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Asparagine

Asparagine, is an α-amino acid, used in the biosynthesis of proteins. It contains an α-amino group, an α-carboxylic acid group, a side chain carboxamide, classifying it as a polar, aliphatic amino acid, it is non-essential in humans. It is encoded by the codons AAU and AAC. A reaction between asparagine and reducing sugars or other source of carbonyls produces acrylamide in food when heated to sufficient temperature; these products occur in baked goods such as French fries, potato chips, toasted bread. Asparagine was first isolated in 1806 in a crystalline form by French chemists Louis Nicolas Vauquelin and Pierre Jean Robiquet from asparagus juice, in which it is abundant, hence the chosen name, it was the first amino acid to be isolated. Three years in 1809, Pierre Jean Robiquet identified a substance from liquorice root with properties which he qualified as similar to those of asparagine, which Plisson identified in 1828 as asparagine itself; the determination of asparagine's structure required decades of research.

The empirical formula for asparagine was first determined in 1833 by the French chemists Antoine François Boutron Charlard and Théophile-Jules Pelouze. In 1846 the Italian chemist Raffaele Piria treated asparagine with nitrous acid, which removed the molecule's amine groups and transformed asparagine into malic acid; this revealed the molecule's fundamental structure: a chain of four carbon atoms. Piria thought. In 1886, the Italian chemist Arnaldo Piutti discovered a mirror image or "enantiomer" of the natural form of asparagine, which shared many of asparagine's properties, but which differed from it. Since the structure of asparagine was still not known – the location of the amine group within the molecule was still not settled – Piutti synthesized asparagine and thus determined its true structure. Since the asparagine side-chain can form hydrogen bond interactions with the peptide backbone, asparagine residues are found near the beginning of alpha-helices as asx turns and asx motifs, in similar turn motifs, or as amide rings, in beta sheets.

Its role can be thought as "capping" the hydrogen bond interactions that would otherwise be satisfied by the polypeptide backbone. Asparagine provides key sites for N-linked glycosylation, modification of the protein chain with the addition of carbohydrate chains. A carbohydrate tree can be added to an asparagine residue if the latter is flanked on the C side by X-serine or X-threonine, where X is any amino acid with the exception of proline. Asparagine can be hydroxylated in the HIF1 hypoxia inducible transcription factor; this modification inhibits HIF1-mediated gene activation. Asparagine is not essential for humans, which means that it can be synthesized from central metabolic pathway intermediates and is not required in the diet. Asparagine is found in: Animal sources: dairy, beef, eggs, lactalbumin, seafood Plant sources: asparagus, legumes, seeds, whole grains The precursor to asparagine is oxaloacetate. Oxaloacetate is converted to aspartate using a transaminase enzyme; the enzyme transfers the amino group from glutamate to oxaloacetate producing α-ketoglutarate and aspartate.

The enzyme asparagine synthetase produces asparagine, AMP, pyrophosphate from aspartate, ATP. In the asparagine synthetase reaction, ATP is used to activate aspartate, forming β-aspartyl-AMP. Glutamine donates an ammonium group, which reacts with β-aspartyl-AMP to form asparagine and free AMP. Asparagine enters the citric acid cycle in humans as oxaloacetate. In bacteria, the degradation of asparagine leads to the production of oxaloacetate, the molecule which combines with citrate in the citric acid cycle. Asparagine is hydrolyzed to aspartate by asparaginase. Aspartate undergoes transamination to form glutamate and oxaloacetate from alpha-ketoglutarate. Asparagine is required for function of the brain, it plays an important role in the synthesis of ammonia. The addition of N-acetylglucosamine to asparagine is performed by oligosaccharyltransferase enzymes in the endoplasmic reticulum; this glycosylation is important both for protein function. According to a 2018 article in The Guardian, a study found that decreasing levels of asparagine "dramatically" reduced the spread of breast cancer in laboratory mice.

