메뉴 건너뛰기




Volumn 319, Issue 1-2, 2003, Pages 177-187

Characterization of the mouse lysosomal sialidase promoter

Author keywords

Adenovirus; CDP; Footprint; MyoD; Regulation; Sialidosis; Sp 1; Tay Sachs

Indexed keywords

CCAAT DISPLACEMENT PROTEIN; CCAAT ENHANCER BINDING PROTEIN; CIS ACTING ELEMENT; DEOXYRIBONUCLEASE; MYOD PROTEIN; MYOGENIC FACTOR 5; PROTEIN; REGULATOR PROTEIN; SIALIDASE; TRANS ACTING FACTOR; TRANSCRIPTION FACTOR SP1; UNCLASSIFIED DRUG;

EID: 0242352603     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(03)00808-4     Document Type: Article
Times cited : (13)

References (37)
  • 1
    • 0028118470 scopus 로고
    • A new bipartite DNA-binding domain: Cooperative interaction between the cut repeat and homeo domain of the cut homeo proteins
    • Andres V., Chiara M.D., Mahdavi V. A new bipartite DNA-binding domain: cooperative interaction between the cut repeat and homeo domain of the cut homeo proteins. Genes Dev. 8:1994;245-257.
    • (1994) Genes Dev. , vol.8 , pp. 245-257
    • Andres, V.1    Chiara, M.D.2    Mahdavi, V.3
  • 2
    • 0027935887 scopus 로고
    • Sequence-specific DNA binding of individual cut repeats of the human CCAAT displacement/cut homeodomain protein
    • Aufiero B., Neufeld E.J., Orkin S.H. Sequence-specific DNA binding of individual cut repeats of the human CCAAT displacement/cut homeodomain protein. Proc. Natl. Acad. Sci. USA. 91:1994;7757-7761.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7757-7761
    • Aufiero, B.1    Neufeld, E.J.2    Orkin, S.H.3
  • 4
    • 0025572707 scopus 로고
    • Differences and similarities in DNA-binding preferences of MyoD and E2A protein complexes revealed by binding site selection
    • Blackwell T.K., Weintraub H. Differences and similarities in DNA-binding preferences of MyoD and E2A protein complexes revealed by binding site selection. Science. 250:1990;1104-1110.
    • (1990) Science , vol.250 , pp. 1104-1110
    • Blackwell, T.K.1    Weintraub, H.2
  • 5
    • 0034326899 scopus 로고    scopus 로고
    • Novel mutations in lysosomal neuraminidase identify functional domains and determine clinical severity in sialidosis
    • Bonten E.J., Arts W.F., Beck M., Covanis A., Donati M.A., Parini R., Zammarchi E., d'Azzo A. Novel mutations in lysosomal neuraminidase identify functional domains and determine clinical severity in sialidosis. Hum. Mol. Genet. 9:2000;2715-2725.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2715-2725
    • Bonten, E.J.1    Arts, W.F.2    Beck, M.3    Covanis, A.4    Donati, M.A.5    Parini, R.6    Zammarchi, E.7    D'Azzo, A.8
  • 8
    • 0026619682 scopus 로고
    • Bacterial sialidases - Roles in pathogenicity and nutrition
    • Corfield T. Bacterial sialidases - roles in pathogenicity and nutrition. Glycobiology. 2:1992;509-521.
    • (1992) Glycobiology , vol.2 , pp. 509-521
    • Corfield, T.1
  • 9
    • 0023663888 scopus 로고
    • Expression of a single transfected cDNA converts fibroblasts to myoblasts
    • Davis R.L., Weintraub H., Lassar A.B. Expression of a single transfected cDNA converts fibroblasts to myoblasts. Cell. 51:1987;987-1000.
    • (1987) Cell , vol.51 , pp. 987-1000
    • Davis, R.L.1    Weintraub, H.2    Lassar, A.B.3
  • 10
    • 0028283168 scopus 로고
    • Cloning and expression of a soluble sialidase from Chinese hamster ovary cells: Sequence alignment similarities to bacterial sialidases
    • Ferrari J., Harris R., Warner T.G. Cloning and expression of a soluble sialidase from Chinese hamster ovary cells: sequence alignment similarities to bacterial sialidases. Glycobiology. 4:1994;367-373.
    • (1994) Glycobiology , vol.4 , pp. 367-373
    • Ferrari, J.1    Harris, R.2    Warner, T.G.3
  • 13
    • 0030963502 scopus 로고    scopus 로고
    • Cux/CDP homeodomain protein binds to an enhancer in the rat c-mos locus and represses its activity
