Database : MEDLINE
Search on : nadh and dehydrogenase [Words]
References found : 29148 [refine]
Displaying: 1 .. 10   in format [Detailed]

page 1 of 2915 go to page                         

  1 / 29148 MEDLINE  
              next record last record
select
to print
Photocopy
Full text

[PMID]: 29523334
[Au] Autor:Korkegian A; O'Malley T; Xia Y; Zhou Y; Carter DS; Sunde B; Flint L; Thompson D; Ioerger TR; Sacchettini J; Alley MRK; Parish T
[Ad] Address:TB Discovery Research, Infectious Disease Research Institute, Seattle, WA, USA.
[Ti] Title:The 7-phenyl benzoxaborole series is active against Mycobacterium tuberculosis.
[So] Source:Tuberculosis (Edinb);108:96-98, 2018 Jan.
[Is] ISSN:1873-281X
[Cp] Country of publication:Scotland
[La] Language:eng
[Ab] Abstract:We identified a series of novel 7-phenyl benzoxaborole compounds with activity against Mycobacterium tuberculosis. Compounds had a range of activity with inhibitory concentrations (IC ) as low as 5.1 µM and no cytotoxicity against eukaryotic cells (IC > 50 µM). Compounds were active against intracellular mycobacteria cultured in THP-1 macrophages. We isolated and characterized resistant mutants with mutations in NADH dehydrogenase (Ndh) or the regulatory protein Mce3R. Mutations suggest that Ndh may be the target of this series.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:In-Data-Review

  2 / 29148 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 29523164
[Au] Autor:Wu Y; Li L; Zhu G; Li W; Zhang N; Li S; Yao G; Tian W; Fu B; Yin H; Zhu X; Yan H; Jia W
[Ad] Address:State Key Laboratory of Veterinary Etiological Biology/Key Laboratory of Veterinary Parasitology of Gansu Province/Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, 730046, Gansu Province, People's Republic of China.
[Ti] Title:Mitochondrial genome data confirm that yaks can serve as the intermediate host of Echinococcus canadensis (G10) on the Tibetan Plateau.
[So] Source:Parasit Vectors;11(1):166, 2018 Mar 09.
[Is] ISSN:1756-3305
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:BACKGROUND: Cervids used to be considered the only animal intermediate hosts of the G10 genotype of Echinococcus canadensis. Yaks are often herded in the Qinghai-Tibet Plateau, China, where echinococcosis remains prevalent. However, no E. canadensis G10 cases have been recorded in yaks until now. The aim of our study was to identify causative agents of echinococcosis in yaks in this region. METHODS: Total genomic DNA was extracted from the germinal layer of one hydatid using a Blood and Tissue Kit. Full-length mitochondrial (mt) cytochrome c oxidase subunit 1 (cox1) and NADH dehydrogenase subunit 1 (nad1) genes were amplified by PCR. All purified PCR products were directly sequenced in both directions. Then seven pairs of overlap primers were designed to amplify the entire mt genome sequence of a suspected E. canadensis G10 isolate. Phylogenetic analyses were performed based on concatenated nucleotides from the 12 protein-coding genes of mt genomes of Echinococcus species in a Bayesian framework using MrBayes v3.1 and implementing the GTR + I + G model. RESULTS: Hydatids were found in yaks (n = 129) when organs were inspected at the slaughterhouse in Maqu county, Gannan Tibetan Autonomous Prefecture, Gansu Province, China in October 2016. Of these, 33 (25.6%) harbored up to a dozen hydatid cysts. One cyst from each yak was characterized by sequencing its mitochondrial (mt) cox1 and nad1 genes. On the basis of these sequence data, 32 cysts were identified as Echinococcus granulosus (sensu stricto) (G1-G3) and the remaining one was identified as the G10 genotype of E. canadensis. Its mt genome was then fully sequenced and compared with that of the G10 genotype in GenBank (AB745463). Phylogenetic analysis using complete mt genomes confirmed the Chinese cyst as belonging to the G10 genotype. CONCLUSIONS: To our knowledge, this is the first report globally of E. canadensis (G10) from yaks in China, which suggests that the G10 genotype has a wider geographical distribution and broader host range than previously believed. This genotype has therefore potential risks to human health and animal husbandry.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:In-Data-Review
[do] DOI:10.1186/s13071-018-2684-0

