Database : MEDLINE
Search on : cytochrome and c and group [Words]
References found : 26023 [refine]
Displaying: 1 .. 10   in format [Detailed]

page 1 of 2603 go to page                         

  1 / 26023 MEDLINE  
              next record last record
select
to print
Photocopy
Full text

[PMID]: 29524634
[Au] Autor:Robson E; Tweedy C; Manzanza N; Taylor JP; Atkinson P; Randall F; Reeve A; Clowry GJ; LeBeau FEN
[Ad] Address:Institute of Neuroscience, Newcastle University, Medical School, Framlington Place, Newcastle-upon-Tyne NE2 4HH, UK.
[Ti] Title:Impaired fast network oscillations and mitochondrial dysfunction in a mouse model of alpha-synucleinopathy (A30P).
[So] Source:Neuroscience;, 2018 Mar 07.
[Is] ISSN:1873-7544
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Intracellular accumulation of alpha-synuclein (α-syn) is a key pathological process evident in Lewy body dementias (LBD), including Parkinson's disease dementia (PDD) and dementia with Lewy bodies (DLB). LBD results in marked cognitive impairments and changes in cortical networks. To assess the impact of abnormal α-syn expression on cortical network oscillations relevant to cognitive function, we studied changes in fast beta/gamma network oscillations in the hippocampus in a mouse line that over-expresses human mutant α-syn (A30P). We found an age-dependent reduction in the power of the gamma (20-80 Hz) frequency oscillations in slices taken from mice aged 9-16 months (9+), that was not present in either young 2-6 months old (2+) A30P mice, or in control mice at either age. The mitochondrial blockers potassium cyanide and rotenone both reduced network oscillations in a concentration-dependent manner in aged A30P mice and aged control mice but slices from A30P mice showed a greater reduction in the oscillations. Histochemical analysis showed an age-dependent reduction in cytochrome c oxidase (COX) activity, suggesting a mitochondrial dysfunction in the 9+A30P group. A deficit in COX IV expression was confirmed by immunohistochemistry. Overall, our data demonstrate an age-dependent impairment in mitochondrial function and gamma frequency activity associated with the abnormal expression of α-syn. These findings provide mechanistic insights into the consequences of over-expression of α-syn which might contribute to cognitive decline.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:Publisher

  2 / 26023 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy

[PMID]: 29494565
[Au] Autor:Tan J; Xie Q; Song S; Miao Y; Zhang Q
[Ad] Address:Department of Geriatrics, Tianjin Medical University General Hospital, Tianjin Institute of Geriatrics, Tianjin, China (mainland).
[Ti] Title:Albumin Overload and PINK1/Parkin Signaling-Related Mitophagy in Renal Tubular Epithelial Cells.
[So] Source:Med Sci Monit;24:1258-1267, 2018 Mar 01.
[Is] ISSN:1643-3750
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:BACKGROUND Albumin, as a major urinary protein component, is a risk factor for chronic kidney disease progression. Mitochondrial dysfunction is one of the main causes of albumin-induced proximal tubule cells injury. Mitophagy is considered as a pivotal protective mechanism for the elimination of dysfunctional mitochondria. The objective of this research was to determine whether albumin overload-induced mitochondrial dysfunction can activate PINK1/Parkin-mediated mitophagy in renal tubular epithelial cells (TECs). MATERIAL AND METHODS Immunofluorescence assay and Western blot assay were used to detect the effects of albumin overload on autophagy marker protein LC3. Transmission electron microscopy and Western blot assay were used to investigate the role of albumin in mitochondrial injury. Western blot assay and co-localization of acidic lysosomes and mitochondria assay were employed to detect the activation of mitophagy induced by albumin. Finally, we explored the role of PINK1/Parkin signaling in albumin-induced mitophagy by inhibiting mitophagy by knockdown of PARK2 (Parkin) level. RESULTS Immunofluorescence and Western blot results showed that the expression level of LC3-II increased, and the maximum increase point was observed after 8 h of albumin treatment. Transmission electron microscopy results demonstrated that albumin overload-induced mitochondrial injury and quantity of autophagosomes increased. Additionally, expression of PINK1 and cytosolic cytochrome C increased and mitochondria cytochrome C decreased in the albumin group. The co-localization of acidic lysosomes and mitochondria demonstrated that the number of albumin overload-induced mitophagy-positive dots increased. The transient transfection of PARK2 siRNA result showed knockdown of the expression level of PARK2 can inhibit mitophagy induced by albumin. CONCLUSIONS In conclusion, our study suggests that mitochondrial dysfunction activates the PINK1/Parkin signaling and mitophagy in renal tubular epithelial cells under albumin overload condition.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180311
[Lr] Last revision date:180311
[St] Status:In-Process

