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Volumn 416, Issue 1-2, 2008, Pages 85-91

Molecular cloning and structural organization of the gene encoding the mouse lysosomal di-N-acetylchitobiase (ctbs)

Author keywords

Chitobiase; Glycosidase; Lysosome; Promoter

Indexed keywords

N ACETYL BETA GLUCOSAMINIDASE; N ACETYLGLUCOSAMINE; OLIGOSACCHARIDE;

EID: 43049157942     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2008.03.009     Document Type: Article
Times cited : (5)

References (25)
  • 1
    • 0024850749 scopus 로고
    • Lysosomal degradation of Asn-linked glycoproteins
    • Aronson Jr. N.N., and Kuranda M. Lysosomal degradation of Asn-linked glycoproteins. FASEB J. 3 (1989) 2615-2622
    • (1989) FASEB J. , vol.3 , pp. 2615-2622
    • Aronson Jr., N.N.1    Kuranda, M.2
  • 2
    • 0024386785 scopus 로고
    • Rat liver chitobiase: purification, properties, and role in the lysosomal degradation of Asn-linked glycoproteins
    • Aronson N.N., Backes M., and Kuranda M.J. Rat liver chitobiase: purification, properties, and role in the lysosomal degradation of Asn-linked glycoproteins. Arch. Biochem. Biophys. 272 (1989) 290-300
    • (1989) Arch. Biochem. Biophys. , vol.272 , pp. 290-300
    • Aronson, N.N.1    Backes, M.2    Kuranda, M.J.3
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principles of protein dye-ligand
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principles of protein dye-ligand. Anal. Biochem. 12 (1976) 248-254
    • (1976) Anal. Biochem. , vol.12 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0028172714 scopus 로고
    • Mammalian alpha-mannosidases-multiple forms but a common purpose
    • Daniel P.F., Winchetser B., and Warren C.D. Mammalian alpha-mannosidases-multiple forms but a common purpose. Glycobiology 4 (1994) 551-566
    • (1994) Glycobiology , vol.4 , pp. 551-566
    • Daniel, P.F.1    Winchetser, B.2    Warren, C.D.3
  • 7
    • 0026703209 scopus 로고
    • Cloning and expression of the cDNA sequence encoding the lysosomal glycosidase Di-N-acetylchitobiase
    • Fisher K.J., and Aronson Jr. N.N. Cloning and expression of the cDNA sequence encoding the lysosomal glycosidase Di-N-acetylchitobiase. J. Biol. Chem. 267 (1992) 19607-19616
    • (1992) J. Biol. Chem. , vol.267 , pp. 19607-19616
    • Fisher, K.J.1    Aronson Jr., N.N.2
  • 8
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases
    • Henrissat B., and Bairoch A. Updating the sequence-based classification of glycosyl hydrolases. Biochem. J. 316 (1996) 695-696
    • (1996) Biochem. J. , vol.316 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 9
    • 0024546509 scopus 로고
    • The scanning model for translation: an update
    • Kozak M. The scanning model for translation: an update. J. Cell Biol. 108 (1989) 229-241
    • (1989) J. Cell Biol. , vol.108 , pp. 229-241
    • Kozak, M.1
  • 10
    • 0024448304 scopus 로고
    • MyoD is a sequence-specific DNA binding protein requiring a region of myc homology to bind to the muscle creatine kinase enhancer
    • Lassar A.B., et al. MyoD is a sequence-specific DNA binding protein requiring a region of myc homology to bind to the muscle creatine kinase enhancer. Cell 58 (1989) 823-831
    • (1989) Cell , vol.58 , pp. 823-831
    • Lassar, A.B.1
  • 11
    • 0033046225 scopus 로고    scopus 로고
    • Structure of the human gene for lysosomal di-N-acetylchitobiase
    • Liu B., Ahmad W., and Aronson Jr. N.N. Structure of the human gene for lysosomal di-N-acetylchitobiase. Glycobiology 9 (1999) 589-593
    • (1999) Glycobiology , vol.9 , pp. 589-593
    • Liu, B.1    Ahmad, W.2    Aronson Jr., N.N.3
  • 12
    • 0030032332 scopus 로고    scopus 로고
    • Chitinases, chitosanases, and lysozymes can be divided into prokaryotic and eukaryotic families sharing a conserved core
    • Monzingo A.F., Marcotte E.M., Hart P.J., and Robertus J.D. Chitinases, chitosanases, and lysozymes can be divided into prokaryotic and eukaryotic families sharing a conserved core. Nat. Struct. Biol. 3 2 (1996) 133-140
    • (1996) Nat. Struct. Biol. , vol.3 , Issue.2 , pp. 133-140
    • Monzingo, A.F.1    Marcotte, E.M.2    Hart, P.J.3    Robertus, J.D.4
  • 13
    • 0025602652 scopus 로고
    • Negative regulation of the rat stromelysin gene promoter by retinoic acid is mediated by an API binding site
    • Nicholson R.C., Mader S., Nagpal S., Leid M., Rochette E.C., and Chambon P. Negative regulation of the rat stromelysin gene promoter by retinoic acid is mediated by an API binding site. EMBO J. 9 (1990) 4443-4454
    • (1990) EMBO J. , vol.9 , pp. 4443-4454
    • Nicholson, R.C.1    Mader, S.2    Nagpal, S.3    Leid, M.4    Rochette, E.C.5    Chambon, P.6
  • 14