The article noted. GMD MS Spectrum Why Asparagus Makes Your Pee Stink

Nicholas J. Wade

Nicholas J. Wade is a British psychologist and academic, he is an emeritus professor in the psychology department of the University of Dundee in Scotland, the author of books and technical articles. His work has focused on visual perception. Wade, N. Circles: Science and Symbol. Dundee: Dundee University Press. ISBN 978-1-84586-019-6. Details Piccolino, M. and Wade, N. J. Insegne Ambiguë. Percorsi Obliqui tra Storia, Scienza e Arte, da Galileo a Magritte. Pisa: Edizioni ETS. ISBN 978-88-467-1736-8. Details Wade, N. J. and Tatler, B. W; the Moving Tablet of the Eye: The Origins of Modern Eye Movement Research. Oxford: Oxford University Press. ISBN 0-19-856616-6, 0198566174 Details Wade, N. J. Perception and Illusion. Historical Perspectives. New York: Springer. Details Wade, N. J. Müller’s Elements of Physiology. 4 vols. Bristol: Thoemmes. Details Wade, N. J. Destined for Distinguished Oblivion: The Scientific Vision of William Charles Wells. New York: Kluwer/Plenum. Wade, N. J. Thomas Young's Lectures on Natural Philosophy and the Mechanical Arts.

Bristol: Thoemmes. Wade, N. J. and Swanston, M. Visual Perception: An Introduction. 2nd edition. London: Psychology Press. Wade, N. J. and Brozek, J. Purkinje's Vision; the Dawning of Neuroscience. Mahwah, NJ: Lawrence Erlbaum Associates. Wade, N. J; the Emergence of Neuroscience in the Nineteenth Century. 8 vols. London: Routledge/Thoemmes Press. Wade, N. J. Helmholtz's Treatise on Physiological Optics. 3 vols. Bristol: Thoemmes Press. Wade, N. J. A Natural History of Vision. Cambridge, MA: MIT Press. Wade, N. Psychologists in Word and Image. Cambridge, MA: MIT Press. Wade, N. J. and Swanston, M. Visual Perception: An Introduction. London: Routledge. Wade, N. Visual Allusions: Pictures of Perception. London: Lawrence Erlbaum. Wade, N. J. Brewster and Wheatstone on Vision. London: Academic Press. Wade, N; the Art and Science of Visual Illusions. London: Routledge & Kegan Paul

Convoy Busters

Convoy Busters is a 1978 poliziotteschi film directed by Stelvio Massi and starring Maurizio Merli. Maurizio Merli: Inspector Francesco Olmi Olga Karlatos: Anna Massimo Serato: Degan Sr. Mario Feliciani: Quaestor Mimmo Palmara: Corchi Marco Gelardini: Degan Jr. Attilio Duse: Brigadier Ballarin Nello Pazzafini:criminal Convoy Busters was filmed on location in Rome and Civitanova Marche. Convoy Busters was distributed theatrically in Italy by P. A. C. - Produzioni Atlas Consorziate on 23 December 1978. It grossed a total of 989,390,960 Italian lira on its domestic release. Italian film historian and critic Roberto Curti stated that this gross was no par with Maurizio Merli's previous films noting that his star power was beginning to fade at this point; the film released by NoShame on DVD in the United States. Curti stated that the film was "unusually well-received by critics", including Vittorio Spiga who praised the film as Massi's best work, referring to Massi as managing "to renew the genre somehow: by borrowing the style of the Italian Western, its violence and characters, while taking the spectacular angle and the fast pacing from American cinema."

Tom Milne of the Monthly Film Bulletin stated that "Although Stelvio Massi places numbing reliance on the zoom lens, it is competently enough done, with a sound performance by Maurizio Merli in the Eastwood role." Milne commented on the dubbing, declaring it "horribly dubbed and stultifyingly tedious."In a retrospective review, Curti declared the film to be "perhaps Stelvio Massi's best effort, one of the better late Italian poliziotteschi" Convoy Busters on IMDb