  3 / 26023 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 29522708
[Au] Autor:Ma JQ; Liu CM; Yang W
[Ad] Address:School of Chemical Engineering, Sichuan University of Science and Engineering, No. 180, Huixing Road, 643000, Zigong City, Sichuan Province, PR China. Electronic address: a1032042419@126.com.
[Ti] Title:Protective effect of rutin against carbon tetrachloride-induced oxidative stress, inflammation and apoptosis in mouse kidney associated with the ceramide, MAPKs, p53 and calpain activities.
[So] Source:Chem Biol Interact;, 2018 Mar 06.
[Is] ISSN:1872-7786
[Cp] Country of publication:Ireland
[La] Language:eng
[Ab] Abstract:Rutin, a natural flavonoid, possess beneficial health effects. However, its renoprotective effect against carbon tetrachloride (CCl ) induced injury and the underlying mechanism is not clarified. The current study aims is to identify the therapeutic effects of rutin on oxidative stress, inflammation and apoptosis in mouse kidney exposed to CCl . ICR mice received CCl with or without rutin co-administration for one week. Compared with the control group, mice receiving CCl alone showed kidney injury as evidenced by elevation in serum biochemical markers, inflammation, caspase-3 activity and apoptosis in kidney, while rutin administration significantly attenuated these pathophysiological changes. Exploration of the underlying mechanisms of its action demonstrated that rutin reduced the ROS, calpain and ceramide levels in mouse kidneys. Rutin significantly decreased the p53, TNF-α, IL-1ß activities and mitogen-activated protein kinase (MAPK) phosphorylation in the kidneys. In addition, rutin increased the levels of Bcl-2 protein and reduced levels protein of Bax. Rutin also inhibited the release of cytochrome C from mitochondria in kidneys of the CCl -treated mice. Taken together, rutin ameliorates CCl -induced oxidative stress, inflammation and apoptosis through regulating the ceramide, MAPK, p53 and calpain activities and thereby suppressing apoptosis by the mitochondrial pathway.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:Publisher