    • Higgy N.A., Tarnasky H.A., Valarche I., Nepveu A., van der Hoorn F.A. Cux/CDP homeodomain protein binds to an enhancer in the rat c-mos locus and represses its activity. Biochim. Biophys. Acta. 1351:1997;313-324.
    • (1997) Biochim. Biophys. Acta , vol.1351 , pp. 313-324
    • Higgy, N.A.1    Tarnasky, H.A.2    Valarche, I.3    Nepveu, A.4    Van Der Hoorn, F.A.5
  • 14
    • 0031975165 scopus 로고    scopus 로고
    • Cloning of the cDNA and gene encoding mouse lysosomal sialidase and correction of sialidase deficiency in human sialidosis and mouse SM/J fibroblasts
    • Igdoura S.A., Gafuik C., Mertineit C., Saberi F., Pshezhetsky A.V., Potier M., Trasler J.M., Gravel R.A. Cloning of the cDNA and gene encoding mouse lysosomal sialidase and correction of sialidase deficiency in human sialidosis and mouse SM/J fibroblasts. Hum. Mol. Genet. 7:1998;115-121.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 115-121
    • Igdoura, S.A.1    Gafuik, C.2    Mertineit, C.3    Saberi, F.4    Pshezhetsky, A.V.5    Potier, M.6    Trasler, J.M.7    Gravel, R.A.8
  • 15
    • 0033006017 scopus 로고    scopus 로고
    • Sialidase-mediated depletion of GM2 ganglioside in Tay-Sachs neuroglia cells
    • Igdoura S.A., Mertineit C., Trasler J.M., Gravel R.A. Sialidase-mediated depletion of GM2 ganglioside in Tay-Sachs neuroglia cells. Hum. Mol. Genet. 8:1999;1111-1116.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 1111-1116
    • Igdoura, S.A.1    Mertineit, C.2    Trasler, J.M.3    Gravel, R.A.4
  • 16
    • 0023614271 scopus 로고
    • Complete cloning of the Duchenne muscular dystrophy (DMD) cDNA and preliminary genomic organization of the DMD gene in normal and affected individuals
    • Koenig M., Hoffman E.P., Bertelson C.J., Monaco A.P., Feener C., Kunkel L.M. Complete cloning of the Duchenne muscular dystrophy (DMD) cDNA and preliminary genomic organization of the DMD gene in normal and affected individuals. Cell. 50:1987;509-517.
    • (1987) Cell , vol.50 , pp. 509-517
    • Koenig, M.1    Hoffman, E.P.2    Bertelson, C.J.3    Monaco, A.P.4    Feener, C.5    Kunkel, L.M.6
  • 17
    • 0034852658 scopus 로고    scopus 로고
    • Harnessing the potential of dystrophin-related proteins for ameliorating Duchenne's muscular dystrophy
    • Krag T.O.B., Gyrd-Hansen M., Khurana T.S. Harnessing the potential of dystrophin-related proteins for ameliorating Duchenne's muscular dystrophy. Acta Physiol. Scand. 171:2001;349-358.
    • (2001) Acta Physiol. Scand. , vol.171 , pp. 349-358
    • Krag, T.O.B.1    Gyrd-Hansen, M.2    Khurana, T.S.3
  • 18
    • 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., Buskin J.N., Lockshon D., Davis R.L., Apone S., Hauschka S.D., Weintraub H. 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    Buskin, J.N.2    Lockshon, D.3    Davis, R.L.4    Apone, S.5    Hauschka, S.D.6    Weintraub, H.7
  • 20
    • 0033582517 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a plasma membrane-associated sialidase specific for gangliosides
    • Miyagi T., Wada T., Iwamatsu A., Hata K., Yoshikawa Y., Tokuyama S., Sawada M. Molecular cloning and characterization of a plasma membrane-associated sialidase specific for gangliosides. J. Biol. Chem. 274:1999;5004-5011.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5004-5011
    • Miyagi, T.1    Wada, T.2    Iwamatsu, A.3    Hata, K.4    Yoshikawa, Y.5    Tokuyama, S.6    Sawada, M.7
  • 21
    • 0033118290 scopus 로고    scopus 로고
    • Cloning and characterization of NEU2, a human gene homologous to rodent soluble sialidases
    • Monti E., Preti A., Rossi E., Ballabio A., Borsani G. Cloning and characterization of NEU2, a human gene homologous to rodent soluble sialidases. Genomics. 57:1999;137-143.
    • (1999) Genomics , vol.57 , pp. 137-143
