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Pesquisa : D12.776.157.530.450.250.875 [Categoria DeCS]
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  1 / 1778 MEDLINE  
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[PMID]:29281635
[Au] Autor:Takahashi M; Takagi S
[Ad] Endereço:Division of Biological Science, Nagoya University Graduate School of Science Chikusa-ku, Nagoya, Japan.
[Ti] Título:Optical silencing of body wall muscles induces pumping inhibition in Caenorhabditis elegans.
[So] Source:PLoS Genet;13(12):e1007134, 2017 12.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Feeding, a vital behavior in animals, is modulated depending on internal and external factors. In the nematode Caenorhabditis elegans, the feeding organ called the pharynx ingests food by pumping driven by the pharyngeal muscles. Here we report that optical silencing of the body wall muscles, which drive the locomotory movement of worms, affects pumping. In worms expressing the Arch proton pump or the ACR2 anion channel in the body wall muscle cells, the pumping rate decreases after activation of Arch or ACR2 with light illumination, and recovers gradually after terminating illumination. Pumping was similarly inhibited by illumination in locomotion-defective mutants carrying Arch, suggesting that perturbation of locomotory movement is not critical for pumping inhibition. Analysis of mutants and cell ablation experiments showed that the signals mediating the pumping inhibition response triggered by activation of Arch with weak light are transferred mainly through two pathways: one involving gap junction-dependent mechanisms through pharyngeal I1 neurons, which mediate fast signals, and the other involving dense-core vesicle-dependent mechanisms, which mediate slow signals. Activation of Arch with strong light inhibited pumping strongly in a manner that does not rely on either gap junction-dependent or dense-core vesicle-dependent mechanisms. Our study revealed a new aspect of the neural and neuroendocrine controls of pumping initiated from the body wall muscles.
[Mh] Termos MeSH primário: Optogenética/métodos
Músculos Faríngeos/metabolismo
Bombas de Próton/metabolismo
[Mh] Termos MeSH secundário: Animais
Caenorhabditis elegans
Proteínas de Caenorhabditis elegans/metabolismo
Ingestão de Alimentos/fisiologia
Locomoção/fisiologia
Neurônios Motores/metabolismo
Músculo Esquelético/metabolismo
Faringe/metabolismo
Serotonina
Transdução de Sinais/fisiologia
Canais de Ânion Dependentes de Voltagem/genética
Canais de Ânion Dependentes de Voltagem/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Proton Pumps); 0 (Voltage-Dependent Anion Channels); 333DO1RDJY (Serotonin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171228
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007134


  2 / 1778 MEDLINE  
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[PMID]:28450383
[Au] Autor:Hong H; Shen R; Zhang F; Wen Z; Chang S; Lin W; Kranz SA; Luo YW; Kao SJ; Morel FMM; Shi D
[Ad] Endereço:State Key Laboratory of Marine Environmental Science, Xiamen University, Xiamen, Fujian, P.R. China.
[Ti] Título:The complex effects of ocean acidification on the prominent N -fixing cyanobacterium .
[So] Source:Science;356(6337):527-531, 2017 05 05.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acidification of seawater caused by anthropogenic carbon dioxide (CO ) is anticipated to influence the growth of dinitrogen (N )-fixing phytoplankton, which contribute a large fraction of primary production in the tropical and subtropical ocean. We found that growth and N -fixation of the ubiquitous cyanobacterium decreased under acidified conditions, notwithstanding a beneficial effect of high CO Acidification resulted in low cytosolic pH and reduced N -fixation rates despite elevated nitrogenase concentrations. Low cytosolic pH required increased proton pumping across the thylakoid membrane and elevated adenosine triphosphate production. These requirements were not satisfied under field or experimental iron-limiting conditions, which greatly amplified the negative effect of acidification.