  4 / 26023 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 28986298
[Au] Autor:Hsiao JC; McGrath AP; Kielmann L; Kalimuthu P; Darain F; Bernhardt PV; Harmer J; Lee M; Meyers K; Maher MJ; Kappler U
[Ad] Address:Centre for Metals in Biology, School of Chemistry and Molecular Biosciences, University of Queensland, St Lucia, QLD 4072, Australia.
[Ti] Title:The central active site arginine in sulfite oxidizing enzymes alters kinetic properties by controlling electron transfer and redox interactions.
[So] Source:Biochim Biophys Acta;1859(1):19-27, 2018 01.
[Is] ISSN:0006-3002
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:A central conserved arginine, first identified as a clinical mutation leading to sulfite oxidase deficiency, is essential for catalytic competency of sulfite oxidizing molybdoenzymes, but the molecular basis for its effects on turnover and substrate affinity have not been fully elucidated. We have used a bacterial sulfite dehydrogenase, SorT, which lacks an internal heme group, but transfers electrons to an external, electron accepting cytochrome, SorU, to investigate the molecular functions of this arginine residue (Arg78). Assay of the SorT Mo centre catalytic competency in the absence of SorU showed that substitutions in the central arginine (R78Q, R78K and R78M mutations) only moderately altered SorT catalytic properties, except for R78M which caused significant reduction in SorT activity. The substitutions also altered the Mo-centre redox potentials (Mo potential lowered by ca. 60-80mV). However, all Arg78 mutations significantly impaired the ability of SorT to transfer electrons to SorU, where activities were reduced 17 to 46-fold compared to SorT , precluding determination of kinetic parameters. This was accompanied by the observation of conformational changes in both the introduced Gln and Lys residues in the crystal structure of the enzymes. Taking into account data collected by others on related SOE mutations we propose that the formation and maintenance of an electron transfer complex between the Mo centre and electron accepting heme groups is the main function of the central arginine, and that the reduced turnover and increases in K are caused by the inefficient operation of the oxidative half reaction of the catalytic cycle in enzymes carrying these mutations.
[Mh] MeSH terms primary: Arginine/chemistry
Bacterial Proteins/chemistry
Sinorhizobium meliloti/enzymology
Sulfite Dehydrogenase/chemistry
[Mh] MeSH terms secundary: Amino Acid Substitution
Arginine/metabolism
Bacterial Proteins/genetics
Bacterial Proteins/metabolism
Catalytic Domain
Electron Transport
Kinetics
Molybdenum
Mutation, Missense
Oxidation-Reduction
Sinorhizobium meliloti/genetics
Sulfite Dehydrogenase/genetics
Sulfite Dehydrogenase/metabolism
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (Bacterial Proteins); 81AH48963U (Molybdenum); 94ZLA3W45F (Arginine); EC 1.8.2.1 (Sulfite Dehydrogenase)
[Em] Entry month:1803
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[Js] Journal subset:IM
[Da] Date of entry for processing:171008
[St] Status:MEDLINE

  5 / 26023 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 29521452
[Au] Autor:Scott KM; Williams J; Porter CMB; Russel S; Harmer TL; Paul JH; Antonen KM; Bridges MK; Camper GJ; Campla CK; Casella LG; Chase E; Conrad JW; Cruz MC; Dunlap DS; Duran L; Fahsbender EM; Goldsmith DB; Keeley RF; Kondoff MR; Kussy BI; Lane MK; Lawler S; Leigh BA; Lewis C; Lostal LM; Marking D; Mancera PA; McClenthan EC; McIntyre EA; Mine JA; Modi S; Moore BD; Morgan WA; Nelson KM; Nguyen KN; Ogburn N; Parrino DG; Pedapudi AD; Pelham RP; Preece AM; Rampersad EA; Richardson JC; Rodgers CM; Schaffer BL; Sheridan NE; Solone MR; Staley ZR; Tabuchi M; Waide RJ
[Ad] Address:Department of Integrative Biology, University of South Florida, 4202 East Fowler Avenue, Tampa, FL 33620, USA.
[Ti] Title:Genomes of ubiquitous marine and hypersaline Hydrogenovibrio, Thiomicrorhabdus, and Thiomicrospira spp. encode a diversity of mechanisms to sustain chemolithoautotrophy in heterogeneous environments.
[So] Source:Environ Microbiol;, 2018 Mar 09.
[Is] ISSN:1462-2920
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Chemolithoautotrophic bacteria from the genera Hydrogenovibrio, Thiomicrorhabdus, and Thiomicrospira are common, sometimes dominant, isolates from sulfidic habitats including hydrothermal vents, soda and salt lakes, and marine sediments. Their genome sequences confirm their membership in a deeply branching clade of the Gammaproteobacteria. Several adaptations to heterogeneous habitats are apparent. Their genomes include large numbers of genes for sensing and responding to their environment (EAL- and GGDEF-domain proteins, and methyl-accepting chemotaxis proteins) despite their small sizes (2.1 - 3.1 Mbp). An array of sulfur-oxidizing complexes are encoded, likely to facilitate these organisms' use of multiple forms of reduced sulfur as electron donors. Hydrogenase genes are present in some taxa, including group 1d and 2b hydrogenases in Hydrogenovibrio marinus and H. thermophilus MA2-6, acquired via horizontal gene transfer. In addition to high-affinity cbb cytochrome c oxidase, some also encode cytochrome bd-type quinol oxidase or ba -type cytochrome c oxidase, which could facilitate growth under different oxygen tensions, or maintain redox balance. Carboxysome operons are present in most, with genes downstream encoding transporters from four evolutionarily distinct families, which may act with the carboxysomes to form CO concentrating mechanisms. These adaptations to habitat variability likely contribute to the cosmopolitan distribution of these organisms. This article is protected by copyright. All rights reserved.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:Publisher
[do] DOI:10.1111/1462-2920.14090

