfe St., Baltimore, MD 21205, USA.
[Ti] Título:Loading strategies of ring-shaped nucleic acid translocases and helicases.
[So] Source:Curr Opin Struct Biol;25:16-24, 2014 Apr.
[Is] ISSN:1879-033X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ring-shaped nucleic acid translocases and helicases catalyze the directed and processive movement of nucleic acid strands to support essential transactions such as replication, transcription, and chromosome partitioning. Assembled typically as hexamers, ring helicase/translocase systems use coordinated cycles of nucleoside triphosphate (NTP) hydrolysis to translocate extended DNA or RNA substrates through a central pore. Ring formation presents a topological challenge to the engagement of substrate oligonucleotides, and is frequently overcome by distinct loading strategies for shepherding specific motors onto their respective substrates. Recent structural studies that capture different loading intermediates have begun to reveal how different helicase/translocase rings either assemble around substrates or crack open to allow DNA or RNA strand entry, and how dedicated chaperones facilitate these events in some instances. Both prevailing mechanistic models and remaining knowledge gaps are discussed.
[Mh] Termos MeSH primário: DNA Helicases/química
DNA Helicases/metabolismo
Proteínas de Transporte de Nucleobases, Nucleosídeos, Nucleotídeos e Ácidos Nucleicos/química
Proteínas de Transporte de Nucleobases, Nucleosídeos, Nucleotídeos e Ácidos Nucleicos/metabolismo
[Mh] Termos MeSH secundário: Chaperonas Moleculares/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; REVIEW
[Nm] Nome de substância:
0 (Molecular Chaperones); 0 (Nucleobase, Nucleoside, Nucleotide, and Nucleic Acid Transport Proteins); EC 3.6.4.- (DNA Helicases)
[Em] Mês de entrada:1501
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140601
[St] Status:MEDLINE


  5 / 18 MEDLINE  
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[PMID]:24052309
[Au] Autor:Pedersen ME; Snieckute G; Kagias K; Nehammer C; Multhaupt HA; Couchman JR; Pocock R
[Ad] Endereço:Biotech Research and Innovation Centre, University of Copenhagen, Ole Maaløes Vej 5, Copenhagen, Denmark.
[Ti] Título:An epidermal microRNA regulates neuronal migration through control of the cellular glycosylation state.
[So] Source:Science;341(6152):1404-8, 2013 Sep 20.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:An appropriate balance in glycosylation of proteoglycans is crucial for their ability to regulate animal development. Here, we report that the Caenorhabditis elegans microRNA mir-79, an ortholog of mammalian miR-9, controls sugar-chain homeostasis by targeting two proteins in the proteoglycan biosynthetic pathway: a chondroitin synthase (SQV-5; squashed vulva-5) and a uridine 5'-diphosphate-sugar transporter (SQV-7). Loss of mir-79 causes neurodevelopmental defects through SQV-5 and SQV-7 dysregulation in the epidermis. This results in a partial shutdown of heparan sulfate biosynthesis that impinges on a LON-2/glypican pathway and disrupts neuronal migration. Our results identify a regulatory axis controlled by a conserved microRNA that maintains proteoglycan homeostasis in cells.
[Mh] Termos MeSH primário: Caenorhabditis elegans/fisiologia
Movimento Celular
Epiderme/metabolismo
Proteoglicanas de Heparan Sulfato/biossíntese
MicroRNAs/fisiologia
Neurônios/fisiologia
[Mh] Termos MeSH secundário: Animais
Caenorhabditis elegans/metabolismo
Proteínas de Caenorhabditis elegans/biossíntese
Proteínas de Caenorhabditis elegans/genética
Proteínas de Caenorhabditis elegans/metabolismo
Glicosilação
Glicosiltransferases/metabolismo
Glipicanas/biossíntese
Glipicanas/genética
Proteoglicanas de Heparan Sulfato/genética
MicroRNAs/genética
Proteínas de Transporte de Monossacarídeos/metabolismo
Proteínas de Transporte de Nucleobases, Nucleosídeos, Nucleotídeos e Ácidos Nucleicos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Glypicans); 0 (Heparan Sulfate Proteoglycans); 0 (LON-2 protein, C elegans); 0 (MIRN79 microRNA, C elegans); 0 (MicroRNAs); 0 (Monosaccharide Transport Proteins); 0 (Nucleobase, Nucleoside, Nucleotide, and Nucleic Acid Transport Proteins); 0 (sqv-7 protein, C elegans); EC 2.4.- (Glycosyltransferases); EC 2.4.- (sqv-5 protein, C elegans)
[Em] Mês de entrada:1310
[Cu] Atualização por classe:130920
[Lr] Data última revisão:
130920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130921
[St] Status:MEDLINE
[do] DOI:10.1126/science.1242528