[Mh] Termos MeSH primário: Fixação de Nitrogênio
Nitrogênio/metabolismo
Água do Mar/química
Água do Mar/microbiologia
Trichodesmium/crescimento & desenvolvimento
Trichodesmium/metabolismo
[Mh] Termos MeSH secundário: Dióxido de Carbono/metabolismo
Concentração de Íons de Hidrogênio
Ferro/deficiência
Nitrogenase/metabolismo
Oceanos e Mares
Bombas de Próton/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 (Proton Pumps); 142M471B3J (Carbon Dioxide); E1UOL152H7 (Iron); EC 1.18.6.1 (Nitrogenase); N762921K75 (Nitrogen)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180117
[Lr] Data última revisão:
180117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1126/science.aal2981


  3 / 1778 MEDLINE  
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[PMID]:28634030
[Au] Autor:Li M; Khan S; Rong H; Tuma R; Hatzakis NS; Jeuken LJC
[Ad] Endereço:School of Biomedical Sciences, University of Leeds, LS2 9JT Leeds, UK.
[Ti] Título:Effects of membrane curvature and pH on proton pumping activity of single cytochrome bo enzymes.
[So] Source:Biochim Biophys Acta;1858(9):763-770, 2017 09.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The molecular mechanism of proton pumping by heme-copper oxidases (HCO) has intrigued the scientific community since it was first proposed. We have recently reported a novel technology that enables the continuous characterisation of proton transport activity of a HCO and ubiquinol oxidase from Escherichia coli, cytochrome bo , for hundreds of seconds on the single enzyme level (Li et al. J Am Chem Soc 137 (2015) 16055-16063). Here, we have extended these studies by additional experiments and analyses of the proton transfer rate as a function of proteoliposome size and pH at the N- and P-side of single HCOs. Proton transport activity of cytochrome bo was found to decrease with increased curvature of the membrane. Furthermore, proton uptake at the N-side (proton entrance) was insensitive to pH between pH6.4-8.4, while proton release at the P-side had an optimum pH of ~7.4, suggesting that the pH optimum is related to proton release from the proton exit site. Our previous single-enzyme experiments identified rare, long-lived conformation states of cytochrome bo where protons leak back under turn-over conditions. Here, we analyzed and found that ~23% of cytochrome bo proteoliposomes show ΔpH half-lives below 50s after stopping turnover, while only ~5% of the proteoliposomes containing a non-pumping mutant, E286C cytochrome bo exhibit such fast decays. These single-enzyme results confirm our model in which HCO exhibit heterogeneous pumping rates and can adopt rare leak states in which protons are able to rapidly flow back.
[Mh] Termos MeSH primário: Citocromos/metabolismo
Proteínas de Escherichia coli/metabolismo
Concentração de Íons de Hidrogênio
Proteolipídeos/metabolismo
Bombas de Próton/metabolismo
[Mh] Termos MeSH secundário: Transporte Biológico
Citocromos/genética
Técnicas Eletroquímicas/instrumentação
Transporte de Elétrons
Escherichia coli/enzimologia
Escherichia coli/ultraestrutura
Proteínas de Escherichia coli/genética
Corantes Fluorescentes
Lipossomos/metabolismo
Microscopia de Fluorescência
Oxirredução
Proteolipídeos/ultraestrutura
Bombas de Próton/genética
Prótons
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cytochromes); 0 (Escherichia coli Proteins); 0 (Fluorescent Dyes); 0 (Liposomes); 0 (Proteolipids); 0 (Proton Pumps); 0 (Protons); 0 (cytochrome bo3, E coli); 0 (proteoliposomes)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171025
[Lr] Data última revisão:
171025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170622
[St] Status:MEDLINE


  4 / 1778 MEDLINE  
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[PMID]:28512024
[Au] Autor:Bi Y; Might M; Vankayalapati H; Kuberan B
[Ad] Endereço:Department of Medicinal Chemistry, University of Utah, Salt Lake City, Utah 84112, United States.
[Ti] Título:Repurposing of Proton Pump Inhibitors as first identified small molecule inhibitors of endo-ß-N-acetylglucosaminidase (ENGase) for the treatment of NGLY1 deficiency, a rare genetic disease.