  3 / 29148 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 29522317
[Au] Autor:Murugesan D; Ray PC; Bayliss T; Prosser GA; Harrison JR; Green K; Soares de Melo C; Feng TS; Street LJ; Chibale K; Warner DF; Mizrahi V; Epemolu O; Scullion P; Ellis L; Riley J; Shishikura Y; Ferguson L; Osuna-Cabello M; Read KD; Green SR; Lamprecht DA; Finin PM; Steyn AJC; Ioerger TR; Sacchettini J; Rhee KY; Arora K; Barry Iii CE; Wyatt PG; Boshoff HIM
[Ti] Title:2-Mercapto-quinazolinones as inhibitors of NDH-2 and Mycobacterium tuberculosis: Structure-activity relationships, mechanism of action and ADME characterization.
[So] Source:ACS Infect Dis;, 2018 Mar 09.
[Is] ISSN:2373-8227
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Mycobacterium tuberculosis (MTb) possesses two non-proton pumping type II NADH dehydrogenase (NDH-2) enzymes which are predicted to be jointly essential for respiratory metabolism.. Furthermore, the structure of a closely related bacterial NDH-2 has been reported recently, allowing for the structure-based design of small-molecule inhibitors. Herein, we disclose MTb whole-cell structure-activity relationships (SAR) for a series of 2-mercapto-quinazolinones which target the ndh encoded NDH-2 with nanomolar potencies. The compounds were inactivated by glutathione-dependent adduct formation as well as quinazolinone oxidation in microsomes. Pharmacokinetic studies demonstrated modest bioavailability and compound exposures. Resistance to the compounds in MTb was conferred by promoter mutations in the alternative non-essential NDH-2 encoded by ndhA in MTb. Bioenergetic analyses revealed a decrease in oxygen consumption rates in response to inhibitor in cells in which membrane potential was uncoupled from ATP production, while inverted membrane vesicles showed mercapto-quinazolinone-dependent inhibition of ATP production when NADH was the electron donor to the respiratory chain. Enzyme kinetic studies further demonstrated non-competitive inhibition, suggesting binding of this scaffold to an allosteric site. In summary, while the initial MTb SAR showed limited improvement in potency, these results, combined with structural information of the bacterial protein, will aid in the future discovery of new and improved NDH-2 inhibitors.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:Publisher
[do] DOI:10.1021/acsinfecdis.7b00275

  4 / 29148 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 29385648
[Au] Autor:Otani T; Kato Y; Shikanai T
[Ad] Address:Department of Botany, Graduate School of Science, Kyoto University, Kyoto, 606-8502, Japan.
[Ti] Title:Specific substitutions of light-harvesting complex I proteins associated with photosystem I are required for supercomplex formation with chloroplast NADH dehydrogenase-like complex.
[So] Source:Plant J;, 2018 Jan 31.
[Is] ISSN:1365-313X
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:In Arabidopsis, the chloroplast NADH-dehydrogenase-like (NDH) complex is sandwiched between two copies of photosystem I (PSI) supercomplex, consisting of a PSI core and four light-harvesting complex I (LHCI) proteins (PSI-LHCI) to form the NDH-PSI supercomplex. Two minor LHCI proteins, Lhca5 and Lhca6, contribute to the interaction of each PSI-LHCI copy with the NDH complex. Here, large-pore blue-native gel electrophoresis revealed that, in addition to this complex, there were at least two types of higher-order association of more LHCI copies with the NDH complex. In single-particle images, this higher-order association of PSI-LHCI preferentially occurs at the left side of the NDH complex when viewed from the stromal side, placing subcomplex A at the top (Yadav et al., Biochim. Biophys. Acta - Bioenerg., 1858, 2017, 12). The association was impaired in the lhca6 mutant but not in the lhca5 mutant, suggesting that the left copy of PSI-LHCI was linked to the NDH complex via Lhca6. From an analysis of subunit compositions of the NDH-PSI supercomplex in lhca5 and lhca6 mutants, we propose that Lhca6 substitutes for Lhca2 in the left copy of PSI-LHCI, whereas Lhca5 substitutes for Lhca4 in the right copy. In the lhca2 mutant, Lhca3 was specifically stabilized in the NDH-PSI supercomplex through heterodimer formation with Lhca6. In the left copy of PSI-LHCI, subcomplex B, Lhca6 and NdhD likely formed the core of the supercomplex interaction. In contrast, a larger protein complex, including at least subcomplexes B and L and NdhB, was needed to form the contact site with Lhca5 in the right copy of PSI-LHCI.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:Publisher
[do] DOI:10.1111/tpj.13846

