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Fig. 25 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 25. Reaction catalyzed by 4′-phosphopantothenoylcysteine decarboxylase. The enzyme uses non-covalently bound FMN, which is transiently reduced in the first half-reaction (substrate oxidation) yielding a thioaldehyde intermediate (top). At this stage, decarboxylation occurs (right) and the generated enethiolate is then subject to reduction to the final product 4′-phosphopantetheine (bottom). Thus the flavin serves as a transient electron sink during the decarboxylation reaction.
Fig. 9 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 9. The first step of proline degradation. Proline dehydrogenase 1 and 2 catalyze the two-electron oxidation of the C–N bond in the pyrollidine-ring as shown. The enzymes are peripherally associated with the inner mitochondrial membrane enabling direct transfer of the electrons to CoQ.
Fig. 11 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 11. Reactions catalyzed by xanthine dehydrogenase. The enzyme oxidizes hypoxanthine to xanthine and further to uric acid. The initial oxidation occurs at the Moco and electrons are transferred to two iron-sulfur-complexes operating in-line to reduce the FAD cofactor, which in turn reduces NAD+ to NADH. Alternatively, the enzyme may reduce dioxygen either to hydrogen peroxide or superoxide when present in its oxidase conformation. The oxygen atom incorporated in the products is derived from water (shown in red, for details of the reaction mechanism, see Nishino et al., 2013). (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 4 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 4. Reaction catalyzed by the lipoamide dehydrogenase subunit (E3). This subunit is present in the pyruvate, α-ketoglutarate and branched-chain α-keto acid dehydrogenase complex where the dithiol of the lipoamide moiety first reduces the internal disulfide bridge (top) and subsequently the reduced internal dithiol reduces the FAD (right), which in turn reduces NAD+ (left) leading to the resting state of the enzyme.
Fig. 22 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 22. Reactions catalyzed by pyridoxamine/pyridine 5′-phosphate oxidase. The enzyme accepts pyridoxamine and pyridoxine 5′-phosphate as substrate. The oxidation of pyridoxamine 5-phosphate leads to the imine, which is hydrolyzed to the aldehyde and ammonia (upper curved arrow). In both reactions the reduced cofactor FMN is re-oxidized by dioxygen resulting in the generation of hydrogen peroxide (upper and lower curved arrow).
Fig. 3 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 3. Oxidation of succinate to fumarate catalyzed by succinate dehydrogenase (complex II). The reduced FAD donates the electrons to a pair of iron-sulfur clusters from where they are finally delivered to a cytochrome leading to the reduction of ubiquinone (CoQ) in the inner mitochondrial membrane.
Fig. 6 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 6. Reaction catalyzed by D-lactate dehydrogenase. The reduced FAD cofactor is reoxidized by cytochrome c in the intermembrane space of mitochondria and the electrons are transferred to cytochrome c oxidase (complex IV) of the mETC.
Fig. 2 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 2. Biosynthesis of riboflavin in A. thaliana. The biosynthesis of riboflavin starts with GTP (top left), which is converted in four enzymatic steps to 5-amino-6- ribityl-aminouracil (center). The second component needed is D-ribulose-5-phosphate (center, left), which is converted to 3,4-dihydroxy-2-butanone-4-phosphate (shown in blue). The second ring is generated by condensation of the two intermediates, a reaction catalyzed by lumazine synthase (RibE) yielding 6,7-dimethyl- 8-ribityl lumazine. The last step of the biosynthesis is a dismutation reaction involving two lumazine molecules resulting in the generation of riboflavin and 5- amino-6-ribityl-aminouracil, which reenters riboflavin biosynthesis. For clarity, the two lumazine molecules are highlighted in red/blue and red/green, respectively. The double headed green arrow (top, right) indicates the swap of reactions compared to riboflavin biosynthesis in E. coli and S. cerevisiae. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 42 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 42. Reaction catalyzed by monolignol oxidoreductases. The enzymes were shown to accept monolignols with different substitution patterns in the aromatic ring (R1 and R2 = H, p-coumaryl alcohol; R1 = H and R2 = methoxy, coniferyl alcohol; R1 and R2 = methoxy, sinapyl alcohol) (Daniel et al., 2015). In contrast to the other members of the BBE-like enzyme family, most of the enzymes catalyzing this reaction are dehydrogenases, with the exception of AtBBE24 (Zafred et al., 2015). The electron acceptor for the dehydogenases is yet unknown.
Fig. 20 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 20. Two flavoenzymes involved in ascorbate biosynthesis and maintenance. L-Galactono-1,4-lacton dehydrogenase catalyzes the last step in the Smirnoff-Wheeler pathway to yield ascorbate from L-galactono-1,4-lactone (top). The substrate-derived electrons are passed on to cytochrome c and thus enter the mETC. The detoxification of ROS or ferric iron leads to the generation of the monodehydroascorbate radical (right), which is recycled to ascorbate by the action of monodehydroascorbate dehydrogenase (left-center). For details of the latter reaction see text.
Fig. 44 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 44. Reaction of flavin-containing monooxygenases (clade 3). The seven enzymes characterized so far were all shown to be S-glucosinolate oxidases that catalyze the S-monooxygenation of methylthioalkyl glucosinolates to the corresponding methylsulfinyl glucosinolates (Hansen et al., 2007; Kong et al., 2016; Li et al., 2008). For the nine uncharacterized members a similar catalytic function is hypothesized, but remains to be confirmed.
