Bibliografie tematiche / Porphobilinogène

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Letteratura scientifica selezionata sul tema "Porphobilinogène"

Autore: Grafiati
Pubblicato: 29 marzo 2025

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Articoli di riviste sul tema "Porphobilinogène"

1

Deybach, J. C., and H. Puy. "Porphobilinogène (PBG) : précurseur de la biosynthèse de l'hème." EMC - Biologie médicale 5, no. 3 (2010): 1–4. http://dx.doi.org/10.1016/s2211-9698(10)71427-8.

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Deybach, J. C., and H. Puy. "Porphobilinogène (PBG) : précurseur de la biosynthèse de l'hème." EMC - Biologie Médicale 5, no. 3 (2010): 1–4. https://doi.org/10.1016/s0000-0000(10)51137-9.

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3

Schmitt, C., A. Poli, H. Manceau, H. Puy, L. Gouya, and T. Lefebvre. "Acide delta-aminolévulinique et porphobilinogène : précurseurs de la biosynthèse de l’hème." EMC - Biologie Médicale 18, no. 1 (2023): 1–7. https://doi.org/10.1016/s2211-9698(22)43395-4.

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4

Mami, I., A. Karras, H. Puy, P. Beaune, É. Thervet, and N. Pallet. "Caractérisation des modifications phénotypiques épithéliales rénales induites par l’acide delta aminolévulinique et le porphobilinogène." Néphrologie & Thérapeutique 9, no. 5 (2013): 380–81. http://dx.doi.org/10.1016/j.nephro.2013.07.356.

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5

Leeper, Finian J., and Martin Rock. "Interaction of analogues of porphobilinogen with porphobilinogen deaminase." Journal of the Chemical Society, Perkin Transactions 1, no. 21 (1996): 2643. http://dx.doi.org/10.1039/p19960002643.

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6

SHOOLINGIN-JORDAN, Peter M., Martin J. WARREN, and Sarah J. AWAN. "Discovery that the assembly of the dipyrromethane cofactor of porphobilinogen deaminase holoenzyme proceeds initially by the reaction of preuroporphyrinogen with the apoenzyme." Biochemical Journal 316, no. 2 (1996): 373–76. http://dx.doi.org/10.1042/bj3160373.

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Abstract (sommario):
The assembly process of the dipyrromethane cofactor of Escherichia coli porphobilinogen deaminase holoenzyme is initiated by the reaction of the porphobilinogen deaminase apoenzyme with preuroporphyrinogen. The resulting enzyme-bound tetrapyrrole (bilane) is equivalent to the holoenzyme intermediate complex ES2 and yields the dipyrromethane cofactor by reactions of the normal catalytic cycle. These observations indicate that preuroporphyrinogen, rather than porphobilinogen, is the preferred precursor for the dipyrromethane cofactor and explain the existence of the D84A and D84N deaminase mutan
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Jordan, P. M., and P. N. Gibbs. "Mechanism of action of 5-aminolaevulinate dehydratase from human erythrocytes." Biochemical Journal 227, no. 3 (1985): 1015–20. http://dx.doi.org/10.1042/bj2271015.

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Abstract (sommario):
Purified 5-aminolaevulinate dehydratase (porphobilinogen synthase, EC 4.2.1.24) from human erythrocytes was incubated initially with limiting amounts of 5-amino [5-14C]laevulinate in a rapid-mixing apparatus. The single-turnover reaction with respect to the bound labelled 5-aminolaevulinate was completed by the addition of unlabelled 5-aminolaevulinate and the resulting radioactive porphobilinogen was isolated and degraded. The 14C label was found to be located predominantly at C-2 of the product, demonstrating that, of the two substrate molecules participating in the reaction, the 5-aminolaev
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Hsiao, Kwang-Jen, Fa-Yauh Lee, Shew-Jen Wu, and Wei-Jan Chang. "Determination of erythrocyte porphobilinogen deaminase activity using porphobilinogen as substrate." Clinica Chimica Acta 168, no. 2 (1987): 257–58. http://dx.doi.org/10.1016/0009-8981(87)90296-8.

