To install click the Add extension button. That's it.
The source code for the WIKI 2 extension is being checked by specialists of the Mozilla Foundation, Google, and Apple. You could also do it yourself at any point in time.
How to transfigure the Wikipedia
Would you like Wikipedia to always look as professional and up-to-date? We have created a browser extension. It will enhance any encyclopedic page you visit with the magic of the WIKI 2 technology.
Try it — you can delete it anytime.
Install in 5 seconds
Yep, but later
4,5
Kelly Slayton
Congratulations on this excellent venture… what a great idea!
Alexander Grigorievskiy
I use WIKI 2 every day and almost forgot how the original Wikipedia looks like.
QDPR (quinoid dihydropteridine reductase) is a humangene that produces the enzyme quinoid dihydropteridine reductase. This enzyme is part of the pathway that recycles a substance called tetrahydrobiopterin, also known as BH4. Tetrahydrobiopterin works with an enzyme called phenylalanine hydroxylase to process a substance called phenylalanine. Phenylalanine is an amino acid (a building block of proteins) that is obtained through the diet; it is found in all proteins and in some artificial sweeteners. When tetrahydrobiopterin interacts with phenylalanine hydroxylase, tetrahydrobiopterin is altered and must be recycled to a usable form. The regeneration of this substance is critical for the proper processing of several other amino acids in the body. Tetrahydrobiopterin also helps produce certain chemicals in the brain called neurotransmitters, which transmit signals between nerve cells.
The QDPR gene is located on the short (p) arm of chromosome 4 at position 15.31, from base pair 17,164,291 to base pair 17,189,981.
In melanocytic cells QDPR gene expression may be regulated by MITF.[5]
Related conditions
Mutations in the QDPR gene cause dihydropteridine reductase deficiency, one of the subtypes of tetrahydrobiopterin deficiency. More than 30 disorder-causing mutations in this gene have been identified, including aberrant splicing, amino acid substitutions, insertions, or premature terminations. These mutations completely, or almost completely, inactivate quinoid dihydropteridine reductase, which prevents the normal recycling of tetrahydrobiopterin. In the absence of usable tetrahydrobiopterin, the body cannot process phenylalanine correctly. As a result, phenylalanine from the diet builds up in the bloodstream and other tissues and can lead to brain damage. Neurotransmitters in the brain are also affected, resulting in delayed development, seizures, movement disorders, and other symptoms.
In addition, a reduction in the activity of quinoid dihydropteridine reductase may cause calcium to build up abnormally in certain parts of the brain, resulting in damage to nerve cells.
Romstad A, Kalkanoglu HS, Coskun T, Demirkol M, Tokatli A, Dursun A, Baykal T, Ozalp I, Guldberg P, Guttler F (2000). "Molecular analysis of 16 Turkish families with DHPR deficiency using denaturing gradient gel electrophoresis (DGGE)". Hum Genet. 107 (6): 546–53. doi:10.1007/s004390000407. PMID11153907. S2CID22889048.
Shintaku H (2002). "Disorders of tetrahydrobiopterin metabolism and their treatment". Curr Drug Metab. 3 (2): 123–31. doi:10.2174/1389200024605145. PMID12003346.
Kaufman S, Holtzman NA, Milstien S, et al. (1975). "Phenylketonuria due to a deficiency of dihydropteridine reductase". N. Engl. J. Med. 293 (16): 785–90. doi:10.1056/NEJM197510162931601. PMID1160969.
Altmann P, Al-Salihi F, Butter K, et al. (1987). "Serum aluminum levels and erythrocyte dihydropteridine reductase activity in patients on hemodialysis". N. Engl. J. Med. 317 (2): 80–4. doi:10.1056/NEJM198707093170204. PMID3587329.
Brown RM, Dahl HH (1987). "Localization of the human dihydropteridine reductase gene to band p15.3 of chromosome 4 by in situ hybridization". Genomics. 1 (1): 67–70. doi:10.1016/0888-7543(87)90106-6. PMID3666748.
Nakanishi N, Hasegawa H, Yamada S, Akino M (1986). "Purification and physicochemical properties of NADPH-specific dihydropteridine reductase from bovine and human livers". J. Biochem. 99 (3): 635–44. doi:10.1093/oxfordjournals.jbchem.a135522. PMID3711039.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID8125298.
Su Y, Varughese KI, Xuong NH, et al. (1994). "The crystallographic structure of a human dihydropteridine reductase NADH binary complex expressed in Escherichia coli by a cDNA constructed from its rat homologue". J. Biol. Chem. 268 (36): 26836–41. doi:10.2210/pdb1hdr/pdb. PMID8262916.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID9373149.
Lin CM, Tan Y, Lee YM, et al. (1998). "Expression of human phenylalanine hydroxylase activity in T lymphocytes of classical phenylketonuria children by retroviral-mediated gene transfer". J. Inherit. Metab. Dis. 20 (6): 742–54. doi:10.1023/A:1005303331218. PMID9427141. S2CID22653168.
1dhr: CRYSTAL STRUCTURE OF RAT LIVER DIHYDROPTERIDINE REDUCTASE
1dir: CRYSTAL STRUCTURE OF A MONOCLINIC FORM OF DIHYDROPTERIDINE REDUCTASE FROM RAT LIVER
1hdr: THE CRYSTALLOGRAPHIC STRUCTURE OF A HUMAN DIHYDROPTERIDINE REDUCTASE NADH BINARY COMPLEX EXPRESSED IN ESCHERICHIA COLI BY A CDNA CONSTRUCTED FROM ITS RAT HOMOLOGUE
This page was last edited on 15 August 2023, at 02:22