  6 / 26023 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 29462686
[Au] Autor:Singh J; Dwivedi A; Ray L; Chopra D; Dubey D; Srivastva AK; Kumari S; Yadav RK; Amar SK; Haldar C; Ray RS
[Ad] Address:Photobiology Laboratory, Systems Toxicology and Health Risk Assessment Group, CSIR-Indian Institute of Toxicology Research (CSIR-IITR), Vishvigyan Bhavan, 31, Mahatma Gandhi Marg, Lucknow 226001, Uttar Pradesh, India; Academy of Scientific and Innovative Research (AcSIR), CSIR-IITR Campus, Lucknow 2
[Ti] Title:PLGA nanoformulation of sparfloxacin enhanced antibacterial activity with photoprotective potential under ambient UV-R exposure.
[So] Source:Int J Pharm;541(1-2):173-187, 2018 Feb 17.
[Is] ISSN:1873-3476
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:Sparfloxacin (SPFX) is a broad spectrum antibiotic which inhibits bacterial DNA gyrase enzyme activity. However, photodegradation in the presence of UVA limits its antibacterial activity and induces phototoxicity. Thus, to encounter this problem, we have developed poly d,l-lactic-co-glycolic acid (PLGA) loaded SPFX nanoparticles. Here, we have performed a comparative antibacterial activity of SPFX and its nanoparticles (NPs) through molecular docking and plate sensitivity assay. Under environmental UVA exposure, photoexcited SPFX significantly generates ROS, DNA damage and mitochondrial mediated cell death in comparison to PLGA-SPFX-NPs (nano SPFX) in human skin cell line (HaCaT). In presence of UVA, bulk SPFX induced cell cycle arrest with appearance of sub-G1 peak showing apoptosis while nano SPFX did not show any change. SPFX triggered apoptosis via alteration in membrane integrity of mitochondria and lysosome in comparison to PLGA-SPFX-NPs. Involvement of mitochondrial mediated cell death was confirmed by down-regulation of anti-apoptotic Bcl-2 and procaspase-3 and upregulation of pro-apoptotic Bax, cytochrome-c and caspase-3 proteins expression. Specific caspase inhibitor, Z-VAD-FMK showed involvement of caspase cascade pathway in apoptosis. Our finding suggests that controlled release of SPFX from PLGA-SPFX-NPs can reduce its side effects and enhance its antibacterial activity. Thus, nanotization of fluoroquinolones will be a significant step to reduce the problem of resistance and phototoxicity of this group.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180308
[Lr] Last revision date:180308
[St] Status:Publisher