Fig. 23 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 23. Reaction catalyzed by NDC1/demethylphylloquinone reductase. The penultimate step in the biosynthesis of phylloquinol affords demethylphylloquinol by two-electron reduction of the demetyhlphylloquinone (top reaction). Through nucleophilic attack of the aromatic ring onto the methyl group (in red) of SAM the final methylated product, phylloquinol is formed and S-adenosylhomocysteine (SAH) is released (R = prenyl side chain). (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 24 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 24. Reaction catalyzed by COQ6 in ubiquinone biosynthesis. The FAD-dependent hydroxylation occurs in the 5-position of the aromatic ring as indicated (highlighted in red). COQ6 belongs to the class A FPMOs and depends on NAD(P)H as reductant. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 29 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 29. Reaction catalyzed by carotene cis-trans isomerase. The reaction shown requires reduced FAD for the redox-neutral cis-to-trans isomerization at position 9 and 9′ of prolycopene and generates the linear all-trans-lycopene. The reduced FAD is probably generated at the expense of NAD(P)H. Thus, the enzyme appears to possess a second activity that enables the transfer of a hydride from the reduced nicotinamide to the bound FAD cofactor.
Fig. 47 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 47. Reaction catalyzed by D-amino acid oxidase. Regeneration of the reduced FAD occurs by dioxygen leading to the production of hydrogen peroxide (top). Note that the direct product of the oxidation, the corresponding imino acid, is non-enzymatically hydrolyzed to yield the α-keto acid and ammonia.
Fig. 33 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 33. Reaction of flavin-dependent monooxygenases involved in auxin biosynthesis. All enzymes forming clade 2 were shown to play an important role in auxin biosynthesis, as they were identified to mediate the conversion of indole-3-pyruvic acid to indole-3-acetic acid (Dai et al., 2013; Mashiguchi et al., 2011).
Fig. 28 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 28. Reaction of phytoene dehydrogenase/desaturase. The enzyme introduces two double bonds at position 11 and 11′ and mediates the concomitant trans-to-cis isomerization at position 9 and 9'. Reoxidation of the reduced cofactor is achieved by electron transfer to plastoquinone in the plastid membrane.
Fig. 7 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
Fig. 7. Reactions catalyzed by isovaleryl-CoA dehydrogenase in valine and isoleucine degradation. Reoxidation of reduced FAD occurs by electron donation to ETF, which in turn feeds the electrons into the mETC via ETF-QO.
Strategies and interventions to strengthen pharmacovigilance systems in low- and middle-income countries: A scoping review
<div><strong>Objectives</strong></div> <div>The slow progress of pharmacovigilance (PV) in low-and-middle-income countries (LMIC) raises questions about core challenges on the growth of PV, and the appropriateness of strategies used so far to develop PV. Therefore, this scoping review aims to describe strategies and interventions to strengthen PV in LMIC and to propose recommendations for future investments in PV capacity building.</div> <div> </div> <div><strong>Inclusion criteria</strong></div> <div>Publications included were primary studies, articles, and policy and guideline papers, describing interventions to strengthen PV in LMIC. </div> <div> </div> <div><strong>Methods</strong></div> <div>The review was conducted following the Joanna Briggs Institute (JBI) guidelines on conducting scoping reviews. Literature searches were performed in MEDLINE, EMBASE, Web of Science, PDQ-evidence, CINAHL and relevant websites from 1990 to January 2021. Two reviewers independently screened titles, abstracts and full-texts. One reviewer performed data extraction and descriptive analysis, which were reviewed by two other reviewers.</div> <div> </div> <div><strong>Results</strong></div> <div>10,922 unique titles were screened and 152 were eligible for full text review. Of these, 57 and an additional 13 reports from grey literature fulfilled eligibility criteria for inclusion in the review. These were grouped into two categories: i) Interventions aimed at increasing PV knowledge and adverse drug reactions (ADR) reporting (45 papers), primarily education of healthcare professionals (HCP), alone or in combination with other interventions such as mobile and electronic reporting; ii) Interventions aimed at strengthening various components of the national PV system (25 papers), describing strategies or mixed interventions implemented at the national level, targeting different components of the national PV system.</div> <div> </div> <div><strong>Conclusions</strong></div> <div>Results of this review suggest that educating HCP on ADR reporting is the most common approach to build PV capacity in LMIC. Though important, education alone is insufficient and should ideally be organised within the holistic framework of strengthening national PV systems, with a focus on building capacity for advanced activities such as signal detection.</div>
A Study Comparing a Disposable Flexible Cystoscope With Reusable Scopes in Adult Patients.
ClinicalTrials.gov study NCT06422312. IPD Sharing: NO. Countries: 1. Publications: 5.
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Allen Brain Atlas
Allen Brain Atlas is an Allen Institute collection of brain map atlases, datasets, APIs, and analysis tools covering mouse, human, and non-human primate brain resources.
Annotated Behaviour and Observability Dataset (ABODe)
ABODe is a University of Edinburgh DataShare dataset for behavior classification in group-housed mice using home-cage video, identities, bounding boxes, ground-plate positions, and annotator labels.
DANDI Archive for NWB datasets
DANDI is a BRAIN Initiative archive for publishing and sharing neurophysiology data, including electrophysiology, optophysiology, and behavioral data packaged as NWB and related standards.
International Brain Laboratory public data
The International Brain Laboratory public data releases expose standardized mouse decision-making experiments, including Neuropixels recordings, widefield calcium imaging, behavior, and session metadata accessed through the ONE API.
OpenNeuro
OpenNeuro is a free, open platform for sharing neuroimaging datasets, with public search, dataset pages, and download paths for web, S3, DataLad, and the OpenNeuro CLI.