    • Monti, E.1    Preti, A.2    Rossi, E.3    Ballabio, A.4    Borsani, G.5
  • 22
    • 0035972762 scopus 로고    scopus 로고
    • Role of the multifunctional CDP/Cut/Cux homeodomain transcription factor in regulating differentiation, cell growth and development
    • Nepveu A. Role of the multifunctional CDP/Cut/Cux homeodomain transcription factor in regulating differentiation, cell growth and development. Gene. 270:2001;1-15.
    • (2001) Gene , vol.270 , pp. 1-15
    • Nepveu, A.1
  • 23
    • 0034689287 scopus 로고    scopus 로고
    • An enhanced system for construction of adenoviral vectors by the two-plasmid rescue method
    • Ng P., Parks R.J., Cummings D.T., Evelegh C.M., Graham F.L. An enhanced system for construction of adenoviral vectors by the two-plasmid rescue method. Hum. Gene Ther. 11:2000;693-699.
    • (2000) Hum. Gene Ther. , vol.11 , pp. 693-699
    • Ng, P.1    Parks, R.J.2    Cummings, D.T.3    Evelegh, C.M.4    Graham, F.L.5
  • 24
    • 0018832224 scopus 로고
    • Sialidosis: Delineation of subtypes by neuraminidase assay
    • O'Brien J.S., Warner T.G. Sialidosis: delineation of subtypes by neuraminidase assay. Clin. Genet. 17:1980;35-38.
    • (1980) Clin. Genet. , vol.17 , pp. 35-38
    • O'Brien, J.S.1    Warner, T.G.2
  • 25
    • 0031712378 scopus 로고    scopus 로고
    • The therapeutic reactivation of fetal haemoglobin
    • Olivieri N.F., Weatherall D.J. The therapeutic reactivation of fetal haemoglobin. Hum. Mol. Genet. 7:1998;1655-1658.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 1655-1658
    • Olivieri, N.F.1    Weatherall, D.J.2
  • 28
    • 0029797439 scopus 로고    scopus 로고
    • Sialic acids: Structure, analysis, metabolism, occurrence, recognition
    • Reuter G., Gabius H.-J. Sialic acids: structure, analysis, metabolism, occurrence, recognition. Biol. Chem. Hoppe-Seyler. 377:1996;325-342.
    • (1996) Biol. Chem. Hoppe-Seyler , vol.377 , pp. 325-342
    • Reuter, G.1    Gabius, H.-J.2
  • 29
    • 0029257376 scopus 로고
    • The MyoD family of transcription factors and skeletal myogenesis
    • Rudnicki M.A., 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
  • 31
    • 0030727680 scopus 로고    scopus 로고
    • Biochemistry of glycosphingolipid degradation
    • Sandhoff K., Kolter T. Biochemistry of glycosphingolipid degradation. Clin. Chim. Acta. 266:1997;51-61.
    • (1997) Clin. Chim. Acta , vol.266 , pp. 51-61
    • Sandhoff, K.1    Kolter, T.2
  • 32
    • 0015179162 scopus 로고
    • Enzyme alterations and lipid storage in three variants of Tay-Sachs disease
    • Sandhoff K., Harzer K., Wassle W., Jatzkewitz H. Enzyme alterations and lipid storage in three variants of Tay-Sachs disease. J. Neurochem. 18:1971;2469-2489.
    • (1971) J. Neurochem. , vol.18 , pp. 2469-2489
    • Sandhoff, K.1    Harzer, K.2    Wassle, W.3    Jatzkewitz, H.4
  • 33
    • 0031880987 scopus 로고    scopus 로고
    • Sphingolipid metabolism. Sphingoid analogs, sphingolipid activator proteins, and the pathology of the cell
    • Sandhoff K., Kolter T., Van Echten-Deckert G. Sphingolipid metabolism. Sphingoid analogs, sphingolipid activator proteins, and the pathology of the cell. Ann. NY Acad. Sci. 845:1998;139-151.
    • (1998) Ann. NY Acad. Sci. , vol.845 , pp. 139-151
    • Sandhoff, K.1    Kolter, T.2    Van Echten-Deckert, G.3
  • 36
    • 0029906168 scopus 로고    scopus 로고
    • Amelioration of the dystrophic phenotype of mdx mice using a truncated utrophin transgene
    • Tinsley J.M., Potter A.C., Phelps S.R., Fisher R., Trickett J.I., Davies K.E. Amelioration of the dystrophic phenotype of mdx mice using a truncated utrophin transgene. Nature. 384:1996;349-353.
    • (1996) Nature , vol.384 , pp. 349-353
    • Tinsley, J.M.1    Potter, A.C.2    Phelps, S.R.3    Fisher, R.4    Trickett, J.I.5    Davies, K.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.