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9

Hart, G. J., C. Abell, and A. R. Battersby. "Purification, N-terminal amino acid sequence and properties of hydroxymethylbilane synthase (porphobilinogen deaminase) from Escherichia coli." Biochemical Journal 240, no. 1 (1986): 273–76. http://dx.doi.org/10.1042/bj2400273.

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Abstract (sommario):
Hydroxymethylbilane synthase (porphobilinogen deaminase) was purified to apparent homogeneity from Escherichia coli. The enzyme is a monomer of Mr approx. 40,000. The Km for porphobilinogen and relative Vmax. values have been obtained at various pH values over the range 6.2-8.8, enabling pK values for ionizable groups important for activity to be determined. The N-terminal amino acid sequence is presented.
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10

Heinemann, Ilka U., Claudia Schulz, Wolf-Dieter Schubert, et al. "Structure of the Heme Biosynthetic Pseudomonas aeruginosa Porphobilinogen Synthase in Complex with the Antibiotic Alaremycin." Antimicrobial Agents and Chemotherapy 54, no. 1 (2009): 267–72. http://dx.doi.org/10.1128/aac.00553-09.

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Abstract (sommario):
ABSTRACT The recently discovered antibacterial compound alaremycin, produced by Streptomyces sp. A012304, structurally closely resembles 5-aminolevulinic acid, the substrate of porphobilinogen synthase. During the initial steps of heme biosynthesis, two molecules of 5-aminolevulinic acid are asymmetrically condensed to porphobilinogen. Alaremycin was found to efficiently inhibit the growth of both Gram-negative and Gram-positive bacteria. Using the newly created heme-permeable strain Escherichia coli CSA1, we are able to uncouple heme biosynthesis from bacterial growth and demonstrate that ala
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Tesi sul tema "Porphobilinogène"

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Poli, Antoine. "Physiopathologie des porphyries : développement de méthodes d'analyses par spectrométrie de masse et application en contexte clinique, biodisponibilité du fer et porphyries érythropoïétiques : efficacité clinique de l'induction d'une carence martiale et caractérisation d'un modèle cellulaire." Electronic Thesis or Diss., Université Paris Cité, 2024. http://www.theses.fr/2024UNIP5206.

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Abstract (sommario):
Les porphyries sont des maladies génétiques causées par une dysfonction d'une enzyme de la voie de biosynthèse de l'hème responsable de l'accumulation de métabolites toxiques. On distingue les porphyries d'origine hépatique, où l'hème est le principal régulateur de sa synthèse, des porphyries érythropoïétiques, où c'est la biodisponibilité du fer qui est le déterminant majeur de la synthèse d'hème. Lors de ce travail, des méthodes de dosages par spectrométrie de masse ont été développées afin de mieux caractériser la physiopathologie des porphyries. En premier lieu, le dosage des précurseurs d
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2

Delaunay, Anne-Marie. "5-aminolevulinate deshydratase : clonage et expression du gène de rhodobacter sphaeroïdes." Rouen, 1990. http://www.theses.fr/1990ROUE5009.

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Abstract (sommario):
La construction d'une banque génomique de rhodobacter sphaeroïdes dans une souche d'escherichia coli (SHSP3) hem b#), mutée sur le gène codant pour la 5-aminolevulinate deshydratase (5-ALAD, E. C. 4. 2. 1. 24) a été réalisée. La 5-ALAD est une enzyme oligomérique synthétisant à partir de 5-ALA le porphobilinogène, monopyrrole précurseur des hemes. La banque obtenue après transformation de la souche SHSP3 présente des colonies de phénotypes différents. Certaines sont caractérisées par une croissance rapide. Nous avons sélectionné parmi ces colonies, 2 clones présentant une activité 5-ALAD, acco
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3

Chretien, Stany. "Étude du gène de la Porphobilinogène Désaminase humaine : mise en évidence pour un même gène de deux promoteurs : l'un érythroïde spécifique, l'autre ubiquitaire." Paris 12, 1987. http://www.theses.fr/1987PA120043.

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Raich, Natacha. "Clonage des ADNc et expression des gènes humains codant deux enzymes de la voie de biosynthèse de l'hème : la porphobilinogène désaminase et l'uroporphyrinogène décarboxylase." Paris 11, 1987. http://www.theses.fr/1987PA112456.