  6 / 18 MEDLINE  
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[PMID]:23712905
[Au] Autor:Salzer R; Herzberg M; Nies DH; Biukovic G; Grüber G; Müller V; Averhoff B
[Ad] Endereço:Molecular Microbiology and Bioenergetics, Institute of Molecular Biosciences, Goethe University Frankfurt, Max-von-Laue-Str. 9, 60438 Frankfurt am Main, Germany.
[Ti] Título:The DNA uptake ATPase PilF of Thermus thermophilus: a reexamination of the zinc content.
[So] Source:Extremophiles;17(4):697-8, 2013 Jul.
[Is] ISSN:1433-4909
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The DNA-translocator ATPase PilF of Thermus thermophilus HB27 is a hexamer built by six identical subunits. Despite the presence of a conserved zinc-binding site in every subunit, only one zinc atom per hexamer was found. Re-examination of the zinc content of PilF purified from cells grown in complex media with different lots of yeast extract revealed six zinc atoms per hexamer. These data demonstrate that the low zinc content reported before was most likely a result of zinc depletion of the yeast extract used.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Proteínas de Transporte de Nucleobases, Nucleosídeos, Nucleotídeos e Ácidos Nucleicos/química
Thermus thermophilus/enzimologia
Zinco/análise
[Mh] Termos MeSH secundário: Proteínas de Bactérias/metabolismo
Sítios de Ligação
DNA/metabolismo
Proteínas de Transporte de Nucleobases, Nucleosídeos, Nucleotídeos e Ácidos Nucleicos/metabolismo
Subunidades Proteicas/química
Subunidades Proteicas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Nucleobase, Nucleoside, Nucleotide, and Nucleic Acid Transport Proteins); 0 (Protein Subunits); 9007-49-2 (DNA); J41CSQ7QDS (Zinc)
[Em] Mês de entrada:1401
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM; S
[Da] Data de entrada para processamento:130529
[St] Status:MEDLINE
[do] DOI:10.1007/s00792-013-0544-6


  7 / 18 MEDLINE  
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[PMID]:23333341
[Au] Autor:Chang Y; Gu W; Zhang F; McLandsborough L
[Ad] Endereço:Department of Food Science, University of Massachusetts, Amherst, MA 01003, USA.
[Ti] Título:Disruption of lmo1386, a putative DNA translocase gene, affects biofilm formation of Listeria monocytogenes on abiotic surfaces.
[So] Source:Int J Food Microbiol;161(3):158-63, 2013 Feb 15.
[Is] ISSN:1879-3460
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The distribution and survival of Listeria monocytogenes (L. monocytogenes) in food processing environment is linked to its ability to form biofilms, however the genetic mechanisms remain unclear. In our previous study, a Himar1 mariner-based transposon mutagenesis was performed and 42 mutants were confirmed to have reduced biofilm formation. Among the 42 biofilm deficient mutants, two isolates (s25-10C and s55-1D) harbored single insertion in lmo1386, a gene encoding a putative DNA translocase. The lmo1386 mutants had impaired biofilm formation in both static and flow conditions. The mutant strain s55-1D was complemented by cloning the entire lmo1386 gene into pPL2-gtcAP, a derivative of the integration vector pPL2 with the L. monocytogenes gtcA promoter. The genetically complemented mutant restored its biofilm phenotype, demonstrating the role of lmo1386 in the biofilm formation of L. monocytogenes. The lmo1386 mutant had reduced initial adhesion ability, which could at least partially contribute to the impaired biofilm phenotype. Additionally, the lmo1386 mutant formed elongated cell chains when grown in a nutrient TSBYE media, while no obvious cell morphology changes were observed when grown in the minimal MWB media. Overall, our findings suggest that the disruption of lmo1386, a putative DNA translocase gene affects the biofilm formation of L. monocytogenes on abiotic surfaces, which may further advance the understanding of the complicated process of biofilm formation.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Biofilmes/crescimento & desenvolvimento
Listeria monocytogenes/genética
Proteínas de Transporte de Nucleobases, Nucleosídeos, Nucleotídeos e Ácidos Nucleicos/genética
[Mh] Termos MeSH secundário: Aderência Bacteriana
Proteínas de Bactérias/metabolismo
Clonagem Molecular
DNA Bacteriano/genética
Listeria monocytogenes/crescimento & desenvolvimento
Mutagênese Insercional
Proteínas de Transporte de Nucleobases, Nucleosídeos, Nucleotídeos e Ácidos Nucleicos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (DNA, Bacterial); 0 (Nucleobase, Nucleoside, Nucleotide, and Nucleic Acid Transport Proteins)
[Em] Mês de entrada:1307
[Cu] Atualização por classe:130204
[Lr] Data última revisão:
130204
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130122
[St] Status:MEDLINE