  5 / 29148 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 29320825
[Au] Autor:Kim HJ; Yong TS; Shin MH; Lee KJ; Park GM; Suvonkulov U; Kovalenko D; Yu HS
[Ad] Address:Department of Parasitology and Tropical Medicine, School of Medicine, Pusan National University, Yangsan 50612, Korea.
[Ti] Title:Practical Algorisms for PCR-RFLP-Based Genotyping of Echinococcus granulosus Sensu Lato.
[So] Source:Korean J Parasitol;55(6):679-684, 2017 Dec.
[Is] ISSN:1738-0006
[Cp] Country of publication:Korea (South)
[La] Language:eng
[Ab] Abstract:Echinococcus granulosus sensu lato (s.l.) is a causative agent of cystic echinococcosis or cystic hydatid disease in humans and domestic and wild animals. The disease is a serious health problem in countries associated with poverty and poor hygiene practices, particularly in livestock raising. We introduced a practical algorism for genotyping the parasite, which may be useful to many developing countries. To evaluate the efficiency of the algorism, we genotyped 3 unknown strains isolated from human patients. We found that unknowns 1 and 3 were included in G1, G2, and G3 genotypes group and unknown 2 was included in G4 genotype (Echinococcus equinus) according to the algorisms. We confirmed these results by sequencing the 3 unknown isolates cox1 and nad1 PCR products. In conclusion, these new algorisms are very fast genotype identification tools that are suitable for evaluating E. granulosus s.l. isolated from livestock or livestock holders, particularly in developing countries.
[Mh] MeSH terms primary: Algorithms
Echinococcosis/parasitology
Echinococcosis/veterinary
Echinococcus granulosus/genetics
Genotype
Genotyping Techniques/methods
Polymerase Chain Reaction
Polymorphism, Restriction Fragment Length
[Mh] MeSH terms secundary: Animals
Animals, Domestic
Cyclooxygenase 1/genetics
Echinococcus granulosus/isolation & purification
Electron Transport Complex I/genetics
Humans
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:EC 1.14.99.1 (Cyclooxygenase 1); EC 1.6.5.3 (Electron Transport Complex I)
[Em] Entry month:1803
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[Js] Journal subset:IM
[Da] Date of entry for processing:180112
[St] Status:MEDLINE
[do] DOI:10.3347/kjp.2017.55.6.679

  6 / 29148 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 29518557
[Au] Autor:Zhang Y; Gao G; Lin R; Aweya JJ; Tao M; Wang F
[Ad] Address:Department of Biology, Guangdong Provincial Key Laboratory of Marine Biotechnology, Shantou University, Shantou 515063, China.
[Ti] Title:Transcriptome analyses reveal Litopenaeus vannamei hemocytes response to lipopolysaccharide.
[So] Source:Fish Shellfish Immunol;, 2018 Mar 05.
[Is] ISSN:1095-9947
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Although vertebrate immunity has been well studied for the past decades, invertebrate immunity was much less explored. One possible reason was that in vitro culture system was not well established. In this study, Litopenaeus vannamei was applied as an invertebrate study model. Primary culture conditions for L. vannamei hemocytes were optimized to get relatively quiescent state cells. LPS was used as an immune stimulator and the responses of primary cultured hemocytes were transcriptomically analyzed. Our results showed that around 1600 genes were upregulated and 800 genes were downregulated from LPS treated hemocytes. The altered genes could be classified into three categories: upregulated, downregulated, upregulated and then downregulated. Further qPCR validation showed that ubiquitin, ubiquitin-conjugating enzyme E2 C, ubiquitin-conjugating enzyme H1 and ubiquitin-conjugating enzyme H5b in ubiquitin-proteasome pathway were upregulated, cytochrome c oxidase 1, NADH dehydrogenase 1, Inosine-5'-monophosphate dehydrogenase 1b and phospholipid-transporting ATPase IA in mitochondria oxidation phosphorylation were downregulated. Our results showed that L. vannamei hemocyte inflammation responses share a lot of similarities with mammalian macrophage inflammation responses.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180308
[Lr] Last revision date:180308
[St] Status:Publisher