[So] Source:Bioorg Med Chem Lett;27(13):2962-2966, 2017 07 01.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:N-Glycanase deficiency, or NGLY1 deficiency, is an extremely rare human genetic disease. N-Glycanase, encoded by the gene NGLY1, is an important enzyme involved in protein deglycosylation of misfolded proteins. Deglycosylation of misfolded proteins precedes the endoplasmic reticulum (ER)-associated degradation (ERAD) process. NGLY1 patients produce little or no N-glycanase (Ngly1), and the symptoms include global developmental delay, frequent seizures, complex hyperkinetic movement disorder, difficulty in swallowing/aspiration, liver dysfunction, and a lack of tears. Unfortunately, there has not been any therapeutic option available for this rare disease so far. Recently, a proposed molecular mechanism for NGLY1 deficiency suggested that endo-ß-N-acetylglucosaminidase (ENGase) inhibitors may be promising therapeutics for NGLY1 patients. Herein, we performed structure-based virtual screening utilizing FDA-approved drug database on this ENGase target to enable repurposing of existing drugs. Several Proton Pump Inhibitors (PPIs), a series of substituted 1H-benzo [d] imidazole, and 1H-imidazo [4,5-b] pyridines, among other scaffolds, have been identified as potent ENGase inhibitors. An electrophoretic mobility shift assay was employed to assess the inhibition of ENGase activity by these PPIs. Our efforts led to the discovery of Rabeprazole Sodium as the most promising hit with an IC of 4.47±0.44µM. This is the first report that describes the discovery of small molecule ENGase inhibitors, which can potentially be used for the treatment of human NGLY1 deficiency.
[Mh] Termos MeSH primário: Inibidores Enzimáticos/farmacologia
Doenças Genéticas Inatas/tratamento farmacológico
Inibidores da Bomba de Prótons/farmacologia
Bombas de Próton/metabolismo
Rabeprazol/farmacologia
Bibliotecas de Moléculas Pequenas/farmacologia
[Mh] Termos MeSH secundário: Relação Dose-Resposta a Droga
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
Doenças Genéticas Inatas/genética
Seres Humanos
Manosil-Glicoproteína Endo-beta-N-Acetilglucosaminidase/antagonistas & inibidores
Manosil-Glicoproteína Endo-beta-N-Acetilglucosaminidase/metabolismo
Estrutura Molecular
Peptídeo-N4-(N-acetil-beta-glucosaminil) Asparagina Amidase/deficiência
Peptídeo-N4-(N-acetil-beta-glucosaminil) Asparagina Amidase/metabolismo
Inibidores da Bomba de Prótons/síntese química
Inibidores da Bomba de Prótons/química
Rabeprazol/síntese química
Rabeprazol/química
Bibliotecas de Moléculas Pequenas/síntese química
Bibliotecas de Moléculas Pequenas/química
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Proton Pump Inhibitors); 0 (Proton Pumps); 0 (Small Molecule Libraries); 32828355LL (Rabeprazole); EC 3.2.1.96 (Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase); EC 3.5.1.52 (Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase)
[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:170518
[St] Status:MEDLINE


  5 / 1778 MEDLINE  
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[PMID]:28486745
[Au] Autor:Mahmoud S; Planes MD; Cabedo M; Trujillo C; Rienzo A; Caballero-Molada M; Sharma SC; Montesinos C; Mulet JM; Serrano R
[Ad] Endereço:Instituto de Biología Molecular y Celular de Plantas, Universidad Politécnica de Valencia-Consejo Superior de Investigaciones Científicas, Spain.
[Ti] Título:TOR complex 1 regulates the yeast plasma membrane proton pump and pH and potassium homeostasis.
[So] Source:FEBS Lett;591(13):1993-2002, 2017 Jul.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We have identified in yeast a connection between two master regulators of cell growth: a biochemical connection involving the TORC1 protein kinase (which activates protein synthesis, nutrient uptake, and anabolism) and a biophysical connection involving the plasma membrane proton-pumping H -ATPase Pma1 (which drives nutrient and K uptake and regulates pH homeostasis). Raising the temperature to nonpermissive values in a TOR thermosensitive mutant decreases Pma1 activity. Rapamycin, a TORC1 inhibitor, inhibits Pma1 dependent on its receptor Fpr1 and on the protein phosphatase Sit4, a TORC1 effector. Mutation of either Sit4 or Tco89, a nonessential subunit of TORC1, decreases proton efflux, K uptake, intracellular pH, cell growth, and tolerance to weak organic acids. Tco89 does not affect Pma1 activity but activates K transport.