  8 / 18 MEDLINE  
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[PMID]:22857534
[Au] Autor:Choi JS; Berdis AJ
[Ad] Endereço:Department of Pharmacology, Case Western Reserve University, 10900 Euclid Avenue, Cleveland, OH 44106, USA.
[Ti] Título:Nucleoside transporters: biological insights and therapeutic applications.
[So] Source:Future Med Chem;4(11):1461-78, 2012 Jul.
[Is] ISSN:1756-8927
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Nucleoside transporters play important physiological roles by regulating intra- and extra-cellular concentrations of purine and pyrimidine (deoxy)nucleosides. This review describes the biological function and activity of the two major families of membrane nucleoside transporters that exist in mammalian cells. These include equilibrative nucleoside transporters that transport nucleosides in a gradient-dependent fashion and concentrative nucleoside transporters that import nucleosides against a gradient by coupling movement with sodium transport. Particular emphasis is placed on describing the roles of nucleoside transport in normal physiological processes, including inflammation, cardiovascular function and nutrient transport across the blood-brain barrier. In addition, the role of nucleoside transport in pathological conditions such as cardiovascular disease and cancer are discussed. The potential therapeutic applications of manipulating nucleoside transport activities are discussed, focusing on nucleoside analogs as anti-neoplastic agents. Finally, we discuss future directions for the development of novel chemical entities to measure nucleoside transport activity at the cellular and organismal level.
[Mh] Termos MeSH primário: Proteínas de Transporte de Nucleobases, Nucleosídeos, Nucleotídeos e Ácidos Nucleicos/metabolismo
Nucleosídeos/química
[Mh] Termos MeSH secundário: Antineoplásicos/química
Antineoplásicos/farmacologia
Antineoplásicos/uso terapêutico
Barreira Hematoencefálica/efeitos dos fármacos
Doenças Cardiovasculares/tratamento farmacológico
Seres Humanos
Neoplasias/tratamento farmacológico
Proteínas de Transporte de Nucleobases, Nucleosídeos, Nucleotídeos e Ácidos Nucleicos/antagonistas & inibidores
Nucleosídeos/farmacologia
Nucleosídeos/uso terapêutico
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.; REVIEW
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Nucleobase, Nucleoside, Nucleotide, and Nucleic Acid Transport Proteins); 0 (Nucleosides)
[Em] Mês de entrada:1212
[Cu] Atualização por classe:120803
[Lr] Data última revisão:
120803
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120804
[St] Status:MEDLINE
[do] DOI:10.4155/fmc.12.79


  9 / 18 MEDLINE  
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[PMID]:21596779
[Au] Autor:Sieber F; Placido A; El Farouk-Ameqrane S; Duchêne AM; Maréchal-Drouard L
[Ad] Endereço:Institut de Biologie Moléculaire des Plantes, UPR 2357-CNRS, Université de Strasbourg, 12 rue du Général Zimmer, F-67084 Strasbourg Cedex, France.
[Ti] Título:A protein shuttle system to target RNA into mitochondria.
[So] Source:Nucleic Acids Res;39(14):e96, 2011 Aug.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mitochondria play a key role in essential cellular functions. A deeper understanding of mitochondrial molecular processes is hampered by the difficulty of incorporating foreign nucleic acids into organelles. Mitochondria of most eukaryotic species import cytosolic tRNAs. Based on this natural process, we describe here a powerful shuttle system to internalize several types of RNAs into isolated mitochondria. We demonstrate that this tool is useful to investigate tRNA processing or mRNA editing in plant mitochondria. Furthermore, we show that the same strategy can be used to address both tRNA and mRNA to isolated mammalian mitochondria. We anticipate our novel approach to be the starting point for various studies on mitochondrial processes. Finally, our study provides new insights into the mechanism of RNA import into mitochondria.
[Mh] Termos MeSH primário: Mitocôndrias/metabolismo
Proteínas de Transporte de Nucleobases, Nucleosídeos, Nucleotídeos e Ácidos Nucleicos/metabolismo
Transporte de RNA
[Mh] Termos MeSH secundário: Sequência de Bases
Larix/genética
ATPases Mitocondriais Próton-Translocadoras/metabolismo
Dados de Sequência Molecular
Edição de RNA
Precursores de RNA/química
Precursores de RNA/metabolismo
Processamento Pós-Transcricional do RNA
RNA Mensageiro/metabolismo
RNA de Transferência/metabolismo
RNA de Transferência de Histidina/química
RNA de Transferência de Histidina/metabolismo
Solanum tuberosum/metabolismo
Tetra-Hidrofolato Desidrogenase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Nucleobase, Nucleoside, Nucleotide, and Nucleic Acid Transport Proteins); 0 (RNA Precursors); 0 (RNA, Messenger); 0 (RNA, Transfer, His); 9014-25-9 (RNA, Transfer); EC 1.5.1.3 (Tetrahydrofolate Dehydrogenase); EC 3.6.3.- (Mitochondrial Proton-Translocating ATPases)
[Em] Mês de entrada:1110
[Cu] Atualização por classe:150204
[Lr] Data última revisão:
150204
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110521
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkr380