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H., Engelbrecht J., Brunak S., and von Heijne G. Identification of prokaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10 (1997) 1-6
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 16
    • 27744518375 scopus 로고    scopus 로고
    • Characterization of a human core-specific lysosomal α1-6mannosidase involved in N-glycan catabolism
    • Park C., et al. Characterization of a human core-specific lysosomal α1-6mannosidase involved in N-glycan catabolism. J. Biol. Chem. 280 (2005) 37204-37216
    • (2005) J. Biol. Chem. , vol.280 , pp. 37204-37216
    • Park, C.1
  • 17
    • 0242317675 scopus 로고    scopus 로고
    • Experimental validation of novel and conventional approaches to quantitative real-time PCR data analysis
    • Peirson S.N., Butler J.N., and Foster R.G. Experimental validation of novel and conventional approaches to quantitative real-time PCR data analysis. Nucleic Acids Res. 31 14 (2003) e73
    • (2003) Nucleic Acids Res. , vol.31 , Issue.14
    • Peirson, S.N.1    Butler, J.N.2    Foster, R.G.3
  • 18
    • 0028971143 scopus 로고
    • MatInd and MatInspector - new fast and versatile tools for detection of consensus matches in nucleotide sequence data
    • Quandt K., Frech K., Karas H., Wingender E., and Werner T. MatInd and MatInspector - new fast and versatile tools for detection of consensus matches in nucleotide sequence data. Nucleic Acids Res. 23 (1995) 4878-4884
    • (1995) Nucleic Acids Res. , vol.23 , pp. 4878-4884
    • Quandt, K.1    Frech, K.2    Karas, H.3    Wingender, E.4    Werner, T.5
  • 19
    • 0037435395 scopus 로고    scopus 로고
    • Assumption-free analysis of quantitative real-time polymerase chain reaction (PCR) data
    • Ramakers C., Ruijter J.M., Lekanne Deprez R.H., and Moorman A.F.M. Assumption-free analysis of quantitative real-time polymerase chain reaction (PCR) data. Neurosci. Lett. 339 (2003) 62-66
    • (2003) Neurosci. Lett. , vol.339 , pp. 62-66
    • Ramakers, C.1    Ruijter, J.M.2    Lekanne Deprez, R.H.3    Moorman, A.F.M.4
  • 20
    • 0029257376 scopus 로고
    • The MyoD family of transcription factors and skeletal myogenesis
    • Rudnicki M.A., and Jaenisch R. The MyoD family of transcription factors and skeletal myogenesis. BioEssays 17 (1995) 203-209
    • (1995) BioEssays , vol.17 , pp. 203-209
    • Rudnicki, M.A.1    Jaenisch, R.2
  • 21
    • 33750475626 scopus 로고    scopus 로고
    • Quantitative real-time RT-PCR data analysis: current concepts and the novel "gene expression's CT difference" formula
    • Schefe J.H., Lehmann K.E., Buschmann I.R., Unger T., and Funke-Kaiser H. Quantitative real-time RT-PCR data analysis: current concepts and the novel "gene expression's CT difference" formula. J. Mol. Med. 84 11 (2006) 901-910
    • (2006) J. Mol. Med. , vol.84 , Issue.11 , pp. 901-910
    • Schefe, J.H.1    Lehmann, K.E.2    Buschmann, I.R.3    Unger, T.4    Funke-Kaiser, H.5
  • 22
    • 0015952498 scopus 로고
    • Human N-acetyl-beta-hexosaminidase: hydrolysis of N,N′ diacetylchitobiose by a low molecular weight enzyme
    • Stirling J.L. Human N-acetyl-beta-hexosaminidase: hydrolysis of N,N′ diacetylchitobiose by a low molecular weight enzyme. FEBS Lett. 39 (1974) 171-175
    • (1974) FEBS Lett. , vol.39 , pp. 171-175
    • Stirling, J.L.1
  • 23
    • 43049153511 scopus 로고    scopus 로고
    • Thomas, G.H., 2001. Disorders of glycoprotein degradation: alpha-mannosidosis, beta-mannosidosis, fucosidosis, and sialidosis. In The Metabolic and Molecular Basis of Inherited Disease, 8edn (Scriver CR, Beaudet AL, Valle D, Sly WS, eds; Childs B, Kinzler KW, Vogelstein B, assoc eds), pp 2529-2561. McGraw-Hill, NY.
    • Thomas, G.H., 2001. Disorders of glycoprotein degradation: alpha-mannosidosis, beta-mannosidosis, fucosidosis, and sialidosis. In The Metabolic and Molecular Basis of Inherited Disease, 8edn (Scriver CR, Beaudet AL, Valle D, Sly WS, eds; Childs B, Kinzler KW, Vogelstein B, assoc eds), pp 2529-2561. McGraw-Hill, NY.
  • 24
    • 0031888202 scopus 로고    scopus 로고
    • Tissue-specific in vivo transcription start site of the human and murine cystic fibrosis genes
    • White N.L., Higgins C.F., and Trezise A.E.O. Tissue-specific in vivo transcription start site of the human and murine cystic fibrosis genes. Hum. Mol. Genet. 7 (1998) 363-369
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 363-369
    • White, N.L.1    Higgins, C.F.2    Trezise, A.E.O.3
  • 25
    • 0033976586 scopus 로고    scopus 로고
    • TRANSFAC: an integrated system for gene expression regulation
    • Wingender E., et al. TRANSFAC: an integrated system for gene expression regulation. Nucleic Acids Res. 28 (2000) 316-319
    • (2000) Nucleic Acids Res. , vol.28 , pp. 316-319
    • Wingender, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.