[Mh] Termos MeSH primário: Membrana Celular/metabolismo
Homeostase
Complexos Multiproteicos/metabolismo
Potássio/metabolismo
Bombas de Próton/metabolismo
Saccharomyces cerevisiae/citologia
Saccharomyces cerevisiae/metabolismo
Serina-Treonina Quinases TOR/metabolismo
[Mh] Termos MeSH secundário: Transporte Biológico
Concentração de Íons de Hidrogênio
Espaço Intracelular/química
Alvo Mecanístico do Complexo 1 de Rapamicina
Mutação
Proteína Fosfatase 2/genética
Proteína Fosfatase 2/metabolismo
ATPases Translocadoras de Prótons/metabolismo
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (Multiprotein Complexes); 0 (Proton Pumps); 0 (Saccharomyces cerevisiae Proteins); 0 (Tco89 protein, S cerevisiae); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.11.1 (Mechanistic Target of Rapamycin Complex 1); EC 3.1.3.16 (Protein Phosphatase 2); EC 3.1.3.16 (SIT4 protein, S cerevisiae); EC 3.6.1.- (PMA1 protein, S cerevisiae); EC 3.6.3.14 (Proton-Translocating ATPases); RWP5GA015D (Potassium)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170510
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12673


  6 / 1778 MEDLINE  
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[PMID]:28371597
[Au] Autor:Kobliakov VA
[Ad] Endereço:Blokhin Russian Cancer Research Center, Russian Ministry of Health, Moscow, 115478, Russia. kobliakov@rambler.ru.
[Ti] Título:Role of Proton Pumps in Tumorigenesis.
[So] Source:Biochemistry (Mosc);82(4):401-412, 2017 Apr.
[Is] ISSN:1608-3040
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:One of the differences between normal and cancer cells is lower pH of the extracellular space in tumors. Low pH in the extracellular space activates proteases and stimulates tumor invasion and metastasis. Tumor cells display higher level of the HIF1α transcription factor that promotes cell switch from mitochondrial respiration to glycolysis. The terminal product of glycolysis is lactate. Lactate formation from pyruvate is catalyzed by the specific HIF1α-dependent isoform of lactate dehydrogenase A. Because lactate accumulation is deleterious for the cell, it is actively exported by monocarboxylate transporters. Lactate is cotransported with proton, which acidifies the extracellular space. Another protein that contributes to proton concentration increase in the extracellular space is tumor-specific HIF1α-dependent carbonic anhydrase IX, which generates a proton in the reaction between carbon dioxide and water. The activity of Na+/H+ exchanger (another protein pump) is stimulated by stress factors (e.g. osmotic shock) and proliferation stimuli. This review describes the mechanisms of proton pump activation and reviews results of studies on effects of various proton pump inhibitors on tumor functioning and growth in cell culture and in vivo. The prospects of combined application of proton pump inhibitors and cytostatics in cancer therapy are discussed.
[Mh] Termos MeSH primário: Carcinogênese
Bombas de Próton/fisiologia
[Mh] Termos MeSH secundário: Ácidos/metabolismo
Catálise
Proteínas de Transporte de Cátions/metabolismo
Seres Humanos
Concentração de Íons de Hidrogênio
Subunidade alfa do Fator 1 Induzível por Hipóxia/metabolismo
L-Lactato Desidrogenase/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
Trocador 1 de Sódio-Hidrogênio
Trocadores de Sódio-Hidrogênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Acids); 0 (Cation Transport Proteins); 0 (HIF1A protein, human); 0 (Hypoxia-Inducible Factor 1, alpha Subunit); 0 (Proton Pumps); 0 (SLC9A1 protein, human); 0 (Sodium-Hydrogen Exchanger 1); 0 (Sodium-Hydrogen Exchangers); EC 1.1.1.27 (L-Lactate Dehydrogenase); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.2 (pyruvate dehydrogenase (acetyl-transferring) kinase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170404
[St] Status:MEDLINE
[do] DOI:10.1134/S0006297917040010


  7 / 1778 MEDLINE  
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[PMID]:28319196
[Au] Autor:Wright BJ; Bickham-Wright U; Yoshino TP; Jackson MB
[Ad] Endereço:Department of Neuroscience, School of Medicine and Public Health, University of Wisconsin-Madison, Madison, Wisconsin, United States of America.
[Ti] Título:H+ channels in embryonic Biomphalaria glabrata cell membranes: Putative roles in snail host-schistosome interactions.