  10 / 18 MEDLINE  
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[PMID]:19818813
[Au] Autor:Riegelhaupt PM; Cassera MB; Fröhlich RF; Hazleton KZ; Hefter JJ; Schramm VL; Akabas MH
[Ad] Endereço:Department of Physiology and Biophysics, Albert Einstein College of Medicine of Yeshiva University, Bronx, NY 10461, USA.
[Ti] Título:Transport of purines and purine salvage pathway inhibitors by the Plasmodium falciparum equilibrative nucleoside transporter PfENT1.
[So] Source:Mol Biochem Parasitol;169(1):40-9, 2010 Jan.
[Is] ISSN:1872-9428
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Plasmodium falciparum is a purine auxotroph. The transport of purine nucleosides and nucleobases from the host erythrocyte to the parasite cytoplasm is essential to support parasite growth. P. falciparum equilibrative nucleoside transporter 1 (PfENT1) is a major route for purine transport across the parasite plasma membrane. Malarial parasites are sensitive to inhibitors of purine salvage pathway enzymes. The immucillin class of purine nucleoside phosphorylase inhibitors and the adenosine analog, tubercidin, block growth of P. falciparum under in vitro culture conditions. We sought to determine whether these inhibitors utilize PfENT1 to gain access to the parasite cytosol. There is considerable controversy in the literature regarding the K(m) and/or K(i) for purine transport by PfENT1 in the Xenopus oocyte expression system. We show that oocytes metabolize adenosine but not hypoxanthine. For adenosine, metabolism is the rate limiting step in oocyte uptake assays, making hypoxanthine the preferred substrate for PfENT1 transport studies in oocytes. We demonstrate that the K(i) for PfENT1 transport of hypoxanthine and adenosine is in the 300-700microM range. Effects of substrate metabolism on uptake studies may explain conflicting results in the literature regarding the PfENT1 adenosine transport K(m). PfENT1 transports the tubercidin class of compounds. None of the immucillin compounds tested inhibited PfENT1 transport of [(3)H]hypoxanthine or [(3)H]adenosine. Although nucleobases are transported, modifications of the ribose ring in corresponding nucleoside analogs affect substrate recognition by PfENT1. These results provide new insights into PfENT1 and the mechanism by which purine salvage pathway inhibitors are transported into the parasite cytoplasm.
[Mh] Termos MeSH primário: Inibidores Enzimáticos/farmacologia
Redes e Vias Metabólicas/efeitos dos fármacos
Proteínas de Transporte de Nucleobases, Nucleosídeos, Nucleotídeos e Ácidos Nucleicos/antagonistas & inibidores
Proteínas de Transporte de Nucleobases, Nucleosídeos, Nucleotídeos e Ácidos Nucleicos/metabolismo
Plasmodium falciparum/metabolismo
Proteínas de Protozoários/antagonistas & inibidores
Proteínas de Protozoários/metabolismo
Purinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Transporte Biológico/efeitos dos fármacos
Cinética
Proteínas de Transporte de Nucleobases, Nucleosídeos, Nucleotídeos e Ácidos Nucleicos/química
Proteínas de Transporte de Nucleobases, Nucleosídeos, Nucleotídeos e Ácidos Nucleicos/genética
Oócitos/química
Oócitos/efeitos dos fármacos
Oócitos/crescimento & desenvolvimento
Oócitos/metabolismo
Plasmodium falciparum/química
Plasmodium falciparum/efeitos dos fármacos
Plasmodium falciparum/genética
Plasmodium falciparum/crescimento & desenvolvimento
Proteínas de Protozoários/química
Proteínas de Protozoários/genética
Nucleosídeos de Purina/farmacologia
Purinas/química
Pirimidinonas/farmacologia
Tubercidina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ENT1 protein, Plasmodium falciparum); 0 (Enzyme Inhibitors); 0 (Nucleobase, Nucleoside, Nucleotide, and Nucleic Acid Transport Proteins); 0 (Protozoan Proteins); 0 (Purine Nucleosides); 0 (Purines); 0 (Pyrimidinones); 426X066ELK (forodesine); M351LCX45Y (Tubercidin)
[Em] Mês de entrada:1001
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:091013
[St] Status:MEDLINE
[do] DOI:10.1016/j.molbiopara.2009.10.001



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