Biology:GANC
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Neutral alpha-glucosidase C is an enzyme that in humans is encoded by the GANC gene.[1][2][3]
Function
Glycoside hydrolase enzymes hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. This gene encodes a member of glycosyl hydrolases family 31. This enzyme hydrolyses terminal, non-reducing 1,4-linked alpha-D-glucose residues and releases alpha-D-glucose. This is a key enzyme in glycogen metabolism and its gene localizes to a chromosomal region (15q15) that is associated with susceptibility to diabetes.[3]
References
- ↑ "Assignment of the gene for human neutral alpha-glucosidase C to chromosome 15". Cytogenetics and Cell Genetics 27 (2–3): 168–75. Oct 1980. doi:10.1159/000131478. PMID 6995030. http://www.escholarship.org/uc/item/6jr7980p.
- ↑ "Computer assisted cloning of human neutral alpha-glucosidase C (GANC): a new paralog in the glycosyl hydrolase gene family 31". Proceedings of the National Academy of Sciences of the United States of America 99 (21): 13642–6. Oct 2002. doi:10.1073/pnas.202383599. PMID 12370436. Bibcode: 2002PNAS...9913642H.
- ↑ 3.0 3.1 "Entrez Gene: GANC glucosidase, alpha; neutral C". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2595.
Further reading
- "AIDS and glycosylation". Glycobiology 1 (1): 17–23. Sep 1990. doi:10.1093/glycob/1.1.17. PMID 2136376.
- "Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum". Biochimie 83 (8): 783–90. Aug 2001. doi:10.1016/S0300-9084(01)01314-1. PMID 11530211.
- "Alpha-glucoside formation of xenobiotics by rat liver alpha-glucosidases". Drug Metabolism and Disposition 20 (2): 309–15. 1992. PMID 1352226.
- "Effect of a glucosidase inhibitor on the bioactivity and immunoreactivity of human immunodeficiency virus type 1 envelope glycoprotein". The Journal of General Virology 72 (8): 1919–26. Aug 1991. doi:10.1099/0022-1317-72-8-1919. PMID 1678778.
- "Inhibition of HIV and SIV infectivity by blockade of alpha-glucosidase activity". Virology 181 (1): 180–92. Mar 1991. doi:10.1016/0042-6822(91)90483-R. PMID 1704656.
- "Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 transmembrane envelope function". Virology 187 (1): 377–82. Mar 1992. doi:10.1016/0042-6822(92)90331-I. PMID 1736542.
- "Temporal expression of HIV-1 envelope proteins in baculovirus-infected insect cells: implications for glycosylation and CD4 binding". Genetic Analysis, Techniques and Applications 7 (6): 160–71. Oct 1990. doi:10.1016/0735-0651(90)90030-J. PMID 2076345.
- "Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1". AIDS Research and Human Retroviruses 6 (3): 371–80. Mar 1990. doi:10.1089/aid.1990.6.371. PMID 2187500. https://zenodo.org/record/1235229.
- "Effect of N-(3-phenyl-2-propenyl)-1-deoxynojirimycin on the lectin binding to HIV-1 glycoproteins". Japanese Journal of Medical Science & Biology 43 (3): 75–87. Jun 1990. doi:10.7883/yoken1952.43.75. PMID 2283726.
- "Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells". The Journal of Biological Chemistry 265 (18): 10373–82. Jun 1990. doi:10.1016/S0021-9258(18)86956-3. PMID 2355006.
- "Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1". Proceedings of the National Academy of Sciences of the United States of America 86 (9): 3384–8. May 1989. doi:10.1073/pnas.86.9.3384. PMID 2541446. Bibcode: 1989PNAS...86.3384P.
- "Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport". Journal of Virology 63 (6): 2452–6. Jun 1989. doi:10.1128/jvi.63.6.2452-2456.1989. PMID 2542563.
- "Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein". Journal of Acquired Immune Deficiency Syndromes 2 (2): 163–9. 1989. PMID 2649653.
- "Inhibition of human immunodeficiency virus syncytium formation and virus replication by castanospermine". Proceedings of the National Academy of Sciences of the United States of America 84 (22): 8120–4. Nov 1987. doi:10.1073/pnas.84.22.8120. PMID 2825177. Bibcode: 1987PNAS...84.8120W.
- "Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis". AIDS Research and Human Retroviruses 3 (3): 265–82. 1988. doi:10.1089/aid.1987.3.265. PMID 2829950.
- "Interference with HIV-induced syncytium formation and viral infectivity by inhibitors of trimming glucosidase". Nature 330 (6143): 74–7. 1987. doi:10.1038/330074a0. PMID 2959866. Bibcode: 1987Natur.330...74G.
- "Glycosylation inhibitors block the expression of LAV/HTLV-III (HIV) glycoproteins". Biochemical and Biophysical Research Communications 141 (1): 33–8. Nov 1986. doi:10.1016/S0006-291X(86)80330-8. PMID 3099781.
- "alpha-Glucosidase isoenzymes in normal and acid maltase-deficient human skeletal muscles". Muscle & Nerve 11 (4): 365–71. Apr 1988. doi:10.1002/mus.880110413. PMID 3135493.
- "Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1". Proceedings of the National Academy of Sciences of the United States of America 85 (23): 9248–52. Dec 1988. doi:10.1073/pnas.85.23.9248. PMID 3264072. Bibcode: 1988PNAS...85.9248M.
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