[So] Source:PLoS Negl Trop Dis;11(3):e0005467, 2017 Mar.
[Is] ISSN:1935-2735
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The human blood fluke Schistosoma mansoni causes intestinal schistosomiasis, a widespread neglected tropical disease. Infection of freshwater snails Biomphalaria spp. is an essential step in the transmission of S. mansoni to humans, although the physiological interactions between the parasite and its obligate snail host that determine success or failure are still poorly understood. In the present study, the B. glabrata embryonic (Bge) cell line, a widely used in vitro model for hemocyte-like activity, was used to investigate membrane properties, and assess the impact of larval transformation proteins (LTP) on identified ion channels. Whole-cell patch clamp recordings from Bge cells demonstrated that a Zn2+-sensitive H+ channel serves as the dominant plasma membrane conductance. Moreover, treatment of Bge cells with Zn2+ significantly inhibited an otherwise robust production of reactive oxygen species (ROS), thus implicating H+ channels in the regulation of this immune function. A heat-sensitive component of LTP appears to target H+ channels, enhancing Bge cell H+ current over 2-fold. Both Bge cells and B. glabrata hemocytes express mRNA encoding a hydrogen voltage-gated channel 1 (HVCN1)-like protein, although its function in hemocytes remains to be determined. This study is the first to identify and characterize an H+ channel in non-neuronal cells of freshwater molluscs. Importantly, the involvement of these channels in ROS production and their modulation by LTP suggest that these channels may function in immune defense responses against larval S. mansoni.
[Mh] Termos MeSH primário: Biomphalaria/embriologia
Biomphalaria/enzimologia
Membrana Celular/enzimologia
Bombas de Próton/metabolismo
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Técnicas de Patch-Clamp
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Proton Pumps); 0 (Reactive Oxygen Species)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170930
[Lr] Data última revisão:
170930
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170321
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pntd.0005467


  8 / 1778 MEDLINE  
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[PMID]:28259641
[Au] Autor:Carvalheda CA; Pisliakov AV
[Ad] Endereço:Computational Biology, School of Life Sciences, University of Dundee, Dow Street, Dundee, DD1 5EH, United Kingdom; Physics, School of Sciences and Engineering, University of Dundee, Nethergate, Dundee, DD1 4HN, United Kingdom. Electronic address: c.a.c.dossantos@dundee.ac.uk.
[Ti] Título:Insights into proton translocation in cbb oxidase from MD simulations.
[So] Source:Biochim Biophys Acta;1858(5):396-406, 2017 05.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Heme-copper oxidases are membrane protein complexes that catalyse the final step of the aerobic respiration, namely the reduction of oxygen to water. The energy released during catalysis is coupled to the active translocation of protons across the membrane, which contributes to the establishment of an electrochemical gradient that is used for ATP synthesis. The distinctive C-type (or cbb ) cytochrome c oxidases, which are mostly present in proteobacteria, exhibit a number of unique structural and functional features, including high catalytic activity at low oxygen concentrations. At the moment, the functioning mechanism of C-type oxidases, in particular the proton transfer/pumping mechanism presumably via a single proton channel, is still poorly understood. In this work we used all-atom molecular dynamics simulations and continuum electrostatics calculations to obtain atomic-level insights into the hydration and dynamics of a cbb oxidase. We provide the details of the water dynamics and proton transfer pathways for both the "chemical" and "pumped" protons, and show that formation of protonic connections is strongly affected by the protonation state of key residues, namely H243, E323 and H337.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Complexo IV da Cadeia de Transporte de Elétrons/metabolismo
Metabolismo Energético
Simulação de Dinâmica Molecular
Bombas de Próton/metabolismo
Pseudomonas stutzeri/enzimologia
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Transporte Biológico
Complexo IV da Cadeia de Transporte de Elétrons/química
Complexo IV da Cadeia de Transporte de Elétrons/genética
Bicamadas Lipídicas
Mutação
Oxigênio/metabolismo
Conformação Proteica
Prótons
Pseudomonas stutzeri/genética
Solventes/química
Relação Estrutura-Atividade
Água/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Lipid Bilayers); 0 (Proton Pumps); 0 (Protons); 0 (Solvents); 059QF0KO0R (Water); 8L70Q75FXE (Adenosine Triphosphate); EC 1.9.3.- (cbb3 oxidase); EC 1.9.3.1 (Electron Transport Complex IV); S88TT14065 (Oxygen)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170824
[Lr] Data última revisão:
170824
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170306
[St] Status:MEDLINE


  9 / 1778 MEDLINE  
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[PMID]:28252411
[Au] Autor:Gawthrop PJ
[Ti] Título:Bond Graph Modeling of Chemiosmotic Biomolecular Energy Transduction.
