- GANC
Glucosidase, alpha; neutral C, also known as GANC, is a human
gene .cite web | title = Entrez Gene: GANC glucosidase, alpha; neutral C| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2595| accessdate = ]PBB_Summary
section_title =
summary_text = Glycosyl 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.cite web | title = Entrez Gene: GANC glucosidase, alpha; neutral C| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2595| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Feizi T, Larkin M |title=AIDS and glycosylation. |journal=Glycobiology |volume=1 |issue= 1 |pages= 17–23 |year= 1992 |pmid= 2136376 |doi=
*cite journal | author=Land A, Braakman I |title=Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum. |journal=Biochimie |volume=83 |issue= 8 |pages= 783–90 |year= 2001 |pmid= 11530211 |doi=
*cite journal | author=Kamimura H, Ogata H, Takahara H |title=Alpha-glucoside formation of xenobiotics by rat liver alpha-glucosidases. |journal=Drug Metab. Dispos. |volume=20 |issue= 2 |pages= 309–15 |year= 1992 |pmid= 1352226 |doi=
*cite journal | author=Fenouillet E, Gluckman JC |title=Effect of a glucosidase inhibitor on the bioactivity and immunoreactivity of human immunodeficiency virus type 1 envelope glycoprotein. |journal=J. Gen. Virol. |volume=72 ( Pt 8) |issue= |pages= 1919–26 |year= 1991 |pmid= 1678778 |doi=
*cite journal | author=Ratner L, vander Heyden N, Dedera D |title=Inhibition of HIV and SIV infectivity by blockade of alpha-glucosidase activity. |journal=Virology |volume=181 |issue= 1 |pages= 180–92 |year= 1991 |pmid= 1704656 |doi=
*cite journal | author=Dedera DA, Gu RL, Ratner L |title=Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 transmembrane envelope function. |journal=Virology |volume=187 |issue= 1 |pages= 377–82 |year= 1992 |pmid= 1736542 |doi=
*cite journal | author=Murphy CI, Lennick M, Lehar SM, "et al." |title=Temporal expression of HIV-1 envelope proteins in baculovirus-infected insect cells: implications for glycosylation and CD4 binding. |journal=Genet. Anal. Tech. Appl. |volume=7 |issue= 6 |pages= 160–71 |year= 1991 |pmid= 2076345 |doi=
*cite journal | author=Kalyanaraman VS, Rodriguez V, Veronese F, "et al." |title=Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1. |journal=AIDS Res. Hum. Retroviruses |volume=6 |issue= 3 |pages= 371–80 |year= 1990 |pmid= 2187500 |doi=
*cite journal | author=Shimizu H, Tsuchie H, Honma H, "et al." |title=Effect of N-(3-phenyl-2-propenyl)-1-deoxynojirimycin on the lectin binding to HIV-1 glycoproteins. |journal=Jpn. J. Med. Sci. Biol. |volume=43 |issue= 3 |pages= 75–87 |year= 1991 |pmid= 2283726 |doi=
*cite journal | author=Leonard CK, Spellman MW, Riddle L, "et al." |title=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. |journal=J. Biol. Chem. |volume=265 |issue= 18 |pages= 10373–82 |year= 1990 |pmid= 2355006 |doi=
*cite journal | author=Pal R, Hoke GM, Sarngadharan MG |title=Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 9 |pages= 3384–8 |year= 1989 |pmid= 2541446 |doi=
*cite journal | author=Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP |title=Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport. |journal=J. Virol. |volume=63 |issue= 6 |pages= 2452–6 |year= 1989 |pmid= 2542563 |doi=
*cite journal | author=Kozarsky K, Penman M, Basiripour L, "et al." |title=Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein. |journal=J. Acquir. Immune Defic. Syndr. |volume=2 |issue= 2 |pages= 163–9 |year= 1989 |pmid= 2649653 |doi=
*cite journal | author=Walker BD, Kowalski M, Goh WC, "et al." |title=Inhibition of human immunodeficiency virus syncytium formation and virus replication by castanospermine. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 22 |pages= 8120–4 |year= 1987 |pmid= 2825177 |doi=
*cite journal | author=Robinson WE, Montefiori DC, Mitchell WM |title=Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis. |journal=AIDS Res. Hum. Retroviruses |volume=3 |issue= 3 |pages= 265–82 |year= 1988 |pmid= 2829950 |doi=
*cite journal | author=Gruters RA, Neefjes JJ, Tersmette M, "et al." |title=Interference with HIV-induced syncytium formation and viral infectivity by inhibitors of trimming glucosidase. |journal=Nature |volume=330 |issue= 6143 |pages= 74–7 |year= 1987 |pmid= 2959866 |doi= 10.1038/330074a0
*cite journal | author=Blough HA, Pauwels R, De Clercq E, "et al." |title=Glycosylation inhibitors block the expression of LAV/HTLV-III (HIV) glycoproteins. |journal=Biochem. Biophys. Res. Commun. |volume=141 |issue= 1 |pages= 33–8 |year= 1987 |pmid= 3099781 |doi=
*cite journal | author=Usuki F, Ishiura S, Nonaka I, Sugita H |title=alpha-Glucosidase isoenzymes in normal and acid maltase-deficient human skeletal muscles. |journal=Muscle Nerve |volume=11 |issue= 4 |pages= 365–71 |year= 1988 |pmid= 3135493 |doi= 10.1002/mus.880110413
*cite journal | author=Montefiori DC, Robinson WE, Mitchell WM |title=Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 23 |pages= 9248–52 |year= 1988 |pmid= 3264072 |doi=PBB_Controls
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