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Abstract (sommario):
Les enzymes de la voie de biosynthèse de l'hème sont présentes dans toutes les cellules et leur activité augmente au cours de la différenciation érythrocytaire. Cette dualité d'expression n’a pas de base moléculaire. Ce mémoire traite d'une part du clonage et de la structure de deux ADNc codant deux enzymes de ce métabolique : la porphobilinogène désaminase (PBG-D° ET l'uroporphyrinogène décarboxylase (URO-D), et d'autre part de l'expression de ces deux gènes. Deux banques humaines ADNc ont été construites et criblées avec les sondes murines correspondant à ces deux enzymes. Nous avons ainsi i
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5

Goodwin, C. "Mechanistic studies of porphobilinogen synthase." Thesis, University of Cambridge, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.599517.

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Abstract (sommario):
Porphobilinogen Synthase (PBGS) is a key enzyme involved in tetrapyrrole biosynthesis. The enzyme catalyses the condensation of two molecules of 5-aminolevulinic acid (1) (ALA) to give the pyrrole porphobilinogen (2) (PBG) and is believed to exist in all organisms. This thesis describes mechanistic studies carried out on PBGS from bovine liver and <i>Bacillus subtilis</i>. Stereospecifically deuteriated ALA, (<i>S</i>)-[3-D<sub>1</sub>]ALA 3<i>S</i>, and (<i>R</i>)-[3-D<sub>1</sub>]ALA 3<i>R</i>, were synthesised in 13 steps from (<i>S</i>)- and (<i>R</i>)-glutamic acid respectively. The kinet
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Picken, Nichola Caryl. "Structural studies of porphobilinogen deaminase." Thesis, Birkbeck (University of London), 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.314290.

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George, Sharon Deena. "Mechanistic studies in porphobilinogen biosynthesis." Thesis, University of St Andrews, 1993. http://hdl.handle.net/10023/15431.

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Abstract (sommario):
[4-15c]ALA.HC1 (50% enriched) and [15N]ALA.HC1 (50% enriched) have been synthesised and utilised in mechanistic studies. The synthesis of the former was achieved via a modified literature procedure, employing [2-13C] glycine (99.8% enriched) as the starting material. The NMR spectral data of the labelled materials have been fully characterised. 13C NMR studies of [4-13C]ALA.HCl (50% enriched) have demonstrated the forms of ALA and its autocondensation products under physiological conditions, 17O and 1H NMR studies have confirmed the existence of the alternative forms of ALA and its condensatio
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Mosley, Julie Elizabeth. "Studies on recombinant ubiquitous and erythroid human porphobilinogen deaminase and mutational analysis of E. Coli porphobilinogen deaminase." Thesis, University of Southampton, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.273856.

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Ahmed, R. A. A. "Rational design of inhibitors of porphobilinogen deaminase." Thesis, University of Cambridge, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.595387.

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The thesis describes the synthesis of new analogues (53-57) of PBG and their inhibition of and mechanistic studies on the enzyme PBG deaminase from <i>E. coli</i>. The analogues with an additional alkyl group, 53 and 54, were successfully obtained in good yields in 10 steps. The caged compound 97 was also obtained but the final step of hydrogenolysis of the benzyl protecting groups also caused reduction of the nitro group on the 2-nitrobenzyl substituent. Testing of analogues 53 and 54 with the enzyme (PBGD), however, showed no inhibition. A new route for the synthesis of the conformationally
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Warren, M. J. "Investigations into the mechanisms of porphobilinogen deaminase." Thesis, University of Southampton, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.233456.

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Libri sul tema "Porphobilinogène"

1

Deegan, Patrick. Porphyria. Edited by Patrick Davey and David Sprigings. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780199568741.003.0179.

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Abstract (sommario):
This chapter discusses six diseases caused by inborn errors of metabolism affecting the biosynthesis of haem. Haem is a tetracyclic metal-binding compound involved in oxygen transport (in haemoglobin and myoglobin) and redox reactions (e.g. in the cytochrome P450 system). Each of these conditions is caused by a single gene defect in one of the enzymes involved in the biosynthesis of haem. Inheritance is usually autosomal dominant with incomplete penetrance. The enzyme defect results in disease, not as a result of deficiency of the reaction product, but as a result of accumulation of precursors
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Capitoli di libri sul tema "Porphobilinogène"

1

Arndt, T., and T. Stauch. "Porphobilinogen." In Lexikon der Medizinischen Laboratoriumsdiagnostik. Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-49054-9_2483-1.