  7 / 26023 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 29438775
[Au] Autor:Roh T; De U; Lim SK; Kim MK; Choi SM; Lim DS; Yoon S; Kacew S; Kim HS; Lee BM
[Ad] Address:Division of Toxicology, School of Pharmacy, Sungkyunkwan University, Seobu-ro 2066, Suwon, Gyeonggi-do, 440-746, South Korea.
[Ti] Title:Detoxifying effect of pyridoxine on acetaminophen-induced hepatotoxicity via suppressing oxidative stress injury.
[So] Source:Food Chem Toxicol;114:11-22, 2018 Feb 10.
[Is] ISSN:1873-6351
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:The detoxifying effect of pyridoxine against acetaminophen (APAP)-induced hepatotoxicity was investigated. HepG2 cells were co-treated with APAP and pyridoxine to compare with betaine or methionine for 24 h. LDH, ALT and AST activities were measured to determine direct cells damage in vitro and in vivo. Lipid peroxidation, antioxidant enzymes activity, and glutathione level were measured. Cytochrome c releaseand procaspase-3, cleaved caspase-3, Bcl-2, or Bax protein levels were measured to determine APAP-induced apoptotic cell death. Pyridoxine treatment significantly increased cell viability and decreased leakage of LDH activity against APAP-induced hepatotoxicity in HepG2 cells. ALT and AST activities were dose-dependently reduced by pyridoxine treatment compared to APAP-treated group. Significant increases in activities of GST and GPx were observed after co-treatment with APAP and pyridoxine. Although APAP-induced Nrf2 and HO-1 expression levels were gradually reduced in HepG2 cells by pyridoxine treatment, induction of antioxidant enzymes activities were dose-dependently increased. These protected effects of pyridoxine against APAP-induced hepatoxicity were closely associated with suppression of APAP-induced oxidative stress and apoptotic cell death in HepG2 cells. These data indicated that the protective action of pyridoxine against hepatic cell injuries was involved in the direct antioxidant activity which provides a pivotal mechanism for its potential hepatoprotective action.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180308
[Lr] Last revision date:180308
[St] Status:Publisher

  8 / 26023 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 29411391
[Au] Autor:Ren B; Li D; Si L; Ding Y; Han J; Chen X; Zheng Q
[Ad] Address:Key Laboratory of Xinjiang Phytomedicine Resource and Utilization, Ministry of Education, School of Pharmacy, Shihezi University, Shihezi, Xinjiang, China.
[Ti] Title:Alteronol induces cell cycle arrest and apoptosis via increased reactive oxygen species production in human breast cancer T47D cells.
[So] Source:J Pharm Pharmacol;70(4):516-524, 2018 Apr.
[Is] ISSN:2042-7158
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:OBJECTIVE: Emerging evidence showed that alteronol has a potential antitumour effect in several tumour cells. However, the antitumour effect of alteronol on breast cancer has not been reported. This study investigated the mechanisms of alteronol-induced cell proliferation inhibition in human breast cancer T47D cells. METHODS: After treatment with alteronol, T47D cell proliferation was examined by MTT assay. The cell cycle distribution, cell apoptosis, reactive oxygen species level and mitochondrial membrane potential were evaluated via flow cytometry. Next, the protein levels of cyclin B1, cdc2, p21, p-cyclin B1, p-cdc2, p53, Bax, Bcl-2 and cytochrome c were analysed using Western blot analysis. Meanwhile, the mRNA levels of cyclin B1, cdc2, p21 and p53 were examined by qRT-PCR. KEY FINDINGS: Our data showed that alteronol inhibited the proliferation of T47D cells via inducing G2-phase arrest and cell apoptosis. Compared with control group, alteronol significantly increased ROS level and triggered mitochondrial dysfunction in alteronol-treated T47D cells. Further studies showed that the mRNA and protein levels of cdc2 and cyclin B1 were downregulated, while the mRNA and protein levels of p21, p53, p-cyclin B1, p-cdc2 and cytochrome c were upregulated. In addition, the expression level of Bax was increased, and the expression level of Bcl-2 was decreased. CONCLUSIONS: Alteronol induced T47D cell cycle arrest and cell apoptosis through increasing ROS production and triggering mitochondrial dysfunction, and subsequently inhibiting T47D cell proliferation.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:In-Process
[do] DOI:10.1111/jphp.12879