  7 / 29148 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 28463416
[Au] Autor:Kaja S; Payne AJ; Naumchuk Y; Koulen P
[Ad] Address:Departments of Ophthalmology and Molecular Pharmacology & Therapeutics, Stritch School of Medicine, Loyola University Chicago, Maywood, Illinois.
[Ti] Title:Quantification of Lactate Dehydrogenase for Cell Viability Testing Using Cell Lines and Primary Cultured Astrocytes.
[So] Source:Curr Protoc Toxicol;72:2.26.1-2.26.10, 2017 May 02.
[Is] ISSN:1934-9262
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Drug discovery heavily relies on cell viability studies to assess the potential toxicity of drug candidates. L-Lactate dehydrogenase (LDH) is a cytoplasmic enzyme that catalyzes the concomitant interconversions of pyruvate to L-lactate and NADH to NAD during glycolysis, and the reverse reactions during the Cori cycle. In response to cellular damage, induced by endogenous cellular mechanisms or as a result of exogenously applied insults, LDH is released from the cytoplasm into the extracellular environment. Its stability in cell culture medium makes it a well-suited correlate for the presence of damage and toxicity in tissues and cells. We herein present protocols for a reproducible and validated LDH assay optimized for several cell types. In contrast to commercially available LDH assays, often associated with proprietary formulations and high cost, our protocols provide ample opportunities for experiment-specific optimization with low variability and cost. © 2017 by John Wiley & Sons, Inc.
[Mh] MeSH terms primary: Astrocytes/enzymology
Cell Survival
L-Lactate Dehydrogenase/analysis
Toxicology/methods
[Mh] MeSH terms secundary: Animals
Cell Culture Techniques
Cell Line
Cell Line, Tumor
Culture Media/chemistry
Cytoplasm/enzymology
Extracellular Space/enzymology
Glycolysis
Humans
Neurons/drug effects
Neuroprotective Agents/pharmacology
Optic Nerve/cytology
Optic Nerve/drug effects
Primary Cell Culture
Rats
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Culture Media); 0 (Neuroprotective Agents); EC 1.1.1.27 (L-Lactate Dehydrogenase)
[Em] Entry month:1803
[Cu] Class update date: 180308
[Lr] Last revision date:180308
[Js] Journal subset:IM
[Da] Date of entry for processing:170503
[St] Status:MEDLINE
[do] DOI:10.1002/cptx.21

  8 / 29148 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 29294080
[Au] Autor:Park J; Shim JK; Kang JH; Choi J; Chang JH; Kim SY; Kang SG
[Ad] Address:Department of Neurosurgery, Brain Tumor Center, Severance Hospital, Yonsei University College of Medicine, Seoul, Republic of Korea.
[Ti] Title:Regulation of bioenergetics through dual inhibition of aldehyde dehydrogenase and mitochondrial complex I suppresses glioblastoma tumorspheres.
[So] Source:Neuro Oncol;, 2017 Dec 23.
[Is] ISSN:1523-5866
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Background: Targeted approaches for treating glioblastoma (GBM) attempted to date have consistently failed, highlighting the imperative for treatment strategies that operate on different mechanistic principles. Bioenergetics deprivation has emerged as an effective therapeutic approach for various tumors. We have previously found that cancer cells preferentially utilize cytosolic NADH supplied by aldehyde dehydrogenase (ALDH) for ATP production through oxidative phosphorylation (OxPhos). This study is aimed to examine therapeutic responses and underlying mechanisms of dual inhibition of ALDH and OxPhos against GBM. Methods: For inhibition of ALDH and OxPhos, the corresponding inhibitors, gossypol and phenformin were used. Biological functions, including ATP levels, stemness, invasiveness, and viability, were evaluated in GBM tumorspheres (TSs). Gene expression profiles were analyzed using microarray data. In vivo anticancer efficacy was examined in a mouse orthotopic xenograft model. Results: Combined treatment of GBM TSs with gossypol and phenformin significantly reduced ATP levels, stemness, invasiveness, and cell viability. Consistently, this therapy substantially decreased expression of genes associated with stemness, mesenchymal transition, and invasion in GBM TSs. Supplementation of ATP using malate abrogated these effects, whereas knockdown of ALDH1L1 mimicked them, suggesting that disruption of ALDH-mediated ATP production is a key mechanism of this therapeutic combination. In vivo efficacy confirmed remarkable therapeutic responses to combined treatment with gossypol and phenformin. Conclusion: Our findings suggest that dual inhibition of tumor bioenergetics is a novel and effective strategy for the treatment of GBM.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1801
[Cu] Class update date: 180308
[Lr] Last revision date:180308
[St] Status:Publisher
[do] DOI:10.1093/neuonc/nox243