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Arndt, T., and T. Stauch. "Porphobilinogen." In Springer Reference Medizin. Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_2483.

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Schomburg, Dietmar, and Margit Salzmann. "Porphobilinogen synthase." In Enzyme Handbook 1. Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-86605-0_149.

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Schomburg, Dietmar, and Margit Salzmann. "Porphobilinogen deaminase." In Enzyme Handbook 1. Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-86605-0_228.

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5

Braun-Falco, Markus, Henry J. Mankin, Sharon L. Wenger, et al. "Porphobilinogen Deaminase Deficiency." In Encyclopedia of Molecular Mechanisms of Disease. Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-29676-8_8133.

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6

Falk, J. E. "Haem and Porphyrin Formation from Porphobilinogen Glycine, δ-Aminolaevulic Acid and Porphobilinogen." In Novartis Foundation Symposia. John Wiley & Sons, Ltd., 2008. http://dx.doi.org/10.1002/9780470718940.ch5.

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Lambert, R., P. D. Brownlie, S. C. Woodcock, et al. "Structural Studies on Porphobilinogen Deaminase." In Ciba Foundation Symposium 180 - The Biosynthesis of the Tetrapyrrole Pigments. John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514535.ch6.

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Formijne, P., and Nine J. Poulie. "Precursors of Porphyrin and Porphobilinogen." In Novartis Foundation Symposia. John Wiley & Sons, Ltd., 2008. http://dx.doi.org/10.1002/9780470718940.ch17.

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Schultz, Matthew J., Patricia L. Hall, and Silvia Tortorelli. "Porphyrins, Porphobilinogen, and δ-Aminolevulinic Acid." In Laboratory Guide to the Methods in Biochemical Genetics. Springer International Publishing, 2024. http://dx.doi.org/10.1007/978-3-031-58819-8_16.

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Gajdos, Alfred, and Marianne Gajdos-Torok. "Metabolism of Porphobilinogen and of Porphyrins in the Rabbit." In Novartis Foundation Symposia. John Wiley & Sons, Ltd., 2008. http://dx.doi.org/10.1002/9780470718940.ch16.

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Atti di convegni sul tema "Porphobilinogène"

1

Neier, Reinhard. "A Novel Synthesis of Porphobilinogen: Synthetic and Biosynthetic Studies." In The 3rd International Electronic Conference on Synthetic Organic Chemistry. MDPI, 1999. http://dx.doi.org/10.3390/ecsoc-3-01765.

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Moghe, Akshata, Csilla K. Hallberg, Ruksana Huda, et al. "04156 Recurrent acute intermittent porphyria attacks after normalization of porphobilinogen on givosiran prophylaxis." In Abstracts of the International Conference of Porphyrins and Porphyrias, Pamplona, Spain, 21–25 September 2024. BMJ Publishing Group Ltd, 2024. http://dx.doi.org/10.1136/bmjgast-2024-icpp.41.

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Heckl, C., A. Lang, M. Vogeser, et al. "Rapid spectrophotometric quantification of urinary porphyrins and porphobilinogen as screening tool for attacks of acute porphyria." In Translation of Lasers and Biophotonics Technologies and Procedures: Toward the Clinic, edited by Lothar D. Lilge and Carsten M. Philipp. SPIE, 2019. http://dx.doi.org/10.1117/12.2527105.

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Neels, Antonia, Helen Stoeckli-Evans, Reinhard Neier, Pavel Bobál, and André Chaperon. "A Chemical Synthesis of Porphobilinogen Imitating the Pathway Proposed by Shemin for the Biosynthesis: Comparing Inhibition Studies with Investigations of Chemical Reactivity." In The 2nd International Electronic Conference on Synthetic Organic Chemistry. MDPI, 1998. http://dx.doi.org/10.3390/ecsoc-2-01693.

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