  9 / 26023 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 29516517
[Au] Autor:Fasura Amorim P
[Ad] Address:Federal University of Rio de Janeiro, Institute of Biology, Laboratory of Systematics and Evolution of Teleost Fishes, Avenue Carlos Chagas Filho, 373, Rio de Janeiro, 21941-902, Rio de Janeiro, Brazil.
[Ti] Title:Jenynsia lineata species complex, revision and new species description (Cyprinodontiformes: Anablepidae).
[So] Source:J Fish Biol;, 2018 Mar 07.
[Is] ISSN:1095-8649
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:The Jenynsia lineata species complex comprises J. lineata from Montevideo, Uruguay and Jenynsia multidentata, from coastal basins of Brazil, Uruguay and Argentina up to 1200 m a.s.l. Taxonomic divisions within this group were tested using three different species delimitation methods, which found the two existing names to be synonyms and revealed a new cryptic species. Jenynsia darwini sp. nov. is distinguished from all congeners by having a unique combination of character states, including the shape of the dorsal postcleithrum (three times higher than wide v. less than two times higher than wide) and female colour pattern in the half of the caudal peduncle with rows of chromatophores segmented in unaligned spots (v. aligned spots forming lines). The new species also differs from J. lineata by having 26 nucleotide substitutions in the mitochondrial gene cytochrome c oxidase I (coI). Phylogenetic analysis of the genus based on morphological characters proposed by previous studies corroborates monophyly of the subgenera Plesiojenynsia and Jenynsia, with the new species being allocated to the subgenus Jenynsia as the sister group of J. lineata.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180308
[Lr] Last revision date:180308
[St] Status:Publisher
[do] DOI:10.1111/jfb.13587

  10 / 26023 MEDLINE  
              first record previous record
select
to print
Photocopy
Full text

[PMID]: 29514522
[Au] Autor:Wang ZL; Wang TZ; Zhu HF; Wang ZY; Yu XP
[Ad] Address:a Zhejiang Provincial Key Laboratory of Biometrology and Inspection and Quarantine, College of Life Sciences , China Jiliang University , Hangzhou , Zhejiang , People's Republic of China.
[Ti] Title:DNA barcoding evaluation and implications for phylogenetic relationships in ladybird beetles (Coleoptera: Coccinellidae).
[So] Source:Mitochondrial DNA A DNA Mapp Seq Anal;:1-8, 2018 Mar 08.
[Is] ISSN:2470-1408
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Ladybird beetles (Coleoptera: Coccinellidae), with broad morphological diversity, wide geographic distribution and substantial agricultural significance, are a challenging group for taxonomists and phylogenetics. As a promising tool to identify and discover new species, DNA barcoding might offer significant potential for identification, taxonomy and phylogeny of ladybird beetles. In the present study, a total of 1364 COI (cytochrome C oxidase subunit I) sequences representing 128 species from 52 genera of ladybird beetles were screened for barcoding evaluation and phylogenetic analysis. Our results from the barcoding analysis revealed that COI displays a similar level of species identification efficiency (nearly 90%) either based on Kimura two-parameter (K2P) distances calculation or on simplified neighbour-joining (NJ) tree construction. The phylogenetic relationships within the family Coccinellidae was analyzed by Bayesian-inference (BI) method. The phylogenetic results confirmed the monophyly of the subfamilies Microweisinae and Coccinellinae sensu Slipinski (2007), and suggested that the subfamilies Coccidulinae, Chilocorinae and Scymninae are paraphyletic. However, the phylogenetic relationships among different subfamilies are not clearly defined and thus remain to be thoroughly studied. Overall, our study confirmed the usefulness of DNA barcoding for coccinellid species identification and phylogenetic inference.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180308
[Lr] Last revision date:180308
[St] Status:Publisher
[do] DOI:10.1080/24701394.2018.1446950


page 1 of 2603 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