  9 / 29148 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 29194006
[Au] Autor:Gavya SL; Arora N; Ghosh SS
[Ad] Address:a Department of Biosciences and Bioengineering , Indian Institute of Technology Guwahati , Guwahati , Assam , India.
[Ti] Title:Retention of functional characteristics of glutathione-S-transferase and lactate dehydrogenase-A in fusion protein.
[So] Source:Prep Biochem Biotechnol;48(2):128-135, 2018 Feb 07.
[Is] ISSN:1532-2297
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:A paradigm shift toward fusion proteins to render multiple functionalities and applications on a single platform has been incurred in enzyme based diagnosis. Herein, we report development and systematic characterizations of glutathione-S-transferase (GST) and human lactate dehydrogenase A (hLDHA) in a fusion protein (GST-hLDHA) to achieve functional activities of GST and hLDHA simultaneously. The GST-pGEX-4T-2 vector system was used for cloning and purification of hLDHA, utilizing the affinity based interaction between GST and GSH in column chromatography. Bacterially purified protein was subjected to the Western blot analysis and structural analysis by circular dichroism spectroscopy, which revealed intact structural framework of the fusion construct. Kinetic characterization of the fusion GST-hLDHA protein toward GSH and NADH, suggested retention of functional activities of GST and hLDHA in fused protein as indicated by the kinetic parameters k and k /k . Further analysis of effect of temperature and pH on GST-hLDHA activity revealed maximum activity around human physiological conditions (37°C and pH 8). Preservation of the structural and functional characteristics of the fusion enzyme paves the way for potential application for the detection of NADH and GSH in conjunction as biomarkers for cancer diagnosis.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1712
[Cu] Class update date: 180308
[Lr] Last revision date:180308
[St] Status:In-Process
[do] DOI:10.1080/10826068.2017.1405022

  10 / 29148 MEDLINE  
              first record previous record
select
to print
Photocopy
Full text

[PMID]: 29494135
[Au] Autor:Grant GA
[Ad] Address:Departments of Developmental Biology and Medicine , Washington University School of Medicine , 660 South Euclid Avenue , Box 8103, St. Louis , Missouri 63110 , United States.
[Ti] Title:Elucidation of a Self-Sustaining Cycle in Escherichia coli l-Serine Biosynthesis That Results in the Conservation of the Coenzyme, NAD .
[So] Source:Biochemistry;, 2018 Mar 06.
[Is] ISSN:1520-4995
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:The equilibrium of the reaction catalyzed by d-3-phosphoglycerate dehydrogenase (PGDH), the first enzyme in the l-serine biosynthetic pathway, is far in the direction away from serine synthesis. As such, the enzyme is usually assayed in this direction. To easily assay it in the direction of l-serine synthesis, it can be coupled to the next enzyme in the pathway, phosphoserine aminotransferase (PSAT), with the activity monitored by the conversion of NAD to NADH by PGDH. However, when PGDHs from several different species were coupled to PSAT, it was found that one of them, ecPGDH, conserves the coenzyme in the production of l-serine by utilizing an intrinsic cycle of NAD /NADH interconversion coupled with the conversion of α-ketoglutarate (αKG) to α-hydroxyglutarate. Furthermore, the cycle can be maintained by production of αKG by the second enzyme in the pathway, PSAT, and does not require any additional enzymes. This is not the case for PGDH from another bacterial source, Mycobacterium tuberculosis, and a mammalian source, human liver, where net consumption of NAD occurs. Both NAD and NADH appear to remain tightly bound to ecPGDH during the cycle, effectively removing a requirement for the presence of an exogenous coenzyme pool to maintain the pathway and significantly reducing the energy requirement needed to maintain this major metabolic pathway.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180306
[Lr] Last revision date:180306
[St] Status:Publisher
[do] DOI:10.1021/acs.biochem.8b00074


page 1 of 2915 go to page                         
   


Refine the search
  Database : MEDLINE Advanced form   

    Search in field  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/PAHO/WHO - Latin American and Caribbean Center on Health Sciences Information