[So] Source:IEEE Trans Nanobioscience;16(3):177-188, 2017 Apr.
[Is] ISSN:1558-2639
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Engineering systems modeling and analysis based on the bond graph approach has been applied to biomolecular systems. In this context, the notion of a Faraday-equivalent chemical potential is introduced which allows chemical potential to be expressed in an analogous manner to electrical volts thus allowing engineering intuition to be applied to biomolecular systems. Redox reactions, and their representation by half-reactions, are key components of biological systems which involve both electrical and chemical domains. A bond graph interpretation of redox reactions is given which combines bond graphs with the Faraday-equivalent chemical potential. This approach is particularly relevant when the biomolecular system implements chemoelectrical transduction - for example chemiosmosis within the key metabolic pathway of mitochondria: oxidative phosphorylation. An alternative way of implementing computational modularity using bond graphs is introduced and used to give a physically based model of the mitochondrial electron transport chain To illustrate the overall approach, this model is analyzed using the Faraday-equivalent chemical potential approach and engineering intuition is used to guide affinity equalisation: a energy based analysis of the mitochondrial electron transport chain.
[Mh] Termos MeSH primário: Metabolismo Energético/fisiologia
Modelos Biológicos
Biologia de Sistemas/métodos
[Mh] Termos MeSH secundário: Trifosfato de Adenosina
Hidrólise
Oxirredução
Fosforilação Oxidativa
Bombas de Próton
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Proton Pumps); 8L70Q75FXE (Adenosine Triphosphate)
[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:170303
[St] Status:MEDLINE
[do] DOI:10.1109/TNB.2017.2674683


  10 / 1778 MEDLINE  
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Fotocópia
[PMID]:28189129
[Au] Autor:Fraser-Kirk K
[Ti] Título:Laryngopharyngeal reflux: A confounding cause of aerodigestive dysfunction.
[So] Source:Aust Fam Physician;46(1):34-39, 2017 Jan/Feb.
[Is] ISSN:0300-8495
[Cp] País de publicação:Australia
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Laryngopharyngeal reflux (LPR) is one of the most common and important disorders of upper airway inflammation. It causes significant impairment to quality of life, and can predict serious laryngeal and oesophageal pathology, yet it remains under-diagnosed and under-treated. OBJECTIVE: This paper attempts to unravel the diagnostic dilemma of LPR and provide a practical, discriminating approach to managing this common condition. DISCUSSION: Historical red flags mandating early referral for specialist review are identified, and pathophysiology, symptomatology and common signs are reviewed. In addition, a comprehensive treatment plan consisting of lifestyle modifications, counselling aids and empirical medical therapy is proposed. A strategy for tracking clinical improvement using Belfasky's validated symptom index is included to aid counselling, compliance and follow-up.
[Mh] Termos MeSH primário: Antiácidos/uso terapêutico
Refluxo Laringofaríngeo
Bombas de Próton/uso terapêutico
[Mh] Termos MeSH secundário: Adenocarcinoma/etiologia
Antiácidos/administração & dosagem
Tosse/etiologia
Transtornos de Deglutição/etiologia
Diagnóstico Diferencial
Neoplasias Esofágicas/etiologia
Azia/etiologia
Rouquidão/etiologia
Seres Humanos
Doenças da Laringe/etiologia
Refluxo Laringofaríngeo/complicações
Refluxo Laringofaríngeo/diagnóstico
Refluxo Laringofaríngeo/fisiopatologia
Refluxo Laringofaríngeo/terapia
Bombas de Próton/administração & dosagem
Perda de Peso
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antacids); 0 (Proton Pumps)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170809
[Lr] Data última revisão:
170809
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170213
[St] Status:MEDLINE



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